organism orgId locusId sysName gene reannotation comment original_desc aaseq Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2554 ABC transporter for L-Histidine, permease component 1 Specific phenotypes on L-Histidine. In a gene cluster that also includes hutD and imidazolonepropionase. Some subunits are annotated as transporting glutamine. Amino acid ABC transporter, permease protein MELDFSPVWAGVPQLLAGALVTVEITAASLLLGCVMGLLVGIGRLNPKRRVVYALCTAYVAAIRGTPLLVQLFILFFGLPQFGILLPAFVCGVIGLGIYSGAYVSEVVRGAIQSIDKGQMEAARSIGMSSGLAMRTVVLPQAVVRMIPPLGNEFIALIKNSALVSLLTIHDLMHEGQKIISVSYRSLEVYLAIAVVYFILTGATTLVLRRIELRLRAGGMVQ Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2555 ABC transporter for L-Histidine, periplasmic substrate-binding component 1 Specific phenotype on L-Histidine. Do not understand why there seem to be two substrate binding proteins for this ABC transporter. Both SBPs have signal peptides, so they seem unlikely to be involved in efflux of a waste product instead. Glutamine ABC transporter, periplasmic glutamine-binding protein (TC 3.A.1.3.2) MNLRRNLLLASLAAAAFCTTGAQAQDNVLRVGTDATFPPMEFVENGKRTGFDIELVEAIAKTMGKQVEWVDIDFKGLIPGLISKRFDMAVSAIYITDERKKVVDFTDSYYAGGLVVMVKADNKAINKLADLDGKKVSVQVGTKSVSYLTEKFPKVQRVEVEKNQEMFNLVDIGRADAAVTGKPAAFQYVRTRPGLRVLDEQLTTEEYGMALRKDTPELTKAVNGAITKLKADGTYAAIVKKWFSNSAAK Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2560 ABC transporter for L-Histidine, ATPase component Specific phenotype on L-Histidine. There may also be a second ATPase component, Ac3H11_2553, but it has no fitness data Urea carboxylase-related ABC transporter, ATPase protein MSSVSIQAVSRVFETAKGQRTQALQPVDFEVRDNDFVTILGPSGCGKSTLLRIVAGLDHATSGRVLLDGAPVEGPGAERGMVFQSYTLFPWLTIEQNIRFGLRERGMPEAQQKERAAYFIAKVGLRGFEQHFPKQLSGGMQQRTAIARALANDPKILLMDEPFGALDNQTRVLMQELLLGIWEAERKTVLFVTHDIDEAIFMANRVAVFSARPGRIKTELAVDLPHPRHYTIKTSPEFMDLKARLTEEIRAESMAADLH Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2561 ABC transporter for L-Histidine, permease component 2 Specific phenotypes on L-Histidine. In a gene cluster that also includes hutD and imidazolonepropionase. Some subunits are annotated as transporting glutamine. ABC transporter, permease protein VSARARWMLGLAFFVVFVAVWAFFTLGGFVSPTFLASPITMAKEGWLLFTEYGFIKDIGMTIWRVVGGFVLAAVIAVPLGIAMGAYKGIEAFFEPFISFCRYLPASAFIPLLILWAGIGEAQKILVIFIGSVFQITLMVAVTVGGARRDLVEAAYTLGAGHKGIVTRVLIPGAAPEIAETLRLVLGWAWTYVIVAELIGSSSGIGHMITDSQSLLNTGQIIFGIIIIGLIGLVSDFAFKALNHRLFAWSFVR Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2562 ABC transporter for L-Histidine, periplasmic substrate-binding component 2 Specific phenotype on L-Histidine. Do not understand why there seem to be two substrate binding proteins for this ABC transporter. Both SBPs have signal peptides, so they seem unlikely to be involved in efflux of a waste product instead. ABC transporter substrate-binding protein MTRSVVKWTSLAAAAACVMALAAPAQAQDTKIVLGMSGWTGFAPLTLADKAGIFKKNGLDVEIKMIPQKDRHLALASKSIQCAATTVETHVAWNANGVPIVQIFQMDKSYGADGIAVRGDIKSFADLKGKTIGVDAPGTAPYFGLAWMLSKNGMSLKDVKTTTLSPQAAAQAFVAGQNDAAMTYEPYLSTVRDNPAAGKILATTLDYPMVMDTVGCDPTWLKANGKAAQALANSYFQALDMIKADPAKSNEIMGAAVKQTGEQFAKSSSFLRWQDKAANQKFFAGELTTFMKDATAILLEAGIIRKANEDLAVTFDASFIK Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2940 D-sorbitol 2-dehydrogenase (EC 1.1.1.14) Specifically important for: D-Sorbitol. Annotated as ribitol dehydrogenase; it could well have both activities, as with AT5G51970 Ribitol 2-dehydrogenase (EC 1.1.1.56) MSAARNLQGQVAAITGAASGIGFASAQTMADAGARVVLIDRDEAALAKACATIGPNALPLVLDLLDARQCASLLQRTLALAGQLDIFHANAGLYVGGDLVDADPDAIDRMLNLNVNVVMKNVHNVLPHMIERGTGDIIVTSSLAAHFPTPWEPVYASSKWAVNCFVQTVRRQVFKHGIRVGSISPGPVITSLLADWPAEKLAEAKASGSLIEAAEVAEVVLFMLTRPRGMTIRDVVMMPTNFDL Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2941 ABC transporter for D-Sorbitol, ATPase component Specific phenotypes on D-Sorbitol. Various polyols ABC transporter, ATP-binding component MAYLQLRGIEKFFGEHRAIKGIDLTIQQGEFIVFVGPSGCGKSTLLRLIAGLEAIDGGSLMLDGRDITDQPSSKRDLAMVFQSYALYPHMSVYENMSFALKLAKVDKQVIDEKVQNAARILNLTQYLQRTPKELSGGQRQRVAIGRAIVRAPKVFLFDEPLSNLDAALRGQTRVEIAKLHRDLGATTIYVTHDQVEAMTLADRVVVLRDGIIEQVGTPLELYDKPANQFVAQFIGTPQMNVVPVDKLPQPVQQQAPAAPAGAAVGAIGLRPENITVRTTGATPVGGQVDLIEALGAETLIYVTTPGGAQFVSRQNDRTDLRVGDAVSLDIDASQAHWFDTAGRVVAGHAA Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2944 ABC transporter for D-Sorbitol, periplasmic substrate-binding component Specific phenotype on D-Sorbitol. Various polyols ABC transporter, periplasmic substrate-binding protein MPRSTRPHTRLALAAAALAASLCGAAAHAQTELVIATVNNGHMIEMQKLSKNFEQAHPDIKLKWVTLEEGVLRQRVTTDIATKGGQFDVMTIGMYEAPIWGKKGWLQELKTDAAYDVDDLLPAVRNGLSIDGKLFAAPFYGESSMLMYRKDLADKAGVQVPERPTWPQIKDLAAKIHDPKNGVYGICLRGKPGWGDNMAFLSTLVNTFGGQWFDMQWKPQLESKPWKEAITFYVDLLKNYGPPGSSANSFNEILALTNSGKCGMWIDATIAASFVSDPKQSKVADQMAFAQAPTMNTPKGANWLWSWNLAIPAGSKKVDAAQKFITWSTSKEYVQLVAKTNGWANVPTGTRKSTYASPEFQKAARFAAAEKVAIDSANPTDSTLPKSPYVGVQFAAIPEFQAIGIAVGQQMSAALAGKTTVDAALKASQVSADREMKKAGYYK Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_4058 required for efflux of an amino acid polymer PFam PF08909.7 (DUF1854). In a conserved cofit operon with a mdlB-like transporter (Ac3H11_4059) and with two cyanophycin synthetase-like genes that produce a different polymer (Ac3H11_4060 and Ac3H11_4061, see PMID:23224585) DUF1854 domain-containing protein VSDLAMNAPLTPSSAPAFQLARNPHGRLVLTLPDGTAHEGVTPVRAFPIAAPGEGLSLVGSDGHELLWIPHVDQVAGPARQLIDEELAVREFVPTIEKIVAVSSFSTPSTWQVETDRGPASLVLKAEEDIRRLGGRTRLLIAGGDGMQFRVKDTTALDRHSRKLLERFL Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_576 required for sulfate utilization, putative electron transport protein for sulfite reductase PFam PF06073.8 (DUF934). conserved cofitness with sulfite reductase; auxotrophic Oxidoreductase probably involved in sulfite reduction MKILASQDHQPPAEGDARTVALANDADALALPLDGVERVDLHFPSFTDGRAFSQAFLLRRRRGFAGDIRATGDVLIDQLVQMQRTGFSSAVLREGVDPADAQRQFERFPGFYQGDAVNPQPLFASKAA Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_614 L-arabinose 1-dehydrogenase; D-galactose 1-dehydrogenase (EC 1.1.1.46; EC 1.1.1.48) Specifically important for: D-Galactose; L-Arabinose. Some other dehydrogenases are known to act on both of these substrates Putative oxidoreductase in arabinose utilization cluster LIDCNIDMTQLFAPSSSSTDATGAPQGLAKFPSLQGRAVFVTGGGSGIGAAIVAAFAEQGARVAFVDVAREASEALAQHIADAGLPRPWWRVCDVRDVQALQACMADAAAELGSDFAVLVNNVASDDRHTLESVTPEYYDERMAINERPAFFAIQAVVPGMRRLGAGSVINLGSTGWQGKGTGYPCYAIAKSSVNGLTRGLAKTLGQDRIRINTVSPGWVMTERQIKLWLDAEGEKELARNQCLPDKLRPHDIARMVLFLASDDAAMCTAQEFKVDAGWV Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_791 ABC transporter for Glycerol, ATPase component 1 Specific phenotype on Glycerol; D-Galactose. Has a TOBE domain after the ATPase domain. The phenotype on galactose is not explained. Glycerol-3-phosphate ABC transporter, ATP-binding protein UgpC (TC 3.A.1.1.3) MQLALDSISKKVGAQTWLYDMSLALQSGAVTVLLGATQAGKTSLMRIMAGLDAPTAGRVTVDGKDVTGMPVRDRNVAMVYQQFINYPSMKVAANIASPLKLRGEKNIDARVREIASRLHIDMFLDRYPAELSGGQQQRVALARALAKGAPLMLLDEPLVNLDYKLREELREELTQLFAAGQSTVVYATTEPGEALLLGGYTAVLDEGQLLQYGPTAEVFHAPNSLRVARAFSDPPMNLMAASATAQGVRLQGGAELTLPLPQGAATAAGLTVGVRASALRVHARPGDVSVAGVVELAEISGSDTFVHASTPWGDLVAQLTGVHYFELGTAITLHLDPAQAYVFGADGRLAQAPARPVTAQGGR Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_792 ABC transporter for Glycerol, ATPase component 2 Specific phenotype on Glycerol. Has a TOBE domain after the ATPase domain. Also mildly important on phenotype on galactose, which is not explained. Glycerol-3-phosphate ABC transporter, ATP-binding protein UgpC (TC 3.A.1.1.3) MARISLDLAHSYKPNPQQDSDYALLPLKMEFEDGGAYALLGPSGCGKTTMLNIMSGLLVPSHGKVLFDGRDVTRASPQERNIAQVFQFPVIYDTMTVAENLAFPLRNRKVPEGQIKQRVGVIAEMLEMSGQLNQRAAGLAADAKQKISLGRGLVRADVAAVLFDEPLTVIDPHLKWQLRRKLKQIHHELKLTLIYVTHDQVEALTFADQVVVMTRGKAVQVGSADALFERPAHTFVGHFIGSPGMNFLPAHRDGENLSVAGHRLASPVGRALPAGALQVGIRPEYLALAQPQQAGALPGTVVQVQDIGTYQMLTAKVGEHTVKARFTPETRLPSSGDTAWLQVLGEHTCYYKNEELLA Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_793 ABC transporter for Glycerol, permease component 1 Specific phenotypes on Glycerol. in a gene cluster for glycerol utilization; see phenotype on both strands Glycerol-3-phosphate ABC transporter, permease protein UgpA (TC 3.A.1.1.3) MSTTTKPVNQKAWFLILPVIICVAFSAILPLMTVVNYSVQDIISPERRVFVGTEWFAAVMRDEELHAALWRQLTFSLAVLAVEIPLGILLALSMPAQGWKSSAVLVVVALSLLIPWNVVGTIWQIYGRADIGLMGRMLQEMGIEYSYTGNATQAWLTVLLMDVWHWTPLVALLAFAGLRSIPDAYYQAARIDGASKFAVFRYIQLPKMRGVLMIAVLLRFMDSFMIYTEPFVLTGGGPGNATTFLSQYLTTKAVGQFDLGPAAAFSLIYFFIILLLCFILYNWMQRVGTVSDEGAGHE Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_794 ABC transporter for Glycerol, permease component 2 Specific phenotype on Glycerol. Glycerol-3-phosphate ABC transporter, permease protein UgpE (TC 3.A.1.1.3) MNEKRFQKRTLFLIAYLLFALLPIYWMVNMSFKTNAEILSTFSFFPQHFTWDNYKTIFTDESWYSGYINSLIYVSINMVITLTVALPAAYAFSRYSFLGDKHVFFWLLTNRMTPPAVFLLPFFQLYTTVGLMDTHIAVALAHLLFSVPLAVWILEGFMSGIPREIDETAYIDGYSFPRFFMTIFLPLIKAGVGVAAFFCFMFSWVELLLARTLTSVNAKPIVATMTRTVSASGMDWATLAAAGVLTIVPGAIVIWFVRHYIAKGFAMGRV Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_796 ABC transporter for Glycerol, periplasmic substrate-binding component Specific phenotype on Glycerol. Has signal peptide but not transmembrane helices, and CDD confirms it in the SBP family, not a permease as sometimes annotated Glycerol-3-phosphate ABC transporter, permease protein UgpA (TC 3.A.1.1.3) MKMQFKAIAFAAAALAMGQAAWAGEAEAKKWIDSEFQPSTLNKDQQMAEMKWFIDAAKKLQAKGVKEISVVSETITTHEYESKTLAKAFEEITGIKVKHDLIQEGDVVEKLQTSMQSGKSIYDGWISDSDLIGTHYRYGKIMNLTDYMGGAGKEWTNPGIDLKDYIGTKFTTGPDGKLYQLPDQQFANLYWFRADLFDRKDIKDKFKAKYGYDLGVPLNWSAYEDIAEFFTNDVKNIDGKPIYGHMDYGKKDPSLGWRFTDAWLSMAGTADIGAPNGLPIDEWGIRVADDKCTPVGASVARGGATNSPAAVYALTKYVDWMKKYAPKEATGMTFGEAGPVPAQGQIAQQIFWYTAFTADMTKPGLPVVNADGTPKWRMAPGPNGPYWKQGMQNGYQDVGSWTFFKDHDANKTAAAWLYAQFVTAKTTSLKKTMVGLTPIRESDIQSKAMTDMAPKLGGLVEFYRSPARVAWSPTGTNVPDYPKLAQLWWKNVAQAVTGEKTPQGAMDTLADEMDQVMARLERAGMAHCAPKLNAKSDPNKWLSDKQAPWKKLANEKPKGETIAYGTLLQAWKDGKTR Shewanella sp. ANA-3 ANA3 7022816 Shewana3_0067 sucrose permease scrT specific phenotype on sucrose; 82% identical to the sucrose transporter scrTII or Sfri_3989, which was validated by complementation (PMCID:PMC2996990); SEED_correct major facilitator transporter (RefSeq) MVSDSNSVENRHHTRIRVLTYLMFFMFAMTSDAVGVIIPQLISEFGLSLSQASAFHYMPMIFIAISGLFLGFLADKIGRKLTILLGLLLFAIACFLFALGESFYYFLLLLALVGLAIGVFKTGALALIGDISRSTKQHSSTMNTVEGFFGVGAMVGPAIVSYLLISGVSWKYLYFGAGVFCLLLCWLAFRADYPQVKRSSTETINLTNTFSMMKNPYALGFSLAIGLYVATEVAIYVWMPSLLQEYQGDYTVLAAYALTIFFTLRAGGRFLGGWILNHFSWQQVMFWFSLAISLCYLGSMLYGVEAAVILLPLSGLFMSMMYPTLNSKGISCFPVAQHGSVAGVILFFTAVSAALAPLCMGLVGDIFGHVKYGFYLATGFAVLLCLLAGVNLIKDPSQALLSRETA Shewanella sp. ANA-3 ANA3 7023996 Shewana3_1204 putative transporter, required for glycine and L-alanine utilization PFam PF03458.9 (UPF0126). Substrates are from the conserved specific phenotypes of UPF0126 hypothetical protein (RefSeq) MQEAQFIGLLWLIGILAEAMTGALAAGRKQMDLFGVVIIGCATAIGGGTLRDMLLGNYPLIWVENVHYLLAIAFASLLTVAIAPVMRYLSKLFLAIDALGLAVFSIVGAQKTLMLGFSPTIAVVMGLVTGVFGGVIRDILCNQVPLIFKKELYAVISLFTAGLYITLNAYQLAEWINLVVCLTLGFSLRMLALRYHWSMPTFDYQANGDQHTH Shewanella sp. ANA-3 ANA3 7024896 Shewana3_2070 L-arabonate dehydratase (EC 4.2.1.25) Specifically important for: L-Arabinose. L-arabonate is an intermediate in the oxidation of L-arabinose (SEED_correct) dihydroxy-acid dehydratase (RefSeq) MCLGRRRCHMNNKKPKTLRSASWFGSDDKNGFMYRSWMKNQGIPEHHFQNKPVIGICNTWSELTPCNGHLRELAQRVKNGIREAGGIPVEFPVFSNGESNLRPSAMLTRNLAAMDTEEAIRGNPIDGVVLLVGCDKTTPALLMGAASCDLPTIVVTGGPMLNGKHKGKDVGSGTLVWELHQEYKAGNISLAAFMNAEADMSRSTGTCNTMGTASTMACMVETLGVSLPHNATIPAVDSRRQVLAHMSGMRIVDMVKEDLTLSKILSRDAFINAIKVNAAIGGSTNAVIHLKAIAGRIGVELSLDDWRHGYTVPTIVNLKPSGQYLMEDFYYAGGLPAVLRQLFEHDLLSKNTLTVNAASLWDNVKEAPCYNQEVIMSLENPLVENGGIRVLRGNLAPRGAVIKPSAASAHLMQHRGKAVVFESFDDYNARIGDPELDIDENSIMVLKNCGPKGYPGMAEVGNMGLPPKLLKKGIKDMVRISDARMSGTAFGTVVLHVAPEAQALGPLAAVQNGDMIALDTYAGTLQLEISDQELQARLAKLATVKSIPVNGGYLSLFKEHVLQADEGCDFDFLVGCRGAEIPAHSH Shewanella sp. ANA-3 ANA3 7024897 Shewana3_2071 L-arabinose 1-dehydrogenase (EC 1.1.1.46) Specifically important for: L-Arabinose. Also, was correctly annotated by PMID:20836887 short-chain dehydrogenase/reductase SDR (RefSeq) MKLTNQYPSLQGKTIFISGGATGIGACLVNAFLEQGAKVAFVDILVEESTQLVADLKQTQPEASVTFYHCDLVDIAALKRVIAQVEDDLGPISVLINNAACDQRHSIDEVTPEYWDQCLNTNLRHYFFAVQAVRPQMQRLGGGSVINLGSMSWHNRQAGMAGYTASKAGAMGLTRGLAADLGKDKIRINTLTPGWVMTKRQLTHWVDKDTAKHIENNQCIKEYVMPEDIAAMALFLAADDSKLCTAQNFIVDGGWI Shewanella sp. ANA-3 ANA3 7024898 Shewana3_2072 L-arabinose 1-epimerase (mutarotase) (EC 5.1.3.3) Specifically important for: L-Arabinose. Was correctly annotated by PMID:20836887 (more specific than EC number); (SEED_correct) aldose 1-epimerase (RefSeq) MQLSVTQKSLQHAAFADELQLVTLTNSHGLEVVLSNYGASIWSVKLYGQAQEPISLSLGYQDIKDWVTNPYYFGITAGRVANRIGKAQFPLAGKTIQLVANEGNNQLHGGPKGLSHCTWQVEMLQDNDSVAAVFSITSPDGDQGFPGNLAITLEYRLNENNELTLNYQAVCDQTTPVCLTNHAYWNLASNKQQGILGHELSIQASHFLALDNEQIPTGELILVDDGAYDFKQPKLIATDIKQLTNGYDHYFVMDRNPDNKNSLQTIAVLKDPLSGRELEISTTEVGVQFYSGNFLDGSHIDDEGYSINQFHGLCLETHGYPNAVNIDHFPSVMLEANTQYQQITVHKFKNI Shewanella sp. ANA-3 ANA3 7024914 Shewana3_2088 L-arabinolactonase (EC 3.1.1.15) Important on L-arabinose; Was correctly annotated by PMID:20836887 (SEED_correct) hypothetical protein (RefSeq) MQTVTVGELLMTIPVGNRLGEGVLWDDLHQSIWWTDILSSVIYRFHLASRSLETFPMPHRVGSFGLTAKPTTLIVAFDIGIAIYDIEDQSLTWLAQPESHFAGNRFNDGRIDRQGRFWAGTMVEQRDTLQQTAALYCLDEKGHCHQHLTNLEISNGLCWSVDGRTLYHADSPKHQIYQYDFDIEQGLLSRKRLFASTSHHIFPDGSDVDAAGYLWNAQWGGGQVVRYRPDGEVDLILKLPVTHPTSIAFGGEKRDLLIVTSAKHSLDASQLDQEPQAGDVFIYPLQGIYGVNSPRFCGQL Shewanella sp. ANA-3 ANA3 7025618 Shewana3_2769 Branched-chain acyl-CoA dehydrogenase (EC 1.3.99.12) Specifically important for: L-Isoleucine. specificity for isoleucine indicates that 2-methylbutanoyl-CoA is a substrate (SEED_correct) acyl-CoA dehydrogenase domain-containing protein (RefSeq) MDFNFNEDQRQFADLARQFAADELAPFAAKWDEEHHFPKDVIQKAGELGFCSLYSPESEGGMGLSRLDASIIFEELSKGCTATTAMLTIHNMATWMVTTWGTDTLRQAWSEPLTTGQMLASYCLTEPGAGSDAASLQTKAVREGDEYVVSGSKMFISGAGSTELLVVMCRTGQAGPKGISAIAIPADSEGIIYGKAEDKMGWNAQPTRLVTFDNVRVPVANLLGEEGQGFTFAMKGLDGGRINIATCSVGTAQAALERATQYMNERQQFGKPLAAFQALQFKLADMATELVAARQMVRLAAFKLDSGDPEATAYCAMAKRFATDVGFQVCDAALQIHGGYGYIREYPLERHFRDVRVHQILEGTNEIMRLIIARRLLDENAGQIL Shewanella sp. ANA-3 ANA3 7025962 Shewana3_3110 N-acetylglucosamine transporter nagP specific phenotype on NAG and D-glucosamine. This protein is similar to SO3503, which was named nagP (PMID:16857666). There is another putative glucosamine transporter (nagX, Shewana3_3111) but the phenotype of 3110 on glucosamine does not seem to be a polar effect. (It is observed on both strands, conserved in S. amazonensis SB2B, and 3110 is downstream of nagX). It apears that both nagP and nagX might be required for glucosamine utilization. NagX has weak similarity to acyltransferases (Q3UDW8, or possibly opgC from Rhodobacter sphaeroides) so nagX might convert glucosamine into another compound before transport by nagP. (SEED_correct) glucose/galactose transporter (RefSeq) MTLDKSQQKSSFLPMAIVAALFFILGFATWLNGSLMPYLKQILQLNPFQASLILFSFYIAVTFTALPSAWVIRKVGYKNGMALGMGIMMLAGLLFIPAAKTQIFGLFLCAQLVMGTGQTLLQTAVNPYVVRLGPEESAAARVSVMGILNKGAGVIAPLVFSALILDSFKDRIGTTLTQVQIDEMANSLVFPYLGMAIFIGVLALAVKKSPLPELSNEDEVAEHTDKGQIKAALSHPNLAFGVIALFVYVAVEVIAGDTIGTFALSLGVEHYGVMTSYTMVCMVLGYTLGIILIPRFISQPTALMISAILGLLLTLAILFGDNNSYAIANALLVPFGGVALPDTLLFIAFLGLANAIVWPAVWPLALSGLGKLTSTGSALLIMGIAGGAFGPLFWGLTSSATDMGQQGGYMVMLPCYLFILFYAVKGHKMRHW Shewanella sp. ANA-3 ANA3 7025966 Shewana3_3114 N-acetylglucosamine kinase (EC 2.7.1.59) Specifically important for: D-Glucosamine Hydrochloride; N-Acetyl-D-Glucosamine. The first step in NAG catabolism. The phenotype on glucosamine is strong and is present on both strands, but is not conserved. It may be a polar effect. (SEED_correct) ATPase, BadF/BadG/BcrA/BcrD type (RefSeq) MGLVQTKDQQLFIGVDGGGSKCRATIYTADGTVLGTGVAGRANPLHGLAQTFASIEASTRQALLDAGMKETDSHLLVAGLGLAGVNVPRLYQDVISWQHPFAAMYVTTDLHTACIGAHRGADGAVIITGTGSCGYAHVGDDSLSIGGHGFALGDKGSGAWLGLKAAEHVLLALDGFATPTALTEMLLKHFGVSDALGIVEHLAGKSSSCYAELARSVLDCANAGDEVARGIVQEGADYISEMARKLFSLNPVRFSMIGGLAEPLQAWLGSDVVAKISETLAPPELGAMYFAQQQFNSVNINE Shewanella sp. ANA-3 ANA3 7026137 Shewana3_3279 Vitamin B12 transporter, permease component (fecCD-like) This protein is cofit with the B12-dependent methionine synthase MetH and is FecCD-like. It probably works with Shewana3_3280 (ABC transporter domain protein with similar phenotypes) and Shewana3_3272 (periplasmic binding protein). This protein is similar to SO_1033 which is also involved in B12 uptake (it is strongly cofit with metH; also see PMCid:PMC3219624) transport system permease protein (RefSeq) MIDTLKLVTMNFFSHIFTPLTRQQWLILGLAGFALLTPIAAASFGAANISFLDVLQVFINKLSHLFMADEAVSTSMTERIVMELRLPRIILAFVAGAGLSLAGSVLQTVTRNPLADPYLFGISSGASFGAVVMLTLFTGSGLFGNAGTIANSGIFSGSGTFAGLLWFSLPFGAFIGASLSVLIVLALAGLGLKSQVERMLLSGVATSFMFSALTSLLLYFASPQATASVLFWSLGSFAKASWSLLVLPSLVVLLSFFIILGWKRQIMALQAGDETAHTLGVNVPKLRLNMLLLCSLITAILVATCGGIGFVGLMIPHTVRLLFPGRQPILLTALVGGLFMVWIDVLARCLLGNQELPVGIITAAIGSFFFLLILRRRKLSN Azospirillum brasilense Sp245 azobra AZOBR_RS03845 AZOBR_RS03845 Histidinol-phosphatase [alternative form] (EC 3.1.3.15) Annotated as this by multiple resources. (auxotroph) (SEED_correct) histidinol-phosphate phosphatase MTEPCPTPLVTLAERLADASGPVIRQYFRTPVAVDDKADASPVTIADREAERTIRAIIEAERPDDGIYGEEFGTKNLDAEWVWVIDPIDGTKSFITGRPIFGTLIALLHRGRPVLGVIDQPIVRDRWLGVEGRPTLFNGQPARVRECAGGLAAATLGTTSPDLFPGADQDAFRRVAGAAKVSVYGGDCYSYGLLAAGYYDLVVESGLKLYDFAALVPVVTGAGGLMTDWDGRPLDATSSGRVVAAGDARTHRETLAALAG Azospirillum brasilense Sp245 azobra AZOBR_RS08235 AZOBR_RS08235 L-proline and D-alanine ABC transporter, permease component 1 specific phenotype on L-proline and D-alanine and cofit with other subunits nearby branched-chain amino acid transporter permease subunit LivH MEYFLQQLINGLSLGAIYGLIAIGYTMVYGIIGMINFAHGEIYMIGAFVALITFLAIGSLGITWVPLALLVMLVASMLFTAVYGWTVERIAYRPLRSSPRLAPLISAIGMSIFLQNYVQILQGARSKPLQPILPGNLTLMDGAVSVSYVRLATIVITIALMYGFTQLITRTSLGRAQRACEQDKKMAGLLGVNVDRVISLTFVMGAALAAVAGMMVLLIYGVIDFYIGFLAGVKAFTAAVLGGIGSLPGAMLGGVVIGLIEAFWSGYMGSEWKDVATFTILVLVLIFRPTGLLGRPEIEKV Azospirillum brasilense Sp245 azobra AZOBR_RS10130 AZOBR_RS10130 required for sulfate utilization, putative electron source for sulfite reductase CysI PFam PF11011.4 (DUF2849). conserved cofit with sulfite reductase and has a complementary pattern of gene presence as cysJ hypothetical protein LKAITANRLRDGEVIFLAPGPGLGWVERLDDAALFEDAAAADTALAAAKAQAEGEQFAVDVYAFDLRVTDGQRVPVKTRERIRALGPTVRIDLGKQAAA Azospirillum brasilense Sp245 azobra AZOBR_RS15920 AZOBR_RS15920 Large component of TRAP-type D-gluconate transporter specific phenotype on D-gluconic acid and cofit with other components nearby; 56% identical to SMa0250 of S. meliloti, which is required for gluconate utilization (PMCid:PMC2631997). Also is 56% identical to Atu2743 of A. tumefaciens, which takes up galacturonate (PMCid:PMC4751846), so this might also be a galacturonate transporter (we did not study galacturonate utilizaton in this organism) dehydroascorbate transporter MALAVFLSSLFGLMLLGMPIAFALMLTGVALMVHLDFFDAQLVAQNMLSGADNYPLMAVPFFILAGELMNAGGISQRIINLAVSLVGHIRGGLGYVTIGASVMLASLSGSAIADTAALATLLIPMMRDNGYPVPRSAGLIASGGIIAPIIPPSMPFIIFGVTTNTSISGLFMAGIVPGLLMGAGLVITWMFVVRGMTVKLQPKASWGERRTALVEGVWALALPVIIIGGLRGGIFTPTEAAVVAAVYSLVVALFVYRQVTLKDLVPLLVQAARTTSTVMFLCAAALVSSYMVTLADLPQQMNEMLAPLLHEPKLLMVAITLLLLAVGTVMDLTPTILVLGPVLTPLAAAAGIDPTYFGVMFVLTGTLGLIHPPVCTVLNVVCGVARISLESATRGIWPFLLTYLLLLCLLIAVPEIVTAPLAFFRH Azospirillum brasilense Sp245 azobra AZOBR_RS18550 AZOBR_RS18550 ABC transporter for nitrate, ATPase component Specific phenotype on Sodium nitrate. (SEED_correct) ABC transporter ATPase MAILELKNVAKSYGGTEVLRGIDLSIAEGEFVAIVGFSGAGKTTLVNLMGGLAAPDAGTVLFRGAPVRGPGAERGVVFQNYSLMPWLSVKDNVALAVDAVHKGKPSPERGVLTRRAVETVGLGHATDRRPKELSGGMRQRVGFARALAMSPEMLLLDEPLSALDALTRAKLQDEIEAIWRKDRKTVVLITNDVDEAILLADRIIPLTPGPGATLGPAFAVDLPRPRDRTAVNHDPDFKRLRAEVTAWLMEAGASRAAAAVDESLTMPAATPITAAPPPKAYLAGQPGGLSDDRYVEFSRVTKTFATPKGPLTVVDGFDLKMRKGEFISLIGHSGCGKSTVLSMVAGLADVSSGGIVLDGKEVVGAGPDRAVVFQAPSLFPWLTALENVMLGVDRVYPQAGRGERNDIARYYLSRVGLGNAMHKTAAELSNGMKQRVGIARAFALSPKLLLLDEPFGMLDSLTRWELQEVLMEVWARTQVTAICVTHDVDEAILLADRVVMMSNGPNARIGHILEVDIPHPRTRQALLEHPRYYAYREELLNFLEGGHHGTVKAA Azospirillum brasilense Sp245 azobra AZOBR_RS18555 AZOBR_RS18555 ABC transporter for nitrate, permease component Specific phenotypes on Sodium nitrate; Sodium nitrate. Other substrates proposed by KEGG )sulfonate and taurine) were not tested. (KEGG_correct) nitrate ABC transporter permease MTSVTEASTLSSAEAMRARRKARLAHALNRTAATLQIVGLGWLSPLLRMAAGDSPRQQGQELWQQMGVPLTALMLFLAAWAWLAPQVNTSLGAIPGPAQVWEQIGILHADHKAERAKEAAFYDRQAKRNAELLAKDPAAEVKTRPYAGKPTYLDQILTSLKTVFTGFLLGALVAVPLGVACGLSRTVNAAMNPLIQIFKPVSPLAWLPLVTMVVSATVSSDNPTFEKSFLTSAVTVTLCSLWPTLINTAVGVSSIDKDLMNVGKVLQLSGPTMVRRLVLPSALPYIFTGLRLSLGVGWMVLIAAEMLAQNPGLGKFVWDEFQNGSSSSLARIMVAVFTIGLIGFLLDRVMLAFQAAVSHTGTR Azospirillum brasilense Sp245 azobra AZOBR_RS18560 AZOBR_RS18560 ABC transporter for nitrate, periplasmic substrate-binding component Specific phenotype on Sodium nitrate. (SEED_correct) nitrate ABC transporter substrate-binding protein IRLPASPRTALLSAAATLALMLGSAQAAPLDVEKDQLKLGFIKLTDMAPLAIAAEKGFFEDEGLSVTLEPQANWKVLLDRVISGELDGAHMLAGQPLGATIGFGTQANVVTAFSMDLNGNGITLSNEVWERMKPNLPKGPDGKPLHPIKADALKPVIAQYRAEGKPFTMGMVFPVSTHNYELRYWLAAGGINPGYYAPNDVSGQIQADALLSVTPPPQMPATLEAGTIFGYSVGEPWNQQAVMKGIGVPVITDTEIWKNNPEKVFGVTEGWAAKNPKTHLALVKALIRAAMWLDENGNANRAEAVKILAKSEYVGADAKVIANSMTGTFEYEKGDKRAVPDFNVFFRYNATYPFYSDAVWYLTQMRRWGQIAEAKPDAWYDETARKVYKPEIYLKAARLLVEEGKAKEADFPWTSDGYKPLDNGFIDGIAYDGRKPNEYLTKLPIGLKGGQAVQGGQLVGG Azospirillum brasilense Sp245 azobra AZOBR_RS19025 AZOBR_RS19025 acetylornithine/N-succinyldiaminopimelate aminotransferase [EC:2.6.1.11 2.6.1.17] Annotated as this by KEGG. Bifunctional argD. SEED has only the acetylornithine activity. (essential) (KEGG_correct) acetylornithine aminotransferase VIPVVMPTYARADIVFERGEGPYLYATDGRRFLDFAAGVAVNVLGHANPYLVEALTAQAHKLWHTSNLFRVAGQESLAKRLTEATFADTVFFTNSGAEAWECGAKLIRKYHYEKGDKARTRIITFEQAFHGRTLAAVSAAQQEKLIKGFGPLLDGFDLVPFGDLEAVRNAVTDETAGICLEPIQGEGGIRAGSVEFLRGLREICDEHGLLLFLDEIQCGMGRTGKLFAHEWAGITPDVMAVAKGIGGGFPLGACLATEKAASGMTAGTHGSTYGGNPLATAVGNAVLDKVLEPGFLDHVQRIGGLLQDRLAGLVAENPAVFKGVRGKGLMLGLACGPAVGDVVVALRANGLLSVPAGDNVVRLLPPLNIGEAEVEEAVAILAKTAKELV Azospirillum brasilense Sp245 azobra AZOBR_RS20485 AZOBR_RS20485 histidinol-phosphate aminotransferase [EC:2.6.1.9] Annotated as this by multiple resources. AZOBR_RS08675 is also sometimes annotated with this function but has little phenotype. (auxotroph) (KEGG_correct) histidinol-phosphate aminotransferase MTQPNNGPAPRPGILDIAPYVGGEHAGHIRLASNEGALGPSPRAVEAYRAAAGELHRYPDGGSAKLRKAIAERFGLDADRVVCGAGSDELIALLIRAYAGPGDEVLYSQHGFLMYPIGAKSVGATPVQAPETNLTTDVDSLLAHVTPRTRLVFVANPNNPTGTYITADEMARLHAGLPENAILVIDAAYAEYMNHNDYSAGQELVDRFPNVVMTRTFSKIFALGSVRLGWAYCPAGIADVLNRVRGPFNVSSAAQIAGVAALEDTAFLERSRSHNIEWREWFVQQVHGLGLKTHPSVTNFVLVDFAGQTAGKDDAEAARLFLKGRGILVRQMPAYGLPSCLRVTIGTEAEMREVVQALKDFLAA Burkholderia phytofirmans PsJN BFirm BPHYT_RS02015 BPHYT_RS02015 phenylpyruvate ferredoxin oxidoreductase (EC 1.2.7.8) Specifically important for: L-Phenylalanine. Annotated as indolepyruvate ferredoxin oxidoreductase, which has the same EC number; alternatively, could be a decarboxylase, but did not identify a separate aldehyde dehydrogenase MFS transporter MTARLPIDGTPALADYKLSDNLTATRGRIFLTGTQALVRLVLMQRAADKARGMNTAGFISGYRGSPLGMVDQQLWKAKKLLAASDIRFLPAINEELGGTAVLGTQRVESDPERTVEGVFAMWYGKGPGVDRAGDALKHGNAYGSSPHGGVLVVAGDDHGCVSSSMPHQSDFAMMAWHMPVVNPSNIADMLEFGLYGWELSRFSGAWVGYKAISETVESGSTVDLDALRTDWTMPQDFEVPAGGLHNRWPDLPSLTIESRMHAKLDAVRHFARVNSIDKWIAPSPHANVGIVTCGKAHLDLMETLRRLDLTVADLEAAGVRIYKVGLSFPLEMTRIDAFVSGLSEVLVIEEKGPVIEQQIKDYLYNRTQGTRPIVVGKNAEDGTLLLSSLGELRPSRILPVFANWLAKHKPALDRRERVVDLVAPQILSNAADSVKRTPYFCSGCPHNTSTKVPEGSIAHAGIGCHFMASWMERDTTGLIQMGGEGVDWASHSMFTKTRHVFQNLGDGTYFHSGILAIRQAVAAKATITYKILYNDAVAMTGGQPVDGSISVPQIARQVEAEGVSRFVVVSDEPEKYDGHHDQFPKGTTFHHRSEMDTVQRQLRDTDGVTVLIYDQTCAAEKRRRRKKGEFPDPDKRLFINEEVCEGCGDCGVQSNCLSVEPVETALGRKRRIDQSSCNKDYSCVNGFCPSFVTVEGGKLKKAAGAAFDPQALAARVEALPIPATHLDAAPYDILVTGVGGTGVVTVGALISMAAHLEGKSASVLDFMGFAQKGGSVLSFVRFAARDEWLNQVRIDTQQADVLLACDMVVGASADALQTVRHGRTRIVVNTHAIPNATFVTNPDATLHADALLDKMRHAAGAERMSTCDAQALATRFLGDTIGANILMLGYAWQLGLVPVSFGAMMRAIELNNVAVQMNQLAFSIGRLAAEDPAALEALWQARHLAKQSVRVDTLDELIAHREGRLQTYGGASYVKRYRALVDAARRAETSVDAKSERVTRAVATTFYRLLAVKDEYEVARLHTDAVFREALEAQFEGVAGKDFGIKFNLAPPTLTRPEPGKNPVKKTFGQWMWPVLGTLAKFSSLRGTMLDPFGRTLERKMERELAGDYETTLQRALARLDAGNLEDVAKLADLHARVRGYGHVKLANLAGVKRGERDLAARLQIEAATGESVRKSLEEMKGAGQLRGIPVVVAK Burkholderia phytofirmans PsJN BFirm BPHYT_RS02740 BPHYT_RS02740 N-acetylglucosamine-specific PTS system, I, HPr, and IIA components (nagF) Specifically important on NAG and cofit with the IIBC component nearby (BPHYT_RS02745). 58% identical to nagF or H16_A0311 of R. eutropha, which is important for NAG utilization (PMCid:PMC3127587). 58% similar to PA3760, which is required for NAG utilization in P. aeruginosa (PMCid:PMC2542419) PTS glucose transporter subunit IIA MSHSEGHIVLLAPMTGPVVPLANVPDPVFSGGMFGDGIGVDPLEGRLVAPCDATVTHLARTGHAVTLATAEGAEILLHIGIDTVELNGKGFAPMVAQGAHVRAGDVLIEFDQDQVALNAPSLVSVIAIANSDAFEIVERVQGGLLKAGETPLLVLRARDGAAAEASRQLSSTNVTEEARQQVTLVHAGGLHARPAARAREAARGFDARVEVRYEGRKAAIESVVGLLGLGAGEGATVELLGMGPQAAAAVAAIANELTREAHGEVEEKPARQSSPAPQAVARPAGETLAPNTLAGVCAAPGVAVGKLVRWDDADIDPPEKANGTSAAESRLLDKAIATVDADLDTTVRDASQRGAVGEAGIFSVHRVLLEDPTLLDAARDLISLGKSAGFAWREAIRAQIAILTNIEDALLAERAADLRDIEKRVLRALGYTSATARTLPEEAVLAAEEFTPSDLSTLDRSRVTALVMARGGATSHAAILARQAGIPALVAVGDALHAIPEGTQVVVNATTGRLEFAPTELDVERARLERTRLADVREANRRTSQQAAVTSDGRAIEVAANIATLDDAKTAVENGADSVGLLRTELLFIHRAAAPTTDEHRQSYQAIVDALSGRTAIIRTLDVGADKEVDYLTLPPEPNPALGLRGIRLAQVRPDLLDDQLRGLLAVQPLGAVRILLPMVTDVGELIRIRKRIDEFARELGRTEPIEVGVMIEVPSAALLADQLAQHADFLSIGTNDLTQYTLAMDRCQADLAAQADGLHPAVLRLIAATVQGADKHGKWVGVCGALAGDPLAMPLLVGLGVTELSVDPVSVPGIKARVRNLDYQLCRQRAQDALALESAQAVRAASRETWPLD Burkholderia phytofirmans PsJN BFirm BPHYT_RS02745 BPHYT_RS02745 N-acetylglucosamine-specific PTS system, IIBC components (nagE) Specifically important on NAG and cofit with the I-HPr-IIA component nearby (BPHYT_RS02740). CDD or PFam do not show any sign of this gene containing a IIA component, so the SEED annotation is misleading. 62% similar to H16_A0312 (nagE) and 58% similar to PA3761, which are both involved in NAG utilization (PMCid:PMC3127587, PMCid:PMC2542419). KEGG_correct. PTS system N-acetylglucosamine-specific transporter subunit IIBC MDGNPFLKIQRLGRALMLPIAVLPVAGLLLRLGQPDVFNIKMIADAGGAIFDNLPLLFAIGVAVGFAKDNNGVAGLAGAIGYLIEVAVMKDINDKLNMGVLSGIVAGIVAGLLYNRYKDIKLPDYLAFFGGKRFVPIVTGVVCLVLGIAFGYVWQPVQAVIDTAGHWLTTAGALGAFVFGVLNRLLLVTGLHHILNSLTWFVFGTFTPPGGAAVTGDLHRFFAGDPTAGTFMTGFFPVMMFGLPAACLAMFHEAPKERRAVVGGLLFSMALTSFLTGVTEPIEFSFMFLAPVLYVIHALLTGISLAICSALGIHLGFTFSAGAIDYVLNYGLSTRGWWAIPIGLVYMVVYYGLFRFFIRKFNMATPGREPAAADEQVDSFAAGGFVSPVAGTAVPRAQRYIAALGGASNLSVVDACTTRLRLSVVDSNKVSENELKTIGARGVLKRGSTNVQVIIGPEADIIADEIRTVIAQGGGDAVKPAAAAPAQVVAAAPVAASVAQGSGPLDPDPLRWLAVFGGAGNVLSLDAIAATRLRIVVRDPSAVDRQRLATLDTAWISADTFHIVVGDAAQRYAEKLATRTTQSGGATPLPA Burkholderia phytofirmans PsJN BFirm BPHYT_RS03150 BPHYT_RS03150 Phosphoglycerate dehydrogenase (EC:1.1.1.95) Auxotrophic, and rescued by L-serine or gly-glu. Glycine could yield serine via hydroxymethyltransferase, so this is consistent with a role in serine synthesis. BPHYT_RS31960 is also a possibility but gene context suggests that has a role in catabolism and has little phenotype; BPHYT_RS01425 is a possibility, but fitness data suggests it is cell wall related (auxotroph) FAD-linked oxidase MNAPQVFDPHGAAATVAADPEARLREIPYNYTSFSDREIVIRLLGDEAWAVLAELRAERRTGRSARMLYEVLGDIWVVRRNPYLQDDLLDNPKRRAMLIEALHHRLSEIEKRRRADLTEHGDEAGVDRAARVETLVQAARRAVDEFASEFQKTYDLRKRATKVLGKVTEKDNIKFDGLSRVSHVTDATDWRVEYPFVVLTPDTEAEIAGMIKACFELGLTVIPRGGGTGYTGGAVPLTPFSAVINTEKLEQLGAVEMTELPGVDRKVATIFSGAGVVTRRVTEAAEQAGFVFAVDPTSLDASCVGGNVAMNAGGKKAVLWGTALDNLAWWRMVDPEGNWLEVTRLDHNMGKIHDIEVARFRLDWFDGNYAPGEKLMRTEALDIKGRVFRKEGLGKDVTDKFLAGLPGVQKEGCDGLITSARWVLHKMPAHTRTVCLEFFGQARDAIPSIVEIKDYLFETSKQGGAILAGLEHLDERYLRAVGYATKSKRNAFPKMVLIGDIVGDDADAVAQATSEVVRMANGKSGEGFVAVNAEARKRFWLDRSRTAAIAKHTNAFKINEDVVIPLDRMGEYTDGIERINIELSIKNKLQLVDALEAFFKGGKLPLGKSDDANEIPSAELLEDRVQQALDLLKRVRTRWEFLRDKLDLSLREAQHYLVGLGYEAMAEKFADRVDAQPDVNVFHVTQDRTIRVSWKQEIRAELRQIFNGGEFKPILDEAQAIHKQVLRGRVFVALHMHAGDGNVHTNLPVNSDNYEMLQDAHTAVARIMKLARSLDGVISGEHGIGITKLEFLTEDEISEFRQYKQRVDPHGRFNAGKLLEGADLRNAYTPSFGLMGYESLIMQQSDIGAISESIKDCLRCGKCKPVCATHVPRANLLYSPRNKILATSLLVEAFLYEEQTRRGVSIKHWDEFNDVADHCTVCHKCVTPCPVKIDFGDVTMNMRNLLRKMGKKKFNPGNAAGMFFLNATNPQTINLARTAMMGVGYKAQRLGNEVLKKFTKKQTAHPPATVGKPPVTQQVIHFMNKKMPGNLPKKTARALLDIEDNKIVPIIRNPKTTTADTEAVFYFPGCGSERLFSQVGLATQAMLWEAGVQTVLPPGYLCCGYPQRGSGQFDKAEQIVTDNRVLFHRVANTLNYLDIKTVVVSCGTCYDQLAGYEFEKIFPGCRIIDIHEFLLEKGMKLDGVNGVRYMYHDPCHTPIKTMDPIKLVNQLMGSEKDGYKIEKNDRCCGESGTLAVTRPDISTQVRFRKEEEIRKGAAKLRGIPLVAEAGANGINPANASAGSAGAPEGSVLKAGDGPQPKGATDVKILTSCPSCLQGLSRYNEDAGIEADYIVVEMARHVLGEDWMVDYVQRANNGGIERVLV Burkholderia phytofirmans PsJN BFirm BPHYT_RS03220 BPHYT_RS03220 Acyl-CoA dehydrogenase (EC 1.3.8.7) Specifically important for: Tween 20; Trisodium citrate dihydrate. Tween 20 hydrolyzes to a mix of C12, C14, and C16 fatty acids; this is probably part of beta oxidation. The phenotype on citrate is milder and is not explained, but it is conserved. (SEED_correct) acyl-CoA dehydrogenase MGQYAAPLRDMQFVLHELLNVEAEIKQMPKHADLDADTINAVLEEAGKFCSEVLFPLNHSGDQEGCTYVGDGVVTTPKGFKEAYAQYVEAGWPALGCDPEYGGQGLPAFVNNALYEMLNSANQAWTMYPGLSHGAYECLHAHGTPELQQRYLPKLVAGVWTGTMCLTEPHCGTDLGILRTKAEPNSDGSYAISGTKIFISSGEHDLAENIVHLVLARLPGAPNGTKGISLFIVPKFVPNEAGEPGERNGVKCGSIEHKMGIHGNATCVINLDNAKGWLVGEPNKGLNAMFVMMNAARLGVGMQSLGLTEIGYQNSLTYAKERLQMRSLTGPKAPEKAADPIIVHPDVRRMLLTQKAYAEAARAFSYWSALHIDKELSHADESVRKEAADLVALLTPILKAFLSDNAFESTNHAMQIYGGHGFIAEWGMEQYVRDARINMIYEGTNAIQALDLLGRKILGDMGAKMKKFGKLVSDFVEAEGVKPEMQEFINPLADIGEKVQKLTMEIGMKAMQNPDEVGAAAVPYLRTVGHLVFSYFWARMARVALDKEASGDPFYKAKLATARFYFAKLLPETAMTIRQARAGSKSLMDVEEALF Burkholderia phytofirmans PsJN BFirm BPHYT_RS03625 BPHYT_RS03625 Histidinol-phosphatase (EC:3.1.3.15) Auxotrophic, and rescued by histidne. It is usually annotated as phosphoserine phosphatase but that does not match its phenotypes and there is another putative serB. The only homolog of the traditional hisB phosphatase part is the essential protein BPHYT_RS03340, which seems more likely to be ghmB for cell wall synthesis. (auxotroph) phosphoserine phosphatase MANLALFDLDHTLIPTDSDHEWGRFMVKHGMVDAENFARENDRFFADYKAGKLDIHAYLIAMLTPLSKYTRAQLADFHAQYMHEVIKPAIFPVALELVKQHRETGDLCCVVTATNEFITRPIAQAFGVDALIACEAETVDGEPHSPYTGRPTGTPSYKEGKIVRTEAWLASLGKTWSDFERSYFYSDSHNDIPLLEKVTDPIATNPDDTLRAHAQAKGWRILELFQPS Burkholderia phytofirmans PsJN BFirm BPHYT_RS04730 BPHYT_RS04730 required for sulfate utilization, putative electron transport protein for sulfite reductase PFam PF06073.8 (DUF934). conserved cofitness with sulfite reductase; auxotrophic oxidoreductase MASIIKNRAIVNDDWTVVRAAEDGTLPTVNELPAGKVLVPLALWQAERDALIASRSAAEIGVWLAPDSEPADIVADFDKIALIGVDFPVFRDGRGYSIGRLLRERYGYKGELRAIGDVLRDQLAFMFRCGFDAYALRADKDFDDALKAFDEFSFNYQGAVNSSPLFRRREAGELAKASA Burkholderia phytofirmans PsJN BFirm BPHYT_RS07675 BPHYT_RS07675 ABC transporter for L-Arginine, permease component 2 Very important for utilization of L-arginine histidine/lysine/arginine/ornithine ABC transporter permease HisQ MFLYGFGPVLLAGTIQTIELSVLSLAAAVLLGLAGAAAKLSFNRPLRAIATGYTTLIRSVPDLVLMLLLFYSIQIAVNNLTDALNLPQFDIDPFVAGVLTLGFIYGAYFTETFRGAFLAVPRGQLEAGSAYGMSGARVFTRILFPQMMRFALPGIGNNWQVLVKATALVSIIGLADVVKAAQDAGKSTFNMFFFILVAALIYLAITTASNLVLIWLEKRYSIGVRHAEL Burkholderia phytofirmans PsJN BFirm BPHYT_RS07680 BPHYT_RS07680 ABC transporter for L-Arginine, permease component 1 Specific phenotypes on L-Arginine. no phenotype on histidine histidine/lysine/arginine/ornithine ABC transporter permease HisM MIDILNQFWRAFLYWDGQRMSGLAVTLWLLVASVGIGFCAAIPLAVARVSKKRWLSTPVRLYTYVFRGTPLYVQLLLIYTGMYSLEFVRSHQLLDAFFRSGFHCAILAFALNTCAYTTEIFAGAIRSTSHGEVEAARAYGMSWFTMYRRIVIPSALRRALPLYSNEVILMLHATTVAFTATVPDILKVARDANSATYQSFDAFGLAALIYLVVSFVLVALFRRAERHWLGYLAVRTH Burkholderia phytofirmans PsJN BFirm BPHYT_RS07685 BPHYT_RS07685 ABC transporter for L-Arginine, putative ATPase component This is presumably the ATPase component but lacks fitness data. histidine ABC transporter ATP-binding protein MLHTTQTEACKLAVQDIHKRYGDNEVLKGVSLNANKGDVISIIGASGSGKSTFLRCINFLERPNAGQIVVDGEMVKTKTDRAGNLEVADHKQLQRIRTKLAMVFQHFNLWAHMNVLENIVEAPIHVLGLKRKEAEDRAREYLEKVGLAPRLEKQYPSHLSGGQQQRVAIARALAMNPDVMLFDEPTSALDPELVGEVLKVMQKLAEEGRTMIVVTHEMGFARNVSNHVMFLHQGRTEEEGLPAEVLSAPRSERLKQFLSGSLK Burkholderia phytofirmans PsJN BFirm BPHYT_RS07735 BPHYT_RS07735 ABC transporter for L-Arginine, periplasmic substrate-binding component Specific phenotype on L-Arginine. Not near the permease components ABC transporter substrate-binding protein MKMNWRNIAALALFAAASATAGTAAAADIKEVHFGVEASYAPFESKSPSGELQGFDIDVGNAVCAKLKAKCVWVENSFDGLIPALQARKFNAINSDMTITDQRRQAVDFTDPIYTIPNQMIAKKGSGLLPTPASLKGKHVGVLQGTIQETYAKARWAPAGVDVVPYQTQDQIYADLASGRLDAAFQDAEAASKGFLKKPQGAGFEFAGPAVTDEKLLGAGVGFGVRKGDKALKDALNQALKELKADGTIDRFAAKYFDVKVVLK Burkholderia phytofirmans PsJN BFirm BPHYT_RS11290 BPHYT_RS11290 2-ketogluconate 6-phosphate reductase (EC 1.1.1.43) Specifically important for: D-Gluconic Acid sodium salt. Gluconate is probably primarily catabolized via gluconate kinase (BPHYT_RS16720) and the Entner-Doudoroff pathway (starting with phosphogluconate dehydratase, BPHYT_RS16735). However it appears that there is a side pathway involving gluconate 2-dehydrogenase (BPHYT_RS14520, which has no phenotype because this side path is not beneficial), 2-ketogluconate kinase (BPHYT_RS11300, no fitness data), and 2-ketogluconate-6-P reductase (this gene). A similar side path is known in P. putida (PMCID:PMC4646247) and this gene is similar to the P. putida 2-ketoglutarate-6-phosphate reductase (PP3376). (SEED_correct) bifunctional glyoxylate/hydroxypyruvate reductase B MKKIVAWKSLPEDVLAYLQQHAQVVQVDATQHDAFVAALKDADGGIGSSVKITPAMLEGATRLKALSTISVGFDQFDVADLTRRGIVLANTPDVLTESTADTVFSLILASARRVVELAEWVKAGHWQHSIGPALFGVDVQGKTLGIVGLGRIGGAVARRAALGFNMKVLYTNRSANPQAEEAYGARRVELAELLATADFVCLQVPLTPETKHLIGAAELKSMKKSAILINASRGATVDEKALIEALQNGTIHGAGLDVFETEPLPSDSPLLKLANVVALPHIGSATHETRHAMARNAAENLVAALDGTLTSNIVNREVLSK Burkholderia phytofirmans PsJN BFirm BPHYT_RS16050 BPHYT_RS16050 xylitol 2-dehydrogenase (EC 1.1.1.9) Specifically important for: Xylitol. (SEED_correct) iditol 2-dehydrogenase MTTQSTDHDQQNMTAIVCHAPKDYRVEQVSKPRAGAHELVIRIAACGICASDCKCHSGAKMFWGGPSPWVKAPVIPGHEFFGFVEEIGEGAADHFGVKMGDRVIAEQIVPCGKCRYCKSGQYWMCEVHNIFGFQREVADGGMAEYMRIPPTAIVHKIPDGISLEDAAIIEPLACAIHTVNRGEVQLDDVVVIAGAGPLGLMMTQIAHLKTPKKLVVIDLVEERLALAREYGADVTINPKQDDALAIIHSLTDGYGCDVYIETTGAPIGVNQGMDLIRKLGRFVEFSVFGADTTLDWSVIGDRKELDVRGAHLGPYCYPIAIDLLARGLVTSKGIVTHGFSLEEWDEAIKIANSLDSIKVLLKPRA Burkholderia phytofirmans PsJN BFirm BPHYT_RS16095 BPHYT_RS16095 ABC transporter for D-Sorbitol, ATPase component Specific phenotype on D-Sorbitol. sugar ABC transporter ATP-binding protein MASVTLRNIRKAYDENEVMRDINLDIADGEFVVFVGPSGCGKSTLMRMIAGLEDISGGDLTIDGMRVNDVAPAKRGIAMVFQSYALYPHMTLYDNMAFGLKLAGTKKPEIDAAVRNAAKILHIDHLLDRKPKQLSGGQRQRVAIGRAITRKPKVFLFDEPLSNLDAALRVKMRLEFARLHDELKTTMIYVTHDQVEAMTLADKIVVLSAGNLEQVGSPTMLYHAPANRFVAGFIGSPKMNFMEGVVQSVTHDGVTVRYETGETQRVAVEPAAVKQGDKVTVGIRPEHLHVGMAEDGISARTMAVESLGDAAYLYAESSVAPDGLIARIPPLERHTKGETQKLGATPEHCHLFDSAGKAFQRKIVEVLAA Burkholderia phytofirmans PsJN BFirm BPHYT_RS16115 BPHYT_RS16115 ABC transporter for D-Sorbitol, periplasmic substrate-binding component Specific phenotype on D-Sorbitol. sugar ABC transporter substrate-binding protein MKPALKSTLKAVSAGAVACFALSASAATVTIATLNNPDMIELKKLSPEFEKANPDIKLNWVILEENVLRQRATTDITTGSGQFDVMTIGAYETPQWGKRGWLTPLTNLPADYDLNDVVKTARDGLSSGGQLYALPFYVESSMTYYRKDLFEKAGLKMPDQPTYDQIKQFADKLTDKANGIYGICLRGKAGWGENMAYGTTVVNTFGGRWFDEKWNAQLTSPEWKKAMTFYVDLLKKDGPPGASSNGFNENLTLMSSGKCAMWIDATVAAGMLYNKQQSQIADKVGFAAAPVAVTPKGSHWLWAWALAIPKSSKQADAAKKFITWATSKQYIELVAKDEGWASVPPGTRKSTYARAEYKQAAPFGDFVLKAIETADPEHPTLKPVPYTGVQFVGIPEFQSFGTVVGQSISGAIAGQMTIDQALAAGNATADRAVKQAGYQK Burkholderia phytofirmans PsJN BFirm BPHYT_RS16120 BPHYT_RS16120 sorbitol dehydrogenase, D-fructose forming (EC 1.1.1.14) Specifically important for: D-Sorbitol. The KEGG EC number implies that sorbose would be the product, but it is not clear how sorbose would be consumed. The only other genes with specific phenotypes on sorbitol are an ABC transporter, the fructokinase BPHYT_RS02045, and an apparent polar effect on mannose isomerase BPHYT_RS02050. Also this protein is 60% similar to DHSO_RHOSH (polS), which is annotated in UniProt as forming sorbose but is believed to form D-fructose, see PMID: 15805591 (SEED_correct) sorbitol dehydrogenase MAARLQDKVAILTGAASGIGEAVARRYLDEGARCVLVDVKPADSFGDSLRATYGDRVLTVSADVTRRDDIQRIVASTLERFGQIDILFNNAALFDMRPILEESWDVFDRLFAVNVKGMFFLMQAVAQKMVEQGCGGKIINMSSQAGRRGEALVSHYCATKAAVLSYTQSAALALAPHKINVNGIAPGVVDTPMWNEVDALFARYENRPLGEKKRLVGEAVPLGRMGVPDDLTGAALFLASADADYITAQTLNVDGGNWMS Burkholderia phytofirmans PsJN BFirm BPHYT_RS16405 BPHYT_RS16405 galactonate dehydratase [EC: 4.2.1.6] Specifically important for: D-Galactose. galactonate is an intermediate in galactose oxidation (KEGG_correct) galactonate dehydratase MKITKLETFIVPPRWCFLKIETDEGIVGWGEPVVEGRAHTVAAAVEELSDYLIGKDPLLIEDHWQVMYRSGFYRGGPITMSAIAGVDQALWDIKGKHHGVPIHALLGGQVRDKIKVYSWIGGDRPSDVANNARAVVERGFKAVKMNGSEELQIIDTFDKVQGVINNVAAVREAVGPNIGIGVDFHGRVHKPMAKVLAKELDPYKLLFIEEPVLSENAEALRDIVNQTNTPIALGERLYSRWDFKHILSGGYVDIIQPDASHAGGITECRKIASMAEAYDVALALHCPLGPIALATCLQIDAVSYNAFIQEQSLGIHYNQGNDLLDYIKNPEVFKYEDGFVSIPQGPGLGIEVNEEKVREMAKVGHRWRNPVWRHEDGSVAEW Burkholderia phytofirmans PsJN BFirm BPHYT_RS16725 BPHYT_RS16725 gluconate:H+ symporter (gntT) Specific phenotype on gluconate and 72% identical to the gluconate permease (gntT, ACIAD0544) of A. baylayi ADP1 (PMCid:PMC4254613). KEGG_correct permease MEAVHGSTLLVFAVIAIALLILLITRYKVYPFLVLIIVSLLLGLASGMPMATIVKSFETGNGNTLGHIAIVVGLGTMLGKMMAESGGAERIATTLIDFFGEKNIHWAMMIVAIIVGLPVFFEVGFVLLIPIAFNVAKRTNKSLLLVGLPMVAGLSVVHGLLPPHPAAMLAVQAYHADIGRTIAYGLIVGVPTAIVAGPLFALMISRYIKLPKENALAAQFLGHGDETKNGAQTAAQNVAPKRELPSFGITLLTILLPVILMLVGSWADLFTTPKTLPNDLLHFAGNSDVALLIAVLVSFWTFGASRGFTREQIQKFCGDCLAPIAGITLIVGAGGGFGRVLMDSGISKEIVNVATAMHLSPLLFGWLVAALIRLATGSATVAMTTACGIVAPIASASGVHVEPELLVLATGSGSLIFSHVNDGGFWLIKEYFGMTVGQTFKTWSLLETIISLMGLGLTFALAAVV Burkholderia phytofirmans PsJN BFirm BPHYT_RS19730 BPHYT_RS19730 L-arabonate dehydratase (EC 4.2.1.25) Specifically important for: L-Arabinose. L-arabonate is an intermediate in the oxidation of L-arabinose (SEED_correct) dihydroxy-acid dehydratase MADSNQTKKPLRSQAWFGLKDRDGFLHRSWMKNQGIPHDEFDGRPVIGICNTWSELTPCNAHFRELAEYVKKGVHEAGGLPLEFPVMSLGETNLRPTAMLFRNLASMDVEESIRGNPMDGVILLVGCDKTTPALLMGAASCNLPALAVSGGPMLNGRFRGKNIGSGTGVWQMSEEVRAGTMTQEEFTEAESCMNRSRGHCMTMGTASTMASMVESLGMGLPHNAAIPAVDARRQVLAHLAGRRIVDMVREDLTMDKILTRQAFENAIRTNAAIGGSTNAVVHLIALAKRIGVELSLEDWELGSNVPCLVNLQPSGEYLMEDFYYAGGLPAVLKQLGEQGLLHKEALTVNGKTLWDNVRNAANYDEKVITTFAEPFKPKAGIAVLKGNLAPNGAVIKPSAATASLLKHRGRAVVFENIEELHAKIDDESLDIDEHCIMVLKGAGPKGYPGFAEVGNMPLPKKVLQKGITDMVRISDGRMSGTAYGAVVLHVSPEAAAGGPLAFVQTGDMIELDVEERRLHLDVTDEELARRRAAWQAPEAPKRGYYKLYVEHVLQADQGADLDFLVGSSGAPVPRDSH Burkholderia phytofirmans PsJN BFirm BPHYT_RS23155 BPHYT_RS23155 Gamma-aminobutyrate:alpha-ketoglutarate aminotransferase (EC 2.6.1.19) Important for utilization of putrescine as C or N source. This is the only transamination reaction in putrescine catabolism via gamma-glutamylputrescine (formed by BPHYT_RS23160), gamma-glutamylpurescine oxidase (possibly redundant, BPHYT_RS23125 or BPHYT_RS22700, neither has a phenotype), gamma-glutamylbutyraldehyde dehydrogenase (BPHYT_RS23175), and gamma-glutamyl-gamma-aminobutyrate hydrolase (probably BPHYT_RS23165, but no fitness data). Another gene (BPHYT_RS22435) likely has this activity as well, and is important (but with a weaker phenotype) on putresine as a carbon source. However that gene is not important with putrescine as a nitrogen source, which suggests that this gene is providing the activity. aminotransferase MSYRTEEVAYVQPAQPAASAQASQAAQQQRSTAEYRALDAAHHIHPFSDMGSLNRSGSRVIVKAQGVYLWDSEGNKVIDGMAGLWCVNVGYGRKELADAAYKQMQELPYYNTFFKTTHPPVIELSALLAELAPEAFNHFFYCNSGSEGNDTVLRIVHQYWATQGKHSKKFVISRKNGYHGSTIAGGTLGGMGYMHEQMPSKVENIVHIDQPYFFGEAQGNLTPEEFALARAQQLEAKILEIGADNVAAFIGEPFQGAGGVIFPASTYWPEIQRICRKYDILLVADEVIGGFGRTGEWFAHQHFGFEPDLITLAKGLTSGYVPMGAVGLHDRVAKAIIENGDFNHGLTYSGHPVAAAVAVANLKLLRDEKIVDRVKNDTGPYFQKQLRETFANHPIIGEISGTGLVAGLQLAQDPKARKRFANGGDVGTICRDFCFNGNLIMRATGDRMLLSPPLVINKLEIDEIVSKAKKAIDATAQQLGIS Burkholderia phytofirmans PsJN BFirm BPHYT_RS23160 BPHYT_RS23160 Gamma-glutamyl-putrescine synthetase (EC 6.3.1.11) Specifically important for: Putrescine Dihydrochloride. The first step in putrescine catabolism via gamma-glutamyl-putrescine (SEED_correct) glutamine synthetase MHDIDDFLKKNRVTEIEAIIPDMAGIARGKIIPRSKFESGESMRLPQAVMIQTVTGDYPEDGTLTGVTDPDMVCVPDASTIRMIPWAVDPTAQVIHDCVHFDGTPVAISPRRVLRRVLELYKAKGWKPVIAPELEFYLVDMNKDPDLPLQPPIGRTGRPETGRQAYSIEAVNEFDPLFEDIYEYCEVQELEVDTLIHEVGAAQMEINFMHGDPLKLADSVFLFKRTVREAALRHKMYATFMAKPMEGEPGSAMHMHQSLVDEETGHNLFTGPDGKPTSLFTSYIAGLQKYTPALMPIFAPYINSYRRLSRFMAAPINVAWGYDNRTVGFRIPHSGPAARRIENRIPGVDCNPYLAIAATLAAGYLGMTQKLEATEPLLSDGYELPYQLPRNLEEGLTLMGACEPIAEVLGEKFVKAYLALKETEYEAFFRVISSWERRHLLLHV Burkholderia phytofirmans PsJN BFirm BPHYT_RS34210 BPHYT_RS34210 2,4-diketo-3-deoxy-L-rhamnonate hydrolase (EC 3.7.1.-) Specifically important for: L-Fucose; L-Rhamnose monohydrate. The substrate is also known as 2,4-diketo-3-deoxy-L-fuconate, and is an intermediate in both L-rhamnose and L-fucose degradation (SEED_correct) ureidoglycolate lyase MKLLRYGPKGQEKPGLLDAQGKIRDLSKVVADIDGAALTDEGLAKLRALDPASLPLVEGNPRMGPCVGKIGKFICIGLNYADHAAESNLPVPAEPVIFNKWTSAISGPNDDVEIPRGSKKTDWEVELGVVIGKPAKYIDEANALDYVAGYCVINDVSEREWQIEKGGTWDKGKGFDTFGPIGPWVVTRDEVADPQNLSLWLEVDGHRYQNGSTKTMVFGVAKLVSYVSQCMSLQPGDVISTGTPPGVGMGVKPNPVFLKPGQTIRLGIEGLGEQTQKTYAAE Burkholderia phytofirmans PsJN BFirm BPHYT_RS34230 BPHYT_RS34230 L-fuconate dehydratase; L-rhamnonate dehydratase (EC 4.2.1.68; EC 4.2.1.90) Specifically important for: L-Rhamnose monohydrate; L-Fucose. annotated by SEED for fuconate activity only hydrolase MPVAAQQPTLEGYLRGDGRKGIRNVVAVAYLVECAHHVAREIVTQFREPLDAFDDPSAEREPPVHLIGFPGCYPNGYAEKMLERLTTHPNVGAVLFVSLGCESMNKHYLVDVVRASGRPVEVLTIQEKGGTRSTIQYGVDWIRGAREQLAAQQKVPMALSELVIGTICGGSDGTSGITANPAVGRAFDHLIDAGATCIFEETGELVGCEFHMKTRAARPALGDEIVACVAKAARYYSILGHGSFAVGNADGGLTTQEEKSLGAYAKSGASPIVGIIKPGDIPPTGGLYLLDVVPDGEPRFGFPNISDNAEIGELIACGAHVILFTTGRGSVVGSAISPVIKVCANPATYRNLSGDMDVDAGRILEGRGTLDEVGREVFEQTVAVSRGAASKSETLGHQEFILTYKTFEPVGPACLPSSAAAQHRVVAIEPH Burkholderia phytofirmans PsJN BFirm BPHYT_RS34235 BPHYT_RS34235 putative accessory domain for L-fuconate/L-rhamnonate dehydratase (EC 4.2.1.68; EC 4.2.1.90) Important for L-fucose and perhaps L-rhamnose catabolism, but seems to have milder phenotypes than the adjacent dehydratase _RS34230. CDD suggests (see cd11613) that it might be a dimerization domain for the dehydratase, but that wouldn't make sense for a separate ORF. Some homologs of this gene are fused to the dehydratase (which has a GD_AH_C domain). hydrolase MTSRLLPLQTDPRLILLSPADNCLIAAARLDCGTQVEIEGERVTLTRTIDLGHKVARHELAKDDKVLRYGAVIGHVTEAVARGAHLHTHNLESDYLPTYTHDAGHEFVHH Burkholderia phytofirmans PsJN BFirm BPHYT_RS35445 BPHYT_RS35445 2-aminobenzoate-CoA ligase [EC: 6.2.1.32] Specifically important for: L-Tryptophan. B. phytofirmans catabolizes tryptophan via 2-aminobenzoyl-CoA (KEGG_correct) 2-aminobenzoate-CoA ligase MEPSAHVDTFARDNLPPQDQWPVFLLDNPDVAYPARLNCASELLDRTIDAGHRDDPAIWSDVDGAPRATTYGELLALVNRSAHVLVDEMGLQPGNRVLLRGPNTLHMAVTALAALKVGLVVVPTMPLLRAKELKQIIDKAQVGAALCDARLTAELARCSDPEDEFYCAGLMQTRLFHDDSPDSLDTLAVNKPDHFTACDTAADDVCLIAFTSGTTGAPKGCMHFHRDVVAMCDLFPRHVLKPTSSDIFCGTPPLAFTFGLGGLLCFPLRVGASTVLIEKLTPETLLQTVERFHATVMFTAPTFYRQMAPLVAHHDVSSLKKTVSAGEALPDSTRRLWRDATGIDMIDGIGGTELIHIFISAQGDEIRPNAIGRAVPGYAVQAVDDDMQPVAPGTIGKLAVRGPTGCRYLADERQMKFVRDGWNLPGDSVYLDEDGYVFYQARADDMIVSAGYNISGPEVESVLLQHDAVSECGVIGVPDETRGQIVKAFVVVNPGYERDDKLVAQLQEFVKNSVAPYKYPRDIVFVDSLPRTETGKLKRFELRTMA Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS03025 RR42_RS03025 Inner membrane protein (FUSC-like) required for 4-hydroxybenzoate transport, together with NodT, MFP, and DUF1656 proteins (RR42_RS03040, RR42_RS03035, and RR42_RS03030) specific phenotype on 4-hydroxybenzoate and cofit with other nearby components. Not clear if this is primarily an efflux pump (because of the high and potentially toxic concentration of hydroxybenzoate) or for uptake transporter MVSWPTGRDWIFSLKAFAAAMLALFIALYLGLPRPYWAMASVYIVAHPLTGATRSKALYRVLGTLLGAAASVAIVPPLVNAPVLLMAAVALWTGILLYVALLHRTPRSYVFMLAAYTLPMVALPSVSDPSGVFDIAVARAEEICLGIVCASIVGSTIFPAKVATVLGQKSAQWLADAALWATDMLSAHPAAKVSRHHSRHRLAADILALDQLISHLSYDAESAARVKHAQELRGRMTMLLPVLSSLASVVDALHQHAAGIPQRLSHNMALVSAWISAGAQAPLPALQLSQDAPIDDAGLEPGSAGPDWHAALAATAEGRLRELMELWQDCVSLQRRIGEAAPQGDWAPVFRRWGVGAARHYDHGMLLFSTATTALAIFSMGMVWIWTGWADGAGAVALGAVSCCFFAAMDEPAPMIRSFFRWNVVCLVLATIYLFVVLPNAHDFEMLVLMFAVPYLIIGVMMAQPRLALIAMPLAVVTANDIGIQGAYNADFNAFFNGNVAGIAGILFALVWTLVARPFGTRAAVRRLVRASWGDIARNATGREPGEHAHLRARMLDRLAQLVPRLAASEDETTGDGFTEVRVELSTLALQRELSALAPEHQHSVRRVLQGVASYYQARLDARAEAPPQVLRDRLAKAIRKVASRADQASREAFAALVEMHVALF Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS03030 RR42_RS03030 required for 4-hydroxybenzoate transport, together with NodT, MFP, and FUSC proteins (RR42_RS03040, RR42_RS03035, and RR42_RS03025) PFam PF07869.8 (DUF1656). Specifically important for utilization of 4-hydroxybenzoate (at 20 mM). Not clear if this system is for uptake or for efflux (as this compound is likely to be toxic at 20 mM) membrane protein MSGEVDVYGVFVPSLLAWMLVAFLITACARAVLAHVGFYRLVWHRSLFNLALYVIVLGGIVYLAYRLQS Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS03040 RR42_RS03040 Outer membrane protein (NodT-like) required for 4-hydroxybenzoate transport, together with FUSC, MFP, and DUF1656 proteins (RR42_RS03025, RR42_RS03035, and RR42_RS03030) specific phenotype on 4-hydroxybenzoate and cofit with other nearby components. Not clear if this is primarily an efflux pump (because of the high and potentially toxic concentration of hydroxybenzoate) or for uptake RND transporter MNTLRKALLPALVPLLFAACTTVGPDYHVPDNAAVKAQAANGPLLGTNNPAVSIAEVPDGWWRLYDDPKLDQLVQQALVANTDLRVAAANLKRAIAVYHEVEAENLPEARLSAGAERGQIAGEPLLKEEKIPVMNFGDVGFKVSYLIDFFGKLARADEAALAGAQASQAALDQARIGVVAETVRAYVQGCAATHELTVAEHQLALQSRGVELARKMVDAGRGQPLDLLRAQAQADVLRAALPRFKAEQEGAAYRLAVMLGKPPSATSQAEYACHEEPRLRQALPVGDGAALLKRRPDVRQAERELASATAKIGVATADLYPSIRIGASAGFTGILDHLGQAPTAHWGYGPLITWNIPTSGTRARVHGTEAGAEAALAHFDGVVLKALRETQSALSSYTRELERTQALRDARDKANEVARQNRQLYQAGRSPYLSSLDADRTLASTEASLAASESQVALDQINLFLALGGGWQNAPKVESRTMSEQAH Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS04420 RR42_RS04420 required for efflux of an amino acid polymer PFam PF08909.7 (DUF1854). In a conserved cofit operon with a mdlB-like transporter (RR42_RS04415) and with two (apparently cytoplasmic) cyanophycin synthetase-like genes that produce a different polymer (RR42_RS04410 and RR42_RS04405, see PMID:23224585) hypothetical protein MGAHMQQVDFKLSRNALGRLVMTTADGVVHDGVVPVRAFPIAAPDDGVGLVSADGRELAWLPRLDTLPAPVREMIEAELASREFMPEIRRIRSVSTYATPSTWEVETDRGLTSLVLRGEEDIRRLAGSTLLISDSHGIHYLVRNLASLDKGSRKILDRFL Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS13535 RR42_RS13535 2-aminobenzoate-CoA ligase (EC 6.2.1.32) Specifically important for: L-Tryptophan. This bacterium catabolizes tryptophan via 2-aminobenzoyl-CoA; (KEGG_correct); SEED has a very broad annotation (Acyl-coenzyme A synthetases/AMP-(fatty) acid ligases) 2-aminobenzoate-CoA ligase MASTAHLDTYALDRLPPPQQWPAFLFNADTRYPERMNCALELVERHVREGRGERVAIRYEQDGAHRTVSYAELAALSNRIAHVLTGDMKLVPGSRVLLRGPNNLMMAACWLAVVKAGLIAVPTMPLLRAKELKQVIDRAAVSAALCDERLREELEANLKPGGEHHCPSLTQALYFNSSGAGSVEAAMANKPDGFEACDTAADDICLIAFTSGTTGQPKGTVHFHRDVIAMCDLFPRHVLKPGPDDIFCGTPPLAFTFGLGGILCFPLRVGASTVLAERLTPESLLALIQSWRATIVFTAPTFYRQMAALAPGYDLSSLQKSVSAGEALPDATRQSWKAATGIEMTDGIGGTEMMHIFISSAGADVRPGAIGKVVPGYIAQIVDEQMQPVPHGTVGKLAVRGPTGCRYLDDPRQANYVKDGWNLPGDTFKADADGYYYYQARSDDMIVSAGYNIAGPEVESALMRHEAVAECGVVGMPDPERGQIVAAYVVLRPGVAASDETCAALQSYVKAEIAPYKYPRKVIFVDALPRTETGKLQRFRLRQMAEQSGAPEGARQP Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS13555 RR42_RS13555 anthraniloyl-CoA monooxygenase (EC 1.14.13.40) Specifically important for: L-Tryptophan. Antrhanioyl-CoA is a synonym for 2-aminobenzoyl-CoA, an intermediate in the degradation of Trp via 2-aminobenzoate (KEGG_correct) salicylyl-CoA 5-hydroxylase MRVLCIGGGPSGLYFGLLMKLRDPSSEVYVVERNRPYDTFGWGVVFSDATMDNLKQADPVSAEQINAAFNHWDDIDIHIGGRTLRSGGHGFIGIGRKRLLNILQARCEALGVHLVFETDVTDDQALAQQYQADIVIASDGINSRVRGRYAETFQPDIDTRLCRFVWLGTRKLFDAFTFAFEKTEHGWFQAHAYRFDDNTSTFIVEAPEPVWRAAGIEQMSQEEGVAFCERLFARYLDGNALISNATHLRGSANWIRFPRVICGTWVHWNTLAGGRRVPVVLMGDAAHTAHFSIGSGTKLALEDAIDLANNIRDAGPGGADVLPQALERYQATRSVEVLKIQNAARNSTEWFENVERYAGLAPEQFAYSLLTRSQRISHENLRVRDPGYVEGFERWLAGQAAANVANATSTGQAAEARVVPPMFTPLRVRNVTLKNRVVVSPMAMYSCEDGVPGDFHLTHLGARALGGAGMVVAEMTCTSPDARITPGCPGLWNDEQRDAWRRIVDFVHANSDARIAMQIGHAGRKGSTQLGWEQMDYPLAEGNWPVLSASPLPYMPGISQVPREMSRADMDAVRDDFVASARRAAQAGFDWLELHCAHGYLLSSFISPLTNQRSDEYGGSLQARLRYPLEVFAAVRAVWPQERPMSVRISAHDWVEGGITPDDAIEIARAFKAAGADMIDCSSGQVSPDQAPVYGRMYQTPFADRIRNEAGIATIAVGAIFEADHVDSIIAAGRADLCAIARPHLADPAWTIHEAARLGHRDLAWPKQYQAGKRQLETNLERAAQQARQARQPEDH Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS16265 RR42_RS16265 required for sulfate utilization, putative electron transport protein for sulfite reductase PFam PF06073.8 (DUF934). conserved cofitness with sulfite reductase; auxotrophic oxidoreductase MAKIIQLQRGEGANPVPVIIDDAWTVLRGAEGAALTDEQIAAAAQGKDAVLFPLAAWLAHKDGVLAGRAADITGIWLAPEDEPADAQAAFASVAVVAVDFPVFRDGRGFSTAYLLRTRYNWTGQLRAIGDVLRDQLNFMKRCGFDAFAVRADKNIDDAIKGFTEFTVAYQASVDEPLPLFRRNRAEALGKETA Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS25930 RR42_RS25930 glycine dehydrogenase (deaminating) (EC 1.4.1.10) Specifically important for: L-Threonine. Annotated as D-amino acid dehydrogenase; SEED has it as the small subunit but do not see why another subunit is expected (i.e. E. coli dadA). Important on Thr as well as Gly because Thr is cleaved (via the threonine dehydrogenase and kbl) to glycine. The electron acceptor is uncertain -- the given EC number implies that NAD is the electron acceptor, which is consistent with an N-terminal NAD binding domain (PF13450). amino acid dehydrogenase MKTIAVIGGGITGVTTAYALAKRGFSVTLLEKHRYAAMETSFANGGQLSASNAEVWTHWSTILKGIKWMLKSDAPLLVNPRPSWHKLSWFAEFIAAIPHYRKNTIETTRLAIAARDHLFSWAAAEGIDFDLKKEGILHIYRDKAGFEHAGRVSKLLAEGGLARHAVTPEEMRAIEPTLAGQYYGGYFTQSDSTGDIHKFTSGMAAAIDRLGVRCLYNQDVQSVSTDGRQVTIVSGDGRQAESRVFDGVVVCAGTASRALAASLGDRVNIYPVKGYSITVNLNDAQSQAAAPVVSLLDDETKLVTSRLGVDRFRVAGTAEFNGYNRDIRADRIRPLVEWVNQCFPGVSTRSVVPWAGLRPMMPTMLPRVGRGRASCVFYNTGHGHLGWTLSAVTADMIGDVVQQAMGARRAHGVQEPVALVTP Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS28300 RR42_RS28300 L-threonine 3-dehydrogenase (EC 1.1.1.103) Specifically important for: L-Threonine. The first step in Thr catabolism (SEED_correct) NAD-dependent epimerase MTKPARVLIIGANGQLGTELASALADRYGKQNVVTSDMVPHGRHLHLTHEMLDVTDRAHLRDVIERHGITQIYHLAAALSATGEKSPTWAWQLNMNGLLNVLEAARHQKLDKVFWPSSIAAFGPTTPPDGTPQSTIMEPKTVYGISKLAGEGWCRWYFENHGVDVRSLRYPGLISYKTPPGGGTTDYAIDIFHSALRAQPYACFLEKDEALPMMYMPDAVRATMELMEAPRASISERGSYNLAGLSFTPGEIANEIRRHCPGFDVRYEPDFRQEIAAGWPDSIDDSVARRDWNWRPEFGLKEMVADMLKNLATLNQGSALECVS Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS28835 RR42_RS28835 gluconate:H+ symporter (gntT) 67% identical to the gluconate permease (gntT, ACIAD0544) of A. baylayi ADP1 (PMCid:PMC4254613). KEGG_correct permease DsdX MGAVTGTTLLLYALIAVIALVVLIAKFKLNPFITLVVVSVLLGFAVGMPMGDIVKSFEAGVGGTLGHIALVVGLGTMLGKMMAESGGAERIARTLIDAFGEKNVHWAMVTIAFIVGLPVFFEVGFVLLVPIAFNVAKRTGTSMVLVGIPMVAGLSVVHGLIPPHPAALLAVTAYKADIGKTILYALIVGIPTAAIAGPLFAKLMTRYVTLPDVNPLAAQFTEEDEGVKASHELPGFGITLFTILLPVILMLIGSWADLITTPKTFANDFLKLIGNSVIALLIAALVSFYTFGKRRGFTRENILRFTNECVAPTAIITLVVGAGGGFGRVLRDSGISNAIVDVATGAHVSVLLLGWLVAVLIRIATGSATVAMTTAAGIVAPIAASVPGTRPELLVLTTGAGSLILSHVNDGGFWLVKEYFNMTVAQTFKTWSVCETLISVIALLLTLALATVV Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS34240 RR42_RS34240 putative efflux pump, required for thallium (I) resistance PFam PF02694.11 (UPF0060). conserved specific phenotype of UPF0060 membrane protein MKTFALYLITACAEILGCYFPYLWLRQGASAWLLVPGALSLALFAWLLSLHPDASGRVYAAYGGIYIAVAILWLWLVDGVKPSHWDLAGVAVAIAGMAMIVFQPR Dinoroseobacter shibae DFL-12 Dino 3607124 Dshi_0546 ABC transporter for Xylitol, ATPase component Specific phenotype on Xylitol. ABC transporter related (RefSeq) MAGIKIDKINKFYGTTQALFDINLDIEDGEFVVFVGPSGCGKSTLLRTLAGLEGVSSGRIEIGGRDVTTVEPADRDLAMVFQSYALYPHMTVRENMEFGMKVNGFEPDLRKERIAEAARVLQLEDYLDRKPGQLSGGQRQRVAIGRAIVKNPSVFLFDEPLSNLDAKLRVQMRVELEGLHKQLGATMIYVTHDQVEAMTMADKIVVLNRGRIEQVGSPMDLYHKPNSRFVAEFIGSPAMNVFSSDVGLQDISLDASAAFVGCRPEHIEIVPDGDGHIAATVHVKERLGGESLLYLGLKGGGQIVARVGGDDETKVGAAVSLRFSRHRLHQFDEAGRAI Dinoroseobacter shibae DFL-12 Dino 3607125 Dshi_0547 ABC transporter for Xylitol, periplasmic substrate-binding component Specific phenotype on Xylitol. extracellular solute-binding protein family 1 (RefSeq) MKTLRNLLCSAAVASVMASGAMADGHGWSLKDAAAPYAGTTVDVVFLLRPGYEAIEAMLPAFEEETGIKVNVIKHPYENALGEQVRDFVAGGDLDVALIDLVWIGSFAENEWILPLADVQAKFPDAVDPDLDIDDFFPLVLNAFGGWNDTIYGLPFDNYSGLMFYNRCMLEEAGFDGPPSTWEELKDVYGPALTKDGKYAFALQSKRNETQSADSFARMLWPFGGSFLNEEFRSNLMSEGSQAGLKFRQELMEYMPDGIVAYDHAETVNAFSQGDVAMITEWSAFYSSVVSPETSRVADCVEIAPEPMGPAGRKPALGGFSLAVASQADEAEQAAAYLFIQWATSKANAREYLERGGVPARQSVYQQDGLEEFKFVPALVESWQDGVPEFRPRFAEWPEITEIVQEWGTKMMLGEVTTEEGAQEIGTRMEEVLDAAGYYSGEKPLAQ Dinoroseobacter shibae DFL-12 Dino 3607126 Dshi_0548 ABC transporter for Xylitol, permease component 1 Specific phenotypes on Xylitol; Xylitol. Phenotype is very specific binding-protein-dependent transport systems inner membrane component (RefSeq) MSGQVPRKTVFAFIGPAVIGLALVGIAPLLYALWTSLHFYNLTKLRRVEFIGLENYWTVLTDEVFWQAMGRTFFLLGTALPLQIALGLGIALVLHQPGLTLVKTLARLSLVLPMATTYAVVGLLGQVMFNQKFGVVNQLLGGADINWIGDPENAFAMIIFWDVWQWTPFVALVLLAGLTMVPGEVEEAARLETKSKWTVLRYVQLPFLLPGLVAVLILRTADTLKLFDMVFTLTRGGPGSSTEFISLMIQRVGFRGFDQGLASAQAIILLIITIVLAQIYIRVFYKEV Dinoroseobacter shibae DFL-12 Dino 3607127 Dshi_0549 ABC transporter for Xylitol, permease component 2 Specific phenotypes on Xylitol; Xylitol. Phenotype is very specific binding-protein-dependent transport systems inner membrane component (RefSeq) MTSTRSLFSQIALLVLIITVCVFPFYWMVTTSLKTQIVALEAPPVWIFEPTLSNYREALFEDGVLRTLINSLIIAISTTFLALVLGVPAAFALARFEFRGKKDLWFWFITNRMISPIVLALPFFLIARNLGLLDKHITLILIYLTFNLPIVIWIVTDQFRGIPYDLDEAARLEGASQFTIMRKICLPLAMPGVAVSAIFSFIFSWNELMFGLILTRSEAKTAPAMAVSFMEGYNLPYGKIMATSTLIVIPVLIFALIASKQLVRGLTMGAVK Dinoroseobacter shibae DFL-12 Dino 3607710 Dshi_1119 DNA damage response helicase, ligase-associated Conserved and specific phenotype: important for resisting cisplatin. Related to Lhr, which is either a DNA:DNA or DNA:RNA helicase, but lacks the long C-terminal extension that might have a regulatory role (see putative winged helix domain in E. coli lhr). This is also related to the archael protein saci_1500, which has also been linked to DNA damage response, as a mutant is sensitive to UV (PMID: 26148716) DEAD/H associated domain protein (RefSeq) MPAAPPPSLPNEITRWIAAQGWALHPHQREMLARSQDPALLLIAPTGGGKTLAGFLPTLAELGPAPPPGLHTLYISPLKALAADIKRNLRRPIEEAGLAIRVEDRTGDTSQTQRKRQRADPPHILLTTPESLALMLSYEDAARTFAGVQRVIVDEIHALAESKRGDQLMLGLARLQSLVPGLRRVGLSATVEDPPAIARFLARHPDPCDILLADPGPAPDITMLQTDEAPPWSGGGGRYAIPAILQAVKAHKTTLIFHNTRAQAELFFHALWLANEDALPIGIHHGSLSREQRQRVEAAMAEGALRAIVCTGSLDLGIDWGDVDLVIQVGAPKNVKRLVQRIGRANHRYNAPSKALLVPANRFEVVECHAALKTMADGKLDGEPRAEGPRDVLCQHILAVAAAGPFDADALFAEVTSAGAYRDLTRPAFDDCLEFCATGGYALRAYDRWQRLLHRPDGMWQLRDPRAARQIRMNIGTIIDTETLKVRLKNRRGGTPLGEVEEGFAATLTPGDTFLIGGQIVRYEGLNELTVEVTRRADKQPKIATFMGTKFATSTQLSHTILEMFRQPDWPELPSATCEWLHLQRKVSKLPEADRMLMETFGHEDRQYLVCYGFAGRNAQQTLGLLLSQRMELAGLAPIGFVATDYATMLWGLEEVRDPAALVRPDGLRDSFEQWLSGNAVMKRTFRAAAIIAGLIDRNTPGRRKTGRQATFSSDILYDTLLKYDPDHVLMQITREEARRGLVDFGRIEELLARTTGRVDHRRLDRISPLAAPLLLERGTVPVAGAAEDRLLAQAAEALMQEAGLPA Dinoroseobacter shibae DFL-12 Dino 3608852 Dshi_2244 DNA repair endonuclease mmcB (DUF1052) Conserved and specific phenotype: important for resisting cisplatin. Also see PMID:26162909 which suggests a role for a homologous protein from Caulobacter in creating substrates for translesion synthesis protein of unknown function DUF1052 (RefSeq) MTDLLQPGQRLARGVCRHLRSLDFACVEEFTPDRGLRVDVMALGPKGELWVVECKSSRADFTSDSKWQGYLDWCDRYFWAVDSAFPCDLLPENTGLILADAYDAEIQRMPDLHKLPAARRRALTQRFARAAALRLQATRDPEMTLA Dinoroseobacter shibae DFL-12 Dino 3609040 Dshi_2429 Rhamnulokinase RhaK in alpha-proteobacteria (EC 2.7.1.5) Specifically important for: L-Rhamnose monohydrate. The second step in rhamnose catabolism (SEED_correct) carbohydrate kinase FGGY (RefSeq) MTRHVAVIDIGKTNAKLALVDRQSLTEISVITRPNTVLPGPPWPHFDVDGHWAFLLDGLRDFQARHGIDAISITTHGACAALLQKDGALAAPILDYEHPGPDDTALAYDALRPPFSETGSPRLAGGLNIGAQLFWQFHTDPALRDRTRQIVTYPQFWGAKLTGVTATDVTSLGCHTDLWNPHAGAVSSLVDRLGLTGKLAPVRKPHDILGPVLPAVAAQTGLAPGTPVHCGIHDSNASLLPYVLTQTSPFSVISTGTWVVAMSVGGRPVVLDPDLDTLINVTALGQPAPSARFMGGREHDLATEGTGPPPSAQDLDHILSRQILLLPAVVPDTGPFKGQASRWEGDAPAPGTGARGAAVALYLALVTAECLSNIGHAGKIIVEGPFAGNRLYLEMLSVAMEADVVRASGTTGTSAGAALLAGGDAGAPPRPDSLVALPAASKTRLRHYAAHWRQRARRRTP Dinoroseobacter shibae DFL-12 Dino 3609047 Dshi_2436 rhamnulose-1-phosphate aldolase (EC 4.1.2.19) / lactaldehyde dehydrogenase (EC 1.2.1.22) Specifically important for: L-Rhamnose monohydrate. Part of rhamnose catabolism via rhamnulose. TIGR annotates the C terminal part as alcohol dehydrogenase rather than as lactaldehyde dehydrogenase but do not see why (SEED_correct) rhamnulose-1-phosphate aldolase/alcohol dehydrogenase (RefSeq) MLKSLETQLLESRWDDEVAKGMSESELLLYRSNILGADKRVTNYGGGNTSAKVMEADPLTGAQVEVLWVKGSGGDIGSIKMDGFATLYMDKLRALKGLYRGVAFEDEMVSYLPHCTFRLNPRAASIDTPLHAYVPRKHVDHVHADAIIAIAASDNSKELTQEIFGNRIGWLPWKRPGFELGLWLEKFCRENPEADGVVLESHGLFTWADTAKECYDQTIDVINVATRWLAERSAGVPAFGGAIHESLPAAARREVAARLMPAIRGFVSDNQHMVGHFNDSDAVLEFVNARDMEALAALGTSCPDHFLRTKIRPLVVPFDPAQNNILAVLSELPDQVAAYREAYAAYYARCKHDDSPALRDPNAVVYLVPGVGMITFAKDKATARISGEFYVNAINVMRGASAVSTYQGLPEQEAFDIEYWLLEEAKLQRMPKPKSLAGRVALVTGGAGGIGAATAERFLAEGACVVLADINEDSLASTQERLSERFGADVVRSVVMNVTREEAVAAAFAEASVEFGGVDILVSNAGIASSAPIEETSLALWNKNMDILSTGYFLVSRAAFKLMRVQDMGGAVVFVASKNGLAASPNAAAYCTAKASEIHLARCLALEGAEAGIRVNVVNPDAVLRGSKIWEGDWLEQRAGTYGTDKDGLEEMYRQRSLLKRSVLPEDIAEACYFFAADASSKSTGNIINVDAGNVQAFTR Dinoroseobacter shibae DFL-12 Dino 3609201 Dshi_2587 DNA damage response exonuclease, associated with a ligase Conserved and specific phenotype: important for resisting cisplatin. In a conserved operon with a DNA ligase exonuclease of the beta-lactamase fold involved in RNA processing-like protein (RefSeq) MAEPLLTFTDRGIHCPAGGFHIDPWRPVDRALITHGHADHARPGHRAYLATEAAAPVMRHRLGDIALDTIRYGETRRIGAVEVSFHPAGHVPGSAQIRIAHRGEVWVVSGDYKIDADGFSEPFEPVRCHAFISECTFGLPVFRWDPQDDVMAAIHRWWATCAAAGKTAVLGAYALGKAQRILAHLDPAQGPILTHGAVEGTNRILRAQGLSLPPTTQVTAEITAKTHPGALVLATPSALGTPWMKRFGPAETGFASGWMRMRGVRRRRGADRGFVMSDHADWTGLNTAIAETGAERIFVTHGYTSVFGKWLEDQGYDAQIVETEFEGESIDAPDPEPEGAAP Dinoroseobacter shibae DFL-12 Dino 3609738 Dshi_3121 Tricarboxylate transport membrane protein TctA specific phenotype on citrate and cofit with other nearby components; SEED_correct protein of unknown function DUF112 transmembrane (RefSeq) MLEGLLIGLQTAFSIQNLAMVIGGCLIGTFIGMLPGLGPMSIIAIMIPVAISLGDPSAALILLAGVYYGAIFGGSTSSILLNAPGVAGTVATSFDGYPMAQQGKAGKALTIAAIASFAGGTIGAILLMVFAPALSSVALLFHSAEYFALMVVGLSAIAAFAGTGQVAKALLMTILGLIMATVGEGALFASPRFTMGLMDLQSGFGFITLAMAMFALPEALFLVMNPLRAASGQGGGEIKDLRITRAEARSIAPVIGRQSVQGFFIGVLPGAGATIASFLGYAVERNIASKDEQAEFGKGSVKGLAAPETANNAACTGSFVPLLTLGIPGSGTTAILLGALLALNVSPGPRLMIDAPEIFWAVIMSMFIGNLVLLILNLPLIPYIAKILSVPRNYLIPFILFFTLMGAYIGQNNATELLLLVGFGICATILKFADYPLAPLLIGFILGGLLENNFSRAMQLYDGISFIWERPMTLGLLVIAALLIILPSYRNRRAKARAAGVADGD Dinoroseobacter shibae DFL-12 Dino 3609739 Dshi_3122 Tricarboxylate transport protein TctB specific phenotype on citrate and cofit with other nearby components; SEED_correct hypothetical protein (RefSeq) MALDRWIALVLLGVCLIYGYTAWFTMDADLAPFMRRNPIWPSTFPKVLSVLGAVAALVILLGLEGPQKPPKAGDIDYRRLGDYKIGQAALLLGLMVGYALLLRPAGFLVSTTSFLILGSVILGERNWPVMIGVAVVATGAIWYLVQEVLGIFLRPLPMFMGV Dinoroseobacter shibae DFL-12 Dino 3609740 Dshi_3123 Tricarboxylate transport protein TctC specific phenotype on citrate and cofit with other nearby components; SEED_correct hypothetical protein (RefSeq) MTLEFTRRTLIAAAAALAMTGGAHAEGEQMLESIHFLIPGGAGGGWDGTARGTGEALTKAGLVGSASYENMSGGGGGKAIAYLIENANSSHGTLMVNSTPIVIRSLTGEISQSFRDLTLVAGTIGDYAAIVVGKDSPINSMADLIAAYDADPNATAVGGGSVPGGMDHLVAAMVMEAAGKDALGVKYIPYDAGGKAMAALLSGEIAALSTGFSEAIDLAEAGEVKIIGVTAPERVAAYDSAPTMVEQGIDTTFVNWRGFFAAPGLPEEQLAAYQATLEKMYDTPEWEEVRARNGWVNIHNSGADFQSFLEAQEAQIGDLMKKLGFL Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS07185 HSERO_RS07185 Ornithine carbamoyltransferase (EC 2.1.3.3) Annotated as this by multiple resources. (essential) (SEED_correct) ornithine carbamoyltransferase MAIKHYLQFSDFTLDEYEYVIERSRVIKRKFKNYEPHHTLADRTLVMVFEKNSTRTRLSFEAGMHQMGGAAIYLNTRDSQLGRGEPVEDAAQVMSRMCDVIMIRTYGQEIIERFAKHSRVPVINGLTNEQHPCQVLADVFTYIEHHGSIQGKIVAWVGDANNMLYSWLQAAEVFGFHVNVSTPKGYDIDPAQVSPGNKNYTFFADPADACQDADLVTTDVWTSMGFEAENNARLKAFDGWIVDQAKMARAKKDALFMHCLPAHRGEEVAAEVIDGPQSVVWEEAENRLHVQKALLEYLVHGRFD Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS19500 HSERO_RS19500 Putative phosphoglycerate dehydrogenase (EC:1.1.1.95) The annotation of this essential protein is based on its homology to BPHYT_RS03150. Orthologs in Acidovorax sp. GW300-3H11 (Ac3H11_4791) and Dechlorosoma suillum PS (Dsui_0736) are also essential. HSERO_RS21555 is another plausible candidate for this reaction, but it has little phenotype and its ortholog in Cupriavidus basilensis 4G11 (RR42_RS20535) seems to be involved in cell wall synthesis. (essential) FAD-linked oxidase MNAPAQIQALLTDAPHGATPPRLREIPYNYTSFSDREIVIRLLGEESWSLLDELRGKRQTGRSARMLYEVLGDIWVVRRNPYLQDDLLDNPKRRAALIEALNHRLGEVDKRRLATDQAEAGDAEAQRRSASVEALLKAAKKAIADFAEEFRQTYDLRKRATKVLGRFTAKDNIKFDGLSRVSHVTDATDWRVEYPFVVLTPDTEDEMAGLVKACIELGLTIIPRGGGTGYTGGAIPLTPMSAVINTEKLEQLGAVEMEILPGLDKPYATIYSGAGVVTKRVSDAAEKAGFVFAVDPTSAEASCIGGNVAMNAGGKKAVLWGTALDNLASWRMVDPQGDWLEVTRLDHNLGKIHDVEVARFKLEWSHPGEKGQKTEVFKTEILEISGKKFRKEGLGKDVTDKFLSGLPGVQKEGCDGLITSARWILHKMPKQTRTVCLEFFGQARDAIPSIVEIKDYLDAETKKGGAILAGLEHLDERYLRAVGYATKSKRGVLPKMVLIGDIVGDDENAVAAAASEVIRMANNRVGEGFVAVSPEARKKFWLDRSRTAAIAKHTNAFKINEDVVIPLNRMGEYTDGIERINIELSIKNKLQLLAELDSFFVKGNLPLGKSDDAEGDDIPAAEMLEDRVHQAESLLEQTHARWSYLLANLDKPLGEAKGELAALGLEKMLPVFEQRLVDQPEAAVFHVVQDRTVRISWKQEVRAQLRQIFSGAAFKLILEECQAIHKRVLRGRVFVALHMHAGDGNVHTNIPVNSDHYEMLQDAHVAVARIMKLARSLNGVISGEHGIGITKLEFLTEDEIGEFREYKKRVDPEGRFNKGKLLNLPGMEADLSNAYTPSFGLMGHESLIMQQSDIGAIASSVKDCLRCGKCKPVCSTHVPRANLLYSPRNKILATSLLVEAFLYEEQTRRGVSIKHWEEFEDVADHCTVCHKCVTPCPVDIDFGDVSMNMRNLLRKMGKKSFNAGTNAAMFFLNATDPATINATRKVMTQWGFKAQRLGNDLMKKFAKKQTQKPPATVGKPPVKEQVIHFINKKMPGNLPKKTARALLDIEDDKIVPIIRNPKTTTADTEAVFYFPGCGSERLFSQVGLATQAMLWNVGVQTVLPPGYLCCGYPQRGTGDFEKGEKIITDNRVLFHRMANTLNYLDIKTVVVSCGTCYDQLQGYEFEKIFPGCRIIDIHEYLLEKGVKLEGVTGTRYMYHDPCHSPMKQQDPLKTVNSLITTIDAQKIEKNDRCCGESGTFGVSRPDVSTQVRFRKEEEMRKGSDKVRADGFTGDVKILTSCPSCFQGLSRYNEDAGTTADYIVVEMARHLLGENWMPEYVERANNGGIERILV Kangiella aquimarina DSM 16071 Kang B158DRAFT_1333 B158DRAFT_1333 component of chlorite stress sensing system with B158DRAFT_1334 (DUF2063) PFam PF05114.9 (DUF692). conserved specific phenotype and conserved cofitness Uncharacterized protein conserved in bacteria MKQQKLIIGAGLGLRRDFLDEYEALDQSTVDFMEVAPENWIPYGGRLKDQFKRYAERFPFVIHGLSLSIGGPTPLDTDFVKQVAEFIKTYDIQCYSEHLSYCSDDGHMYDLMPIPFTEEAVHYVAKRIQQVQDIIGQQIAMENVSYYAAPGQEMSELEFLLAVLEEADCKLLLDVNNIYVNSINHKYNPEQFLKALPKERIAYGHIAGHYDEAEDLKVDTHGSDVKPEVWNLLDLAYEQFGVFPTLLERDFNIPSMAKLLKEVEQIKALQNKYQQAPAAIA Kangiella aquimarina DSM 16071 Kang B158DRAFT_1334 B158DRAFT_1334 component of chlorite stress sensing system with PGA1_c21010 (DUF692) PFam PF09836.5 (DUF2063). conserved specific phenotype and conserved cofitness Uncharacterized protein conserved in bacteria MNKHSELPKFQQIQFEFAKNLRNPAKFQAPEGIEARRMKVYQDLFYNNIQNFCANSFPILRSLIADDKWHRMVRSFFTEYRAHSPYFADISAEFLNYLSNEREAEQDDFPFMTELAHWEWMEVSLLANKQDILAIPHDRNGDLFNQNIVISPLAVANAYEFPVHRIGKAYIPEEKPDQPTFLIICRDRKHKIEFMETNLFTFRLLQIFLEHLEQGSQINGQQALQQLAVETQFPNPQQLIEGGKQMLDSLLQRDVILGVNS Escherichia coli BW25113 Keio 15310 b1188 ycgB ycgB component of nitrogen-related signalling system (of yeaGH-ycgB) conserved cofitness; yeaG is a protein kinase hypothetical protein (NCBI) MATIDSMNKDTTRLSDGPDWTFDLLDVYLAEIDRVAKLYRLDTYPHQIEVITSEQMMDAYSSVGMPINYPHWSFGKKFIETERLYKHGQQGLAYEIVINSNPCIAYLMEENTITMQALVMAHACYGHNSFFKNNYLFRSWTDASSIVDYLIFARKYITECEERYGVDEVERLLDSCHALMNYGVDRYKRPQKISLQEEKARQKSREEYLQSQVNMLWRTLPKREEEKTVAEARRYPSEPQENLLYFMEKNAPLLESWQREILRIVRKVSQYFYPQKQTQVMNEGWATFWHYTILNHLYDEGKVTERFMLEFLHSHTNVVFQPPYNSPWYSGINPYALGFAMFQDIKRICQSPTEEDKYWFPDIAGSDWLETLHFAMRDFKDESFISQFLSPKVMRDFRFFTVLDDDRHNYLEISAIHNEEGYREIRNRLSSQYNLSNLEPNIQIWNVDLRGDRSLTLRYIPHNRAPLDRGRKEVLKHVHRLWGFDVMLEQQNEDGSIELLERCPPRMGNL Escherichia coli BW25113 Keio 15901 b1783 yeaG yeaG component of nitrogen-related signalling system (of yeaGH-ycgB) conserved cofitness; yeaG is a protein kinase conserved protein with nucleoside triphosphate hydrolase domain (NCBI) MNIFDHYRQRYEAAKDEEFTLQEFLTTCRQDRSAYANAAERLLMAIGEPVMVDTAQEPRLSRLFSNRVIARYPAFEEFYGMEDAIEQIVSYLKHAAQGLEEKKQILYLLGPVGGGKSSLAERLKSLMQLVPIYVLSANGERSPVNDHPFCLFNPQEDAQILEKEYGIPRRYLGTIMSPWAAKRLHEFGGDITKFRVVKVWPSILQQIAIAKTEPGDENNQDISALVGKVDIRKLEHYAQNDPDAYGYSGALCRANQGIMEFVEMFKAPIKVLHPLLTATQEGNYNGTEGISALPFNGIILAHSNESEWVTFRNNKNNEAFLDRVYIVKVPYCLRISEEIKIYEKLLNHSELTHAPCAPGTLETLSRFSILSRLKEPENSSIYSKMRVYDGESLKDTDPKAKSYQEYRDYAGVDEGMNGLSTRFAFKILSRVFNFDHVEVAANPVHLFYVLEQQIEREQFPQEQAERYLEFLKGYLIPKYAEFIGKEIQTAYLESYSEYGQNIFDRYVTYADFWIQDQEYRDPDTGQLFDRESLNAELEKIEKPAGISNPKDFRNEIVNFVLRARANNSGRNPNWTSYEKLRTVIEKKMFSNTEELLPVISFNAKTSTDEQKKHDDFVDRMMEKGYTRKQVRLLCEWYLRVRKSS Escherichia coli BW25113 Keio 15902 b1784 yeaH yeaH component of nitrogen-related signalling system (of yeaGH-ycgB) PFam PF04285.8 (DUF444). conserved cofitness; yeaG is a protein kinase hypothetical protein (NCBI) MTWFIDRRLNGKNKSMVNRQRFLRRYKAQIKQSISEAINKRSVTDVDSGESVSIPTEDISEPMFHQGRGGLRHRVHPGNDHFVQNDRIERPQGGGGGSGSGQGQASQDGEGQDEFVFQISKDEYLDLLFEDLALPNLKQNQQRQLTEYKTHRAGYTANGVPANISVVRSLQNSLARRTAMTAGKRRELHALEENLAIISNSEPAQLLEEERLRKEIAELRAKIERVPFIDTFDLRYKNYEKRPDPSSQAVMFCLMDVSGSMDQSTKDMAKRFYILLYLFLSRTYKNVEVVYIRHHTQAKEVDEHEFFYSQETGGTIVSSALKLMDEVVKERYNPAQWNIYAAQASDGDNWADDSPLCHEILAKKLLPVVRYYSYIEITRRAHQTLWREYEHLQSTFDNFAMQHIRDQDDIYPVFRELFHKQNATAKG Escherichia coli BW25113 Keio 16293 b2184 yejH DNA damage response helicase (yejH or radD) Conserved and specific phenotype: important for resisting cisplatin. Also important for resisting ionizing radiation and UV radiation (PMID:25425430) predicted ATP-dependet helicase (NCBI) MIFTLRPYQQEAVDATLNHFRRHKTPAVIVLPTGAGKSLVIAELARLARGRVLVLAHVKELVAQNHAKYQALGLEADIFAAGLKRKESHGKVVFGSVQSVARNLDAFQGEFSLLIVDECHRIGDDEESQYQQILTHLTKVNPHLRLLGLTATPFRLGKGWIYQFHYHGMVRGDEKALFRDCIYELPLRYMIKHGYLTPPERLDMPVVQYDFSRLQAQSNGLFSEADLNRELKKQQRITPHIISQIMEFAATRKGVMIFAATVEHAKEIVGLLPAEDAALITGDTPGAERDVLIENFKAQRFRYLVNVAVLTTGFDAPHVDLIAILRPTESVSLYQQIVGRGLRLAPGKTDCLILDYAGNPHDLYAPEVGTPKGKSDNVPVQVFCPACGFANTFWGKTTADGTLIEHFGRRCQGWFEDDDGHREQCDFRFRFKNCPQCNAENDIAARRCRECDTVLVDPDDMLKAALRLKDALVLRCSGMSLQHGHDEKGEWLKITYYDEDGADVSERFRLQTPAQRTAFEQLFIRPHTRTPGIPLRWITAADILAQQALLRHPDFVVARMKGQYWQVREKVFDYEGRFRLAHELRG Escherichia coli BW25113 Keio 17022 b2943 galP galactose:H+ symporter (galP) A characterized E. coli protein, see EcoCyc. Not sure why SEED has it as transporting arabinose. KEGG_correct. D-galactose transporter (NCBI) MPDAKKQGRSNKAMTFFVCFLAALAGLLFGLDIGVIAGALPFIADEFQITSHTQEWVVSSMMFGAAVGAVGSGWLSFKLGRKKSLMIGAILFVAGSLFSAAAPNVEVLILSRVLLGLAVGVASYTAPLYLSEIAPEKIRGSMISMYQLMITIGILGAYLSDTAFSYTGAWRWMLGVIIIPAILLLIGVFFLPDSPRWFAAKRRFVDAERVLLRLRDTSAEAKRELDEIRESLQVKQSGWALFKENSNFRRAVFLGVLLQVMQQFTGMNVIMYYAPKIFELAGYTNTTEQMWGTVIVGLTNVLATFIAIGLVDRWGRKPTLTLGFLVMAAGMGVLGTMMHIGIHSPSAQYFAIAMLLMFIVGFAMSAGPLIWVLCSEIQPLKGRDFGITCSTATNWIANMIVGATFLTMLNTLGNANTFWVYAALNVLFILLTLWLVPETKHVSLEHIERNLMKGRKLREIGAHD Escherichia coli BW25113 Keio 17664 b3603 lldP (R)-lactate / (S)-lactate / glycolate:H+ symporter LldP This protein is annotated by EcoCyc as transporting both stereoisomers of lactate and glycolate, which is consistent with our genetic data and a more detailed study (PMID:11785976). The previous study found that yghK (glcA) also transported glycolate and was important for glycolyate utilization. We instead observed a very subtle defect of the glcA mutant during growth on glycolate (fitness = -0.5). L-lactate permease (NCBI) MNLWQQNYDPAGNIWLSSLIASLPILFFFFALIKLKLKGYVAASWTVAIALAVALLFYKMPVANALASVVYGFFYGLWPIAWIIIAAVFVYKISVKTGQFDIIRSSILSITPDQRLQMLIVGFCFGAFLEGAAGFGAPVAITAALLVGLGFKPLYAAGLCLIVNTAPVAFGAMGIPILVAGQVTGIDSFEIGQMVGRQLPFMTIIVLFWIMAIMDGWRGIKETWPAVVVAGGSFAIAQYLSSNFIGPELPDIISSLVSLLCLTLFLKRWQPVRVFRFGDLGASQVDMTLAHTGYTAGQVLRAWTPFLFLTATVTLWSIPPFKALFASGGALYEWVINIPVPYLDKLVARMPPVVSEATAYAAVFKFDWFSATGTAILFAALLSIVWLKMKPSDAISTFGSTLKELALPIYSIGMVLAFAFISNYSGLSSTLALALAHTGHAFTFFSPFLGWLGVFLTGSDTSSNALFAALQATAAQQIGVSDLLLVAANTTGGVTGKMISPQSIAIACAAVGLVGKESDLFRFTVKHSLIFTCIVGVITTLQAYVLTWMIP Escherichia coli BW25113 Keio 17808 b3748 rbsD D-ribose pyranase [EC:5.4.99.62] This is a ribose pyranase, not a transporter, see PMID:15060078 or UniProt:RBSD_ECOLI (KEGG_correct) D-ribose high-affinity transport system; membrane-associated protein (VIMSS) MKKGTVLNSDISSVISRLGHTDTLVVCDAGLPIPKSTTRIDMALTQGVPSFMQVLGVVTNEMQVEAAIIAEEIKHHNPQLHETLLTHLEQLQKHQGNTIEIRYTTHEQFKQQTAESQAVIRSGECSPYANIILCAGVTF Escherichia coli BW25113 Keio 18096 b4068 yjcH required for glycolate transport, with actP PFam PF04341.8 (DUF485). This gene is specifically important for glycolate utilization and is conserved cofit with actP. conserved inner membrane protein involved in acetate transport (NCBI) MNGTIYQRIEDNAHFRELVEKRQRFATILSIIMLAVYIGFILLIAFAPGWLGTPLNPNTSVTRGIPIGVGVIVISFVLTGIYIWRANGEFDRLNNEVLHEVQAS Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1497 Ga0059261_1497 required for sulfate utilization, putative electron source for sulfite reductase CysI PFam PF11011.4 (DUF2849). conserved cofit with sulfite reductase and has a complementary pattern of gene presence as cysJ Protein of unknown function (DUF2849) MKILTGNDLPTGDVTWWTGSGWSRHVEDAVDVGDQGEAIAHAEEGARRVNGPYVIDATETPEGPRPAHIKDRIRALGPTVRPDLTLKPADPNAGSWVI Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1499 Ga0059261_1499 required for sulfate utilization, putative electron transport protein for sulfite reductase PFam PF06073.8 (DUF934). conserved cofitness with sulfite reductase; auxotrophic Uncharacterized protein conserved in bacteria MADQTLRFRNDEVHDEPAVTLDSFLGQSNATAVRLESSDDARALLPHLERLSLVEVSFPKFRDGRGYSAGRILREAGYTGELRAQGDVLVDQIPLMRRCGFDSFAPEAEVDEAVLAASLARYDHVYQAAADPAVPVWKRRHG Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1577 Ga0059261_1577 L-glutamine and L-histidine transporter Specific phenotype on glutamine; also important for histidine utilization; detrimental to fitness on some other amino acids (proline, alanine) which may indicate that it likes these amino acids amino acid/polyamine/organocation transporter, APC superfamily (TC 2.A.3) MAGGLFRTKRVKDAAEQAPEHRLAATLSWPHLVALGVGAIVGTGILTLIGVGAGKAGPAVIMSFVIAGAICACAALAYAEMATMMPASGSAYAYSYAVLGEIIAWVVGWSLILEYSLVVSTVAVGWSGYAAPLLHAWTGMPLELMAGPHANGIVNLPAIFIIAVVAGLLCLGTKESATLNAALVVVKIIALAVFVAVALPYFNGANLEPFAPFGFAKTISPDGVERGVMAAAAIIFFAFYGFDAISTAAEETKNPGRDLAIGIVGSMIACVAIYMLVAVAAVGATPFTHFANSPEPLALILRDLGRPGFATFLAVSAIIALPTVLLGFLFGQSRIFFTMARDGMLPIGLAKVSKRGSPVRITLFTAAIVAVIAGLLPIDEIAALANAGTLAAFTAVAVCMMVLRVRAPDMPRMFRTPLWWLVGAIAVLGCIYLFFSLPVKTQLWFLAWNALGVVIYFAYARPRVSAKGIE Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1581 Ga0059261_1581 Maltose or maltodextrin glucosidase (EC 3.2.1.20) Specifically important for: D-Maltose monohydrate; a-Cyclodextrin. The first step in catabolism of maltose or longer maltodextrin polymers. The phenotype on maltose implies that maltose is also a substrate, which was ambiguous with the original SEED annotation (SEED_correct) Glycosidases MRSLAFALTLLAGTVASAQTAAPAELRARAAETEVLYFLLPDRFENGDPSNDRGGLRGDRLTTGFDPAHKGFFHGGDLKGLIRRLDYIQSLGASAIWLGPIYKNKPVQGGPGQETAGYHGYWITDFTRVDPHFGTNDEMKAFVDAAHARGIKVYLDIITNHTADVIQYRECPKSACDYRSRADYPYQRKGGVKGAAINPGFAGDGVQTPENFAKLSDPNYAYTTVVPEAERTVKVPAWLNDPIHYHNRGNTTFRNESSTMGDFVGLDDLMTESPRVLQGFIDIYGAWIDQFGIDGFRIDTARHVNPEFWQGFSKAMIERAKARGIPNFHIFGEVANEGDVGDLALHTRVHQLPSVLDFGFRAAVQHTVAGEKGPDMLAAMFDRDALYEGGAEAALRLPTFISNHDHGRFSTDVRKAFPKASDDEVLARVKLAHAMLLLLRGVPTIYSGDEQGFVSDGNDQDAREDMFPSKVAIYNDNRLLGTDKTTADSNFDTGHPLYMEISKLSAIRKATPALSRGRQVTRAYDEKPGLFAVSRFDPASGAEVLVAFNTSAAPITRQVEVGVSSTAFAPLVGQCAASASAPGSVTVTLPAFGYVACVAAGGAK Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1777 Ga0059261_1777 D-fructose transporter, sugar porter family Specific phenotype on fructose and raffinose; during growth on raffinose, it is probably cleaved to sucrose in the periplasm (by Ga0059261_1166), so this probably is important on raffinose because of the fructose uptake MFS transporter, sugar porter (SP) family MHSVSASFAGAPDEEARATVAIILSAAGAALGGLLFGFDTAVISGATQALQLQFGLTDAMLGFTVASALIGTVLGSLIAGAPADRFGRKGVMLTVAIAYVVSSLGTGLAPDLNAFLVFRFMGGLAIGAASVVTPIYIAEVSPARFRGRLVAMNQLNIVLGILIAFLSNYIIAGLVQYDVAWRWMFGIVAVPSTIFLLVTLLLPESPRWLAIHGQADRARDVMQRLGFADPRAELARIELAEAREEAAGKPRLFQRSHFTPVACAIAIAMFNQLSGINALLYYAPRIFELAGAGADSALLQSIAVGGTNLVFTVAALFLIDRFGRRPLLFVGSVICAATLLLVGWQLESAKPDGTLILFGLLGFIAAFAMSQGAVIWVFISEVFPSAVRGKGQALGSTTHWVMAAAITWAFPVFAASVGGWVFAFFGAMMLLQLLWTWKFMPETNGIALEDMNLGSARA Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1778 Ga0059261_1778 beta-fructosidase for D-raffinose catabolism (EC 3.2.1.26) Specifically important for: D-Raffinose pentahydrate. Uncertain if it acts on raffinose or sucrose (raffinose could be cleaved to galactose + sucrose first). Alternatively, SEED suggests that it hydrolyzes sucrose-6-phosphate, but the basis for this is unclear. Beta-fructosidases (levanase/invertase) MKKLAILLTAAAVLASAASAQQADVRPGYHYGPARNWMNDPNGLVYYDGEYHLFYQYNPHGDRWGHMNWGHAVSRDLVNWEELPVAIPETDVMAFSGTAVIDWNNTTGFGKNGKPPMIAIYTGHDPKTERQSQYLAYSNDRGRTFTIHGEVLNAGNEKHFRDPKVFWHAPTRRWVMVVLKAAANTAEIYTSPNLKDWTHRSSFGPAGGRGKFWECPDLFELPVEGGAPGETRWVLSINLGDNAIGGGSGGQYFVGDFDGEKFTLVPGWPAAPQWMDYGADFYATISWNDMPKGDPRRVWMGWANDWRYAEAIPTWPARGIMTVARTVALRKTAEGYHLLQAPVRELATLRGTPQRAPALALSETPVPLPIEGGKADIELELDTGTADQVSIALTDGQGWQTRIGVNPTVNEVFVDRTRSGPHFHDGFANRHVAPVDLKSRKVKLRVLADESIVEVFVNDGRQTITDRFYRGGGALTWSATARGGKATMNLTAWPMRSMESRK Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1893 Ga0059261_1893 Xylonolactonase (EC 3.1.1.68) Specifically important for: D-Xylose. xylonolactone is an intermediate in the oxidation of xylose (SEED_correct) Gluconolactonase MGVVLTAPEPVWALGAPLLEGPVWVQRDAALWFVDIKSHRIHRFDPASGERRSWDAPAQVGFCLPAANGKFVAGLQTGLAIFDPADRSFTPLTDPEPALPGNRLNDGTVDPAGRLWFGTMDDGESEATGRIYRLGGDGRCVAETAAVSISNGPAVSPDGRTLYHVDTLGGVIHSAAIGDDGILGDSRVFATIPNSEGFPDGPAVDAEGCVWIGLYNGAAVRRYSPAGELLDVVAFPVGAITKVAFGGPDLRTVYATTASKHLDADGRAEEPHAGDLFAFRVSVPGMPGTEVSVGL Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1894 Ga0059261_1894 D-xylose 1-dehydrogenase (EC 1.1.1.175) Specifically important for: D-Xylose. the first step in xylose oxidation (SEED_correct) Dehydrogenases with different specificities (related to short-chain alcohol dehydrogenases) MTQPAAASAAAVYPSLKGKRVLVTGGGSGIGAGIVEGFARQGADVTFFDIAGAESQLLVERLSADGHKACFERVDLTDVASLQAVIARLIKGAGGFDILVNNAANDDRHAIDEITEAYWDERLSVNLKHIFFCAQAVVPAMRARGGGAIVNLGSISWHLGLSDLVLYQTCKAAIEGLTRSLARDLGRDGIRATCVIPGNVRTPRQLKWYSPEGEAEIVAAQCLDGRLAPEDVAAMVLFLASDDARLVTGHSYFVDAGWR Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1896 Ga0059261_1896 Ketoglutarate semialdehyde dehydrogenase (EC 1.2.1.26) Specifically important for: D-Xylose. The KEGG annotation is vague; xylose is oxidized to alpha-ketoglutarate semialdehyde (SEED_correct) NAD-dependent aldehyde dehydrogenases MELTGGLFIGGERRQSDARFHAYDPAAGADIADAGFASASEQDVADACAAAEAAFLPYSTKPLEARARFLETIADEIEALGDVLIERACRESGLPAARITGERGRTVGQLRLFAKEVRDGAWQKLRIDHADRERTPPRPDLRLRMVPLGPVAVFGASNFPLAFSTAGGDTASAFAAGCPVVVKGHRAHPGTAELIATAIIRAVETCGMPAGTFGMVNGTSRKVGETLVADPRIQAVGFTGSRGGGEALMRIAAARPRPIPVYAEMAAINPVILMPQALKARGPALAEAFVASLAMGAGQFCTNPGLVMGIDGPELDAFVARAGEVLSGQAAQVMLTDGIWEAFESGKAKLAGSAFVTKVAEGVEADGPNRGRAALFSVAGKDFLADPVHLHEVFGVSSVVVRCASLEELKAVLGELEGQLTATLQVDEGDYPEAQALLPVLERTVGRVIANGWPTGVEVTHAMVHGGPYPSTSDPRSTSVGTLAIDRFLRPVSYQDLPEALLPAALRENAQAGTVARIDGSWTI Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1941 Ga0059261_1941 DNA damage response helicase, ligase-associated Conserved and specific phenotype: important for resisting cisplatin. Related to Lhr, which is either a DNA:DNA or DNA:RNA helicase, but lacks the long C-terminal extension that might have a regulatory role (see putative winged helix domain in E. coli lhr). This is also related to the archael protein saci_1500, which has also been linked to DNA damage response, as a mutant is sensitive to UV (PMID: 26148716) DEXH box helicase, DNA ligase-associated MSDLPPVLEHWFASRGWTPRRHQLDMLAAGRAGRHALLVAATGAGKTLAGFLPTLTELIEQPGEGLHTLYISPLKALAVDVQRNLLTPIEEMGLDIRVETRTGDTSHEKKVRQRARPPQILLTTPESLSLLLSYEDSFLMFAGLRTVVVDEVHAFATGKRGDLLALALARLQTLAPGMRRVALSATVADPDGYRAWLAPHGEIDAVELVTGESGAEPDIAILLPEGRVPWSGHSGLYAIPQVMAEIETHKTTIVFCNTRSLAELVFQNLWKVNELKLPIGVHHGSLSLEARQRAEQAMAEGRLRALVATASLDLGVDWGDVDCVIQMGAPKGSSRLLQRIGRANHRLDEPSEAVLVPGNRFEYLEARAALDAVEAGELDPDIFRPGALDVLAQHVMGLACAAPFDAAELLREIQGALPYSALSEDVFEAVLNFIADGGYALRAYDRFKRLTRDKDGLWRVTKPAFVAQHRLNAGIIVEAPMLEVRFRNGRRLGRVEEAFGASLSPGDRFFFAGLALEVERVEVTDIIVRATTKTARFVSYMGARLAITSTLAARVRRFFAEPETWSRFPADVREWLEVQAHRSRLPAPGKLLVETFPHDGRHHMVAYCFEGWNAHQSLGMLVTRRMEALGLKPVGFVANDYALAVYGLEKIEDPAPLFSPDILEHEFVEWVQGSALLKRAFREVAIIGGLVERQQPGKKKTGRQVTFSTDLIYDVLRKYEPDHLLLRAAWADARARMTDIGRLARLLDTAVDRIEHVDLDRVSPMAVPVLIMIGRETVAQGAAEDAMLIEAEALAAEAMRID Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1942 Ga0059261_1942 putative efflux pump, required for thallium (I) resistance PFam PF02694.11 (UPF0060). conserved specific phenotype of UPF0060 Uncharacterized conserved protein MTLFAYVLAALAEIAGCFAFWAWLRLGKSPWWLVPGIAALIVFAWALTWIETSHAGRAYAAYGGIYITAAILWLWAVEGARPDRWDVIGGAVALAGTAIILFGPRSASA Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_2035 Ga0059261_2035 Histidinol-phosphatase [alternative form] (EC 3.1.3.15) Annotated as this by multiple resources. (auxotroph) (SEED_correct) histidinol-phosphatase, inositol monophosphatase family MPVSQADIDLAGRLADAAGAAIRPYFRAEHGLESKDDSSPVTLADKAAEAAMRRLIIAERPMDAIIGEEEDDRPGTSGRIWVLDPIDGTRSFIVGRPIFGTLIALLEDGWPVLGIIDQPIIKERWLGVTGRETLFNGKPARARTCRELSKALLATTSPALFTDGQLHAFEHVDAAVMSTVLGGDCYNYGLVASGHLDIVIEAGLKLHDFAALVPVVEGAGGRMCDWQGDPLHAGSNGEVIAAGDPARIEELVEALACQGH Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_3194 Ga0059261_3194 O-acetylhomoserine sulfhydrylase (EC:2.5.1.49) Annotated as this by multiple resources. KEGG suggests that it is O-succinylhomoserine sulfhydrylase but there is an O-acetyltransferase (Ga0059261_2301) with auxotrophic phenotypes (auxotroph) (SEED_correct) Cystathionine beta-lyases/cystathionine gamma-synthases MKRRTGQDRSITQNWKPATQAIRGGTARSEWGETSEALFLTSGYAYDCAGDAAARFSGDQQGMTYSRLQNPTVEMLEQRIALLEGAEACRATASGMAAMTAALLCQLSAGDHLIGGRAAFGSCRWLTDTQLPKFGIETTVVDARDPQQFIDAIRPNTKVFFFETPANPTMDVVDLKAVCAIARERGIVTVVDNAFATPALQRPMDFGADVVAYSATKMMDGQGRVLAGAVCGTEEFINNTLLPFHRNTGPTLSPFNAWVVLKGLETLDLRIQRQSENALKVARFLEGRVPRVNFPGLPSHPQHNLAMSQMAAAGPIFSIELDGGRTQAHGLLDALGLIDISNNIGDSRSLMTHPASTTHSGVAEDQRLLMGVGEGMLRLNVGLEDPEDLIADLDQALGSVGL Marinobacter adhaerens HP15 Marino GFF1367 HP15_1334 Error-prone polymerase for DNA repair (imuB or polY like) Conserved and specific phenotype: important for resisting cisplatin. Related to imuB from Caulobacter. Also similar to PA0670, which is induced by the SOS response, even though it does not seem to have mutant phenotypes related to DNA repair. conserved hypothetical protein MLWLYLHFPHLVLDHIRRTREDEGALVVVEGSGQKVIQACPDARSQGIRSGMRLKTAISLAPDLGMVRADETQEARILEDQARWLYRYAAHIVLVPPDGLLAEIGSLQKLYGGLPAVWQTVEQGLNERQLNAWIGIGYTPLAARLIARAGKGECTADKGHILRSLSQMPLLAAEFNEKACTRLRRLGLNTLGEVFDLPPGELARRLSPELLAYIQKIQGTRPDPRTPWQPPHSFRQQADFVQEIEHTQGLLFPLQRMLVELEEDLCWRQQDTDSLRLVLKHRHAEPTRLQIRTSGPEHRADHFLNLVRLRLEQHSLSAPVISMVLLVKRFLSREAPSGQDLLGETQDLNEAWHTLISRLQARLGDQALRQLSPQADHRPERAWSASEVLRKTGTPLVPAAELPRRPLWLLKGPQPLTEAPVTWFSGPERISGGWWDGQRVHRDYYIAQLSSGQLAWVFRDAREGWFVHGWFG Marinobacter adhaerens HP15 Marino GFF1839 HP15_1796 required for sulfate utilization, putative electron transport protein for sulfite reductase PFam PF06073.8 (DUF934). Conserved cofitness with sulfite reductase; auxotrophic. uncharacterized conserved protein UCP030820 MPNVISPDGSIRQDNWVVVPRPAEGESLDIPADQPALIPADLWLAGYEHFTGRQEIGVWFDSHDEPEILDGRVNELPVIAVNFPKFSDGRGYSIGRLLRERFGYKNELRAIGDVLLDQLQFMKRCGFDAYVLRADKDINKAARCLNFFSQGYQAATDTEIPLFRRRAS Marinobacter adhaerens HP15 Marino GFF217 HP15_216 DNA damage response protein (yhgF like) Conserved and specific phenotype: important for resisting cisplatin. Also important for resisting ionizing radiation in E. coli (PMID:25049088) transcriptional accessory protein MNSISRRIAEELGVREQQVNATVELLDEGATVPFIARYRKEITGSLDDSQLRNLEERLRYLRELEDRRATILKSIEEQGKLTDELKATIQDADTKNRLEDLYLPYKPKRRTKAQIAREAGLEPLADALYDDPTLDPEITAQGYLNKEAGVEDTKAALDGARYILMERFAEDAELLGSLRDFIWQEGQLKVTVVEGKENEGAKFRDYFDHVEPLKKVPSHRALAILRGRNEGVLGYTIVVGDAEDDRRAPHPAEQRIAARWNIRDNGRAADKWLSEVVRWTWRVKLSTQIETDLMAQVREAAETEAINVFAANLKDLLLLAPAGPRPTLGLDPGLRTGVKVAVIDGTGQVAGHGAIFPHAPQNQWDRSIEQLAAWCREYKIELVAIGNGTASRETEKLVGDLSKRYPELKLARIVVSESGASVYSASEFASKELPDLDVTIRGAVSIARRLQDPLAELVKIEPKSIGVGQYQHDVSQVQLSRSLDAVVEDCVNGVGVDLNTASAPLLARVSGLNQTIAQNIIEFRNQNGMFRNRKQLLKVTRLGDRTFEQAAGFLRIAGGENPLDRSSVHPEAYGVVEAIARKNNREVGDIIGDSSFLRGLNPQDYVTEQFGLPTIKDIISELEKPGRDPRPEFRFASFEEGVETLSDLKPGMVLEGSVTNVTNFGAFVDIGVHQDGLVHISALSHTFVKDPREVVKAGDIVKVKVMDVDIPRKRIALTMRMDDQPGEKNEGKPMAANRSGASRKGGNRNAGNGGSGQKSPQGAMAGALAQALASARKDS Marinobacter adhaerens HP15 Marino GFF2534 HP15_2478 Acyl-CoA dehydrogenase (EC 1.3.8.7) Specifically important for: Tween 20. tween 20 hydrolyzes to a mix of C12, C14, and C16 fatty acids; this is probably part of beta oxidation (SEED_correct) acyl-CoA dehydrogenase family protein MRFVLNEVFDAPALWASLPKVAEHVDPETADAILEEAGKISSGVLAPLNREGDEQGCKWNDGEVTSPEGFKEAYQTIVEGGWNGLGGNPDFGGMGMPKTLVAQFEEMMQGANMAFGLAPMLTAGACLALDAHGSDELKEKYLPNMYSGVWSGAMDLTEPHAGTDLGIIRTKAEPNDDGSFNVTGTKIFITWGEHDMAENIIHLVLAKLPDAPKGPKGISMFLVPKFLVNDDGSLGERNSFSCGSLEKKMGIKGSATCVMNFDGAKGWLVGEENKGLAAMFTMMNYERLGVGIQGIGAAEASLQSAREYALDRIQSRAPTGAQQPEKAADPILVHPDVRRMLLTMKSYVEGGRTFSTYVAQWLDIAKFAEDDERRKHAEGMVALLTPVAKAFLTDRGLDTCIMGQQVFGGHGFIREWGQEQLVRDCRITQIYEGTNGIQALDLMGRKVVGTQGKLYELFAQDVANFLEENSGNDHLRPFLEPLAAAVERLDDVTEHVIKQAGDNPNAIGAASVDYLDLFGLTALGYMWAKIVKAAAPQADSDTSGFYSGKLKTARFYFDRLLPKTVSLAEGIRSGSDSMMALTAEEF Marinobacter adhaerens HP15 Marino GFF2749 HP15_2693 3-hydroxyacyl-CoA dehydrogenase PaaC (EC 1.1.1.-) Specifically important for: L-Phenylalanine. Part of phenylalanine catabolism via phenylacetate (SEED_correct) 3-hydroxybutyryl-CoA dehydrogenase MPALDTQTKVAVVGAGAMGSGIAQVAAQAGHQVYLHDQREGAAEAGRDGIAKQLQRRVDKGKMQQQELDDVIGRIHPVAKLDDVADAGLVIEAIIEDLQIKRQLLASLEDLCTADAILATNTSSISVTALGADMSKPERLVGMHFFNPAPLMALVEVVMGLATSKTVADTVHATATAWGKKPVYATSTPGFIVNRVARPFYAESLRLLQEQATDAATLDAIIREAGQFRMGAFELTDLIGHDVNYAVTSSVFNSYYQDPRFLPSLIQKELVEAGRLGRKSGQGFYPYGESAEKPQPKTEPAHQSDESVIIAEGNPGVAAPLLERLKAAGLTIIERDGPGQIRFGDAVLALTDGRMATERAACEGVANLVLFDLAFDYSKASRLALAPADQASDAAVSCACALLQKAGIEVSLIADRPGLVIMRTVAMLANEAADAALHGVATVADIDLAMKAGLNYPDGPLSWSDRLGAGHVFKVLTNIQTSYAEDRYRPALLLRKNAFAQKGFYS Marinobacter adhaerens HP15 Marino GFF2751 HP15_2695 Beta-ketoadipyl CoA thiolase (EC 2.3.1.-) Specifically important for: L-Phenylalanine. The second SEED annotation (beta-ketoadipyl-CoA thiolase) is part of phenylalanine catabolism via phenylacetate. Not clear if the acetyl-CoA acetyltransferase annotation is correct, so it was removed, but it remains plausible (SEED_correct) acetyl-CoA acetyltransferase MSADNILKDAYIVDAIRTPIGRYGGALSAVRADDLGAIPIKALAERYPDLDWSKIDDVLYGCANQAGEDNRDVARMSLLLAGLPVDVPGSTINRLCGSGMDAVGSAARAIRTGETQLMIAGGVESMSRAPFVMGKADSAFSRKAEIFDTTIGWRFVNPVLKKQYGIDSMPETAENVAADFGISREDQDAFALRSQQRTAAAQKEGRLAAEITPVTIPRRKQDPLVVDTDEHPRETSLEKLASLPTPFRENGTVTAGNASGVNDGACALLLAGADALKQYNLKPRARVVAMATAGVEPRIMGFGPAPATRKVLATAGLELADMDVIELNEAFAAQALAVTRDLGLPDDAEHVNPNGGAIALGHPLGMSGARLVTTALNELERRHAAGQKARYALCTMCIGVGQGIALIIERMDAVA Marinobacter adhaerens HP15 Marino GFF2888 HP15_2832 DNA damage response helicase (yejH or radD) Conserved and specific phenotype: important for resisting cisplatin. Also important for resisting ionizing radiationa and UV radiation in E. coli (PMID:25425430) type III restriction protein res subunit MNAPFKLRPYQREAVDATLAHFRKTDESAVIVLPTGAGKSLVIAELARLAKRKILVVTHVKELVEQNHAKYQSYGLTGGIFSAGLKRKESHHQVTFASVQSVSANLDQFRDEYSLVIIDECHRVSGEETSQYQRIIELLRQQNDSLKVLGLTATPYRLAMGWIYRYHYRGFVRGEDDKPFQHCIYELPLSYMINRGYLTRPELVNAAVAQYDFSALPKDRFGEYAERDVNQLLSKHKRVTRAIIEQVVELAAERQGVMIFAATVEHAREVAGYLPEHETALITGATDLKDRDLLIQRFKQRQLKYLVNVSVLTTGFDAPHVDFIAILRPTQSVSLYQQIVGRGLRLDEGKQDCLVIDYAGNHVNLHHPEVGEPKPNPDSEPVQVFCPGCGFANIFWGKTDDDGRVIEHYGRRCQGLLEPVDGVQDERPQQCDYRFRFKECPHCGAENDIAARNCHQCHKAIIDPDDQLRDALKLKDAMVIRCAGISLVADGSKLKITYHGEDGEELGESFDFSKPGQRAVFNKLFGRRFANSQAPKAFSSADEVLELEALLPAPDFVIARKQKHYWQVQERVFDYQGQFRKANEV Marinobacter adhaerens HP15 Marino GFF3193 HP15_3135 ethanol oxidation regulatory protein ercA Specifically important for: Ethanol; D-Trehalose dihydrate. Similar to ercA (PA1991) which apparently has a regulatory role (PMCID: PMC3754586) rather than being directly involved in catabolism. Also this gene is adjacent to an apparent ercS (HP15_3134). Do not see why SEED annotates it as aldehyde dehydrogenase. HP15_3164 is probably the ethanol dehydrogenase and HP15_3144 the acetaldehyde dehydrogenase. iron-containing alcohol dehydrogenase MSHDISSLRKFVSPEIVFGAGSRKSVANFASNFGARHVFLVSDPGVAAAGWVDEIVTLLTDAGIRSTVYTGVSPNPKVDEVMTGAELYKSNECDVIVAIGGGSPMDCAKGIGIVATHGRSILEFEGVDTITNPSPPLILIPTTAGTSADVSQFAIISDPNRRFKFSIISKAVVPDVSLIDPEVTETMDAYLTACTGVDALVHAIEAYVSTGSGPLTDTHALEAIRLINRNLEPLVDNTADPYLREQIMLASMQAGLAFSNAILGAVHAMSHSLGGFLDLPHGLCNALLLEHVVAYNFQSAEDRFRRVAEAMDIDTRGMAKPEIKKRLMNRIVELKRRVGLEARLAQLGVSVSDIPHLSGFALQDPCILTNPRKSSLRDVQVVYEEAL Marinobacter adhaerens HP15 Marino GFF3778 HP15_3720 DNA damage response nuclease Conserved and specific phenotype: important for resisting cisplatin. Contains a VRR-NUC domain that is predicted to have nuclease activity. protein containing VRR-NUC domain MSPAKRQSTQLATADLDNPLYYLENMETVLGWVQSHHGDLLTAEELDRLASFHTLSMPARALLTRMVMRTGDLFRSDKLKYPELGVPEASALDEITEAGWLDTDPLLSLDELFRLFTLGELRPAMEPLLKAAGEPANLPKGRMRDALLLRFPDPLIVADWLGQHARPVIRLKTMALFDRVRLMFFGNLRQSWSDFVLVELGHQQFEPVTFTPDSRAFQQRSEVDLYLAMHQCREWLDQGVPALEVWQAVPSPSNNAWLTSRRDRLLLELGRQAERQGERELALEAFASSGHREARLKQLRLLERMKRHREAWAIASEWQNQELSDAEAQGLARILKRLASRLGEIAPPPPEQPLIREITLTLPKPEVGSVEYAVRDHLYRDEAPVLYVENTLINGLFGLLCWQTIFEPVPGAFFHPFHVGPADLTREDFVSRRKGSFEQCFARLADGSYRERILANYRAKQGTTNPFVIWPVITEELLSLALDCLPPPDLERLFRRLLLNIREHRSGFPDLIRFLPNVAEPDKRYEMIEVKGPGDRLQDHQIRWLEFFAAEGIPASVCYVRWQASEAME Marinobacter adhaerens HP15 Marino GFF473 HP15_461 Histidinol-phosphatase (EC:3.1.3.15) Similar to the proposed hisB in pseudomonads, and is most cofit with histidinol dehydrogenase and histidinol-phosphate aminotransferase. Another candidate for this activity is HP15_3738 (annotated as bifunctional by SEED), but it has weak phenotypes and is more likely involved in cell wall synthesis (auxotroph) HAD-superfamily hydrolase MTLAIFDLDNTLLAGDSDHAWGEFLVEEGIVDAEEYRLANDRFYQEYLNGELDILHYLGFALQPLASHNMEELLAWREAFMEKKVRPMMQATANTLLDSHREQGHTLMIITATNRFVTEPIAEALGIEHLIATEPELVNGRYTGEVAGTPSFQDGKVTRLDDWLSAHNRTLEGAWFYSDSHNDLPLLKKVDNPVAVDPDPTLAQYARDNGWKVMSLRG Marinobacter adhaerens HP15 Marino GFF879 HP15_858 phenylalanine aminotransferase (EC 2.6.1.57) Specifically important for: L-Phenylalanine. The donor for the amine group is uncertain, but this gene is specifically involved in catabolism of phenylalanine via phenylpyruvate (the product of this enzyme) aspartate aminotransferase MFEALQPLPQDPILQLMQTFLEDDRPDKVDLGIGVYKDDAGNTPIMAAVHEAERRLLEGETTKSYVGPAGSAGFNSAMAELILGSNSPLVRDGRVSVIQTPGGCGALRMAAEFLRLCKADTKVWVSTPTWANHLPLLGGAGLTIREYPYLNPETLQVDFGAMLETLERADAGDVVLLHGCCHNPSGADLSLAQWQEVTSLIQRKGLLPFVDMAYQGLGEGLDADAAGLRHLASAVPEMLIAASCSKNFGLYRERTGALALVSETATVNAAATSQLLSVIRSHYSMPPAHGASIVETILGDDDLRAQWQQELNGMCKRILHLRHAFADALSPVGDFDFIARQRGMFSFLGISPEQVGRLRKEHGIHMLESSRVNVAGLNDHVLPQVASALREVLGK Marinobacter adhaerens HP15 Marino GFF880 HP15_859 phenylpyruvate ferredoxin oxidoreductase (EC 1.2.7.8) Specifically important for: L-Phenylalanine. This is the second step in phenylalanine catabolism (to phenylacetyl-CoA). Alternatively, could be a decarboxylase (forming phenylacetaldehyde), but we did not identify a separate aldehyde dehydrogenase. Annotated as indolepyruvate ferredoxin oxidoreductase, which has the same EC number but is part of tryptophan catabolism.. pyruvate ferredoxin/flavodoxin oxidoreductase MSADTPQLDDYKLEDRYLRESGRVFLTGTQALVRIPLMQAALDRKQGLNTAGLVSGYRGSPLGAVDQALWQAKDLLDENRIDFVPAINEDLAATILLGTQQVETDEDRQVEGVFGLWYGKGPGVDRAGDALKHGTTYGSSPHGGVLVVAGDDHGCVSSSMPHQSDVAFMSFFMPTINPANIAEYLEFGLWGYALSRYSGCWVGFKAISETVESAASVEIPPAPDFVTPDDFTAPESGLHYRWPDLPGPQLETRIEHKLAAVQAFARANRIDRCLFDNKEARFGIVTTGKGHLDLLEALDLLGIDEDKARDMGLDIYKVGMVWPLERRGILDFVHGKEEVLVIEEKRGIIESQIKEYMSEPDRPGEVLITGKQDELGRPLIPYVGELSPKLVAGFLAARLGRFFEVDFSERMAEISAMTTAQDPGGVKRMPYFCSGCPHNTSTKVPEGSKALAGIGCHFMASWMGRNTESLIQMGGEGVNWIGKSRYTGNPHVFQNLGEGTYFHSGSMAIRQAVAAGINITYKILFNDAVAMTGGQPVDGQITVDRIAQQMAAEGVNRVVVLSDEPEKYDGHHDLFPKDVTFHDRSELDQVQRELRDIPGCTVLIYDQTCAAEKRRRRKRKQFPDPAKRAFINHHVCEGCGDCSVQSNCLSVVPRKTELGRKRKIDQSSCNKDFSCVNGFCPSFVTIEGGQLRKSRGVDTGSVLTRKLADIPAPKLPEMTGSYDLLVGGVGGTGVVTVGQLITMAAHLESRGASVLDFMGFAQKGGTVLSYVRMAPSPDKLHQVRISNGQADAVIACDLVVASSQKALSVLRPNHTRIVANEAELPTADYVLFRDADMKADKRLGLLKNAVGEDHFDQLDANGIAEKLMGDTVFSNVMMLGFAWQKGLLPLSEAALMKAIELNGVAIDRNKEAFGWGRLSAVDPSAVTDLLDDSNAQVVEVKPEPTLDELINTRHKHLVNYQNQRWADQYRDAVAGVRKAEESLGETNLLLTRAVAQQLYRFMAYKDEYEVARLFAETDFMKEVNETFEGDFKVHFHLAPPLLSGETDAQGRPKKRRFGPWMFRAFRLLAKLRGLRGTAIDPFRYSADRKLDRAMLKDYQSLVDRIGRELNASNYETFLQLAELPADVRGYGPVREQAAESIREKQTQLIKALDTGRPTLIRTQQANEEANHV Desulfovibrio vulgaris Miyazaki F Miya 8499265 DvMF_0044 Homocysteine formation from aspartate semialdehyde (COG2122 or apbE like component) Mutants in all three genes of this putative system are rescued by casamino acids or methionine but not by threonine. We propose that these three genes act together to enable the formation of homocysteine from asparate semialdehyde (the pathway proposed by Allen et al 2015 (PMID:25938369)). (auxotroph) hypothetical protein (RefSeq) MSTRRNDTGKRPAPATPDAPTVHTDHVRGYRKRTARHPDEVVFQVVVEETDLWVTARSGLSGQPGQPVQPDLPDRIAAYVTELRGQIKAWMLLAPDFRTSLVPVPTPASAPEVARRMAHGADIAGVGPFAAVAGTVAQMVAERFAPVSPDIIVENGGDIYICSQRDRVVGLLPDPASGEMIGVVVKAADCPVSLCSSSATIGHSLSLGVGNIAAVRARDASLADAAATLFGNMLQGPDDVARVTERAAAMAHLGIEGVYAQCGGRVGIWGNMELAVA Desulfovibrio vulgaris Miyazaki F Miya 8500213 DvMF_0971 aroK Homoserine kinase (EC:2.7.1.39) Annotated as shikimate kinase, which is a similar reaction, but there is another shikimate kinase; rescued by threonine or CASamino acids (but not by methionine) (auxotroph) shikimate kinase (RefSeq) MTTPDPLLALDPARIAPDGCVSIIGMAGAGKTTVGRELALQLGWAHVDTDNLIEATYGTRLQAVADSMDKESFLDVEAGVIRRIGARRTVLSTGGSVVYRHEAMAHLAALGPLVYLDVSLPLILKRIAMNPDRGLAIAPGQTIEDLYNERIALYRRYATFTVAADALSPGGCATRIVAWLTGGEA Desulfovibrio vulgaris Miyazaki F Miya 8500650 DvMF_1398 ATP-dependent reduction of co(II)balamin (RamA-like) Cofit with the B12-dependent methionine synthase (DvMF_0476), which lacks a standard domain for the reactivation of vitamin B12. iron-sulfur cluster-binding protein, putative (RefSeq) MSPHSSSEQPPCPAGNDTGCATARPEGRSGPVTPATPDRPGCPSTPGTQPASGAAAEVTLPDGRILHLPLSQSVSLSGQAAAGAAPASTLAQLVWMSGQVDPPALCSGLGRCGRCAARFTRGTPAPHPAEEAHFSPAELADGWRLLCRHALPAPASRSPSSPQGTDPNGNAASPPDARCTMAFTLPAGSAPRRFRAADAPLPDAIQASATGTSPATYTSPATGTSPATGTSPATGAPLLLAIDLGTTTLHWSALTPDGRRVAHGAELNPQMGAGSEVMSRLAVASSPQGLAALRRLTLAAVARIAAGLPGPVRGLCVAGNSAMTAILLGHDVSGLATAPYRLDYAGGTAEILPELADVTYRAGLPDLPDSPGRAAVPEVWIPPQPAPFVGGDVGAGMAALLYGGLVSGGGAGVAANTLQAAATAPAPAASPRFPFLLADLGTNGEFVLATGPDSALVTSVALGPALEGIGLSCGGVAQPGAIAAFTLGPAGLAPTVLPEDDGAPAAPTHLCGTGYLSLLRVLLRAGLLDEDGRFVMEPHSPLARRLAASLVEVRGERRLPLPGGLHLSAGDVEEVLKVKAAFSLAYERLLAEAGMSGTALDAVYLAGALGEHARPDDLETLGFLPAGVAGRTRAVGNASLRGAELLLLQPELRARINAWRTGCRVVDLTTASDFSAAFLRHMRFR Desulfovibrio vulgaris Miyazaki F Miya 8500721 DvMF_1464 Homocysteine formation from aspartate semialdehyde (DUF39 component) Mutants in all three genes of this putative system are rescued by casamino acids or methionine but not by threonine. We propose that these three genes act together to enable the formation of homocysteine from asparate semialdehyde (the pathway proposed by Allen et al 2015 (PMID:25938369)). (auxotroph) protein of unknown function DUF39 (RefSeq) MASFKVNKTIAEINERIRQGKAVVLNAEEMTEAVRRMGKEKAAREIDVVTTGTFSPMCSSGLLFNIGQQDPPTLKTAKVWMNDVPAYAGLAAVDSYLGATEPTEDDPLNKVYPGRFKYGGGHVIEDLVRGKAVHLRAEAYGTDCYPRKSLDKKITLSELPYAHLLNPRNCYQNYNAAVNLTSRIIYTYMGPLKPNLRNVNFATAGRISPLFNDPLFRTIGLGTRIFLGGGTGYVLGAGTQHVAAPKRTERGLPLSPAGTLMLKGDLKGMNARYLRGLSFLGYGCSLAVGVGIPIPILNEEIAWFTGVDDSDIQMPVKDYGHDYPNCLPRVIQHVTYEDLKSGEVEIMGKKVETVPMTSYPLSLEVANTLKSWIEKGEFLLTEPVELLPSA Shewanella oneidensis MR-1 MR1 200453 SO1275 gabD succinate-semialdehyde dehydrogenase (NADP+) [EC: 1.2.1.16] Specifically important for: L-Isoleucine. Also very important with putrescine as the N source. The more specific KEGG annotation is consistent its role on N putrescine (which is converted to 4-aminobutyrate and then to succinate semialdehyde). Its role on isoleucine is unclear but a close homolog, Shewana3_3092, also has this phenotype (albeit milder). Also note that isoleucine is catabolized to propionyl-CoA and Shewana3_3092 is very important for propionate utilization. The annotation of son:SO_1275 in KEGG has been updated to list glutarate-semialdehyde as an additional substrate. (KEGG_correct) succinate-semialdehyde dehydrogenase (NCBI ptt file) MLLNDPSLLRQQCYINGQWCDANSKETVAITNPATGAVIACVPVMGQAETQAAIAAAEAALPAWRALTAKERGAKLRRWFELLNENSDDLALLMTSEQGKPLTEAKGEVTYAASFIEWFAEEAKRIYGDTIPGHQGDKRIMVIKQPVGVTAAITPWNFPAAMITRKAAPALAAGCTMVVKPAPQTPFTALALAVLAERAGIPAGVFSVITGDAIAIGNEMCTNPIVRKLSFTGSTNVGIKLMAQCAPTLKKLSLELGGNAPFIVFDDANIDAAVEGAMIAKYRNAGQTCVCANRIYVQAGVYDEFAEKLSMAVAKLKVGEGIIAGVTTGPLINAAAVEKVQSHLEDAIKKGATVLAGGKVHELGGNFFEPTVLTNADKSMRVAREETFGPLAPLFKFNDVDDVIKQANDTEFGLAAYFYGRDISLVWKVAESLEYGMVGVNTGLISTEVAPFGGMKSSGLGREGSKYGIEEYLEIKYICMSV Shewanella oneidensis MR-1 MR1 200494 SO1319 putative transporter, required for glycine utilization PFam PF03458.9 (UPF0126). conserved specific phenotype of UPF0126 conserved hypothetical protein (NCBI ptt file) MNHWIYFFDLCGTAVFALSGALAAGRHRMDPFGVIVLASVTAVGGGSIRDALIGATPVFWIRDPNYIIVILATVVACLLLVRRPRKMPEYVLPVADALGLALFTVIGAEKALNMGLSGMIAVVMGLITGVGGGIIRDLLCRQIPMVLRTEIYATASIIGGIGYTVSLACGMGEKTALFLAMASALIIRLCAIKWHLSLPAFDLKTKRE Shewanella oneidensis MR-1 MR1 201633 SO2492 acyl-CoA dehydrogenase (1.3.8.-) Specifically important for: Tween 20. Tween 20 hydrolyzes to a mix of C12, C14, and C16 fatty acids; this is probably part of beta oxidation. Similar to fadE from E. coli. The specific SEED annotation as butyryl-CoA dehydrogenase seems questionable but could still be correct oxidoreductase, acyl-CoA dehydrogenase family (NCBI ptt file) MLTIIIIALIAIIALFAVKSLRMQFITQPVFHFFKKVLPPLSDTEREAMEAGDVWWEGELFRGNPNWNTLHSYGKPTLTAEEKDFIDNQVMTALTMIDDFDIVHNRKDLPPELWDYFKKEGFFALIIPKKFGGKAFSAYANSTIVSKLASRSVSAAVTVMVPNSLGPGELLTHYGTEEQKERWLPALAKGDEIPCFALTGPEAGSDAGAIPDVGIVCRGEFNGEEVLGLKLTWNKRYITLAPVATVLGLAFQMRDPDGLLGEKKNLGITCALIPTDHPGVVIGRRHNPLNMAFMNGTTQGDEVFIPLDWIIGGPEFAGRGWRMLVECLSAGRGISLPALATASGHMATKTTTAYSYVRHQFGMAIGQFEGVQEALARIIANTYQLEAARRLTTTGIDLKVKPSVVTAIAKFHMTELGRAVMNDAMDIQSGKGIQLGPKNYLGHPYMSNPISITVEGANILTRSLMIFGQGATRCHPYVLAEMEAAAMENQHDALTRFDSLLMGHMGYATRNAFSALFNALTASRFGNAPVSGETKQYYKDMSRLSSALAFMTDISMLIMGGDLKRKEMLSARMGDVLSQLYLGSATLKLFEDNGRQQDDLPAVRYVMANRLHLAAKALEDVIRNFPNRPVAWLLRALIFPIGNHFNAPSDKMATELVSGMLKPSPARERITFLCPEFEGDVGGIAEVEQAFVAQYACKEIYKKLKKAQRSGELPAKVPNLVLFAKALEQGTISNDEHQTLLHADKLRLAAINVNDFEAL Shewanella oneidensis MR-1 MR1 201882 SO2744 DNA damage response helicase (yejH or radD) Conserved and specific phenotype: important for resisting cisplatin. Also important for resisting ionizing radiation and UV radiation in E. coli (PMID:25425430) helicase (NCBI ptt file) MSVNSSPSVILRDYQQQAVDAAIVHFKKSTDSAVLVLPTGAGKSIVIAELARIARGRVLVLTHVKELVAQNAQKVGLLTTEASIYSAGLNKKSSVGKTVVASIQSAARALGQFNEPFSLVIIDECHRVSLEKTSQYQQLLSHLQQRNPQLKLLGLTATPYRLGTGWIYKRHYHGKVGSPELGIFEQCIFELPIRPLIKQGYLTAPTLFDGLSAQYDFSQIKANKNGEYPEAQVNDLLNHAGRATTAIVKQLIELSHHRQGIIIFAATVRHAEEIVSQLNKEHREQTAIVTAQTPDNERDELIERFKARELKFLVNVAVLTTGFDAPHVDLIAILRPTASVSLFQQMIGRGLRICEGKKDCLVIDYAANGYDLYFPEVGQAKPNSKSVPVQVHCPVCQFANIFWGLTDDDGDIIEHFGRRCQGIVEHHGKKQQCDFRFRAKSCPDCGQENDIAARICQHCQSTLIDPDKRLKQVLNKQHHHLFRCQHMTLMDDAGDLKVQYLDIDGNEFNRHFKLQTPAQWRALYALFIFPHSRTPGLKPKQYKQVSELIADSATFKMPDLLLLKKHKKGWDLLESYFDYQGRYQTENKHI Shewanella oneidensis MR-1 MR1 202008 SO2882 yeaG component of nitrogen-related signalling system (of yeaGH-ycgB) conserved cofitness; yeaG is a protein kinase hypothetical Ser protein kinas (NCBI ptt file) MGIFEHYQKRYEQKLDEEYTLQEFLDICKEDRSAYMSASERLLLAIGEAEIIDTAKNPTLSRIFSNRLISRYPAFKDFFGMEDAIEQIVAYLKHSAQGLEESKQILYLLGPVGGGKSSLAEKLKSLMQKVPIYILSANGVRSPVNDHPFCLFDVDEDGQLLRDEFNIPSRYLKTIMSPWAVKRLHEFGGDISKFRVVKVYPSILDQLAIAKTEPGDENNQDISSLVGKVDIRQLEHYSQDDADAYAYSGALCRANQGIMEFVEMFKAPIKVLHPLLTATQEGNYNGTEGLSALPYSGIILAHSNESEWSTFKNNKNNEAFLDRVYIVKVPYCLRVSEELQIYKKLIQNSELSQAPCAPGTIETLAQFSVLSRIKAPENSSIYSKMRVYDGESLKDTDPKAKSYQEYRDYAGVDEGMNGLSTRFAFKILSRVFNFDHSEIAANPVHLFYVLERQIEQEQFPGDTAERYLEFLKGYLIPKYVEFIGKEIQTAYLESYSEYGQNIFDRYVTYADFWIQDQEYRDPETGQLFDRAALNAELEKIEKPAGISNPKDFRNEIVNFVLRARASHEGHNPLWTSYEKLRTVIEKKMFSNTEDLLPVISFNAKTSNDDQRKHDDFVNRMMEKGYTKKQVRLLSEWYLRVRKSS Shewanella oneidensis MR-1 MR1 202009 SO2883 yeaH component of nitrogen-related signalling system (of yeaGH-ycgB) PFam PF04285.8 (DUF444). conserved cofitness; yeaG is a protein kinase conserved hypothetical protein (NCBI ptt file) MANFIDRRLNAKGKSTVNRQRFINRYKQQIKKAVSDAVTRRSVTDVDKGEKISIPTRDISEPMFHQGKGGVRDRVHPGNDQFTRGDKIDRPQGGSGGGAGKGDASDSGEGNDDFVFEISKDEYLELLFEDLELPNLQKNRLNKLVEYQIYRAGFTNDGVPANINIVRSLRSSLARRIAMSASKKKLLKESEQELAELENIPGTKAELILDLKAQIEELKRKIAKVPFIDTFDLRFNNFSRREVPSSQAVMFCLMDVSGSMDQATKDMAKRFYILLYLFLTRTYKNLEVVYIRHHTQAKEVDEHEFFYSQETGGTIVSSALKLMHEIQQARYPADEWNIYAAQASDGDNWADDSPTCKQLLEQKILPLVRYFSYIEITNRAHQTLWREYESLQQHYDNIAVQHIRQAEDIYPVFRELFKKQAV Shewanella oneidensis MR-1 MR1 202010 SO2884 ycgB component of nitrogen-related signalling system (of yeaGH-ycgB) conserved cofitness; yeaG is a protein kinase conserved hypothetical protein (NCBI ptt file) MGMKESKTRIALSDGPDWSFELLQSYLKEIERVAAIYKLNAYPNQIEIITAEQMMDAYAGIGMPIGYTHWSFGKRFIETEQGYKRGQMGLAYEIVINSNPCIAYLMEENTITMQALVMAHACFGHNSFFKNNYLFKTWTDASSIIDYLVFAKNYISDCEQKYGIEQVESVIDSCHALMNYGVDRYKRPAEISFREEQARQKDREAYLQSQVNDLWRTIPTHQQQQPSTTKRRFPAEPQENILYFIEKNAPLLEPWQREIIRIVRKMAQYFYPQKQTQVMNEGWATFWHYTILNHLYDDGVVSDRFMMEFLQSHTGVVAQPEYNSRYYSGINPYALGFAMFTDIRRICEAPTDEDRIWFPDIAGSNWLDTLHFAMQNFKDESFISQYLSPRVIRQFKLFGIHDDEKRNYLSVSAIHDEQGYQDIRNLLSQQYNLSNIEPNIQVHNVEINGDRSLTLRYVPNKDIPLAGSYNEVLKHLHRLWGFSVSLEQVNADNSVTLLSKCPEQPKAD Shewanella oneidensis MR-1 MR1 202450 SO3342 putative transporter, required for L-alanine utilization PFam PF03458.9 (UPF0126). conserved specific phenotype of UPF0126 conserved hypothetical protein (NCBI ptt file) MQEAQFIGLLWLIGILAEAMTGALAAGRKQMDLFGVVIIGCATAIGGGTLRDMLLGNYPLVWVENVHYLIAIAFASLLTVAIAPVMRYLSKLFLAIDALGLAVFSIVGAQKTLMLGFSPTIAVVMGLVTGVFGGVIRDILCNQVPLIFKKELYAVISLFTAGLYITLNAYQLEEWINLVICLTLGFSLRMLALRYHWSMPTFDYQSSGDQHTH Shewanella oneidensis MR-1 MR1 202564 SO3461 Fatty acid transporter Specific phenotype on Tween-20, which is hydrolyzed extracellularly to fatty acids (typically around 12 carbons). This protein is distantly related (PF03547) to auxin efflux transporters in plants and to the malate permease mleT of Lactobacillus casei (PMID: 23835171) transporter, putative (NCBI ptt file) MTILTPLFAVFGIMLLGTLVQKLRFLPVETDQVLNQYVYYIAFPAVLLIALAQQPIEEILQWRFIAGYSAAMLVIYLMCIGISLLVNPKQHAIAAVRALNATFGNTAFIGIPLLVIIFPEQQSALVAAIASLLSVLMFAVALVSLELTTNKHRQHHAVVIMCLAITKNPIVIGCFIGISISALGITLPSGVALMIQQIGNTSSPCALFAVGMVLAKAMRYQKDSKLFSLTNFVELCLINLFKLILQPALVFFMLKSIGVTGDYLVMGVILSALPTAASVYLLAQRYNTQASTCAQGILFGTIVTFFSLPILEQLVKTYS Shewanella oneidensis MR-1 MR1 202604 SO3503 N-acetyl glucosamine transporter, NagP Specific phenotype on NAG. Also see PMID:16857666 (SEED_correct) glucose/galactose transporter (NCBI ptt file) MTLDKSQQKSSFLPMAIVAALFFILGFATWLNGSLMPYLKQILQLNPFQASLILFSFYIAVTFTALPSAWVIRKVGYKNGMALGMGVMMIAGLLFIPAAKTQVFALFLFAQLVMGAGQTLLQTAVNPYVVRLGPEESAAARVSVMGILNKGAGVIAPLVFSALILDSFKDRIGTTLTQVQIDEMANGLVLPYLGMAVFIGILALAVKKSPLPELSNEDEVADHTDKSQIKAALSHPNLALGVLALFVYVAVEVIAGDTIGTFALSLGIDHYGVMTSYTMVCMVLGYILGILLIPRVISQPTALMISAILGLLLTLGILFGDNNSYAIANLLLVPFGGVALPDTLLLIAFLGLANAIVWPAVWPLALSGMGKLTSTGSALLIMGIAGGAFGPVSWGLMSSATDMGQQGGYMVMLPCYLFILFYAVKGHKMRSWSAK Shewanella oneidensis MR-1 MR1 202608 SO3507 N-acetylglucosamine kinase (EC 2.7.1.59) Specifically important for: N-Acetyl-D-Glucosamine. First step in NAG catabolism; (SEED_correct); see PMID 16857666 conserved hypothetical protein (NCBI ptt file) MGLVQTNDQQLFIGVDGGGSKCRATIYTADGTVLGTGVAGRANPLHGLAQTFESIEASAHQALLDAGMKATDSHLLVAGLGLAGVNVPRLYQDVVNWQHPFAAMYVTTDLHTACIGAHRGADGAVIITGTGSCGYAHVGDASLSIGGHGFALGDKGSGAWLGLKAAEHVLLALDGFATPTALTEMLLSHLGVKDALGIVEHLAGKSSSCYAQLARNVLDCANAGDQVAIAIVQEGADYISEMARKLFMLNPVRFSMIGGLAEPLQAWLGSDVVAKISETLAPPELGAMYYAQQQFNSATV Shewanella oneidensis MR-1 MR1 202842 SO3749 Acetylornithine deacetylase (EC:3.5.1.16) see Deutschbauer et al 2011, PMID:22125499 (auxotroph) hypothetical protein (NCBI ptt file) MVSRSPFESFQWKSDIFNCESTDIDNFYLQLEQEMSRLGMVEKKLGEVGKYSVSLYQSPAAKSGLPSLLICAGFHGEESAGPWGLLHFLSEASVELFERVNLSILPLVNPTGFKRGHRFNKFGENPNRGFEFENGKPKANEGTSVEGKLLLEHAQLLIAASRDGILTCHEDVLSHDAYVYSFEPSQVPGRFSLDLRDTLAGYFPIAVDGEIDGCPVKDGLIFNHFDTSFEACLVRSGARVGACTETPALQNFDQRVLANSAAMTHFLALCAPLCD Shewanella oneidensis MR-1 MR1 202985 SO3900 yqiA-like hydrolase, affects the cell envelope PFam PF05728.8 (UPF0227). conserved phenotypes: important for resisting fusidic acid and carbenicillin conserved hypothetical protein (NCBI ptt file) MLLYIHGFNSSPFSDKAVITARYMAEYHPSLTFHQPQLPNTPKAAMALLQSYVEAAQQANEPLNYIGSSLGGYFASYLAERYGGRAVLVNPAVKPFELFDEFMGPQFNPYTQEHYQVLPEHKREVAEFNTPVIRNPERFLVLLQTGDEVLDYREALHKYHHCQLRIESGGDHSFVGYERYLQTVSQFLHLP Shewanella oneidensis MR-1 MR1 203247 SO4164 predicted FeS cluster maintenance protein PFam PF06155.8 (DUF971). conserved cofitness with mrp/apbC (SO2618) and perhaps bolA conserved hypothetical protein (NCBI ptt file) MTTSTPNVTDLKLKRKSRILEISFDNGEQYQLTCEMLRVYSPSAEVHGHGNPKLVTHKKNVNITRIEPVGNYAVKIVFDDGHDTGLFSWQVLYDLATHQVELWEKYLARLRAEKASREPLIAMNIKYN Phaeobacter inhibens BS107 Phaeo GFF3639 PGA1_262p00430 glucose transporter, periplasmic substrate-binding component specific phenotype on glucose and cofit with other nearby components. This is similar (65% identity) to gxyS (Atu3576) of Agrobacterium tumefaciens, which is involved in the transport of glucose, glucosamine, and xylose (PMCID: PMC4135649). It is not clear if the Phaeobacter system transports xylose, as it is not required for utilizing xylose, but no other xylose transport system was identified either. D-xylose-binding periplasmic protein XylF MKFLSGVSALAFAATASMAFAEDVTVGVSWSNFQEERWKTDEAAIKAALEAKGATYVSADAQSSSAKQLSDIESLIAQGVDALIVLAQDAQAIGPAVQAAADEGIPVVAYDRLIEDGRAFYLTFDNVEVGRMQARAVLEAQPSGNYVMIKGSPTDPNADFLRGGQQEIIQAAIDSGDIKIVGEAYTDGWLPANAQRNMEQILTANDNKVDAVVASNDGTAGGVVAALTAQGMEGIAVSGQDGDHAALNRVAKGTQTVSVWKDARDLGKAAANIAVEMAEGAVMGDVAGGAAWTSPAGTELTARFLEPIPVTADNLSVVVDAGWITKEALCQGVTNGPAPCN Phaeobacter inhibens BS107 Phaeo GFF3640 PGA1_262p00440 glucose transporter, permease component specific phenotype on glucose and cofit with nearby xylF (PGA1_262p00430) and xylG (PGA1_262p00450). This is similar to the gxyB (Atu3575) of Agrobacterium tumefaciens, which is involved in the transport of glucose, glucosamine, and xylose (PMCID: PMC4135649). It is not clear if the Phaeobacter system transports xylose, as it is not required for utilizing xylose, but no other xylose transport system was identified either. xylose transport system permease protein XylH MTETTSQPIPEHSKRGLFQQLELDVRLLGMIGAFVILCIGFNILTDGRFLTPRNIFNLTIQTVSVAIMATGMVFVIVTRHIDLSVGALLATCSAVMAVVQTDVLPDMFGLGLNHPATWIITVAVGLAIGTLIGAFQGWMVGFLTIPAFIVTLGGFLVWRNVAWYLTDGQTIGPLDSTFLVFGGTSGTLGTTLSWVVGIVATLLALAALWNSRRAKQGHGFPVKPAWAEAVIAGSIAASILGFVAILNAYQIPARRLKRMMEAQGETMPEGLVVGYGLPISVLILIATAVVMTIIARRTRLGRYIFATGGNPDAAELSGINTRLLTVKIFALMGFLCALSAVVASARLANHSNDIGTLDELRVIAAAVIGGTALSGGFGTIYGAILGALIMQSLQSGMAMVGVDAPFQNIVVGTVLVAAVWIDILYRKRVGARI Phaeobacter inhibens BS107 Phaeo GFF3641 PGA1_262p00450 glucose transporter, ATPase component Important for utilizing glucose and cofit with the other components. This is similar (68% identity) to gxyA (Atu3574) of Agrobacterium tumefaciens, which is involved in the transport of glucose, glucosamine, and xylose (PMCID: PMC4135649). It is not clear if the Phaeobacter system transports xylose, as it is not required for utilizing xylose, but no other xylose transport system was identified either. sugar ABC transporter, ATP-binding protein MSTAKELRAAGATPLVEMKDISISFGGIKAVDHVSVDLYPGEVVGLLGHNGAGKSTLIKVLSGAYQMDAGEIRVNGDKVEITNPRDARSHNIETIYQTLALADNLDAASNLFLGRELVTPFGLVDDSAMEAECRKIMNRLNPNFQKFSEPVSALSGGQRQSVAIARAVYFNAKILIMDEPTAALGPHETQMVAELIQQLKAQGIGIFLIDHDVNAVMELCDRASVMKNGQLVGTVDIDDVTDDDLLSMIILGKRPGEAAA Phaeobacter inhibens BS107 Phaeo GFF33 PGA1_c00330 Error-prone polymerase for DNA repair (imuB or polY like) Conserved and specific phenotype: important for resisting cisplatin. Related to imuB from Caulobacter. Also similar to PA0670, which is induced by the SOS response, even though it does not seem to have mutant phenotypes related to DNA repair. protein imuB-like protein MAHSDARAFCPDLQTAAADIYRDQQFLLILRRWATRYCPWVGLEGRDGLVLDISGSSHLFGGETGMLNAIRNGLMRVGLSAQIGLADTRGAAWALAHYGEGQAATGDMLPALQHLPVAALRLDEKTTTALIRLGLRKIGDLATTPRAPLARRFGANVLMRLDQALGHQAEEITPLTAPPHYGVRMTLPEPIGLISDVMAGTERLLTQLCAKLKTHEMGARIFVITLRRVDLDQQEVELRLARALRDPQRILPLFEKELAEIDAGFGIDQLRLEATQTEALPTQQMSHVAGDGDDRLEDLITRIGTRIGLENIQRFLPADSHIPERSFIVAPAAYSATASGWTCKTPRPLCLFPPEPIPGSGPYPPNHFRWRRVSLTTGHTIGPERITPEWWLEDDNWRSGMRDYWRVETTQGRRLWLFYTPQNPGWFVQGEFA Phaeobacter inhibens BS107 Phaeo GFF90 PGA1_c00920 putative transporter, required for glycine utilization PFam PF03458.9 (UPF0126). conserved specific phenotype of UPF0126 Predicted membrane protein MTILTLLDYASVLVFAASGALVASRAQLDIVGFAFVACLTAVGGGTVRDLLLDRHPVFWIGDSTNILLAAAAAVLVFFTAHLVESRLRWIVWLDSFALAVAVSAGTGAAILTGQPPVIVVLMGMATGTLGGLMRDVVCNEVPLVLKQGELYISCAMAGAITAVVSIAFGLPNRWALVACAVVCWVLRAGSITFGWHLPVYRSRPPRS Phaeobacter inhibens BS107 Phaeo GFF357 PGA1_c03680 (3S)-malyl-CoA thioesterase [EC:3.1.2.30] Specifically important for: L-Threonine; Potassium acetate. This is part of the ethylmalonyl-CoA cycle for acetate assimilation, and hence is important on threonine (cleaved to glycine and acetate via the PGA1_c34330 or kbl) and acetate (where it has a milder phenotype). The annotation of sit:TM1040_3520 has been updated to (3S)-malyl-CoA thioesterase [EC:3.1.2.30]. 69% similar to MCTE_RHOS4 (consistent with the KEGG annotation). SEED suggests that this is the malyl-CoA/methylmalyl-CoA lyase but that activity is probably provided by PGA1_c30490. (KEGG_correct) putative citrate lyase subunit beta MDPRIRPYRSVLYIPGSKLRALEKARSLPVDAIIFDLEDAVSAEEKVNARQTLEEALRAGGYGARMKIVRINGLDTVWGRADAAAAARMDCDAILLPKVSSPEDLDALAVITGDKPLWAMMETPRGMLNAAAIAAHPLLQGMVMGTNDLAKELQTRFRPDRLPLMAGLGQCLLAAKAKGIIIVDGVYNAFKDAEGLEAECDQGRDMGFDGKTLIHPAQVDVANSAFAPSEDEIDLARRQIAAFDAAEAEGQGVAVVDGKIVENLHVATAREILAKADAIAAVSA Phaeobacter inhibens BS107 Phaeo GFF590 PGA1_c06040 DNA damage response helicase, ligase-associated Conserved and specific phenotype: important for resisting cisplatin. Related to Lhr, which is either a DNA:DNA or DNA:RNA helicase, but lacks the long C-terminal extension that might have a regulatory role (see putative winged helix domain in E. coli lhr). This is also related to the archael protein saci_1500, which has also been linked to DNA damage response, as a mutant is sensitive to UV (PMID: 26148716) putative DEAD/DEAH box helicase MSRLPDVITDWFSTRGWTIHPHQQEMLARVDDPATLLIAPTGGGKTMAGFLPTLADLATGDHQGLHTLYVSPLKALAADIKRNLRTPVEDMGLPIRIDDRTGDTPASRKRSQRADPPHILLTTPESLALLTSYEDAPRMFAGLKRVVLDEIHALAESKRGDQLMLALTRLQAICPDMRRVGLSATVDDPAAIAQYLARHPAPCDIVLADPGPAPDIRMLHTDAAPPWAGGGAAHAIPAVLEQIKAHRTTLIFHNTRAQAEIFFRNLWLANDDALPIGIHHGSLDRVQRDRVEAAMVRGELRAVVCTGSLDLGIDWGDVDLVIQIGAPKNVKRLVQRIGRANHRYNAPSKALLVPANRFEVVECRAALEAVEAGTLDGSPRSPGPRDVLCQHILIRACAGPFAADDLFAEVTGAGAYASLTRAEFDACLDFCATGGYALRVYDQWQRLLQRPDGLWQLRDPRAARRIRMNIGTIQDADLLKVRLKRSRGGKPLGEIEEAFAATLTPGDTFLIGGQVVRYESLREMTVEVSRNASKTPKVAVFSGTKFATSTQLSTRILDILQRDSWPDLPSHTADWLALQRQVSEMPRRGQLLLESFPFRGREYLCVYGFAGRNAMQTLGLLLTKRMEELSLDPLGFVATDYATLIWGLSPVADPAPLFDPDKLRAGLDGWLADNAVMKRSFRAVANIAGLIERNTPGQRKSGRQATFSSDILYDTLRKYDPDHLLLDITRQEALGGLVDFGRIEEMLTRINGNITLNRLSQISPLAAPLLLEVGKVPVKGAAQEKLLQRETEDLMRLAGLAALEAPAAPEL Phaeobacter inhibens BS107 Phaeo GFF707 PGA1_c07220 5-keto-2-deoxy-D-gluconate-6 phosphate aldolase (EC 4.1.2.29) Specifically important for: m-Inositol. Part of inositol catabolism via 5-deoxyglucuronate (SEED_correct) putative 6-phospho-5-dehydro-2-deoxy-D-gluconate aldolase MTIATLAEVLQPALRDGYAVAGLVTLGWEDMRAYVAAAEAEGVPVILQAGPSCRVHTPLPILGKMFRHLAEGASVPVVAHLDHGYTAEDCRIAIDSGFTSVMFDGSRNALDDNIAETAAIAGMAHAAGVSCEGEIGFVGYSGGEGSAGTDPEEARRFAQETGVDAMAISVGNVHLQQDKEGGLDIDRIRAIEAITEVPLVIHGGSGVPVAQRRMLARESRICKFNIGTELRMVFGAAMRDAVNSDPDRFDRVSILSETHDPVVAAARSVLRAFKGETQC Phaeobacter inhibens BS107 Phaeo GFF715 PGA1_c07300 Inositol transport system sugar-binding protein Specific phenotype on inositol and cofit with other nearby components (SEED_correct) ABC-type sugar transport system, periplasmic component MTSIFKTFMLATTVAAAPMMLATTASAEGEKYILVSHAPDSDSWWNTIKNGIALAGEQMNVEVEYRNPPTGDLADMARIIEQAAASGPNGIITTLSDYDVLSGPIKAAVDSGVDVIIMNSGTPDQAREVGALMYVGQPEYDAGHAAGMRAKADGVGSFLCVNHYISSPSSTERCQGFADGLGVDLGDQMIDSGQDPAEIKNRVLAYLNTNPETDAILTLGPTSADPTLLALDENGMAGDIYFGTFDLGEEIVKGLKSGVINWGIDQQPFLQAYLPVVVLTNYHRYGVLPGNNINSGPGFVTKDGLEKVEEFAGEYR Phaeobacter inhibens BS107 Phaeo GFF716 PGA1_c07310 Inositol transport system permease protein Specific phenotype on inositol and cofit with other nearby components (SEED_correct) binding protein dependent transport system permease MSDAPTQFAEDERIKTRSKFREAMIRPELGGIIGTITVFAMFLIFAGDSGMFNSQGVMNWSQISAQFMIIAVGACLLMIAGEFDLSVGSMIGFAGMLIAIFSVTLGWPVWLAILVTFAIATAIGALNGFIVVRTGLPSFIVTLAFLFILRGFAIYLPQTIERKTIIGGVADAAEGDWLAALFGGKILTGLFQWFGDNGWIAVFERGTRKGQPVVEGLPMLIVWAILLVIIGHVILTKTRFGNWIFAAGGDAEAARNSGVPVNRVKILMFMFTAFCATVFATCQVMEFGGAGSDRGLLKEFEAIIAVVIGGALLTGGYGSVLGAALGALIFGVVQQGLFFAGVESSLFRVFLGLILLFAVILNTYIRRVITGER Phaeobacter inhibens BS107 Phaeo GFF717 PGA1_c07320 Inositol transport system ATP-binding protein Specific phenotype on inositol and cofit with other nearby components (SEED_correct) sugar ABC transporter, ATP-binding protein MSMSQPLIRMQGIEKHFGSVIALAGVSVDVFPGECHCLLGDNGAGKSTFIKTMSGVHKPTKGDILFEGQPLHFADPRDAIAAGIATVHQHLAMIPLMSVSRNFFMGNEPIRKIGPLKLFDHDYANRITMEEMRKMGINLRGPDQAVGTLSGGERQTVAIARAVHFGAKVLILDEPTSALGVRQTANVLATIDKVRKQGVAVVFITHNVRHALAVGDRFTVLNRGKTLGTAQRGDISAEELQDMMAGGQELATLEGSLGGTV Phaeobacter inhibens BS107 Phaeo GFF883 PGA1_c08960 DNA repair endonuclease mmcB (DUF1052) Conserved and specific phenotype: important for resisting cisplatin. Also see PMID:26162909 which suggests a role for a homologous protein from Caulobacter in creating substrates for translesion synthesis Uncharacterized protein conserved in bacteria MMQELTPGQRLARGVARHMAALGFVTVEEFVPARGLRVDVMALGPKGELWVVECKSSRADFQSDSKWQGYLEWCDRYFWAVDLAFPNELLPDDSGLIIADDYDAEIIRMAPEQKLPAARRKKLIQKFAMDAASRLHRLRDPQPGTAGSWGI Phaeobacter inhibens BS107 Phaeo GFF1248 PGA1_c12640 D-lactate transporter, ATP-binding component Specific phenotype on D-lactate and D,L-lactate and cofit with other components putative high-affinity branched-chain amino acid transport ATP-binding protein MGILEVKNVGKRFGGLQALSDVNLSVRENTVHAIIGPNGAGKSTLLNCLVGKLIPDTGSVMFDGKSVLGRAPYEINQMGISRVFQTPEIFGDLSVLENMMIPCFAKRDGAFEMNAISAVSGQRDILEKAEHMLEEMNMADKRHMNAASMSRGDKRRLEIGMCLSQEPRLLLLDEPTAGMARADTNNTIDLLKQIKSERDITIAIIEHDMHVVFSLADRITVLAQGTPLVEDDPQNIKGNPKVREAYLGESA Phaeobacter inhibens BS107 Phaeo GFF1249 PGA1_c12650 D-lactate transporter, permease component 1 Specific phenotype on D-lactate and D,L-lactate and cofit with other components putative high-affinity branched-chain amino acid transport system permease protein MFTLNKKDKTLLLVVAILTLFAPFILNPFPTGSALAQFNAGYPDLMQRFVIFGIFAIGFNILFGLTGYLSFGHAAFLGVGSYSAVWMFKLLSMNVVPAIVLSVIVAGLFALVIGYVSLRRSGIYFSILTLAFAQMSFNLAYSVLTPITNGETGLQLTLDDPRVLGVSATADGSIPVTSLFGLEMRSTFEMVVGPWAFQFNAGYYLCALILLAAFYLSIRIFRSPFGLMLKAVKSNQQRMNYTGLNTRPYTLAAFVISGMYAGLAGGLMASMDPLAGAERMQWTASGEVVLMTILGGAGTLIGPVLGAGFIKYFENIFSKINDNVLHSWFSFMPDGIEDAMVFIVHPFIGKGWHLTLGILFMLVVIFLPGGLVEGGQKLRGWIQGRKAKKDGPSGKTEPAE Phaeobacter inhibens BS107 Phaeo GFF1250 PGA1_c12660 D-lactate transporter, permease component 2 Specific phenotype on D-lactate and D,L-lactate and cofit with other components putative high-affinity branched-chain amino acid transport system permease protein MDAILLQILNGLDKGSAYALIALGLTLIFGTLGVVNFAHGALFMIGAFCAVTVQRVLSLSFETVDETQKDFLGNPLKVKTPYVESWFGPEVGGAIIDWAVPLAILFAIPIMIGVGYVMERGLIKHFYKRPHADQILVTFGLAIVLQEVVKYFYGANPIQTPAPDALNGVVNLGSIIGMDIVYPVWRVVYFFFAVVIIGGIFSFLQFTTFGMVVRAGMADRETVGLLGINIDRRFTIMFGIAAAVAGLAGVMYTPINSPNYHMGMDFLVLSFVVVVVGGMGSLPGAVLAGFLLGVLESFASMNEIKSLIPGIDQIIIYVVAIIILLTRPRGLMGRKGVMED Phaeobacter inhibens BS107 Phaeo GFF1251 PGA1_c12670 D-lactate transporter, substrate binding component Cofit with the other components and important for growth in various D-lactate and D,L-lactate media ABC-type branched-chain amino acid transport systems, periplasmic component MSKTDVSRRGVLKTGAIAGAGVALPTIFTASSAAAFTNEPTGSTVTLGFNVPQTGPYADEGADELRAYQLAVEHLNGGGDGGMMNTFSSKALQGNGIMGKEVKFVTGDTQTKSDAARASAKSMIEKDGAVMITGGSSSGVAIAVQGLCQEAGVIFMAGLTHSNDTTGKDKKANGFRHFFNGYMSGAALAPVLKNLYGTDRNAYHLTADYTWGWTQEESIAAATEALGWNTVNKVRTPLAATDFSSYIAPVLNSGADVLVLNHYGGNMVNSLTNAVQFGLREKVVNGKNFEIVVPLYSRLMAKGAGANVKGIHGSTNWHWSLQDEGSQAFVRSFGSKYGFPPSQAAHTVYCQTLLYADAVERAGSFNPCAVVEALEGFEFDGLGNGKTLYRAEDHQCFKDVLVVRGKENPTSEFDLLEVVEVTPAEQVTYAPDHPMFAGGALGTCNSGA Phaeobacter inhibens BS107 Phaeo GFF1301 PGA1_c13170 Sorbitol dehydrogenase (EC 1.1.1.14) Specifically important for: D-Sorbitol. First step is sorbitol catabolism; (SEED_correct) sorbitol dehydrogenase PolS MKRLSGKRALITGAARGIGAAFAEAYANEGARVVIADIDTARAEATAAQIGAAAIAVELDVTDQASIDRALSRTVECFGGLDILINNAAVFTAAPLVEVTREAYQRTFDINVSGTLFMMQAAAQQMITQGTGGKIINMASQAGRRGEPLVSVYCATKAAVISLTQSAGLNLISHGINVNAIAPGVVDGEHWDGVDAFFAKYEGKAPGQKKAEVAQSVPYGRMGTAADLTGMAVFLASEDADYVVAQTYNVDGGQWMS Phaeobacter inhibens BS107 Phaeo GFF1302 PGA1_c13180 ABC transporter for D-Sorbitol, ATPase component Specific phenotype on D-Sorbitol. ABC transporter, ATP binding protein MGQIKLESVTKNFGPVEVIPPLDLTIEDGEFTVFVGPSGCGKSTLLRLIAGLEDITSGTIRIDGEDATNIPPAKRGLAMVFQSYALYPHMSVRKNIAFPMKMAGIPADEQKRRIDNAAAALNLTDYLDRRPGQLSGGQRQRVAIGRAIVREPAAFLFDEPLSNLDAALRVGMRLEISELHKRLATTMIYVTHDQVEAMTMADKIVVLQAGVIEQVGSPMELYRAPRNVFVAGFIGSPKMNLLTGPQAAQHNAATIGIRPEHLSISETEGMWAGTIGVSEHLGSDTFFHVQCDAFDDPLTVRASGELDLGYGERVFLTPDMTHLHRFGSDGLRIE Phaeobacter inhibens BS107 Phaeo GFF1305 PGA1_c13210 ABC transporter for D-Sorbitol, periplasmic substrate-binding component Specific phenotype on D-Sorbitol. extracellular solute-binding protein MYLKSALRAATALTVFASTAAFADTITIATVNNGDMIRMQGLTEDFTAKTGHEVEWVTLEENVLRQRVTTDISAKGGQFDIMTIGMYETPIWGKNGWLVPLNDLPADYDVDDILPAMRGGLSHDGTLFAAPFYGESSMIMYRTDLMEKAGLEMPAAPTWDFVADAARQMTDKDNETYGICLRGKAGWGENAAFITAMSNSFGARWFDENWAPQFDSEAWSNTLNFYINLLNDAGPPGASNNGFNENLSLFQQGKCGMWIDATVAASFVTNPNDSTVADKVGFALAPDTGLGKRSNWLWAWALAIPAGTQKEAAAKEFIQWATSKDYIELVAENEGWANVPPGARISLYENANYKDIPFAKMTLESILSADPNNPTVDPVPYVGIQFAAIPEFAGIATQVGQEFSAALAGQQTAEEALAKAQALTADEMEAAGY Phaeobacter inhibens BS107 Phaeo GFF1318 PGA1_c13340 Accessory protein for co(II)balamin reduction (DUF1638) (EC:2.1.1.13) Apparently required for the reactivation of vitamin B12 (auxotroph) Protein of unknown function (DUF1638). MARKGRAARLTERAAFQPPTGRSLEETSLTERGLAAPEKKTGRILLIACGALAREILDIKEANGMGHIDLTCLPAKLHLYPDQIVDAVGGAVAKHKAVYDKIYIVYADCGTGGALERKCADLGVEMIAGPHCYSFFEGNDRFAAQSEAGEITAFYLTDFLVKQFDAFVWRPMGLDKHPELRDMVFGNYTKLIYQSQISDPELVKKARNCADRMGLAFEHRHTGYGELQTALLQWGDTATRD Phaeobacter inhibens BS107 Phaeo GFF1319 PGA1_c13350 Methionine synthase component, B12 binding and B12-binding cap domains (EC:2.1.1.13) PGA1_c13350 is annotated as putative dimethylamine corrinoid protein. Its auxotrophic phenotype is rescued by added methionine. Compared to MetH from E. cli, it has the B12-binding cap (PF02607) and B12 binding (PF02310) domains but lacks methyltransferase (PF02574) or pterin-binding (PF00809) domains or the B12 activation domain (PF02965). (auxotroph) putative dimethylamine corrinoid protein MSEDADDIILADLNDEDLVQQMFDDLYDGLKEEIEESVNILLERGWAPYKVLTEALVGGMTIVGADFRDGILFVPEVLLAANAMKGGMAILKPLLAETGAPRMGSMVIGTVKGDIHDIGKNLVSMMMEGAGFEVVDIGINNPVENYLEALEEHQPDILGMSALLTTTMPYMKVVIDTMIEQGKRDDYIVLVGGAPLNEEFGKAIGADGYCRDAAVAVEMAKDFVARKHNQMSA Phaeobacter inhibens BS107 Phaeo GFF1321 PGA1_c13370 Methionine synthase component, methyltransferase domain (EC:2.1.1.13) PGA1_c13370 has a methyltransferase domain and its auxotrophic phenotype is rescued by added methionine. Also, S. Thole et al. (ISME J. 2012) proposed that PGA1_c13360, which contains a radical SAM domain (PF04055), might be involved in B12 activation, but it lacks phenotypes in our data. (auxotroph) putative homocysteine S-methyltransferase MTNTFTTLLETKDALLADGATGTNLFNMGLQSGDAPELWNVDEPKKITALYQGAVDAGSDLFLTNTFGGTAARLKLHDAHRRVRELNVAGAELGRNVADRSERKIAVAGSVGPTGEIMQPVGELSHALAVEMFHEQAEALKEGGVDVLWLETISAPEEYRAAAEAFKLADMPWCGTMSFDTAGRTMMGVTSADMAQLVEEFDPAPLAFGANCGTGASDILRTVLGFAAQGTTRPIISKGNAGIPKYVDGHIHYDGTPTLMGEYAAMARDCGAKIIGGCCGTMPDHLRAMREALDTRPRGEQLTLERIVEVLGPFTSDSDGTGEDTAPDRRSRRGRRRG Phaeobacter inhibens BS107 Phaeo GFF1501 PGA1_c15200 ATP-dependent reduction of co(II)balamin (RamA-like) (EC:2.1.1.13) Apparently required for the reactivation of vitamin B12. Distantly related to RamA (see PMID: 19043046) (auxotroph) Uncharacterized metal-binding protein MANDPAPEISTETATDPASHPLVVFTPSGKRGRFPVGTPVLTAARQLGVDLDSVCGGRGICSKCQITPSYGEFSKHGVTVADDALTEWNKVEQRYKDKRGLIDGRRLGCQAQVQGDVVIDVPPESQVHRQVVRKRAEARDITMNPSTRLYYVEVEEPDMHKPTGDMERLIEALDAQWDLKGVKTDLHILSVLQPALRKGGWKVTVAVHLGDENHPPKIMHIWPGFYEGSIYGLAVDLGSTTIAAHLCDLKTGDVVASSGIMNPQIRFGEDLMSRVSYSMMNKGGDQEMTRAVREGMNALFTQIAAEAEIDKALIVDAVFVCNPVMHHLFLGIDPFELGQAPFALATSNALALRAVELDLNIHPAARVYLLPCIAGHVGADAAAVALSEAPDKSEDLVLVVDVGTNAEILLGNKDKVLACSSPTGPAFEGAQISSGQRAAPGAIERVEINPETKEPRFRVIGSDIWSDEDGFAAAVATTGITGICGSGIIEAIAEMRMAGLLDASGLIGSAEQTGTTRCIQDGRTNAYLLWDGSVEGGPTITVTNPDIRAIQMAKAALYSGARLLMDKFGIDTVDRVVLAGAFGAHISAKHAMVLGMIPDCPLDKVTSAGNAAGTGARIALLNTEARSEIEATVQQIEKIETAVEPRFQEHFVNASAIPNSAEPFPILSSIVTLPEANFNTGGGDGNEVGGRRRRRRRG Phaeobacter inhibens BS107 Phaeo GFF1582 PGA1_c16040 Methionine synthase component, pterin-binding domain (EC:2.1.1.13) Its auxotrophic phenotype is rescued by methionine. PGA1_c16040 has the pterin-binding domain (auxotroph) pterin binding domain-containing protein MTRTVVESKTKTAILGFDEPFCVIGERINPTGRKKLAAELEAGDFSTVEKDALAQVMAGANILDINAGVVYNSNPNPNETEPPLMTKIVELVQGLTDTPLCIDSSVPGALEAGLQAAEGRPLLNSVTGEEERLEHVLPLVKKYNVPVVAISNDDTGISEDPDVRFAVAKKIVERAADFGIPAHDIVVDPLVMPIGAMATAGQQVFALVRRLREELGVNTTCGASNVSFGLPNRHGINNAFLPMAMGAGMTSAIMNPVALPITQKKIAEKKAEVEAAGIILPEGMEDEAFVQMFGLGSTKPRAGKEMEAIRAANLLTNNDPHGGEWIKANKEPAKEGEEGRGRGGRAGGRRRRA Phaeobacter inhibens BS107 Phaeo GFF2068 PGA1_c21010 component of stress sensing system, with PGA1_c21020 (DUF2063) PFam PF05114.9 (DUF692). Conserved cofitness and pleiotropic phenotypes Uncharacterized protein conserved in bacteria MLDAAPFLPAATGVGYKPQHFADILADAGPVKWLEIHAENYMGDGGRPIAQLRHLCEQFAISVHGVGLSIGGEGPLDADHLARLKHLVGWLNPASFSEHLAWSTHDSHFYNDLLPLPYTDATLARVCDHINQVQDTIGRRMLLENPSSYLAFAESSWSEPEFLTEITRRTGCGLLLDVNNVFVSATNLDFSPQGYIDAFALDQVGEIHLGGHDEDEDDHGKPLLIDSHGAEVVDPVWALLDYTLAKSGPKPVLVEWDTDVPDWPVLAAEATRAATALERVSA Phaeobacter inhibens BS107 Phaeo GFF2069 PGA1_c21020 component of stress sensing system with PGA1_c21010 (DUF692) PFam PF09836.5 (DUF2063). Conserved cofitness and pleiotropic phenotypes Uncharacterized protein conserved in bacteria (DUF2063). MTVSQTEFTHAMMDAGQPVPEGLLDATGQPAGRRFSVYRNNIAVSLSEAMHSAFPLIGKLLGEQNLDGLAGMYLRAHPPSSPLMMHYGAEFPAFLARMEQLKHLGYLPDAARLDLALRRAYHAGDATAVAPARLAALPPEALMATRLTLAPAVALLRSPWPIYDIWRFNTEKNAPKPRHMAQDVLITRPEFDPIIQELPPGGADWITALTSGATLEEALTAVQANHPDFDLSHTLALLLQGGAIIDLDRKG Phaeobacter inhibens BS107 Phaeo GFF2154 PGA1_c21860 Histidinol-phosphatase [alternative form] (EC 3.1.3.15) Annotated as this by multiple resources. (essential) (SEED_correct) putative histidinol-phosphate phosphatase HisN MADAARQAILPYFRSAGLQSDNKLDEGFDPVTIADRAAEQAMRSVLSELRPEDSILGEEFGETHGQSGRTWVLDPIDGTRGFISGTPTWGVLIALGDADGPFLGIVDQPYIGERFIGTPEGASLTGPLGHSALVTRATDSLSEATLFTTFPEVGTEAERAAFQRVSAQVRLTRYGMDCYAYALLAAGQCDLVIEAGLNAYDIQAPIAVIQAAGGVVTNWQGEPAHEGGQVLAAATAELHAAALALIQQTA Phaeobacter inhibens BS107 Phaeo GFF2492 PGA1_c25240 histidinol-phosphate aminotransferase [EC:2.6.1.9] Annotated as this by multiple resources. (essential) (KEGG_correct) histidinol-phosphate aminotransferase HisC MTHIAPQPGILDIALYEGGAAHVKGMSNVTKLSSNENPLGPSPKAIEAMQAAVSEMHRYPSSDHSGLRQAIGEVYGLPMEQIICGAGSDEIITFLCQAYAGPGDEVLFTEHGFAMYRISALAAGATPVEVAERDRVTDVDALLAGCTERTRLVFIANPNNPTGTMIGMADLARLADGLPKGALLVLDGAYAEYVEGYDAGAALVANRDNVVMTRTFSKIYGLGGARVGWGYAPKPIIDVLNRVRGPFNLSSTALAGAEAAVRDTDYTEHCRKENAKWRTWLAEALAELGVPSDTSCANFILARFASPEEAGACDAFLQSRGLIVRRVTGYKLPAALRITVGDETACNALVAAMKVFKDGPA Phaeobacter inhibens BS107 Phaeo GFF2748 PGA1_c27910 N-acetylglucosamine kinase (EC 2.7.1.59) Specifically important for: D-Glucose; N-Acetyl-D-Glucosamine. This is the first step in NAG catabolism. The next step is expected to be N-acetylglucosamine-6-phosphate deacetylase (PGA1_c27880, no data). The phenotype on D-glucose is consistent across replicates and is not explained. It does not seem to be due to polar effects. There is a glucokinase that is important for glucose utilization (PGA1_c05420 ) so we don't expect that this is glucokinase. (SEED_correct) putative ATPase, BadF/BadG/BcrA/BcrD type MTDSRFPYLIAVDGGGTSCRFALLKSGATPPQQLVVTGGSANVYTAPDQAVETLSAGLADLQRQSGLTDEVFHQIPVYAGLAGVIDGESAARVAEALPQAHVRVEDDRMPAVVGALGEDTASLIGVGTGSFLGRQVAGQVTLIGGHGTVLGDEASGGWLGRRALQLTLQAAEGIEPMTPLLRSCLRDFSNETAKIVRFAQTARPVAFGAYAPRVAKAAVEGDAAGRRLMAEGAEYLCNGLQALGRRPEEPVYHIGGVAAQYAAYLPADVADYLRGAEGSPLDGALELARRFAREIAQEVV Phaeobacter inhibens BS107 Phaeo GFF2750 PGA1_c27930 N-Acetyl-D-glucosamine ABC transport system, periplasmic substrate-binding component Specific phenotype on N-Acetyl-D-Glucosamine. (SEED_correct) putative sugar ABC transporter, periplasmic binding protein MTRKLFTLALLGSTMIGGAAAAEDVTLTIESWRNDDLALWQDKIIPAFEAANPGIKLKFTPSAPAEYNAVLNSKLDAGSAGDLITCRPFDASLGLYDKGQLADLSDLDAMGSFSNVAKSAWQTDDGSATFCVPIASVIHGFIYNKDAFAELGVNVPETEDEFFAALEKIKEDGNYVPLAMGTNDQWEAATMGYNNIGPNYWKGEEGRLALIAGEQKLTDDQWVAPYETLSKWGAYMGDGYEAQTYPDSQNIFTLGRAAIYPAGSWEISGFNTQADFAMGAFKPPVKAAGDTCYISDHTDIAVGLNAASPNAEAAKTFLNWVGSAEFASIYANALPGFFSLSNHEVAMEDPLAQEFVSWRGECESTIRSTYQILSRGTPNLENETWGASVAAIKGTKAPADLGAELQEGLASWYEPQK Phaeobacter inhibens BS107 Phaeo GFF2751 PGA1_c27940 N-Acetyl-D-glucosamine ABC transport system, permease component 1 Specific phenotypes on N-Acetyl-D-Glucosamine. (SEED_correct) ABC transporter permease protein MQNTPHKPRRRWHIAVFLAPAVLVYTAIMIFPLFNTLRLALYSESDQIRQFVGLANFETLFGNPNWSEQFWNALGNNFWFFFVHMLVQNPIGVALAAILSHPRLRFAALYRTAIFVPTILSFVIVGFAWKLILSPIWGITPDLLDAIGLKWLFAPWLGKEDYALTTLALISVWQFVGIPMMLIYAALLSIPEEVIEAGEVDGITGMSAFWKIKLPLILPSIGIISILTFVGNFNAFDLIYTTQGALAGPDFSTDILGTFMYRTFFGFQLQLGDPHMGSAIATAMFAIILIGVCIYLFGIQTRLRRYQF Phaeobacter inhibens BS107 Phaeo GFF2752 PGA1_c27950 N-Acetyl-D-glucosamine ABC transport system, permease component 2 Specific phenotypes on N-Acetyl-D-Glucosamine. (SEED_correct) ABC transporter permease protein MMHKSRSNPFNSILAHGALITYTLIALFPVFVILVNSFKTRKAIFRDPLGLPTSDTFSLVGYQTVLKQGDFFLYFQNSMIVTVVSLALVLLFGAMAAFALAEYRFKGNMLLGLYLALGIMIPIRIGTVAILELMVDTGLVNTLTALILVYTAQGLPLAVFILSEFMKQVSDDLKNAGRIDGLSEYTIFFRLVLPLVRPAMATVAVFNMIPIWNDLWFPLILAPAEETKTLTLGSQVFIGQFVTDWNAVLSALSMAILPVMVLYVIFSRQLIRGITSGAVK Phaeobacter inhibens BS107 Phaeo GFF2754 PGA1_c27970 N-Acetyl-D-glucosamine ABC transport system, ATPase component Specific phenotype on N-Acetyl-D-Glucosamine. (SEED_correct) ATP-binding transport protein SmoK MTALQLTNVCKSFGPVEVLKDINLTVEDGEFVVFVGPSGCGKSTLLRVISGLEDATAGEISIGGQTVTTTPPAKRGIAMVFQSYALYPHLSVRENMALALKQERQPKEEIAARVAEASRMLSLEDYLDRRPSELSGGQRQRVAIGRAVVREPKLFLFDEPLSNLDAALRMNTRLEIARLHRQLSASMIYVTHDQIEAMTLADKIVVLRDGRIEQVGTPMELYNNPANRFVAEFIGAPAMNFVPAQRLGGNPGQFIGIRPEYARISPVGPLAGEVIHVEKLGGDTNILVDMGEDLTFTARLFGQHDTNVGETLQFDFDPANCLSFDEAGQRI Phaeobacter inhibens BS107 Phaeo GFF2895 PGA1_c29420 aromatic-amino-acid transaminase [EC:2.6.1.57] Annotated as this by multiple resources. (essential) (KEGG_correct) aromatic-amino-acid aminotransferase TyrB MFETLKPQPADKILALMQMYRDDPRDSKIDLGVGVYKNAEGVTPVMRAIKAAEHKLWEEQTSKSYVGLAGDPAYSDAMIKLILSDSVARANVAAAATPGGTGAVRQAFELIKMANPGARVFVSNPTWPNHISILNYLNIETVAYRYFDRETCGVDFDGMIADLKTANKGDVVLLHGCCHNPTGANLNMVQWQEVVAILNERGLIPMIDIAYQGFGDGLEEDAQGVRYVAANTPECLIAASCSKNFGIYRERTGLLMAVSQDSGAQALNQGTLAFLNRQNYSFPPDHGARLVSMILNDDALRADWAAELEETRLGMLALRQQLADELQRLTGSDRFGFLAQHRGMFSLLGTTPEMVEKMRAESGIYMVGDSRMNIAGLNTQTVPILAQAIVDAGV Dechlorosoma suillum PS PS Dsui_0512 Dsui_0512 Methylmalonyl-CoA epimerase (EC 5.1.99.1) Important on proprionate; this makes sense because of the utilization of the (S)-methylmalonyl-CoA formed by propionyl-CoA carboxylase (SEED_correct) hypothetical protein MSQRPFKVLGIQQIAIGGPSKDKLKTLWVDMLGLEVTGNFVSERENVDEDICAMGKGPFKVEVDLMQPLDPEKKPAVHTTPLNHVGLWIDDLPKAVEWLTANGVRFAPGGIRKGAAGFDICFLHPKGNEESPIGGEGVLIELVQAPAEVVDAFAKLAG Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_1109 2-ketoglutaric semialdehyde dehydrogenase (EC 1.2.1.26) Specifically important for: D-Galacturonic Acid monohydrate. ketoglutarate semialdehyde is an intermedate in the oxidation of galacturonate (SEED_correct) 2-ketoglutaric semialdehyde dehydrogenase (EC 1.2.1.26) VADAKRYDNYINGEWVSGADYSANINPSELTDTIGDYAKADLAQVHAAIDAARAAFPAWSTSGIQARHDSLDKVGTEILARREELGTLLAREEGKTLPEAIGEVTRAGNIFKFFAGECLRLSGDYLPSVRPGVNVEVTREALGVVGLITPWNFPIAIPAWKIAPALAYGNCVVLKPADLVPGCAWALAEIISRAGFPAGVFNLVMGSGRVVGDALVQSPKVDGISFTGSVGVGRQIAVSCVSRQAKVQLEMGGKNPQIILDDADLKQAVELSVQSAFYSTGQRCTASSRFIVTAGIHDKFVEAMAERMKSIKVGHALKTGTDIGPVVSQAQLEQDLKYIDIGQSEGARLVSGGGLVACDTEGYFLAPTLFADSTAAMRISREEIFGPVANIVRVADYEAALAMANDTEFGLSAGIATTSLKYANHFKRHSQAGMVMVNLPTAGVDYHVPFGGRKGSSYGSREQGRYAQEFYTVVKTSYIGS Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_1554 predicted FeS cluster maintenance protein PFam PF06155.8 (DUF971). Conserved cofitness with mrp/apbC (Pf1N1B4_731) FIG028220: hypothetical protein co-occurring with HEAT repeat protein MTQLPTDIKLHKASKTLSLKYASGEEYHLPAEFLRVHSPSAEVQGHGKPILQFGKIGVGLSKVEPAGQYALKLTFDDGHDSGLFTWEYLYQLAVRQEDLWNDYLAELKAAGKTRDPNESVVKLML Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_2254 Gamma-glutamyl-putrescine synthetase (EC 6.3.1.11) Specifically important for: Putrescine Dihydrochloride. This is the first step in putrescine catabolism. Some close homologs are annotated as this by SEED, so not sure why it was missed. Also, another gene is annotated as this activity (Pf1N1B4_4354) but has no phenotype. Gamma-glutamyl-putrescine synthetase (EC 6.3.1.11) MNGVVRGKRIERTSLHKVYEKGINLPASLFALDINGSTVESTGLGLDIGDADRICYPIPDTLCNEPWQKRPTAQLLMTMHELEGDPFFADPREVLRQVVAKFDEMGLTICAAFELEFYLIDQENVNGRPQPPRSPISGKRPHSTQVYLIDDLDEYVDCLQDILEGAKEQGIPADAIVKESAPAQFEVNLHHVADPIKACDYAVLLKRLIKNIAYDHEMDTTFMAKPYPGQAGNGLHVHISILDKDGKNIFASEDPEQNAALRHAIGGVLETLPAQMAFLCPNVNSYRRFGAQFYVPNSPCWGLDNRTVAIRVPTGSSDAVRIEHRVAGADANPYLLMASVLAGVHHGLTNKIEPGAPVEGNSYEQNEQSLPNNLRDALRELDDSEVMAKYIDPKYIDIFVACKESELEEFEHSISDLEYNWYLHTV Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_3431 ABC transporter for L-Arginine and L-Citrulline, periplasmic substrate-binding component Specific phenotype on L-Arginine; L-Citrulline. Arginine/ornithine ABC transporter, periplasmic arginine/ornithine binding protein MKKLVLLGALALSVLSLPTFADEKPLKIGIEAAYPPFASKAPDGSIVGFDYDIGNALCEEMKVKCVWVEQEFDGLIPALKVRKIDAILSSMSITEDRKKSVDFTNKYYNTPARLVMKAGTAVSENLAELKGKNIGVQRGSIHERFAREVLAPLGAEIKPYGSQNEIYLDVAAGRLDGTVADATLLDDGFLKTDAGKGFAFVGPAFTDVKYFGDGVGIAVRKGDALKDKINTAIAAIRENGKYKQIQDKYFAFDIYGK Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_3432 ABC transporter for L-Arginine and L-Citrulline, permease component 1 Specific phenotypes on L-Arginine; L-Citrulline. Arginine/ornithine ABC transporter, permease protein AotQ MLKGYGAVILDGVWLTLQLALSSMVLAIVLGLIGVALRLSPIRWLAWLGDLYSTVIRGIPDLVLILLIFYGGQDLLNRVAPMFGYDDYIDLNPLAAGIGTLGFIFGAYLSETFRGAFMAIPKGQAEAGMAYGMSSFQVFFRVLVPQMIRLAIPGFTNNWLVLTKATALISVVGLQDMMFKAKQAADATREPFTFFLAVAAMYLVITSVSLLALRHLEKRYSVGVRAADL Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_3433 ABC transporter for L-Arginine and L-Citrulline, permease component 2 Specific phenotypes on L-Arginine; L-Citrulline. Arginine/ornithine ABC transporter, permease protein AotM MIFDYNVIWEALPLYLGGLVTTLKLLALSLFFGLLAALPLGLMRVSKQPVVNMSAWLFTYVIRGTPMLVQLFLIYYGLAQFEAVRESFLWPWLSSATFCACLAFAINTSAYTAEIIAGSLRATPNGEIEAAKAMGMSRIKMYKRILLPSALRRALPQYSNEVIMMLQTTSLASIVTLIDITGAARTVNAQFYLPFEAYITAGVFYLCLTFILVRLFKMAEHRWLGYLAPRKH Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_3435 ABC transporter for L-Arginine and L-Citrulline, ATPase component Very important for utilization of L-Arginine or L-Citrulline. Detrimental to fitness in some other minimal media experiments. Arginine/ornithine ABC transporter, ATP-binding protein AotP MYKLEVQDLHKRYGSHEVLKGVSLKAAAGDVISIIGSSGSGKSTFLRCINLLEQPHAGKILLNNEELKLVANKDGALKAADPKQLQRMRSRLSMVFQHFNLWSHMTAMENIMEAPVHVLGMSKTEAREKAEHYLNKVGVAHRKDAYPGHMSGGEQQRVAIARALAMEPEVMLFDEPTSALDPELVGDVLKVMQALAQEGRTMVVVTHEMGFAREVSNQLVFLHKGVVEESGNPREVLVNPQSERLQQFLSGSLK Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_412 L-arabinose 1-dehydrogenase / D-galactose 1-dehydrogenase (EC 1.1.1.46; EC 1.1.1.48) Both of these sugars are catabolized via a 1-dehydrogenase followed by lactonase and dehydratase reactions. This is the only dehydrogenase is specifically important for either of these carbon sources in several Pseudomonas, apart from a alpha-ketoglutarate semialdehyde dehydrogenase that is expected to be the last dedicated step in L-arabinose catabolism (i.e., Pf6N2E2_612). L-arabinose and D-galactose are chemically similar and some dehydrogenases are already known to act on both substrates. 3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100) MAEPLSLPPVPEPPKGERLKNKVVLLTGAAQGIGEAIVATFASQQARLVISDIQGEKVEKVAAHWREQGADVVAIKADVSRQQDLHAMARLAIELHGRIDVLVNCAGVNVFRDPLQMTEEDWHRCFAIDLDGAWYGCKAVLPQMIEQGIGSIINIASTHSTHIIPGCFPYPVAKHGLLGLTRALGIEYAPKGIRVNAIAPGYIETQLNVDYWNGFADPHAERQRAFDLHPPRRIGQPIEVAMTAVFLASDEAPFINASCITIDGGRSVMYHD Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_4511 D-galacturonate dehydrogenase (EC 1.1.1.203) Important on D-galacturonate; KEGG now has pfo:Pfl01_3452 as uronate dehydrogenase which is correct but less specific (KEGG_correct) UDP-glucose 4-epimerase (EC 5.1.3.2) MTNTSPFNRLLLTGAAGGLGKVLRERLRPYANVLRLSDIANMAPAIDDREEVVPCDLADKQAVHQLVEGVDAILHFGGVSVERPFEEILGANICGVFHIYEAARRHGVKRVIFASSNHVIGFYKQDKTLDAHSPRRPDSYYGLSKSYGEDMASFYFDRYGIETVSIRIGSSFPEPQNRRMMSTWLSFDDMTQLLERALYTPNVGHTVVYGMSANKSVWWDNRFAAHLGFAPQDTSEVFREKVEAQPMPAEDDPARVYQGGAFVAAGPFGD Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_4934 DNA damage response nuclease Conserved and specific phenotype: important for resisting cisplatin. Contains a VRR-NUC domain that is predicted to have nuclease activity. Hypothetical protein, restriction endonuclease-like VRR-NUC domain VIVNPLDDPFYYLNNFMQVLDWLEHRYADVLSLEEQDFIRDFNRLPRESQALLVRLVMRKGVHFRAGKLSYVEIGDIDSAAAPLLVSGWIDEQSPLHIEDLFEVLLKAEILQCIGSAIDQPKGKKTDWLPVLSEQFPEAQSFAQWCPALNERLFSLTVMDLCDRLRLMFFGNLYQDWSEFVLADLGIFTYEKVEFCTESRGLRSREDVDACLFLHSCQQRFEAGEDVAAIVEQINGLELGNPWLQRRRGKLLFQIGQHCERVADFSTALNLYRECAYPGARLRLIRVLERCAEYQLAMNLATHAEQAPESAAEHQHLSRVLPRLRRKLGGPPIKRPAPRAMQRLDLQLPRHDPTLSVESYVQAHLADDSAPVHYVENSLINSLFGLLCWPAIFAPLPGAFFHPFQRGPVDLLNEDFHARRADLFQACLAELDDGRYVQTVRERYSAKWGVQSPFVFWGALSEELLEQALACLPAEHLKHWFNRLLLDIKANRAGMPDLIQFWPQHKTYRMIEVKGPGDRLQDNQLRWLEFCHEHQMPIAVCYVQWAEQGA Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_6029 uridine nucleosidase (EC 3.2.2.3) Important on uridine; annotated by SEED as for uridine and inosine; close homologs are important for utilizing uridine (SEED_correct) Inosine-uridine preferring nucleoside hydrolase (EC 3.2.2.1) MQRYAQKLHHLLRSLLLLSLITATSAQAAEKIDLIIDTDPGADDVVALLFALASPDELNIRALTTVAGNVRLDKTSRNARLAREWAGREEVPVYAGAPKPMMRTPIYAENIHGKEGLSGVTVHEPKKGLAEGNAVNYLIDTLKTAKPHSITIAMLGPQTNLALALIQEPEIVQGIKEVVIMGGAHFNGGNITPVAEFNLFADPQAAEVVLKSGVKLTYLPLDVTHKILTSEARLKQIAALNNNASKLVGDILNEYVKGDMEHYGIPGGPVHDATVIAYLLKPELFTGRSVNVVVDSREGPTFGQTIVDWYDGLKAPKNAFWVESGDAQGFFDLLTQRLSRLK Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_718 outer membrane component of uptake system, probably for ferrous iron PFam PF07433.7 (DUF1513). In a conserved cofit operon with two efeO-like genes (Pf1N1B4_715,Pf1N1B4_717) and an efeB-like gene (Pf1N1B4_716) putative exported protein MLRRQALTLGSLLLGAVTLGGWTLFKQKDKSPLLLSARDDGDGKHYAVGYRLDGTRVFATQVGQRCHDIINHPTLPIALFVARRPGTESYLIDLRDGTLLQTVVSQPNRHFYGHAVIHHSGDWLYATENDTSDPGRGLLGVYKFEDERLVHSGELSTHGVGPHQVSWMPDGETLIVANGGIRTEAESRVEMNLNAMEPSLVLMQRDGTLLSKETLAQQMNSVRHLGVASDGTIVAGQQFMGDAHESSELLAIKRPGQPFVAFPVPEHQLQAMGHYTASVAVHSELRLVALTAPRGNRFFIWDLDSGEVRLDAPLPDCAGVGAVADGFVVTSGQGRCRYYDCRQTTLVAKPLELPAGLWDNHLHLMA Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_161 putative transporter, required for glycine utilization PFam PF03458.9 (UPF0126). conserved specific phenotype of UPF0126 putative membrane protein MLLMLYLIAITTEAMTGALSAGRRGMDWFGVVLIACVTALGGGSVRDVLLGHYPLTWVKHPEYLVLTTAAAMITVFTARWMRHLRSLFLVLDAMGLVAFTLIGCITALEMGHGMLVASVSGVITGVFGGILRDIFCNDIPLIFRRELYASVSFAAAWCYMLCIYLQLPDEQSILITLFGGFLLRLLAIRFHWEMPKFVYNDEA Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_1894 ABC transporter for D-Galactose and D-Glucose, periplasmic substrate-binding component Specific phenotype on D-Fructose; L-Aspartic Acid; D-Galactose; L-Lysine. The nitrogen source phenotypes for aspartate and lysine are with glucose as the carbon source. May also transport fructose. Glucose ABC transport system, periplasmic sugar-binding protein MNAISRLATVISLASLSALPLSVLAAESKGSVEVVHWWTSGGEKAAVDVLKAQVEKDGFTWKDGAVAGGGGSTAMTVLKSRAVAGNPPGVAQIKGPDIQEWGSTGLLSTDALKDVSKAENWDGLLSKKVSDTVKYEGDYVAVPVNIHRVNWLWINPEVFKKAGIEKAPTTLEEFYAAGDKLKAAGFIALAHGGQPWQDSTVFEDVVLSVMGADGYKKALVDLDQKTLSGPEMTKSFAELKKITGYMDPNRAGRDWNIAAADVISGKAGMQMMGDWAKSEWTAAKKIAGKDYQCVAFPGTEKAFTYNIDSMAVFKLKADRKGDIAAQQDLAKVALGTDFQKVFSMNKGSIPVRNDMLNEMDKLGFDECAQKSAKDFIADDKTGGLQPSMAHNMATSLAVQGAIFDVVTNFMNDKDADPAKASAQLASAVKAAQ Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_1895 ABC transporter for D-Galactose and D-Glucose, permease component 1 Specific phenotypes on D-Galactose; N L-Lysine. glucose is the C source for the N source experiments with a phenotype (i.e. lysine); may also transport fructose. Glucose ABC transport system, inner membrane component 1 MSSVAVFSKASPFDALQRWLPKLVLAPSMLIVLVGFYGYIIWTFILSFTNSSFMPSYKWVGLQQYMRLMDNDRWWVASKNLALFGGMFISISLVLGVFLAVLLDQRIRKEGFIRTVYLYPMALSMIVTGTAWKWLLNPGLGLDKMLRDWGWEGFRLDWLVDQDRVVYCLVIAAVWQASGFVMAMFLAGLRGVDQSIIRAAQVDGASLPTIYLKIVLPSLRPVFFSAFMILAHIAIKSFDLVAAMTAGGPGYSSDLPAMFMYSFTFSRGQMGIGSASAMLMLGAVLTILVPYLYSELRGKRHD Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_1896 ABC transporter for D-Galactose and D-Glucose, permease component 2 Specific phenotypes on D-Galactose; N L-Lysine. glucose is the C source for the N source experiments with a phenotype (i.e. lysine); may also transport fructose. Glucose ABC transport system, inner membrane component 2 MTNQLGKSGISFSRIAIYATLLLAAAVYLIPLVVMLLTSFKSPEDIRTGNLLSWPTVIDGIGWIKAWDVVGGYFWNSVKITVPAVLISTFIGAMNGYVLSMWRFRGSQLFFGLLLFGCFLPFQTVLLPASFTLGKFGLANTTTGLVLVHVVYGLAFTTLFFRNYYVSIPDALVKAARLDGAGFFTIFLKILLPMSIPIVMVCLIWQFTQIWNDFLFGVVFASGDAQPITVALNNLVNTSTGAKEYNVDMAAAMIAGLPTLLVYIFAGKYFLRGLTSGAVKG Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_1897 ABC transporter for D-Galactose and D-Glucose, ATPase component Specific phenotype on D-Galactose; L-Lysine; L-Aspartic Acid. The nitrogen source phenotypes for aspartate and lysine are with glucose as the carbon source. May also transport fructose. Glucose ABC transporter, ATP-binding subunit (EC 3.6.3.-) MATLELRNVNKTYGPGLPDTLKNIELKIDDGEFLILVGPSGCGKSTLMNCIAGLETISGGAILVDDADISGMSPKDRDIAMVFQSYALYPTMSVRDNIAFGLKIRKMPTAEIDEEVARVSKLLQIEHLLSRKPGQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPKDIYNNPANLFVASFIGSPPMNFIPLRLQRKDGRLLALLDSGQARCELPLGMQDAGLEDREVILGIRPEQIILANGEANGLPTIRAEVQVTEPTGPDTLVFVNLNDTKVCCRLAPDVAPAVGETLTLQFDPAKVLLFDAKTGERLGVAGVPKAEAHADNVAQFKGR Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_2119 L-arabinose 1-dehydrogenase / D-galactose 1-dehydrogenase (EC 1.1.1.46; EC 1.1.1.48) Specifically important for: D-Galactose; L-Arabinose. Both of these sugars are catabolized via a 1-dehydrogenase followed by lactonase and dehydratase reactions. This is the only dehydrogenase is specifically important for either of these carbon sources in several Pseudomonas, except for an alpha-ketoglutarate semialdehyde dehydrogenase that is expected to be the last dedicated step in L-arabinose catabolism (i.e., Pf6N2E2_612). L-arabinose and D-galactose are chemically similar and some dehydrogenases are already known to act on both substrates. 3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100) MAEPLSLPPVPEPPRGERLKNKVVLLTGAAQGIGEAIVATFASQQARLIISDIQGEKVEKVAAHWRDQGADVVAIKADVSRQQDLHAMARLAIDLHGRIDVLVNCAGVNVFRDPLEMTEEDWRRCFAIDLDGAWYGCKAVLPQMIEQGIGSIINIASTHSTHIIPGCFPYPVAKHGLLGLTRALGIEYAPKGVRVNAIAPGYIETQLNVDYWNGFADPHAERQRAFDLHPPRRIGQPIEVAMTAVFLASDEAPFINASCITIDGGRSVMYHD Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_2842 required for sulfate utilization, putative electron transport protein for sulfite reductase PFam PF06073.8 (DUF934). conserved cofitness with sulfite reductase; auxotrophic Oxidoreductase probably involved in sulfite reduction MQRIIKNNEVVDETWHLLPKDFNIDEISNCDDLIVPLQLWREHSRMLLARDGGLGIWLDADEEAEEIGEDVAQFQVIALNFPAFTDGRNYSNARLLRDRYGFKGELRAIGDVLRDQLFYMHRCGFDAFAIRADKDPHEALEGLKDFSVTYQAAADEPLPLFRRR Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_2867 D-glucosaminate dehydratase (EC 4.3.1.9) Specifically important for: D-Glucosamine Hydrochloride. This enzyme had not previously been linked to a gene. This is the second step in catabolism of glucosamine, and the 'beta' form of the enzyme was expected to be PLP-dependent and about this size. Iwamoto et al (2003) purified a non-specific 'alpha' enzyme for this reaction (PMID: 12686150) D-serine deaminase (EC 4.3.1.18) MSSAPNTAAVEKGTAPKGASLVRDVSLPALVLHREALEHNIRWMQAFVSDSGAELAPHGKTSMTPALFRRQLDAGAWGITLASATQTRAAYAHGVRRVLMANQLVGTPNMALIADLLADPTFDFYCMVDHPDNVADLGAYFASRGVRLNVMIEYGVVGGRCGCRSEQQVLDLAKAIAAQPALALTGIEGYEGVIHGDHAVTGIRDFAASLVRLAVQLQDSGAFAIPKPIITASGSAWYDLIAESFEAQNAAGRFLSVLRPGSYVAHDHGIYKEAQCCVLDRRSDLHEGLRPALEVWAHVQSLPEPGFAVIALGKRDVAYDAGLPVPLLRYKAGVVPAEGDDVSVCKVTAVMDQHAFMTVAPGVDLRVGDIISFGTSHPCLTFDKWRVGCLVDEQLNVIETMETCF Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_3314 D-galactono-lactonase (EC 3.1.1.-) Specifically important for: D-Galactose. A 1,5-lactone is probably the product of D-galactose dehydrogenase (PfGW456L13_2119), althought it might rearrange to a 1,4-lactone. Related to E. coli ybhE or pgl, which is 6-phospho-D-glucono-1,5-lactonase. 3-carboxymuconate cyclase MRNLWPLLMAGSIGAMGVQVASAEDYQLLVGSYTAGQSQGIYRLAFDSRTGQIDASPLQVIKSANPSWLTLSKDQRHLFVVNENGPGQTDPVGRVSSFAIDPKTHALSLISQVQSLGNEPTHSSLSIDGSHLFVSNYSVAEDPGGTLAVLPVAADGKLKAVVQMSSHPASRVNPERQASAHVHSTIPSPDGRYVFANDLGADKVFAYRFDPKANPELPLTPATPAFVQLPPGSGPRHLLFSADGKHAWLTMEMSAQVAVFDYHDGQLEQTQMVDLAAGQPVSDKAAAALHASADGKFLYVSNRGTANQLLVFAIDPATGHLSELQRRAVEGDHPREFSLDPSGKFLLIANQKSNQIVVVERDARTGLLGKTVQKLPMDAPSDLRFLLRQ Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4396 tyrosine aminotransferase (EC 2.6.1.57) Specifically important for: L-Phenylalanine. Phenylalanine is hydroxylated to tyrosine (by PfGW456L13_4394) before deamination. KEGG has same EC# but less specific Aspartate aminotransferase (EC 2.6.1.1) MHFDAIGRVPGDPILGLMEAYAQDPNPRKFDLGVGVYKDAQGLTPILESVKLAEQRLVDHQSTKTYIGGHGEPAFGKAINELVLGADSKLISAQRAGATQTPGGTGALRLSADFIAQCLPGRGVWLSNPTWPIHETIFAAAKVKVSHYPYVGSDNRLDVDGMLAALNEAPKGDVVLLHACCHNPTGFDLSQDDWQRVLEVVRKRELLPLIDFAYQGFGDGLEQDAWSTRLFAAELPELLITSSCSKNFGLYRDRTGALIVCAKTADKLVDIRSQLANIARNLWSTPPDHGAAVVATILGDPELKRLWADEVEAMRLRIAQLRSGLVEALEPHGLRERFAHIGVQRGMFSYTGLSPEQVKNLRDHHSVYMVSSGRANVAGIDATRLDLLAEAIASVCK Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4770 ABC transporter for L-Asparagine and possibly other L-amino acids, periplasmic substrate-binding component Specific phenotype on L-Asparagine; Sodium octanoate. Detrimental on glutamine and might leak it. The mild phenotype on octanoate is not explained. Glutamate Aspartate periplasmic binding protein precursor GltI (TC 3.A.1.3.4) MRIVPHILGAAIAAALISTPVFAAELTGTLKKIKESGTITLGHRDASIPFSYIADASGKPVGYSHDIQLKVVEALKKDLDMPNLQVKYNLVTSQTRIPLVQNGTVDLECGSTTNNVERQQQVDFSVGIFEIGTRLLSKADSKYKDFPDLAGKNVVTTAGTTSERILKAMNADKQMGMNVISAKDHGESFQMLETGRAVAFMMDDALLAGEAAKAKKASDWAVTGTPQSYEIYGCMVRKGDEPFKKAVDDAIKATYASGEINKIYEKWFMQPIPPKGLNLNFPMSDELKALIAKPTDKAADDKKS Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4771 ABC transporter for L-Asparagine and possibly other L-amino acids, permease component 1 Specific phenotypes on L-Asparagine; L-Asparagine. also has weak phenotypes on other a.a., but not on aspartate; weak phenotype on glutamate; also is detrimental during growth on glutamine (along with a downstream HK-RR), which could imply that it leaks glutamate; ko:K10003 : glutamate/aspartate transport system permease protein Glutamate Aspartate transport system permease protein GltJ (TC 3.A.1.3.4) MNYNWDWGVFFKSTGVGSETYFDWYVTGLAWTIGIAIAAWIIALTLGSILGVMRTVPNRIVSGIATCYVELFRNVPLLVQLFIWYFLVPDLLPADLQEWYKQDLNPTTSAFLSVVVCLGLFTTARVCEQVRTGIQALPKGQESAARAMGFKLPQIYWNVLLPQAYRIIIPPLTSEFLNVFKNTSVASLIGLMELLAQTKQTAEFSANLFEAFTLATLIYFTLNMSLMLLMRVVEKKVAVPGLISVGGK Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4772 ABC transporter for L-Asparagine and possibly other L-amino acids, permease component 2 Specific phenotypes on L-Asparagine; L-Asparagine. also has weak phenotypes on other a.a., but not on aspartate; weak phenotype on glutamate; also is detrimental during growth on glutamine (along with a downstream HK-RR), which could imply that it leaks glutamate; K10002 : glutamate/aspartate transport system permease protein Glutamate Aspartate transport system permease protein GltK (TC 3.A.1.3.4) MEFDFSGIIPSLPGLWNGMIMTLKLMAMGVIGGIILGTILALMRLSHNKVLSNIAGAYVNYFRSIPLLLVITWFYLAVPFVLRWITGEDTPIGAFASCIVAFMMFEAAYFCEIVRAGVQSIPKGQMGAAQALGMSYGQMMRLIILPQAFRKMTPLLLQQSIILFQDTSLVYAVGLVDFLNASRASGDIIGRSNEFLIFAGLVYFIISFAASQLVKRLQKRFAV Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4773 ABC transporter for L-Asparagine and possibly other L-amino acids, putative ATPase component This is presumably the ATPase component but lacks fitness data. Glutamate Aspartate transport ATP-binding protein GltL (TC 3.A.1.3.4) MISIKSINKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDIVVDGTSIADPKTNLPKLRSRVGMVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLERVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAHEGMTMMCVTHEMGFARKVADRVIFMDQGKIIEDCKKEEFFGDINARAERTQHFLNKILQH Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_506 required for octanoate transport, together with NodT, MFP, and FUSC proteins (PfGW456L13_504, PfGW456L13_505, PfGW456L13_507) PFam PF07869.8 (DUF1656). A conserved cofit operon. This and orthologous operons are important for utilization of octanoate, which is probably toxic at 20 mM, but it could also be for uptake rather than efflux. membrane protein, putative MIGDLDLSGVFLPTLLVLMGITYVLYLLVHGVLTRLHFYRLVWHRALFNVALYALLLGAVDSLSRYLMT Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_925 Gamma-glutamyl-putrescine synthetase (EC 6.3.1.11) Specifically important for: Putrescine Dihydrochloride. The first step in putrescine catabolism. (SEED_correct) Gamma-glutamyl-putrescine synthetase (EC 6.3.1.11) MSVPPRAVQLNEANAFLKEHPEVLYVDLLIADMNGVVRGKRIERTSLHKVYEKGINLPASLFALDINGSTVESTGLGLDIGDADRICYPIPDTLCNEPWQKRPTAQLLMTMHELEGEPFFADPREVLANVVRKFDEMGLTICAAFELEFYLIDQENVNGRPQPPRSPVSGKRPHSTQVYLIDDLDEYVDCLQDILEGAKEQGIPADAIVKESAPAQFEVNLHHVADPIKACDYAVLLKRLIKNIAYDHEMDTTFMAKPYPGQAGNGLHVHISILDKDGKNIFASEDPEQNAALRHAIGGVLETLPAQMAFLCPNVNSYRRFGAQFYVPNSPCWGLDNRTVAIRVPTGSADAVRIEHRVAGADANPYLLMASVLAGVHHGLTNKIEPGAPVEGNSYEQNEQSLPNNLRDALRELDDSEVMAKYIDPKYIDIFVACKESELEEFEHSISDLEYNWYLHTV Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_03040 AO353_03040 ABC transporter for L-Arginine and L-Citrulline, ATPase component Specific phenotype on L-Arginine. Also important on citrulline. amino acid transporter MYKLEVQDLHKRYGSHEVLKGVSLKAAAGDVISIIGSSGSGKSTFLRCINLLEQPHAGKILLNNEELKLVANKDGALKAADPKQLQRMRSRLSMVFQHFNLWSHMTAMENIMEAPVHVLGMSKAEAREKAELYLAKVGVSHRKDAYPGHMSGGEQQRVAIARALAMEPEVMLFDEPTSALDPELVGDVLKVMQALAQEGRTMVVVTHEMGFAREVSNQLVFLHKGVVEESGNPREVLVNPQSERLQQFLSGSLK Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_03045 AO353_03045 ABC transporter for L-Arginine and L-Citrulline, permease component 1 Specific phenotypes on L-Arginine; L-Arginine. also important for citrulline amino acid ABC transporter permease MIFDYNVIWEALPLYFGGLVTTLKLLALSLLFGLLAALPLGLMRVSKQPIVNMSAWLYTYVIRGTPMLVQLFLIYYGLAQFEAVRESFLWPWLSSATFCACLAFAINTSAYTAEIIAGSLRATPNGEIEAAKAMGMSRFKMYKRILLPSALRRALPQYSNEVIMMLQTTSLASIVTLIDITGAARTVNAQYYLPFEAYITAGVFYLCMTFILVRLFKMAEHRWLGYLAPRKH Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_03050 AO353_03050 ABC transporter for L-Arginine and L-Citrulline, permease component 2 Specific phenotypes on L-Arginine; L-Arginine; L-Arginine. possibly citrulline as well ABC transporter MLKGYGAVILDGAWLTLQLALSSMALAIVLGLIGVALRLSPIRWLARLGDLYSTVIRGIPDLVLILLIFYGGQDLLNRVAPLLGYDDYIDLNPLVAGIGTLGFIFGAYLSETFRGAFMAIPKGQAEAGAAYGMSSFQVFFRVLVPQMIRLAIPGFTNNWLVLTKATALISVVGLQDMMFKAKQAADATREPFTFFLAVAAMYLVITSVSLLALRHLEKRYSVGVRAADL Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_03055 AO353_03055 ABC transporter for L-Arginine and L-Citrulline, periplasmic substrate-binding component Specific phenotype on L-Arginine; L-Citrulline. ABC transporter substrate-binding protein MKKLVLLGALALSVLSLPTFADEKPLKIGIEAAYPPFASKAPDGSIVGFDYDIGNALCEEMKVKCVWVEQEFDGLIPALKVRKIDAILSSMSITDDRKKSVDFTNKYYNTPARLVMKAGTQVSDNLAELKGKKIGVQRGSIHNRFAEEVLKPLGAEIKPYGSQNEIYLDVAAGRLDGTVADATLLDDGFLKTDSGKGFAFVGPAFTDEKYFGDGIGIAVRKGDKAELDKINAAIVAIRANGKYKQIQDKYFNFDIYGK Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_03810 AO353_03810 Alpha-ketoglutarate permease, MFS superfamily Specific phenotype on a-ketoglutarate. 86% identical to the a-ketoglutarate transporter in P. aeruginosa (PA5530, see PMCID: PMC4097582) and 56% similar to E. coli kgtP. (KEGG_correct) MFS transporter MDNSQTLPLGSAAVPAKEKTTASRIKSIFSGSVGNMVEWYDWYVYAAFSLYFAKAFFPKGDTTAQLLNTAAIFAVGFLMRPIGGWLMGLYADRAGRKAALMASVYLMCFGSLIIALSPGYETIGVGAPILLVFARLLQGLSVGGEYGTSATYLSEMATKERRGFFSSFQYVTLISGQLIALGVLIVLQQTLTTEQLYDWGWRIPFAIGALCAIVALYLRRGMEETESFAKKEKSKESAMRTLLRHPKELMTVVGLTMGGTLAFYTYTTYMQKYLVNTVGMSISDSTTISAATLFLFMCLQPIIGGLSDKVGRRPILIAFGILGTLFTVPILTTLHTIQTWWGAFFLIMAALIIVSGYTSINAVVKAELFPTEIRALGVGLPYALTVSIFGGTAEYIALWFKSIGMETGYYWYVTACIAVSLLVYVTMKDTRKHSRIETD Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_04460 AO353_04460 N-acetylglucosamine-specific PTS system, I, HPr, and IIA components (nagF) Specifically important for NAG utilization. (SEED_correct) PTS N-acetyl-D-glucosamine transporter MHNNNKDLTLSAPLSGPVLTLAKVPDPVFASGAMGDGIAIDPLNNTLHAPCAGVVVHVARTGHAVTLRADNGAELLLHLGLDTVELQGEGFSMLVKEGTRVSNGQALLRFDLDQVAQGCKSLVSLLVLTNSEDFQVLPITLKSVKVGEPLLHIVPRTTHSAQVEADSSGAEVHGHIRIIHRGGLHARPAALIRQTAHLFNSKSQLHFAGKSASCDSLIGLMGLGIGEQDEVQVSCKGADAKAALQALLNALSTAVNDDSHAAAPTPIAQRTRTAEAGVLNGVCAAPGLVGGPLFQLAAIPLPEDTGKHNAEEQLQALDRALEQVRSEIRETLSHAKKHKHTEEEQIFAAHLALLEDPALLEAAIQSIDQGSAATHAWSQSIEAQCEVLQQLGNPLLAERANDLRDLRQRVLRALLGQDWHYDVPAGAIVAAHELTPSDLLQLSQQGVAGLCMAEGGATSHVAILARGKGLPCLVALSASLLQQPQGQSVVLDADGGRLELTPDSQRLEQVAQAQREHLQRRERQQAQAHTPAHTRDGLRIEVAANVASSNEAADALKGGADGVGLLRTEFLFVDRQTAPDEQEQRQAYQAVLDAMGDKSVIIRTIDVGGDKQLDYLPLPAEANPVLGLRGIRMAQVRPELLDQQLRALLQVSPLQRCRILLPMVTEVDELLYIRQRLDALCAELALTQRLELGVMIEVPAAALLAEQLAEHADFLSIGTNDLSQYTLAMDRDHAGLAARVDALHPALLRLIAQTCIGAAKHQRWVGVCGALASDPLATPVLIGLGISELSVSPPQVGEIKERVRQLDAADCRRFSATLLNLSSATAVRHACHQHWPLS Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_04465 AO353_04465 N-acetylglucosamine-specific PTS system, IIBC components (nagE) Specifically important for NAG utilization. SEED incorrectly implies that this contains the IIA component as well. (KEGG_correct) PTS N-acetyl-D-glucosamine transporter MYQLFIEGLQRLGRALMLPIAILPIAGLLLRLGDTDLLNIAIIHDAGQVIFANLALIFAIGIAVGFARDNNGTAGLAGAIGYLVMVSTLKVLDASINMGMLAGIISGLMAGALYNRFKDIKLPEYLAFFGGRRFVPIATGFSAVGLGVIFGLIWPPIQHGINSFGQLLLESGSIGAFVFGVFNRLLIVTGLHHILNNMAWFIFGSFTDPTTGAIVTGDLARYFAGDPKGGQFMTGMFPMMIFGLPAACLAMYRNALPERRKVMGGIFLSMALTSFLTGVTEPIEFAFMFLAPLLYLLHVLLTGMAMAITNALNIHLGFTFSGGAIDMALGWGKSTNGWLVFPVGLAYAVIYYVVFDFCIRRFNLKTPGREGVVVGEKVVLSENQRAGAYIQALGGAENLITVGACTTRLRLEMVDRNKASDSELKALGAMAVVRPGKGGSLQVVVGPLADSIADEIRQAMPTAGSALVAAVVVTEEAPKAAPVETPEAQKWLNAVGGSDNVLQLDCVAMTRIRLQLADGKALSECQLKDLGCQGVSALDGGVWHLLIGDKALSLSEALEGLVNRSEVSAKV Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_04830 AO353_04830 required for acetate efflux, together with NodT, MFP and FUSC proteins (AO353_04840, AO353_04825, and AO353_04835) PFam PF07869.8 (DUF1656). A conserved cofit operon. This operon and orthologous operons are important on acetate as a carbon source and cholin acetate as a stress, which suggests that acetate is a substrate. Na+-dependent transporter MPREIAFHGVYMPTMTLMFFIAAAMAWALDRFLSGFDLYRFFWHPALLRLSLFTCLFGALALTVYS Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_05485 AO353_05485 Fructose-specific PTS system, I, HPr, and IIA components Specifically important for fructose utilization. The enzyme II B/C components of this PTS system are in AO353_05475 which is cofit and is correctly annotated. AO353_05485 is 73% identical to PA3562, which is also part of a fructose-specific system (PMC:PMC2542419) PTS fructose transporter subunit IIA MLELTIEQISMGQSAVDKAAALHLLADTLVNDGLVAEGYLSGLQAREAQGSTFLGQGIAIPHGTPDTRDLVHTTGVRLLQFPEGVDWGDGHIVYLAIGIAAKSDEHLRLLQLLTRALGETDLGQALRRASSAEALLKLLQGAPQELALDAQMIGLGVSADDFEELVWRGARLLRQADCVSNGFSAVLQQVEALPLGDGLWWLHSEQTVKRPGLAFVTPDKPIRYLGQPLSGLFCLASLGEAHQALLERLCALLIEGRGHELGRATSRRAVLEVLGGELPADWPSARIALANAHGLHARPAKILAQLAKSFEGEIRIRIVDGQDSAVSVKSLSKLLSLGARRGQVLELIAEPSIAADALPALLRAIEEGLGEDIEPLPTVSAQSEVIDEITDVVVAPASGCVIQAVAAAPGIAIGPAHIQVLQAIDYPLRGESTAIERERLKTSLADVRRDIEGLIQRSKAKAIREIFITHQEMLDDPELTDEVDTRLKQGESAEAAWMAVIDAAARQQESLQDALLAERAADLRDIGRRVLAQLCGIETPSEPDQPYILVMDEVGPSDVARLDPTRVAGILTARGGATAHSAIVARALGIPALVGAGAAVLRLASGTPLLLDGQRGRLHVDADAATLQRAAEERDNREQRLQAAAAQRHQPALTTDGHAVEVFANIGESAGVVSAVEQGAEGIGLLRTELIFMAHQQAPDEATQEVEYRRVLDGLAGRPLVVRTLDVGGDKPLPYWPIAKEENPFLGVRGIRLTLQRPQIMEAQLRALLRAADNRPLRIMFPMVGSVDEWRQARDMTERLRLEIPVADLQLGIMIEVPSAALLAPVLAKEVDFFSVGTNDLTQYTLAIDRGHPTLSAQADGLHPAVLQLIDITVRAAHAHGKWVGVCGELAADPLAVPVLVGLGVDELSVSARSIGEVKARVRELSLAQVKHLAQLALAVGSANEVRALVEAL Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_07335 AO353_07335 yeaG component of nitrogen-related signalling system (of yeaGH-ycgB) conserved cofitness; yeaG is a protein kinase serine/threonine protein kinase MSIFSHFQQRFESTRQEELTLQEYLELCKKDRSAYASAAERLLLAIGEPELLDTSTNSRLSRIFSNKVIRRYPAFEDFHGMEECIDQIVSYFRHAAQGLEEKKQILYLLGPVGGGKSSLAEKLKQLIEKVPFYAIKGSPVFESPLGLFNATEDGAILEEDFGIPRRYLNTIMSPWATKRLAEFGGDISQFRVVKLYPSILNQIAVAKTEPGDENNQDISALVGKVDIRKLEEFPQNDADAYSYSGALCRSNQGLMEFVEMFKAPIKVLHPLLTATQEGNYNSTEGLGAIPFTGILLAHSNESEWHTFRNNKNNEAFIDRIYIVKVPYCLRVSDEVKIYDKLLFNSSLAKAHCAPDTLKMLAQFTVLSRLKEPENSNIYSKMRVYDGENLKDTDPKAKSIQEYRDTAGVDEGMNGLSTRFAFKILSKVFNFDPHEIAANPVHLLYVLEQQIEQEQFQAETRERYLRFLKEYLAPRYIEFIGKEIQTAYLESYSEYGQNIFDRYVLYADFWIQDQEYRDPETGEILNRVALNEELEKIEKPAGISNPKDFRNEIVNFVLRARANNNGKNPTWLSYEKLRVVIEKKMFSNTEDLLPVISFNAKASKEDQQKHNDFVTRMVERGYTDKQVRLLSEWYLRVRKSQ Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_07340 AO353_07340 yeaH component of nitrogen-related signalling system (of yeaGH-ycgB) PFam PF04285.8 (DUF444). conserved cofitness; yeaG is a protein kinase hypothetical protein MSYVIDRRLNGKNKSTVNRQRFLRRYRDHIKKAVEEAVSRRSITDMEHGEQISIPGRDIDEPVLHHGRGGKQTIVHPGNKEFTSGEHIARPPGGGGGRGPGKAGNSGEGMDEFVFQITQEEFLEFMFEDLELPNLVKRNLSGTDTFKTVRAGISNEGNPSRINIIRTLRSAHARRIALSGSSREKLRVAKEELARLKQEEPDNFGDIQEIEAEIERLSARINRVPFLDTFDLKYNLLIKQPNPSSKAVMFCLMDVSGSMTQATKDIAKRFFILLYLFLKRNYEKIDVVFIRHHTSAREVDEEEFFYSRETGGTIVSSALKLMQEIMAERYPSNDWNIYAAQASDGDNWNDDSPICRDILINQIMPFVQYYTYVEITPREHQALWYEYERISEAFSDTFAQQQLVSAGDIYPVFRELFQRRLVT Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_07345 AO353_07345 ycgB component of nitrogen-related signalling system (of yeaGH-ycgB) conserved cofitness; yeaG is a protein kinase SpoVR family protein MTAKEQKRQPISTGSEWTFELIQAYDREISRLAARYALDTYPNQIEVITAEQMMDAYASVGMPLGYHHWSYGKHFLSTEKSYSRGQMGLAYEIVINSDPCIAYLMEENTICMQALVVAHACYGHNSFFKGNYLFRTWTDASSIIDYLVFAKQYIMQCEERHGIDAVEDLLDSCHALMNYGVDRYKRPYPISAEEERRRQKDREEHLQKQINDLWRTIPKGADKFNEKDNARFPAEPQENILYFIEKHAPLLEPWQREIVRIVRKIAQYFYPQRQTQVMNEGWATFWHYTLMNDLYDEGLVTDGFMMEFLASHTSVIFQPGFDSPYYNGINPYTLGFSMYRDIRRMCEAPTEEDYRWFPEIAGTDWLSSIKFAMSSFKDESFILQYLSPKVIRDLKLFSILDDDQKDDLLVPAIHDEEGYRTIRETLAAQYNLGNREPNIQIYSIDRRGDRSLTLRHQQHDRKPLGDSTEEVLKHLHRLWGFDIHLETLQGDQVMKTHHVPPKGEHSEGEYGRMDLAVIHL Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_07485 AO353_07485 Acyl-CoA dehydrogenase (EC 1.3.8.7) Specifically important for: Sodium butyrate; Tween 20. The phenotype on Tween 20 suggests that it has activity on longer substrates as well as on butyryl-CoA (SEED_correct) acyl-CoA dehydrogenase MADYKAPLRDMRFVLNEVFEVAKLWAELPALADTVDAETVEAILEEAGKVTSKSIAPLSRAADEEGCHWSDGAVTTPAGFPQAYQTYAEGGWVGVGGDPSYGGMGMPKAVSAQVEEMVNSASLSFGLYPMLTAGACLSINAHASEELKAAYLPNMYAGVWAGSMCLTEPHAGTDLGIIRTKAEPQADGSYKVSGTKIFITGGEHDLTENIIHLVLAKLPDAPAGPKGISLFLVPKFMVNADGSLGARNPANCGSIEHKMGIQASATCVMNFDEAVGYLVGEPNKGLAAMFTMMNYERLGVGIQGLASGERSYQNAVEYARDRLQSRSPTGAQNKDKVADPIIVHPDVRRMLLTMKASNEGGRAFSTYVAMQLDTAKFSEDATIRKRAEDLVALLTPVAKAFLTDLGLETTIHGQQVFGGHGYIREWGQEQLVRDVRITQIYEGTNGIQALDLVGRKIVGSGGAYYKLFADEIRHFTATASADLAEFTKPLNDAVDTLDELTAWLLDRVKNNPNEIGAASVEYLQVFGYVSYAYMWALMAKAAFGKEAQDDFYASKLGTARFYFARLLPRFHSLSASVKAGSESLFLLDAAQF Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_07705 AO353_07705 DgcB Dimethylglycine demethylase subunit B (EC 1.5.3.-) Specifically important for: Carnitine Hydrochloride. Dimethylglycine is an intermediate in L-carnitine metabolism; this gene is similar to PA5399 or dgcB (PMCID: PMC2293255) (Fe-S)-binding protein MLNTLLPILLFAALGLAVLGALRRVAMWRRGRASKVDLIGGLLAMPKRYMVDLHHVVARDKYIANTHVATAGGAVASIVLAILVHGFGLHNRFLGYALLLMTAVMFVGAIFVYLRRRNPPARLSKGPWMRLPKSLLAFSASFFLVTLPVAGILPENFGGWLLAAILGVGVLWGVSELFFGMTWGGPMKHAFAGALHLAWHRRAERFGGGRSTGLKPLDLNDPQAPLGVEKPKDFTWNQLLGFDACVQCGKCEAACPAFAAGQPLNPKKLIQDMVVGLAGGTDAKFAGSPYPGKAIGEHAGNPHQPIVNGLVDAETLWSCTTCRACVEECPMMIEHVDAIVDMRRHLTLEKGATPNKGAEVLENLIATDNPGGFAPGGRMNWAADLNLTLLSEKKSTDVLFWVGDGAFDMRNQRTLRAFVKVLKAAKVDFAVLGLEERDSGDVARRLGDEATFQLLAKRNIQTLAKYSFNRIVTCDPHSFHVLKNEYGAFDGNYLVQHHSTYMAEIIDAGALNLGQHKGDSVTYHDPCYLGRYNGEYEAPRQVLRALGIEVKEMQRSGFRSRCCGGGGGAPITDIPGKQRIPDMRMDDIRETGAELVAVGCPQCTAMLEGVVEPRPLIKDIAELVADALLEDAAPSKSPAPTKRQPAEAH Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_07710 AO353_07710 DgcA Dimethylglycine demethylase subunit A Specifically important for: Carnitine Hydrochloride. Carnitine is catabolized via glycine betaine (trimethylglycine) and then demethylated twice to sarcosine (N-methylglycine) (PMCID: PMC2293255) (SEED_correct) N-methylproline demethylase MAFEAMFQPIQIGKLTIRNRVLSTAHAEVYATDGGMTTDRYVKYYEEKAKGGIGLAICGGSSSVAIDSPQGWWKSVNLADDRIIPHFQNLADAMHKHGAKIMIQITHMGRRSRWDGEHWPTLLSPSGIREPVHRATCKTIEPEEIWRVIGNYASAAARAKAGGLDGVELSAVHQHMIDQFWSPRVNKRTDEWGGSFENRMRFGLEVIKAVRKEVGPDFCVGIRICGDEFHPDGLSHEDMKQIAKYYDDTGMIDFIGVVGSGCDTHNTLANVIPNMSYPPEPFLHLAAGIKEVVKAPVLHAQNIKDPNQATRILEGGYVDMVGMTRAHIADPHLIAKIKMGQIDQIKQCVGANYCIDRQYQGLDVLCIQNAATSREYMGVPHIIEKSTGVKRKVVVVGAGPAGMEAARVAAERGHDVTLFEKKEFIGGQITTASKAPQRDQIAGITRWFQLELARLKVDLRLGVAADAATILDLRPDIVVLAVGGHPFLEQNEHWGAAEGLVVSSWDVLDGKVLPGKNVLVYDTICEFTGMSVADYLADKGSQVEIVTDDIKPGVAIGGTSFPTYYRSMYPKEVIMTGDMMLDKVYREGDKLVAVLENEYTGAKEERVVDQVVVENGVRPDEEIYYALKEGSRNKGQMDIEALFAIKPQPSLSQAGDGYLLFRIGDCVAQRNTHAAIYDALRLCKDF Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_07740 AO353_07740 ABC transporter for Carnitine, substrate-binding component Specific phenotypes on Carnitine Hydrochloride. Similar to CaiX (see PMID:19919675). This transporter may also have a second SBP, AO353_07780, similar to CbcX, which is reported to be an alternate SBP for choline or glycine utilization (ibid). However _07780 is also important for carnitine utilization - it might be an additional necessary subunit of this transporter. glycine/betaine ABC transporter substrate-binding protein MKRLISSCVLALSGTAFLSSGAMAADPAACQNVRMGVVNWTDVIATSAMTQVLLDGLGYKTKQTSASQQIIFAGIRDQRLDMFLGYWNPLMTQTITPFVAGKQVTVLSEPSLKDARATLAVPTYLADKGLKTFADIAKFEKELGGKIYGIEPGSGANTQIKEMIAKNQFGLGKFQLVESSEAGMLAAVDRAVRRNEAVVFFGWAPHPMNVNVKMTYLTGSQDALGPNEGSATVWTVTAPNYASQCPNVSRLLSNLTFTAEDESRMMQPLLDHKDAFESAKQWLKDHPQDKQRWLEGVTTFDGKPAAENLQLSSQ Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_07750 AO353_07750 carnitine 3-dehydrogenase [EC:1.1.1.108] Specifically important for: Carnitine Hydrochloride. Not sure why SEED missed this: some very similar proteins are annotated correctly. pba:PSEBR_a5237 has been updated in KEGG and is now annotated as the carnitine dehydrogenase. (KEGG_correct) 3-hydroxybutyryl-CoA dehydrogenase MSFITEIKTFAALGSGVIGSGWVSRALAHGLDVVAWDPAPGAEVALRKRVANAWGALEKQGLAPGASQDRLRFVATIEECVRDADFIQESAPERLELKLELHSKISAAAKPNALIGSSTSGLLPSEFYEGSTHPERCVVGHPFNPVYLLPLVEVVGGKNTAPEAVQAAMKVYESLGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLAGGDAGMRHFMAQFGPALQLPWTYLPAPELTDKLIDDVVDGTSDQLGKHSISALERYRDDCLLAVLEAVKTTKAKHGMTFSE Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_07755 AO353_07755 betainyl-CoA thiolase (EC 3.1.2.-) Specifically important for: Carnitine Hydrochloride. This is part of the degradation of carnitine (K. Bastard et al, Nature Chem Biol. 2014). Since KEGG had this EC number you could argue that it is correct, but it made a very vague prediction. 4-hydroxybenzoyl-CoA thioesterase MPALTTYTTKIIPDWVDYNGHLRDAFYLLIFSYATDALMDQLGMDSNNREASGNSLFTLELHLNYLHEVKLGAEVEVHTQIIGHDRKRLHLYHSLHLVGEEQELAGNEQMLLHVDLAGPRSAPFSESVLNKLRAMSALQSDLPTPAYIGRVIALPPEK Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_07785 AO353_07785 ABC transporter for Carnitine, permease component Specific phenotypes on Carnitine Hydrochloride. no phenotype in choline stress; annotated as glycine betaine or proline transport. Another issue is that carnitine might be oxidized to choline which is then excreted (MetaCyc Pathway: L-carnitine degradation II) but this would not support growth with carnitine as either C or N source (no C or N extracted). Note that both carnitine and choline are catabolized via glycine betaine and this is clustered with glycine betaine degradation genes. This ABC transporter might also transport choline or glycine betaine with a different SBP (AO353_07780). choline ABC transporter permease subunit MLIDQKIPLGQYIAAFVEWLTQHGASTFDAIATTLETMIHGVTFALTWFNPLALIGLIALLAHFIQRKWGLTAFVIASFLLILNLGYWQETMETLAQVLFATFVCVIIGVPLGIVAAHKPMFYTMMRPVLDLMQTVPTFVYLIPTLTLFGLGVVPGLISTVVFAIAAPIRLTYLGIRDVPQELMDAGKAFGCSRRQLLSRIELPHAMPSIAAGITQCIMLSLSMVVIAALVGADGLGKPVVNALNTADIALGFEAGLAIVLLAIMLDRICKQPDAKVGGDA Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_07790 AO353_07790 ABC transporter for Carnitine, ATPase component Specific phenotypes on Carnitine Hydrochloride. Note that both carnitine and choline are catabolized via glycine betaine and this is clustered with glycine betaine degradation genes. This ABC transporter might also transport choline or glycine betaine with a different SBP (AO353_07780). choline ABC transporter ATP-binding protein MSIIRFDNVDVIFSKDPREALKLLDQGMTRDQILKKTGQIVGVEKASLDIEKGEICVLMGLSGSGKSSLLRCINGLNTVSRGKLFVEHEGRQIDIASCTPAELKMMRTKRIAMVFQKFALMPWLTVRENISFGLEMQGRPEKERRQLVDEKLELVGLTQWRNKKPDELSGGMQQRVGLARALAMDADILLMDEPFSALDPLIRQGLQDELLELQRKLHKTIVFVSHDLDEALKLGSRIAIMKDGRIIQYSKPEEIVLNPADDYVRTFVAHTNPLNVLCGRSLMRTLDNCKRINGSVCLDPGGDSWLDLAEGNTIKGARQNGSSLDLQNWVPGQAVEGLGRRPTLVDSNIGMRDALQIRYQTGNKLVLHDNNKVVGILGDSELYHALLGKNLG Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_08585 AO353_08585 Gamma-aminobutyrate:alpha-ketoglutarate aminotransferase (EC 2.6.1.19) Specifically important for: Putrescine Dihydrochloride. KEGG annotates this as putrescine aminotransferase, probably based on similarity to spuC (PA0299) of P. aeruginosa, but it is believed that only the g-glutamyl- pathway operates in P. aeruginosa (X. Yao et al 2011, PMC:3147493) aminotransferase MTSKNPQTREWQTLSSEHHLAPFSDFKQLKEKGPRIITNAKGVYLWDSEGNKILDGMAGLWCVAIGYGRDELADAASKQMRELPYYNLFFQTAHPPVLELAKAISDIAPEGMNHVFFTGSGSEGNDTMLRMVRHYWAIKGQPNKKVIISRINGYHGSTVAGASLGGMTYMHEQGDLPIPGIVHIPQPYWFGEGGDMTPEEFGIWAANQLEEKILELGVDTVGAFIAEPIQGAGGVIIPPDSYWPRIKEILAKYDILFVADEVICGFGRTGEWFGSDFYGLKPDMMTIAKGLTSGYIPMGGLIVRDEVVEVLNEGGDFNHGFTYSGHPVAAAVALENIRILREEKIIEHVRAETAPYLQKRLRELNDHPLVGEVRGVGLLGAIELVQDKATRARYVGKGVGMICRQFCFDNGLIMRAVGDTMIIAPPLVITKAEIDELVTKARKCLDLTLSALQS Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_08595 AO353_08595 Gamma-glutamyl-putrescine synthetase (EC 6.3.1.11) Specifically important for: Potassium acetate; L-Arginine; Putrescine Dihydrochloride; L-Citrulline. This is the first step in putrescine degradation and is important for the usage of putrescine as either C or N source. The phenotypes on citrulline and arginine might indicate a side pathway where they are converted to putrescine via ornithine decarboxylase (SEED_correct) gamma-glutamylputrescine synthetase MSVPPRAVQLNEANAFLKEHPEVLYVDLLIADMNGVVRGKRIERTSLHKVYEKGINLPASLFALDINGSTVESTGLGLDIGDADRICYPIPNTLCNEPWQKRPTAQLLMTMHELEGEPFFADPREVLANVVRKFDDMGLTICAAFELEFYLIDQENVNGRPQPPRSPVSGKRPHSTQVYLIDDLDEYVDCLQDILEGAKEQGIPADAIVKESAPAQFEVNLHHVADPIKACDYAVLLKRLIKNIAYDHEMDTTFMAKPYPGQAGNGLHVHISILDKDGKNIFASEDPEQNAALRHAIGGVLETLPAQMAFLCPNVNSYRRFGAQFYVPNSPCWGLDNRTVAIRVPTGSADAVRIEHRVAGADANPYLLMASVLAGVHHGLTNKIEPGAPVEGNSYEQNEQSLPNNLRDALRELDDSEVMAKYIDPKYIDIFVACKESELEEFEHSISDLEYNWYLHTV Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_11505 AO353_11505 succinate-semialdehyde dehydrogenase (EC 1.2.1.16) Specifically important for: L-Citrulline; L-Arginine; Putrescine Dihydrochloride. succinate semialdehyde is an intermediate in putrescine catabolism. KEGG has updated its annotation (K00135, see pman:OU5_3276) to include both succinate semialdehyde and glutarate semialdehyde as substrates. The other phenotypes are milder and might indicate a side pathway of conversion of citrulline and arginine to putrescine via ornithine decarboxylase. (KEGG_correct) succinate-semialdehyde dehydrogenase MQLKDTLLFRQQAFIDGAWVDADNGQTINVTNPATGEILGTVPKMGAAETRRAIEAADKALPAWRALTAKERANKLRRWFELIIENQDDLARLMTLEQGKPLAEAKGEIVYAASFIEWFAEEAKRIYGDVIPGHQPDKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPYSAFALAELAQRAGIPKGVLSVVTGSAGDIGSELTSNPIVRKLSFTGSTEIGRQLMAECAKDIKKVSLELGGNAPFIVFDDADLDKAVEGAIISKYRNNGQTCVCANRLYIQDSVYDAFAEKLKVAVAKLKIGNGLEEGTTTGPLIDGKAVAKVQEHIADALSKGATLLAGGKVMEGNFFEPTILTNVPKSAAVAKEETFGPLAPLFRFKDEAEVIAMSNDTEFGLASYFYARDLGRVFRVAEALEYGMVGVNTGLISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYLCLGI Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_11740 AO353_11740 DNA damage response protein (yhgF like) Conserved and mostly specific phenotype: important for resisting cisplatin. Also important for resisting ionizing radiation in E. coli transcription accessory protein MDSINSRIAEELGVRPQQVEAAVALLDEGSTVPFIARYRKEVTGSLDDTQLRHLEERLRYLRELDERRISILASIEEQGKLTPQLERDIKLADTKTRLEDLYLPYKQKRRTKGQIALEAGLGELADGLFNDPNLTPDTEAARFVNAEKGVADVKAALEGAKYILMERFAEDANLLDKLRNYLKQEATLSARVIAGKEEEGAKFRDYFEHDEPLKSMPSHRALAIFRGRNEGILSSALKVGDELPGTMHPCEGMIGQQFGIANQNRPADKWLGEVVRWTWKVKLYTHLETDLLGELRDGAETEAINVFAHNLHDLLLAAPAGPRATLGLDPGLRTGCKVAVVDATGKLLDHATVYPHVPHNKWDQTIAVLAALCAKHSVDLIAIGNGTASRETDKLAADLIKKYPAMKMTKVMVSEAGASVYSASELASKEFPDLDVSIRGAVSIARRLQDPLAELVKIDPKSIGVGQYQHDVSQLKLARGLDAVVEDCVNAVGVDVNTASVALLARISGLNATLAQNIVTHRDENGAFKTRAALKKVARLGEKTFEQAAGFLRVMNGDNPLDSSAVHPEAYPLVQRIAAETDRDIRSLIGDAAFLKRLDPKKYTDETFGLPTVTDILQELEKPGRDPRPEFKTAEFQEGVEDLKDLQLGMILEGVVTNVTNFGAFVDIGVHQDGLVHISALSEKFIKDPREAVKAGDVVKVKVMEVDIPRKRVGLSMRMSDTPGEKIDGARGARPGSAPRQSSNPAPRKETTAAAPGNNAMASLFANAKQLKKR Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_12275 AO353_12275 histidine permease Specific phenotype on histidine. 86% identical to PFLU0368, which is required for histidine utilization (PMCID: PMC1950622). SEED_correct proline-specific permease MQKPANGLKRGLSARHIRFMALGSAIGTGLFYGSASAIQMAGPAVLLAYLIGGAAVFMVMRALGEMAVHNPVAGSFGQYASTYLGPMAGFILGWTYAFEMVIVGMADVTAFGIYMGFWFPEVSRWIWVLGVVSIVGGLNLCNVKVFGEMEFWLSLLKVAAIVAMILGGFGIMLFGISTAPGQVTDISNLWTQGGFMPNGMGGLIASFAVVMFAFGGIEIIGVTAGEAKDPQHVLPRAINAVPLRILLFYVLTMLVLMSIFPWQQIGSQGSPFVQIFDKLGISSAATILNIVVITAAISAINSDIFGAGRMMFGLAQQGHAPKGFAHLSRNGVPWMTVVVMSVALLLGVLLNYLIPENVFLLIASIATFATVWVWLMILFTQVAMRRSMTAEQVAQLKFPVPFWPYAPMAAIAFMLFVFGVLGYFPDTQAALIVGVVWIVLLVLAYLMWVKPAAGQAALVARDPSFSNR Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_12285 AO353_12285 N-formylglutamate deformylase (EC 3.5.1.68) Specifically important for: L-Histidine. KEGG suggests formimidoyl-L-glutamate as the substrate, while SEED suggests N-formylglutamate. This gene is cofit with iminohydrolase (which produces N-formylglutamate) which suggests that the SEED annotation is correct. (SEED_correct) N-formylglutamate deformylase VDKVLNFKQGRVPLLISMPHAGVRLTPAVEAGLIPEAKSLPDTDWHIPTLYEFAAELGASTLAAEYSRFVIDLNRPSDDKPMYVGATTGLYPATLFDGVPLFREGLEPSAEERASYLEKVWTPYHSTLQQELARLKAEFGYALLFDAHSIRSVIPHLFDGKLPDFNLGTFNGASCDPQLASQLEAICARHTDYSHVLNGRFKGGHITRHYGNPAENIHAVQLELGQCTYMEEVEPFRYRPDLAAPTQVVLKELLQGLLAWGQKHYA Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_12420 AO353_12420 predicted FeS cluster maintenance protein PFam PF06155.8 (DUF971). conserved cofitness with yggX (AO353_12045), nfuA (AO353_21625) 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase MTTPLPTAIKLHKASKTLELQYAPDEIYHLSAEFLRVHSPSAEVQGHGKPILQFGKIGVGLTKVEPAGQYALKLTFDDGHDSGLFTWEYLYQLARRYDALWDDYLAELKAAGKTRDPNESVVKLML Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_13110 AO353_13110 putative transporter, required for glycine utilization PFam PF03458.9 (UPF0126). conserved specific phenotype of UPF0126 hypothetical protein MLLMLYLIAITAEAMTGALSAGRRGMDWFGVVLIACVTALGGGSVRDVLLGHYPLTWVKHPEYLVLTSAAAMLTVFTARWMRHLRSLFLVLDAVGLVAFTLIGCMIALETGHGMLVASVSGVITGVFGGILRDIFCNDIPLIFRRELYASVSFAAAWCYMLCLYLQLPDEQAILITLFGGFLLRLLAIRFHWEMPKFVYNDEA Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_13585 AO353_13585 predicted copper homeostasis protein PFam PF11162.4 (DUF2946). conserved cofit with TonB-dependent copper receptor (AO353_13570) and perhaps with copper chaperone CopZ (AO353_13580) hypothetical protein MSRQRLAFAWIACFAVLFNMLAMPMSGAMAQGASQSPAEQLLWGSFCSSSGTKMVAISLGKLEQKAPSNDDHSNMQHCWCCSGSAPLMALPGHVPQLYFARFEANRSRPAPTLDIPTPRQQWPSLNPRASPLV Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_15995 AO353_15995 trehalose-specific PTS system, I, HPr, and IIA components Specific phenotype on trehalose. The IIB/IIC components are provided by AO353_15980. 45% similar to a NAG PTS system (PA3760, PMC:PMC2542419) PTS mannose transporter subunit IIC MTLTQPLQLLAPLSGVLMPLDHVPDPVFASRVIGDGLCIDPTSQVLCAPLAGVVSNLQHSGHAISITDDSGVQVLLHIGLDTVNLKGQGFSALVEQGQRVEAGQPLIEFDADYVALHARSLLTLMLVVSGEPFSLLTPDSGLVACAQPVLRLSLGDPRTVVAQEEGEALFSKPVHLPNPNGLHARPAAVFAQAAKGFAASICLHKQQDSANAKSLVAIMALQTVHGDALQVSAVGEDAELAISTLAQLLADGCGEAVTPVAVVAPVVEAQEVSTKLLRGVCASAGSAFGYVVQVAERTLEMPEFAADQQLERESLERALMHATQALQRLRDNAAGEAQADIFKAHQELLEDPSLLEQAQALIAEGKSAAFAWNSATEATATLFKSLGSTLLAERALDLMDVGQRVLKLILGVPDGVWELPDQAILIAEQLTPSQTAALDTGKVLGFATVGGGATSHVAILARALGLPAVCGLPLQVLSLASGTRVLLDADKGELHLDPAVSVIEQLHAKRQQQRQRHQHELENAARAAVTRDGHHFEVTANVASLAETEQAMSLGAEGIGLLRSEFLYQQRSVAPSHDEQAGTYSAIARALGPQRNLVVRTLDVGGDKPLAYVPMDSEANPFLGMRGIRLCLERPQLLREQFRAILSSAGLARLHIMLPMVSQLSELRLARLMLEEEALALGLRELPKLGIMIEVPAAALMADLFAPEVDFFSIGTNDLTQYTLAMDRDHPRLASQADSFHPSVLRLIASTVKAAHAHGKWVGVCGALASETLAVPLLLGLGVDELSVSVPLIPAIKAAIREVELSDCQAIAHQVLGLESAEQVREALSVQQQAMVETSQVLES Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_16120 AO353_16120 D-alanine and L-alanine transporter Specific phenotype on D-alanine as the carbon source. Also important for utilizing L-alanine as a carbon source. Both of these phenotypes are conserved. For D-alanine as a nitrogen source, there is a mild phenotype, and it may be partly redundant with another amino acid transporter (AO353_04615:04600). Sometimes annotated as a glycine transporter, but neither it nor its orthologs are important on glycine. D-alanine/D-serine/glycine permease MTVGNHLPHGETAQGGPLKRELGERHIRLMALGACIGVGLFLGSAKAIEMAGPAIMLSYIIGGLAILVIMRALGEMAVHNPVAGSFSRYAQDYLGPLAGFLTGWNYWFLWLVTCVAEITAVAVYMGIWFPEVPRWIWALAALVSMGSINLIAVKAFGEFEFWFALIKIVTIIAMVVGGVGVIAFGFGNDGVALGISNLWSHGGFMPNGVQGVLMSLQMVMFAYLGVEMIGLTAGEAKNPQKTIPNAIGSVFWRILLFYVGALFVILSIYPWNEIGTQGSPFVMTFERLGIKTAAGIINFVVITAALSSCNGGIFSTGRMLYSLAQNGQAPAGFAKTSNGVPRRALLLSIGALLLGVLLNYLVPEKVFVWVTAIATFGAIWTWVMILLAQLKFRKGLSPAERAALKYRMWLYPVSSYLALAFLVMVVGLMAYFPDTRVALYVGPAFLVLLTVLFYVFKLQPTGVPQAAVRTAS Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_18575 AO353_18575 tyrosine aminotransferase (EC 2.6.1.57) Specifically important for: L-Phenylalanine. Phenylalanine is catabolized via tyrosine and transamination to 4-hydroxyphenylpyruvate, so tyrosine is the relevant substrate. (KEGG_correct) aromatic amino acid aminotransferase MHFDAIGRVPGDPILGLMEAYAQDSNPCKFDLGVGVYKDAQGLTPIPQSVKLAELRLVDRQTTKTYIGGHGDPAFGKVINELVLGADSALIAEQRVGATQTPGGTGALRLSADFIAHCLPGRGIWLSNPTWPIHETIYATAGLKVSHYPYVGSDNRLDVEAMLATLNLIPKGDVVLLHACCHNPTGFDLSHDDWRRVLEVVRSRELLPLIDFAYQGFGDGLEQDAWAVRLFAAELPELLITSSCSKNFGLYRDRTGALIVCAKDAEKLVDIRSQLANIARNLWSTPPDHGAAVVATILGDPELKQLWADEVEAMRLRIAQLRSGLVEALEPHGLGERFAHIGVQRGMFSYTGLTPAQVKNLRDHHSVYMVSSGRANVAGIDATRLDLLAQAFADVCK Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_19235 AO353_19235 DNA damage response gene with a putative DNA binding domain (PA0922-like) Conserved and specific phenotype: important for resisting cisplatin. Also some homologs are regulated by LexA. transcriptional regulator MVNVEQLKASVNRMSADVVQEAVLELRLDGLVTEGKTPFNKLHFNTCFAEIEALFQRAGYHRQLDVVGYQGLLYALYDPGRWEAVDVLRWLKEFTEAAAQRVSLTA Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_20845 AO353_20845 uridine/adenosine nucleosidase (EC 3.2.2.3; EC 3.2.2.7) Important on adenosine and uridine; annotated by SEED as for uridine and inosine; fitness defect on uridine is subtle but is confirmed by observations for close homologs (SEED_correct) nucleoside hydrolase MYRYAQRLHHLIRSLLLLSLLTATGAHAAEKIDLIIDTDPGADDVVALLFALASPEELNIRALTTVAGNVRLDKTSRNARLAREWAGREDVPVYAGAPKPLMRTPIYAENIHGKEGLSGVTVHEPKKGLAKGDAVSYLIDTLRAAKPHSITIAMLGPQTNLALALIQDPEITQGIKEVVIMGGAHFNGGNITPVAEFNLFADPHAAEVVLKSGVKLTYLPLDVTHKILTSDARLKQIAALNNNASKLVGDILNEYVKGDMEHYGIPGGPVHDATVIAYLLKPELFTGRAVNVVVDSREGPTFGQTVVDWYDGLKAPKNAFWVANGDAQGFFDLLTARLARLK Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_21385 AO353_21385 m-Inositol ABC transporter, ATPase component (itaA) Specific phenotype on m-Inositol and 63% identical to SMb20173 or itaA, which also has this function (see PMC2597717). The periplasmic substrate-binding component (AO353_21380) is not included in this table because it was annotated correclty in both resources. SEED_correct D-ribose transporter ATP-binding protein MFASATASSIPLVGVQPNAIPVDEPYLLEIINVSKGFPGVVALSDVQLRVRPGSVLALMGENGAGKSTLMKIIAGIYQPDAGELRLRGKPVTFDTPLAALQAGIAMIHQELNLMPHMSIAENIWIGREQLNGFHMIDHREMHRCTAQLLERLRINLDPEEQVGNLSIAERQMVEIAKAVSYDSDILIMDEPTSAITDKEVAHLFSIIADLKAQGKGIIYITHKMNEVFSIADEVAVFRDGAYIGLQRADSMDGDSLISMMVGRELSQLFPVREKPIGDLLMSVRDLRLDGVFKGVSFDLHAGEILGIAGLMGSGRTNVAEAIFGITPSDGGEICLDGQPVRISDPHMAIEKGFALLTEDRKLSGLFPCLSVLENMEMAVLPHYAGNGFIQQKALRALCEDMCKKLRVKTPSLEQCIDTLSGGNQQKALLARWLMTNPRILILDEPTRGIDVGAKAEIYRLISYLASEGMAVIMISSELPEVLGMSDRVMVMHEGDLMGTLDRSEATQERVMQLASGMSVRH Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_21390 AO353_21390 m-Inositol ABC transporter, permease component (iatP) Specific phenotype on m-Inositol and 71% identical to SMb20174 or itaP, which also has this function (see PMC2597717). The periplasmic substrate-binding component (AO353_21380) is not included in this table because it was annotated correclty in both resources. SEED_correct ABC transporter MNAILENKPAMAPAKSRRRLPTELSIFLVLIGIGLVFEMFGWIVRDQSFLMNSQRLVLMILQVSIIGLLAIGVTQVIITTGIDLSSGSVLALSAMIAASLAQTSDFARAVFPSLTDLPVWIPVIAGLGVGLLAGAINGSIIAVTGIPPFIATLGMMVSARGLARYYTEGQPVSMLSDSYTAIGHGAMPVIIFLVVAVIFHIALRYTKYGKYTYAIGGNMQAARTSGINVKRHLVIVYSIAGLLAGLAGVVASARAATGQAGMGMSYELDAIAAAVIGGTSLAGGVGRITGTVIGALILGVMASGFTFVGVDAYIQDIIKGLIIVIAVVIDQYRNKRKLKR Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_21740 AO353_21740 D-glucosaminate dehydratase (EC 4.3.1.9) Specifically important for: D-Glucosamine Hydrochloride. This enzyme had not previously been linked to a gene. This is the second step in catabolism of glucosamine, and the 'beta' form of the enzyme was expected to be PLP-dependent and about this size. Iwamoto et al (2003) purified a non-specific 'alpha' enzyme for this reaction (PMID: 12686150) amino acid deaminase MSSALNIAAVEKGAGQPGANLVRDVSLPALVLHREALEHNIHWMQAFVSHSGAELAPHGKTSMTPSLFRRQLEAGAWGITLATVVQTRAAYAHGVRRVLMANQLVGAPNMALIAELLADPSFDFYCMVDHPDNVADLGVFFAARGLRLNVMIEYGVVGGRCGCRSEAEVLALAEAIKAQPGLALTGIEGYEGVIHGDQAVSGIREFAASLVRLAVQLQDSGAFAISKPIITASGSAWYDLIAESFEAQNAGGRFLSVLRPGSYVAHDHGIYKEAQCCVLDRRSDLHEGLRPALEVWAHVQSLPEPGFAVIALGKRDVAYDAGLPVPLLRYRAGVLPAVGDDVSACTVTAVMDQHAFMTVAPGVQLRVGDIISFGTSHPCLTFDKWRTGCLVDEQLNVIESMETCF Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_24750 AO353_24750 DNA damage response nuclease Conserved and specific phenotype: important for resisting cisplatin. Contains a VRR-NUC domain that is predicted to have nuclease activity. nuclease VTVNPLEDPFYYLNNFQQVLAWLEQRYADVLSAEEQQFIVDFGQLPRASQALLVRMVMRKGEHFRLGKLHYAEIGEIASAAEPLLTLGWVDEQAPLSIEQLFEVLLKPEILQCFSTAIEQPKAKKSEWLAALSEQFTEAQSFKNWCPTLDDRLLSLTTMDLCDRLRLMFFGNLYQDWSEFVLADLGIFTYEKVEFCAESRGLRSRDDVEAFLYLHDCQLRFEAGEALEQVVEQIQALQTANPWLERRRAKLLFQIGQHCERIADFPAALTIYRECAYPGARLRLIRVLERCAEFQLALELATHAEHAPESAAEQQQLSRVLPRLRRKLGGPPAPRVKTREVERLDLSLSRIDPALSVEFYVQAHLDEPTAPVHYVENSLINSLFGLLCWPAIFAPLPGAFFHPFQRGPVDLLSEDFHSRRADLFQACLAELDDGRYAETIRQRFRAKSGVQSPFVFWGVLTEELLEQALDCLPAEHLKHWFNRLLLDIKANRAGMPDLIQFWPQHKTYRMIEVKGPGDRLQDNQLRWLEFCHQHQMPIAVCYVQWAEHEA Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_26685 AO353_26685 cobalt efflux pump Strong phenotypes on citrate (as a carbon source) but also on cobalt stress. The citrate phenotype may be due to iron deprivation (via chelation by the citrate) leading to heavy metal stress. The cobalt phenotype is more conserved. It is possible that nickel is also a substrate of this efflux pump, as a slight defect in nickel stress was observed, and this protein is 49% identical to the cobalt and nickel exporter dmeF (Atu0891) of Agrobacterium tumefaciens (PMID:27235438). AO353_26685 is annotated as performing zinc or cadium efflux as well (czcD), but unfortunately, we do not have data for those heavy metal stresses. However a role in zinc stress seems doubtful, as a close homolog in strain GW456-L13 is not important for resisting zinc. cation transporter MRSTPQVSRYSHDHMFLGATHDENARRTLWVVALTFVMMVGEIIAGYITGSMALLADGFHMATHVGALGITAIAYGFARRNAGNARYSFGTGKVGDLAGFASAMVLGLVSIFIAVESVMRLFQPTTVAFTEATLIAVLGLAVNIVSALLLAGNSAHHDHGHGHGHGHGHGHGHHHDNNLRSAYVHVLADAMTSVLAIAALLAGRYLGWVWLDPVMGIVGAIVIANWAYGLMRDSAAVLLDTTDEHVAAEVRELLESTGDVSITDLHVWRVGPQARAAIVSVVTSAAVTADTIRERLAPVHELSHLTVEYRNA Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_29305 AO353_29305 Gamma-glutamyl-GABA hydrolase (EC 3.5.1.94) Specifically important for: Putrescine Dihydrochloride. part of the gamma-glutamyl-putrescine pathway for degrading putrescine (SEED_correct) gamma-glutamyl-gamma-aminobutyrate hydrolase MALKPLIGVTACVKQIGLHPYHVSGDKYLRAVSVAALGLPVVIPSLGELTEIDELLAHLDGLLLTGSPSNVEPFHYQGPASAPGTDHDPARDSTTLPLLRAAIAAGVPVLGICRGFQEMNVAFGGSLHQKVHELPGMLDHREADHPDLAVQYAPAHAVSVQPGGVFQALELPPVFQVNSIHSQGIDRLAPGLRAEAIAPDGLIEAISVEHSKAFALGVQWHPEWQVLANPPYLSIFQAFGDACRQRAALRNTR Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_00010 AO356_00010 ABC transporter for D-Sorbitol, ATPase component Specific phenotype on D-Sorbitol. ABC transporter ATP-binding protein MATLKIENLKKGFEGLSIIKGIDLEVKDKEFVVFVGPSGCGKSTLLRLIAGLEDVTSGTIELDGRDITEVTPAKRDLAMVFQTYALYPHMTVRKNLSFALDLAGEKKPDVERKVAEAARILELGSLLDRKPKQLSGGQRQRVAIGRAIVRNPKIFLFDEPLSNLDAALRVQTRLELSRLHKELQATMIYVTHDQVEAMTLATKVVVLNAGRIEQIGSPLELYHHPANLFVAGFLGTPKMGFLQATVHAVHASGVEVRFASGTTLLIPRDSSALSVGQSVTIGIRPEHLTLGAEGQVLVTTDVTERLGSDTFCHVNVDSGESLTVRVQGDCEVPYAARRYLTLDVAHCHLFDESGLSVSPAASRAA Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_00015 AO356_00015 ABC transporter for D-Sorbitol, permease component 1 Specific phenotypes on D-Sorbitol; D-Sorbitol. (no phenotype on mannitol) sugar ABC transporter permease MMTLKQSRSLQSVLLGTLAWVTALLLFFPIFWMVLTSFKTEIDAFATPPQFIFMPTLENYLHIQERSDYFHFAWNSVLISFSATALCMLIAVPAAYSMAFYETKRTKQTLLWMLSTKMLPPVGVLMPIYLLAKGAGLLDTRIALIVIYTLINLPIVVWMIYTYFKDIPREILEAARLDGATLGQEMLRVLLPISKGGLASTMLLSMILCWNEAFWSLNLTSSSAAPLTALIASYSSPEGLFWAKLSAVSTLACAPILIFGWISQKQLVRGLSFGAVK Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_00020 AO356_00020 ABC transporter for D-Sorbitol, permease component 2 Specific phenotypes on D-Sorbitol; D-Sorbitol. (no phenotype on mannitol) sugar ABC transporter permease MNTSIIRAQLAASAPSRARRLINPGWFLVSPSVALLLLWMIVPLAMTVYFSVIRYNLLNPGENEFVGLENFAYFVTDSGFLPGALNTLILVGSVLLISVIFGVLIAALLEASEFFGRGIVRVLLISPFFIMPTVGSLIFKNLIFHPVSGILAAVWKFFGAQPVDWLAHYPLFSIIVIVSWQWLPFAILLLMTAMQSLDQEQKEAARLDGAGALAIFWHLTLPHLARPIAVVVMIETIFLLSVFAEIFTTTNGGPGFASTNLAYLIYNQALVQFDVGMASAGGLIAVVIANIAAIVLVRMIGKNLTDKA Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_00025 AO356_00025 ABC transporter for D-Sorbitol, periplasmic substrate-binding component Specific phenotype on D-Sorbitol. sugar ABC transporter substrate-binding protein MKITNALILSTGLSFALASHAAETLTIATVNNGDMIRMQRLSKVFEQQHPDIKLNWVVLEENVLRQRLTTDIATQGGQFDVLTIGTYETPMWGAKNWLEPMKDLPAGYDVDDIFPAVRQGLSVNDTLYALPFYGESTITYYRTDLFKAAGLTMPGQPTWSQLGEFAAKLNDPSKDQYGMCLRGKAGWGENMALLTTMANAFGARWFDEKWQPELNGPEWKAAATFYVDTLKKYGPPGVSSNGFNETLALFNSGKCAIWVDASVAGSFTTDKEQSRVVDSVGFAPAPIEVTDKGSSWLYAWSLAIPATSKHKEAAKSFVTWATSKEYIQLVTDKDGITNVPPGTRISTYSDAYLKAAPFAQVTLQMMKHADPSQPSAKPVPYVGIQYVVIPEFQSIGTSVGKLFSAALTGQMSVEQALASAQSTTEREMKRAGYPKK Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_00450 AO356_00450 D-glucosaminate dehydratase (EC 4.3.1.9) Specifically important for: D-Glucosamine Hydrochloride. This enzyme had not previously been linked to a gene. This is the second step in catabolism of glucosamine, and the 'beta' form of the enzyme was expected to be PLP-dependent and about this size. Iwamoto et al (2003) purified a non-specific 'alpha' enzyme for this reaction (PMID: 12686150) amino acid deaminase MSSVIPNAGVEKGAATVGAHLLKDVSLPALVLHRAALEHNIRWMQAFVTDSGAELAPHGKTSMTPALFRRQLDAGAWGLTLATAVQTRAAYAHGVRRVLMANQLVGTPNMALIADLLADPAFEFHCMVDHPDNVADLGAFFASRGMKLNVMIEYGVVGGRCGCRTEAEVLALAEAIRSQPALALTGIEGYEGVIHGDHAISGIRAFAASLVRLAVQLQDDDAFAIDKPIITASGSAWYDLIAESFEAQNAHGRFLSVLRPGSYVAHDHGIYKEAQCCVLERRSDLHEGLRPALEVWAHVQSLPEPGFAVIALGKRDVAYDAGLPVPLKRYTPGSDSVPGDDVSGCKVTAVMDQHAFMSVAAGVELRVGDIIAFGTSHPCLTFDKWRVGCLVDEQLRVVESMETCF Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_00465 AO356_00465 ABC transporter for D-Glucosamine, putative ATPase component This is presumably the ATPase component of the operon, but lacks fitness data. ATP-binding protein MTDISTPSNTQPLLDIRGLRKQYGPLEVLKGVDLSMQRGNVVTLIGSSGSGKTTLLRCVNMLEEFQGGQIVLDGESIGYDDIDGKRVRHPEKLIARHRAMTGMAFQQFNLFPHLTALQNVTLGLLKVKKLPKDEAVALAEKWLERVGLLERRDHFPGQLSGGQQQRVAIARAIAMNPSLMLFDEVTSALDPELVGEVLNVIKGLAEDGMTMLLVTHEMRFAFEVSDKIVFMNQGRIEEQGPPKELFERPQSPRLAEFLKNTRF Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_00470 AO356_00470 ABC transporter for D-Glucosamine, permease component 1 Specific phenotypes on D-Glucosamine Hydrochloride. Detrimental on D-serine as N source ABC transporter permease MYESPSWLHELWVARDTLWAGFLTSVQCSLLAIVLGTLIGLVAGLVLTYGRTWMRAPFRFYVDLIRGTPVFVLVLACFYMAPALGWQIGAFQAGVLGLTLFCGSHVAEIVRGALQALPRGQMEASQAIGLTFYQSLGYVLLPQALRQILPTWVNSSTEIVKASTLLSVIGVAELLLSTQQIIARTFMTLEFYLFAGFLFFIINYAIELLGRHIEKRVALP Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_00475 AO356_00475 ABC transporter for D-Glucosamine, permease component 2 Specific phenotypes on D-Glucosamine Hydrochloride. Detrimental on D-serine as N source amino acid ABC transporter permease MNYQLNFAAVWRDFDTLLAGLGLGLSLALVSIAIGCVIGLAMAFALLSKHRVLRVLASVYVTVIRNTPILVLILLIYFALPSLGIRLDKLPSFVITLSLYAGAYLTEVFRGGLLSIHKGQREAGLAIGLGEWQVKAYVTVPVMLRNVLPALSNNFISLFKDTSLAAAIAVPELTYYARKINVESYRVIETWLVTTALYVAACYLIAMVLRYFEQRLAIRR Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_00480 AO356_00480 ABC transporter for D-Glucosamine, periplasmic substrate-binding component Specific phenotype on D-Glucosamine Hydrochloride. ABC transporter substrate-binding protein MQRRPSLFKACVFLFAATTAAMGVAQAADSKLDSVLQRGKLIVGTGSTNAPWHFQGADGKLQGFDIDIARMVAKGLFNDPEKVEFVVQSSDARIPNLLTDKVDMSCQFITVTASRAQQVAFTLPYYREGVGLLLPANSKYKEIEDLKAAGDDVTVAVLQNVYAEELVHQALPKAKVDQYDSVDLMYQAVNSGRADAAATDQSSVKYLMVQNPGRYRSPAYAWSPQTYACAVKRGDQDWLNFVNTTLHEAMTGVEFPTYAASFKQWFGVELPSPAIGFPVEFK Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_00560 AO356_00560 required for sulfate utilization, putative electron transport protein for sulfite reductase PFam PF06073.8 (DUF934). conserved cofitness with sulfite reductase, auxotrophic oxidoreductase MQRIIKNNEVIDETWHLLPKDATLDGISNCDDLIVPLALWRDHAHALKARDGGLGVWLDADEEAEEIGDDANQLQVIALNFPAFTDGRSYSNARLLRDRYGFKGELRAIGDVLRDQLFYMRRCGFDAFALRADKDPYEALESLKDFSVTYQAATDEPLPLFRRR Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_00940 AO356_00940 uridine/adenosine nucleosidase (EC 3.2.2.3; EC 3.2.2.7) Specifically important for: Uridine. Also important on adenosine. Annotated by SEED as acting on uridine and inosine, and the fitness data suggests that it might also act on inosine (subtle phenotype) nucleoside hydrolase MHRYAEKMHQLIRSLLLLSLITATSAQAAEKIDLIIDTDPGADDVVALLFALASPEELHIRALTTVAGNVRLDKTSRNARLAREWAGREDVPVYAGAPKPLMRTPIYAENIHGKEGLSGVTVHEPKKGLAEGNAVNYLIDTLKAAKPHSITIAMLGPQTNLALALVQEPDIVQGIKEVVIMGGAHFNGGNITPVAEFNLFADPQAAEVVAKSSVKLTYLPLDVTHKILTSEARLKQIAALNNNASKLVGDILNEYVKGDMEHYGMTGGPVHDATVIAYLLKPQLFTGRSVNVVVDSREGPTFGQTIVDWYDGLKAPKNAFWVENGDAQGFFDLLTERLARLK Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_00980 AO356_00980 DNA damage resistance protein PFam PF07867.7 (DUF1654). Conserved (somewhat specific) phenotype for cisplatin resistance, in operon with endonuclease, and close homologs are regulated by LexA hypothetical protein MPTVKYCMPVQLNKDNPVATPSAATTPLDSYTRLGLRVSKIINAPTAQKAKAALIFRLPDEPVDEWERLLEEIDENDNVTLAYRDDGGVQVFWVVPKED Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_01105 AO356_01105 putative hydrolase, required for lysine catabolism PFam PF07063.9 (DUF1338). This gene is specifically important for utilizing lysine, and this phenotype is conserved. It might be the decarboxylating 2-oxoadipate hydrolase of the D-lysine oxidase pathway, which has not been linked to a gene, or the crotonyl-CoA hydratase in the glutaryl-CoA degradation pathway. hypothetical protein MSFVSPDLIRQRFSRAMSDMYRDEVPLYGALMKLVEHTNAQVLSEQPQLAEHLRSTGELERLDLERHGAIRVGTAAELATLGRLFAVMGMQPVGYYDLTPAGVPVHSTAFRAVHESALQVSPFRVFTSLLRLELIENSELRAFAESVLAKRQIFTPGALALIDLAERQGGLTQAQAEDFVLQALETFRWHHSATVTAEQYRQLSAQHRLIADVVAFKGPHINHLTPRTLDIDIVQARMPVHGITPKAVIEGPPRRQCPILLRQTSFKALDEPVAFTDQPQAQGSHSARFGEIEQRGAALTPKGRALYDQLLNAARDALGAFPNEANAERYNALMTEHFVAFPDNHDELRQQALAYFRYFPTPKGLAAKGTLEPAASLEHLLEQQYLRAEPLVYEDFLPVSAAGIFQSNLGDAAQSHYAGQSNRQAFEAALGRATIDELGLYAQTQQRSIDECRAALGV Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_03600 AO356_03600 putative efflux pump, required for thallium (I) resistance PFam PF02694.11 (UPF0060). conserved specific phenotype of UPF0060 hypothetical protein MLNYLWFFLAALFEIAGCYAFWMWLRQGKSAWWIAPALLSLTLFALLLTRIEATYAGRAYAAYGGIYIIASIGWLAVVERVRPLGSDWIGVALCVLGASVILFGPRLSAS Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_05495 AO356_05495 ABC transporter for L-Lysine, periplasmic substrate-binding component Specific phenotype on L-Lysine. Note that this organism has a second ABC transporter that is also important for lysine utilization, which is not explained. ABC transporter substrate-binding protein MKKALLTLSALALCMAAGVATAKEYKELRFGVDPSYAPFESKAADGSLVGFDIDLGNAICAELKVKCKWVESDFDGMIPGLKANKFDGVISSMTVTPAREKVIDFSSELFSGPTAYVFKKGSGLSEDVASLKGKTIGYEQGTIQEAYAKAVLDKAGVKTQAYQNQDQVYADLTSGRLDAAIQDMLQAELGFLKSPKGEGYEVSKPVDSELLPAKTAIGIKKGNSELKALLDKGIKALHDDGKYAEIQKKHFGDLNLYSGK Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_05500 AO356_05500 ABC transporter for L-Lysine, permease component 1 Specific phenotypes on L-Lysine; L-Lysine. Note that this organism has a second ABC transporter operon that is important for lysine utilization, which is not explained. amino acid ABC transporter permease MFEQLLQNLGLSAFSLQGFGPLLMQGTWMTIKLSALSLLLSVLLGLLGASAKLSRVKLLRIPAQLYTTLIRGVPDLVLMLLIFYSLQTWLTSFTDFMEWEYIEIDPFGAGVITLGFIYGAYFTETFRGAILAVPRGQVEAATAYGLKRGQRFRFVVFPQMMRFALPGIGNNWMVMLKATALVSIIGLADLVKAAQDAGKSTYQLFYFLVLAALIYLLITSASNFILRWLERRYAAGAREAVR Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_05505 AO356_05505 ABC transporter for L-Lysine, permease component 2 Specific phenotypes on L-Lysine; L-Lysine. Note that this organism has a second ABC transporter operon that is also important for lysine utilization, which is not explained. amino acid ABC transporter permease MIELLQEYWRPFLYSDGVNITGLAMTLWLLSASLLIGFVVSIPLSIARVSPKFYVRWPVQFYTYLFRGTPLYIQLLICYTGIYSIAAVRAQPMLDSFFRDAMNCTILAFALNTCAYTTEIFAGAIRSMNHGEVEAAKAYGLTGWKLYAYVIMPSALRRSLPYYSNEVILMLHSTTVAFTATVPDVLKVARDANSATFLTFQSFGIAALIYLTVTFALVGLFRLAERRWLAFLGPTH Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_05515 AO356_05515 ABC transporter for L-Lysine, ATPase component Specific phenotype on L-Lysine. Note that this organism has a second ABC transporter operon that is also important for lysine utilization, which is not explained. amino acid transporter MYKLTIEGLHKSYGEHEVLKGVSLKAKTGDVISLIGASGSGKSTFLRCINFLEQPNDGAMTLDGQPVQMIKDRHGMHVADADELQRIRTRLAMVFQHFNLWSHMTVLENITMAPRRVLGVSKQEADDRARRYLDKVGLPARVAEQYPAFLSGGQQQRVAIARALAMEPEVMLFDEPTSALDPELVGEVLKVIQGLAEEGRTMIMVTHEMSFARKVSNQVLFLHQGLVEEEGAPEDVLGNPKSERLKQFLSGNLK Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_07550 AO356_07550 L-lactate and D-lactate permease (lctP family) This gene is often annotated as a L-lactate transporter but has a specific phenotype on D-lactate as well. Although it is difficult to rule out polar effects on the lactate dehydrogenase genes downstream, this gene's phenotype on D-lactate is conserved and is observed on both strands, and no other D-lactate transporter was identified by the mutant fitness data. (There is a zinc ABC transporter with a specific defect on D-lactate, but it is very similar to znuABC of P. aeruginosa, i.e. AO356_11480 is 65% identical to PA5498, so it is unlikely to be a lactate transporter.) Furthermore, the annotation as lactate permease seems to be derived from E. coli glcA or yghK, which transports both isomers of lactate (PMID:11283302). (KEGG_correct) L-lactate permease MQTWQQLYSPLGSLGLSALAAVIPIVFFFLALAVFRLKGHVAGSITLALAIAVAIFAFNMPADMAFAAAGYGFAYGLWPIAWIIVAAVFLYKLTVKSGQFEVIRSSVLSITDDQRLQVLLIGFCFGAFLEGAAGFGAPVAITAALLVGLGFNPLYAAGLCLIANTAPVAFGALGIPIIVAGQVTGIDAFKIGAMTGRQLPLLSLFVPFWLVFMMDGLRGVRETWPAALVAGLSFAITQYFTSNFIGPELPDITSALASLISLTLFLKVWQPKRTAGAQIAGATSSATVTASVGGFGQPRSTVASPYSLGEIIKAWSPFLILTVLVTIWTLKPFKAMFAAGGSMYGWVFNFAIPHLDQMVIKVAPIVINPTAIPAVFKLDPISATGTAIFFSALISMLVLKINIKTGLTTFKETLFELRWPILSIGMVLAFAFVTNYSGMSSTMALVLAGTGAAFPFFSPFLGWLGVFLTGSDTSSNALFSSLQATTAHQIGVNDTLLVAANTSGGVTGKMISPQSIAVACAATGLVGKESDLFRFTLKHSLFFATIVGLITLAQAYWFTGMLVH Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_08325 AO356_08325 predicted copper homeostasis protein PFam PF11162.4 (DUF2946). conserved cofit with TonB-dependent copper receptor (AO356_08330), and cofit with copper chaperone CopZ (AO356_08320) hypothetical protein MSQTRGSWISLFAMLMIFIGPLISQSMPMDQRMPASMNMSMSMDMSMDMPAGVHAEHEASTDEHCPPQREHHALWEKCGYCSLLFNCPALTGGQGFATFETPLANTYTAPSPRLGHARTAFFPGARTRAPPLDA Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_09590 AO356_09590 N-formylglutamate deformylase (EC 3.5.1.68) Specifically important for: L-Histidine. KEGG suggests formimidoyl-L-glutamate as the substrate, while SEED suggests N-formylglutamate. This gene is cofit with iminohydrolase (which produces N-formylglutamate) which suggests that the SEED annotation is correct. (SEED_correct) N-formylglutamate deformylase VEKVLNFKQGRVPLLVSMPHAGLRLTPAVKAGLIPEAQSLPDTDWHIPQLYEFANELGASTLAAEYSRFVVDLNRPSDDKPMYVGATTGLYPATLFDGVPLFREGLEPSAEERATYLQQVWMPYHQALRQELARLKAEFGYALLFDAHSIRSVIPHLFDGKLPDFNLGTFNGASCDPTLASQLEAICARHGQFTHVLNGRFKGGHITRHYGNPAEDIHAVQLELCQSTYMEEFEPFNYRPDLAAPTQVVLRELLEGFLAWGQKTYKH Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_09610 AO356_09610 ABC transporter for L-Histidine, ATPase component Specific phenotype on L-Histidine. This gene cluster also includes a permease of the nucleobase-cation-symport family (AO356_09625) that is important for histidine utilization but whose role is unclear. (SEED_correct) hypothetical protein MSNAAISKIEVKNVFKIFGNRSKEALELIRQNKTKDQVLAETGCVVGVNDLSLSIGTGEIFVIMGLSGSGKSTLVRHFNRLIDPTSGAILVDGEDILQLDMDALREFRRHKISMVFQSFGLLPHKSVLDNVAYGLKVRGESKQVCAERALHWINTVGLKGYENKYPHQLSGGMRQRVGLARALAADTDIILMDEAFSALDPLIRAEMQDQLLELQKTLHKTIVFITHDLDEAVRIGNRIAILKDGKLIQVGTPREILHSPADEYVDRFVQRRAAVV Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_09615 AO356_09615 ABC transporter for L-Histidine, permease component Specific phenotypes on L-Histidine. ABC transporter permease MFPESFTFSIADWVNGWVDSLVTNYGDVFRHISDTLLWAIVNLEGLLRMAPWWLMLAIVGGIAWHATRKVLATAVIVGLLFLVGAVGLWDKLMQTLALMLVATLISVLIGIPLGILSARSNRLRSVLMPLLDIMQTMPSFVYLIPVLMLFGLGKVPAIFATVIYAAPPLIRLTDLGIRQVDGEVMEAINAFGANRWQQLFGVQLPLALPSIMAGINQTTMMALSMVVIASMIGARGLGEDVLVGIQTLNVGRGLEAGLAIVILAVVIDRITQAYGRPRHEVSK Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_09620 AO356_09620 ABC transporter for L-Histidine, periplasmic substrate-binding component Specific phenotype on L-Histidine. This gene cluster also includes a permease of the nucleobase-cation-symport family (AO356_09625) that is important for histidine utilization but whose role is unclear histidine ABC transporter substrate-binding protein MKSNKTLLTTLLSMGLLASAGATQAAGWCESGKPVKFAGLNWESGMLLTDVLQVVLEKGYDCKTDSLPGNSITMENALSSNDIQVFAEEWVGRSEVWNKAEKAGKVVGVGAPVVGAIEGWYVPRYVVEGDAKRKLEAKAPGLKNIADLGQYAAVFKDPEEPSKGRFYNCPAGWTCELDNSEMLKSYGLEKTYTNFRPGTGPALDAAVLSSYKRGEPILFYYWSPTPLMGQVDLVKLEEKPGVDKSVSIKVGLSKTFHDEAPELVAVLEKVNLPIDILNQNLGRMAKERIESPKLAKIFLKEHPEVWHAWVSEDAAKKIDAAL Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_09635 AO356_09635 histidine utilization regulatory protein hutD Specifically important for: L-Histidine. Believed to prevent overexpression of the hut operon (not an enzyme) (PMC:1950622) hypothetical protein MSQLKVLRAADYPRMPWKNGGGSTEEITRDAGTGLEGFGWRLSIADIGESGGFSTFAGYERIISVLQGDGMTLNVDGQATGPLRPLDPFAFSGESHVHCTLLGGPIRDFNLIYAPQRYRARLQWVGGQQRFFSEAETLLVFSAAPGLTIRIGESAVILGLYDCLQLSGNTGLLDITSHGQCCVIELTAR Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_09895 AO356_09895 ABC transporter for L-Lysine, ATPase component Has weaker phenotypes on lysine than the other components, but is in an apparent operon and has the correct domain. Note that this organism has a second ABC transporter operon that is also important for lysine utilization, which is not explained. amino acid transporter MAQATPALEIRNLHKRYGQLEVLKGVSLTARDGDVISILGSSGSGKSTFLRCINLLENPNQGQILVAGEELKLKAAKNGELVAADGKQINRLRSEIGFVFQNFNLWPHMSVLDNIIEAPRRVLGQSKAEAVEVAEALLAKVGIADKRHAYPAELSGGQQQRAAIARTLAMQPKVILFDEPTSALDPEMVQEVLSVIRALAEEGRTMLLVTHEMGFARQVSSEVVFLHQGLVEEQGSPQQVFENPLSARCKQFMSSNR Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_09900 AO356_09900 ABC transporter for L-Lysine, periplasmic substrate-binding component Specific phenotypes on L-Lysine; L-Lysine. Note that this organism has a second ABC transporter operon that is also important for lysine utilization, which is not explained. amino acid ABC transporter MQTYKKFLLAAAVSLVFSANAMAADKLKMGIEAAYPPFNNKDASGQVVGFDKDIGDALCAKMKVECEVVTSDWDGIIPALNAKKFDFLISSLSITEERKQAVDFTDPYYSNKLQFIAPKSAEFKTDKDSLKGKVIGAQRATLAGTWLEDELGSDITTKLYDTQENAYLDLTSGRVDAILADKYVNYDWLKTEAGRAYEFKGDPVVESDKIGIAVRKGDNELRNKLNAALKEIVADGTYKKINDKYFPFNIY Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_09905 AO356_09905 ABC transporter for L-Lysine, permease component 1 Specific phenotypes on L-Lysine; L-Lysine. Note that this organism has a second ABC transporter operon that is also important for lysine utilization, which is not explained. ABC transporter permease MMIDLHGFGPALAAGALMTVKLALSALCLGLVLGLLGALAKTSPYKPLQWLGGTYSTLVRGIPELLWVLLIYFGTVNLMRALGEYLGMPDLALNAFAAGVIALGLCFGAYATEVFRGAILAIPKGHREAGVALGLSKWRIFTRLIMPQMWRIALPGLGNLFMILMKDTALVSVIGLEEIMRHAQIGVTVSKQPFTFYMVAALMYLGLTVLAMLGMHLLERRAARGFARSTQ Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_09910 AO356_09910 ABC transporter for L-Lysine, permease component 2 Specific phenotype on L-Lysine. Note that this organism has a second ABC transporter operon that is also important for lysine utilization, which is not explained. ABC transporter permease MNWDVIIKWLPKLAQGATLTLELVAIAVIAGLLLAIPLGIARSSRLWQVRALPYAYIFFFRGTPLLVQLFLVYYGLAQFDAVRSSALWPYLRDPFWCATVTMTLHTAAYIAEILRGAIQAIPKGEIEAARALGMSRPKALFYIMLPRAARIGLPAYSNEVILMLKASALASTVTLLELTGMARTIIARTYLPVEIFFAAGMFYLLMSFLLVQGFKQLERWLRVDACQGR Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_10845 AO356_10845 succinyl-CoA-glutarate CoA-transferase (EC 2.8.3.13) Specifically important for: L-Lysine. Glutaryl-CoA is an intermediate in lysine catabolism and this reaction would be a way to form it from glutarate before oxidation by AO356_10850. Other reactions in this pathway were also found but the only candidate for glutarate semialdehyde dehydrogenase, AO356_26740, had little phenotype.) Note that this EC number is primarily associated with forming (S)-3-hydroxy-methylglutaryl-CoA. CoA-transferase MGALSHLRVLDLSRVLAGPWAGQILADLGADVIKVERPGNGDDTRAWGPPFLKDARGENTTEAAYYLSANRNKQSVTIDFTRPEGQRLVRELAAKSDILIENFKVGGLAAYGLDYDSLKAINPQLIYCSITGFGQTGPYAKRAGYDFMIQGLGGLMSLTGRPEGDEGAGPVKVGVALTDILTGLYSTAAILAALAHRDHVGGGQHIDMALLDVQVACLANQAMNYLTTGNAPKRLGNAHPNIVPYQDFPTADGDFILTVGNDGQFRKFAEVAGQPQWADDPRFATNKVRVANRAVLIPLIRQATVFKTTAEWVTQLEQAGVPCGPINDLAQVFADPQVQARGLAMELPHLLAGKVPQVASPIRLSETPVEYRNAPPLLGEHTLEVLQRVLGLDEAAVMAFREAGVL Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_13135 AO356_13135 Gamma-glutamyl-putrescine synthetase (EC 6.3.1.11) Specifically important for: Putrescine Dihydrochloride. This is the first step in putrescine catabolism gamma-glutamylputrescine synthetase MSVPPRAVQLNEANAFLKEHPEVLYVDLLIADMNGVVRGKRIERTSLHKVYEKGINLPASLFALDINGSTVESTGLGLDIGDADRICYPIPDTLCNEPWQKRPTAQLLMTMHELEGEPFFADPREVLRQVVTKFDELGLTICAAFELEFYLIDQENVNGRPQPPRSPISGKRPHSTQVYLIDDLDEYVDCLQDILEGAKEQGIPADAIVKESAPAQFEVNLHHVADPIKACDYAVLLKRLIKNIAYDHEMDTTFMAKPYPGQAGNGLHVHISILDKDGKNIFASEDPEQNAALRHAIGGVLETLPAQMAFLCPNVNSYRRFGAQFYVPNSPTWGLDNRTVALRVPTGSADAVRLEHRVAGADANPYLLMAAVLAGVHHGLVNKIEPGAPVEGNSYEQNEQSLPNNLRDALRELDDSEVMAKYIDPKYIDIFVACKESELEEFEHSISDLEYNWYLHTV Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_13140 AO356_13140 Gamma-glutamyl-GABA hydrolase (EC 3.5.1.94) Specifically important for: Putrescine Dihydrochloride. this is part of the gamma-glutamyl-putrescine pathway for putrescine catabolism (SEED_correct) gamma-glutamyl-gamma-aminobutyrate hydrolase MSRLPLIGVTTCSRQMGLHAYHTSGDKYARAVATAAKGLPVLVPSLADLFPPSDILDALDGILLTGSPSNVEPFHYQGPASAPGTAHDPARDATTLPLIRAAVEAGVPVLGICRGFQEMNVAFGGSLHQKVHEVGTFIDHREDDTQAVEVQYGPAHAVDIQPGGILAGLGLPQSIEVNSIHSQGIERLAPGLRAEAVAPDGLIEAVSVPEGKAFALGVQWHPEWEVSSNPHYLAIFQAFGDACRARATQRDADASNNA Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_13150 AO356_13150 Gamma-aminobutyrate:alpha-ketoglutarate aminotransferase (EC 2.6.1.19) Specifically important for: Putrescine Dihydrochloride. KEGG annotates this as putrescine aminotransferase, probably based on similarity to spuC (PA0299) of P. aeruginosa, but it is believed that only the g-glutamyl- pathway operates in P. aeruginosa (X. Yao et al 2011, PMC3147493) aminotransferase MTRNNPQTREWQALSNDHHLAPFSDFKQLKEKGPRIITHAKGVYLWDSEGNKILDGMAGLWCVAVGYGREELADAASQQMRELPYYNLFFQTAHPPVLELSKAIADIAPEGMNHVFFTGSGSEGNDTMLRMVRHYWAIKGQPNKKVIISRKNGYHGSTVAGASLGGMTYMHEQGDLPIPGIVHIAQPYWFGEGGDMSPEEFGVWAANQLEEKILEIGVDNVGAFIAEPIQGAGGVIVPPDSYWPRMKEILAKYDILFVADEVICGFGRTGEWFGTDHYGLKPHMMTIAKGLTSGYIPMGGLIVRDDVVAVLNEGGDFNHGFTYSGHPVAAAVALENIRILRDEKIIERVHSETAPYLQKRLRELNDHPLVGEVRGVGLLGAIELVQDKATRKRYEGKGVGMICRQFCFDNGLIMRAVGDTMIIAPPLVISKAEIDELVTKARHCLDLTLSALQG Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_13805 AO356_13805 ABC transporter for Carnitine, ATPase component Specific phenotype on Carnitine Hydrochloride. Likely to be a choline or glycine betaine transporter as well (with AO356_13855 as the SBP) choline ABC transporter ATP-binding protein MSIIRFEDVDVIFSNRPKAALDLLDKGFSRPEILQQTGLIVGVEKASLSIEKGEICVLMGLSGSGKSSLLRCINGLNTVSRGKLFVEHEGRQIDIASCSPAELKMMRTKRIAMVFQKFALMPWLTVRENISFGLEMQGRPEKERRKLVDEKLELVGLTQWRNKKPDELSGGMQQRVGLARALAMDADILLMDEPFSALDPLIRQGLQDELLELQRKLQKTIVFVSHDLDEALKLGTRIAIMKDGKIIQYSKPEEIVLNPADDYVRTFVAHTNPLNVLCGRSLMRTLDNCKRINGSVCLDPGGDSWLDLAEGNTIKGARQNGAVLDLQNWAPGQSVEELGRRPTLVDSNIGMRDALQIRYQTGNKLVLHDNQKVVGILGDSELYHALLGKNLG Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_13810 AO356_13810 ABC transporter for Carnitine, permease component Specific phenotypes on Carnitine Hydrochloride; Carnitine Hydrochloride. choline ABC transporter permease subunit MLIDQKIPLGQYIAGFVEWLTQNGASTFDAIALFLETMIHGVTFALTWFNPLALIGLIALLAHFIQRKWGLTVFVIASFLLILNLGYWQETMETLAQVLFATLVCVLIGVPLGIVAAHKPMFYTMMRPVLDLMQTVPTFVYLIPTLTLFGLGVVPGLISTVVFAIAAPIRLTYLGIRDVPDELMDAGKAFGCSRRQLLSRIELPHAMPSIAAGITQCIMLSLSMVVIAALVGADGLGKPVVNALNTADIALGFEAGLAIVLLAIMLDRICKQPDAKVGGDA Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_13815 AO356_13815 ABC transporter for Carnitine, periplasmic substrate-binding component 1 Specific phenotype on Carnitine Hydrochloride. This protein is similar to CaiX of P. syringae or P. aeruginosa (Psyr_2916 and PA5388) which has been shown to be a L-carnitine SBP (see PMID:19919675). Another gene in the cluster, AO356_13855, is also a SBP and is specifically important for L-carnitine utilization. AO356_13855 is similar to CbcX of P. aeruginosa or P. syringae (PA5378 or Psyr_4709) which is specific for choline or glycine betaine (ibid). Nevertheless, insertions in _13855 have a specific defect for carnitine utilization. It is possible that these insertions are polar on the beta-cleavage enzyme (_13850) which is required for carnitine catabolism. However insertions in _13855 in either orientation have a strong phenotype. glycine/betaine ABC transporter substrate-binding protein MKGSKPLLLAAMLSLPMLANAADPEKCSTVNFSDVGWTDITVTTATTSVVLDALGYKTKTTMISVPVTYKSLADGKNMDVFLGNWMPTMENDIKAYREAGTVETVRTNLKGAKYTLAVPQALYDKGLHDFADIPKFKKELDGKIYGIEPGNDGNRLIQSMIEKNAFGLKDAGFKVVESSEAGMLSQVDRASKRGTDVVFLGWAPHPMNTRFKIQYLTGGDDFFGPDFGAATVATNTRKGYSQECSNVGQLLKNLEFTVDMESQLMGNVLDDKMKPEAAAKAWLKKNPQVLDTWLAGVTTIDGKPGLEAVKAKLAQ Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_13840 AO356_13840 L-carnitine 3-dehydrogenase, thioesterase-like subunit CdhB (EC 1.1.1.108) Specifically important for: Carnitine Hydrochloride. This is CdhB (PA5385), a subunit of L-carnitine 3-dehydrogenase. See PMC2857723. 4-hydroxybenzoyl-CoA thioesterase MPTLTTYQTRILPEWVDYNGHLRDAFYLLIFSYATDALMDRLGLDSQNREASGHSLFTLELHLNYLHEVKLGAEVQVHTQIIGHDAKRLHLYHSLHLVGGDKELAGNEQMLLHVDLAGPRSAPFTEQTLARLDALLDEQSDLPPPAYIGRVIALPPAR Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_14165 AO356_14165 Acyl-CoA dehydrogenase (EC 1.3.8.7) Specifically important for: Tween 20. tween 20 hydrolyzes to a mix of C12, C14, and C16 fatty acids; this is probably part of beta oxidation (SEED_correct) acyl-CoA dehydrogenase MPDYKAPLRDIRFVRDELLGYEAHYQSLPACQDATPDMVDAILEEGAKFCEQVLAPLNRVGDIEGCTWSESGVKTPAGFKEAYKQFVEGGWPSLAHDVEHGGQGLPESLGLAVSEMVGEANWSWGMYPGLSHGAMNTISEHGTPEQQEAYLTKLVSGEWTGTMCLTEPHCGTDLGMLRTKAEPQADGSYKVSGTKIFISAGEHDMADNIVHIVLARLPDAPAGTKGISLFIVPKFLPNADGSIGQRNAVSCGSLEHKMGIHGNATCVMNFDAATGYLIGPANKGLNCMFTFMNTARLGTALQGLAHAEIGFQGGLKYARDRLQMRSLTGPKAPDKAADPIIVHPDVRRMLLTMKAFAEGNRAMVYFTAKQVDIVKYGVDEEEKKKADALLAFMTPIAKAFMTEVGFESANHGVQIYGGHGFIAEWGMEQNVRDSRISMLYEGTTGIQALDLLGRKVLMTQGEALKGFTKIVHKFCQSNEGNEAVKEFVEPLAALNKEWGELTMKVGMAAMKDREEVGAASVDYLMYSGYACLAYFWADMARLAAEKLAAGTTEEAFYTAKLQTARFYFQRILPRTRTHVATMLSGANNLMDMKEEDFALGY Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_14190 AO356_14190 Acyl-CoA dehydrogenase (EC 1.3.8.7) Specifically important for: Tween 20. tween 20 hydrolyzes to a mix of C12, C14, and C16 fatty acids; this is probably part of beta oxidation (SEED_correct) acyl-CoA dehydrogenase MADYKAPLRDMRFVLNEVFEVAKLWAQLPVLADTVDAETVEAILEEAGKVTSKSIAPLSRAADEEGCHWANGAVTTPAGFPQAYKTYAEGGWVGVGGDPVYGGMGMPKAVSAQVEEMVNSASLSFGLYPMLTAGACLSINAHASEELKAAYLPNMYAGVWAGSMCLTEPHAGTDLGIIRTKAEPQADGSYKVSGTKIFITGGEHDLTENIIHLVLAKLPDAPAGPKGISLFLVPKFMVNADGSLGARNAANCGSIEHKMGIQASATCVMNFDEAVGYLVGEPNKGLAAMFTMMNYERLGVGIQGLASGERSYQNAVEYARDRLQSRSPTGAQNKDKVADPIIVHPDVRRMLLTMKASNEGGRAFSTYVAMQLDTAKFSEDPVTRKRAEDLVALLTPVAKAFLTDLGLETTVHGQQVFGGHGYIREWGQEQLVRDVRITQIYEGTNGIQALDLVGRKIVGSGGAFYRLFADEIRHFTATASSDLAEFTKPLNDAVGTLDELTDWLLDRAKNNPNEIGAASVEYLQAFGYTAYAYMWALMAKAAFGKENQDDFYASKLGTARFYFARLLPRIHSLSASVKAGSESLFLLEPGQF Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_14225 AO356_14225 5-aminopentanamidase (EC 3.5.1.30) Specifically important for: L-Lysine. this is an early step in the oxidation of lysine (SEED_correct) carbon-nitrogen hydrolase MRVALYQCPPLPLDPAGNLHRLHQVALEARGADVLVLPEMFMTGYNIGVDAVNVLAEVYNGEWAQQIGRIAKAANLAIVYGYPERGEDGQIYNAVQLIDAQGERLANYRKSHLFGDLDHAMFSAGDSALPIVELNGWKLGLLICYDLEFPENARRLALAGAELILVPTANMQPYEFIADVTVRARAIENQCFVAYANYCGHEAELQYCGQSSIAAPNGSRPALAGLDEALIVGELDRQLLDDSRAAYNYLHDRRPELYDDLHKH Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_14230 AO356_14230 lysine 2-monooxygenase (EC 1.13.12.2) Specifically important for: L-Lysine. this is the first step in the oxidation of lysine (SEED_correct) amine oxidase MNKNNRHPADGKKPITIFGPDFPFAFDDWIEHPAGLGSIPAHNHGTEVAIVGAGIAGLVAAYELMKLGLKPVVYEASKMGGRLRSQAFNGAEGVIAELGGMRFPVSSTAFYHYVDKLGLETKPFPNPLTPASGSTVIDLEGQTYYAQKLADLPALFQEVADAWADALEDGSRFGDIQQAIRDRDVPRLKELWNTLVPLWDDRTFYDFVATSKAFAKLSFQHREVFGQVGFGTGGWDSDFPNSMLEIFRVVMTNCDDHQHLVVGGVEQVPHGIWNHVPERCAHWPEGTSLNSLHLGAPRSGVKRIARSADGRFSVTDVWENTREYAAVLVTCQSWLLTTQIECEEALFSQKMWMALDRTRYMQSSKTFVMVDRPFWKDKDPETGRDLMSMTLTDRLTRGTYLFDNGDDKPGVICLSYSWMSDALKMLPHPVEKRVKLALDALKKIYPKVDIAARIIGDPITVSWEADPHFLGAFKGALPGHYRYNQRMYAHFMQDDMPAEQRGIFIAGDDVSWTPAWVEGAVQTSLNAVWGIMKHFGGETHAENPGPGDVFHEIGPIALPE Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_14305 AO356_14305 ycgB component of nitrogen-related signalling system (of yeaGH-ycgB) conserved cofitness; yeaG is a protein kinase SpoVR family protein MTAKKEQKRQPISTGSEWTFELIKAYDREISRIADRYALDTYPNQIEVITAEQMMDAYASVGMPLGYHHWSYGKHFLSTEKSYSRGQMGLAYEIVINSDPCIAYLMEENTICMQALVVAHACYGHNSFFKGNYLFRTWTDASSIIDYLVFAKQYIMQCEERHGIDAVEDLLDSCHALMNYGVDRYKRPYPISAEEERRRQKDREEHLQKQINDLWRTIPKGADKYNEKDNARFPAEPQENILYFIEKHAPLLEPWQREIVRIVRKIAQYFYPQRQTQVMNEGWATFWHYTLMNDLYDEGLVTDGFMMEFLTSHTSVVFQPGFDSPYYSGINPYALGFAMYRDIRRMCENPTEEDRRWFPEIAGSDWLSAIKFAMSSFKDESFILQYLSPKVIRDLKLFSILDDDQKDDLVVPAIHDESGYRIIRETLAAQYNLGNREPNVQIYSIDRRGDRSLTLRHQAHNRKPLGDSTDEVLKHLHRLWGFDIHLETLQGDQVMKTHHVPPRGEQAEGDYGRLDLAVIHL Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_14310 AO356_14310 yeaH component of nitrogen-related signalling system yeaH (of yeaGH-ycgB) PFam PF04285.8 (DUF444). conserved cofitness; yeaG is a protein kinase hypothetical protein MSYVIDRRLNGKNKSTVNRQRFLRRYRDHIKKAVEEAVSRRSITDMEHGEQISIPGRDIDEPVLHHGRGGKQTVVHPGNKEFTSGEHIPRPQGGGAGKGPGKAGNSGEGMDEFVFQITQEEFLEFMFEDLELPNLVKRNLTGTDTFKTVRAGISNEGNPSRINIIRTLRSAHARRIALSGSSRAKLREAKEELARLKREEPDNFGDIQDLEAEIEKLSARIHRVPFLDTFDLKYNLLVKQPNPSSKAVMFCLMDVSGSMTQATKDIAKRFFILLYLFLKRNYDKIDVVFIRHHTSAREVDEEEFFYSRETGGTIVSSALKLMQEIMAERYPANEWNIYAAQASDGDNWNDDSPICRDILINQIMPFVQYYTYVEITPREHQALWYEYERIAEAFSDTFAQQQLVSAGDIYPVFRELFQRRLVT Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_14315 AO356_14315 yeaG component of nitrogen-related signalling system (of yeaGH-ycgB) conserved cofitness; yeaG is a protein kinase serine/threonine protein kinase MSIFSHFQQRFESTRQEEYSLQEYLELCKQDRSAYVSAAERLLLAIGEPELLDTSTNSRLSRIFSNKVIRRYPAFADFHGMEECIEQIVSYFRHAAQGLEEKKQILYLLGPVGGGKSSLAEKLKQLIEKVPFYAIKGSPVFESPLGLFNATEDGAILEEDFGIPRRYLNTIMSPWATKRLAEFGGDISQFRVVKLYPSILNQIAVAKTEPGDENNQDISALVGKVDIRKLEEFPQNDADAYSYSGALCRANQGLMEFVEMFKAPIKVLHPLLTATQEGNYNSTEGLGAIPFTGILLAHSNESEWHTFRNNKNNEAFIDRIYIVKVPYCLRVTDEVKIYDKLLFNSSLSKAHCAPDTLKMLAQFTVLSRLKEPENSNIYSKMRVYDGENLKDTDPKAKSIQEYRDNAGVDEGMNGLSTRFAFKILSKVFNFDPHEIAANPVHLLYVLEQQIEQEQFQAETRERYLRFLKEYLAPRYIEFIGKEIQTAYLESYSEYGQNIFDRYVLYADFWIQDQEYRDPETGEILNRVALNEELEKIEKPAGISNPKDFRNEIVNFVLRARANNNGKNPTWLSYEKLRVVIEKKMFSNTEDLLPVISFNAKASKEDQQKHNDFVTRMVERGYTDKQVRLLSEWYLRVRKSQ Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_17240 AO356_17240 required for acetate efflux, together with NodT, MFP and FUSC proteins (AO356_17230, AO356_17245, and AO356_17235) PFam PF07869.8 (DUF1656). A conserved cofit operon. This operon and orthologous operons are important on acetate as a carbon source and cholin acetate as a stress, which suggests that acetate is a substrate. Na+-dependent transporter MPREIAFHGVYMPTMTLMFFIAAGLAWALDRFLSGLDLYRFFWHPALLRLSLFTCLFGALALTVYR Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_17535 AO356_17535 N-acetylglucosamine-specific PTS system, IIBC components (nagE) Specific phenotype on NAG as a carbon source. Not sure why SEED think s this includes the IIA component. (KEGG_correct) PTS N-acetyl-D-glucosamine transporter MYQHFIEGLQRLGRALMLPIAILPIAGLLLRLGDTDLLDIAIIHDAGQAIFANLAMIFAIGIAVGFARDNNGTAGLAGAIGYLVMIATLKVLDASINMGMLAGIISGLLAGALYNRFKDIKLPEYLAFFGGRRFVPIVTGFSAVGLGVVFGLIWPPIQQGINGFGALLMESGSFGAFVFGVFNRLLIVTGLHHILNNMAWFIFGSFTDPATGAVVTGDLSRYFAGDPKGGQFMTGMFPVMLFGLPAACLAMYRNALPQRRKVMGGILLSMALTSFLTGVTEPIEFAFMFLAPLLFLVHALLTGVSMAVTNLLGIHLGFTFSGGFIDMVLGWGKSTNGWLVVPVGLAYAAIYYLVFDFCIRRFDLKTPGREEVPAGDKPAIAENQRAAAYIQALGGADNLITIGACTTRLRLDMVDRNKASDAQLKALGAMAVVRPGNGGSLQVVVGPMADSIADEIRLAVPSSLRPVTAPVPNAPAPTTPAALSSTEAQQWLDALGGQDNVLQLECVATSRLRVRLADDKGLSESRLKGLGCQGMSSLEDGVWHLLLGEKAPRLWQALDGLAHGRKVDAGA Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_17540 AO356_17540 N-acetylglucosamine-specific PTS system, I, HPr, and IIA components (nagF) Specific phenotype on NAG as a carbon source. Not sure why SEED think s this includes the IIA component. (KEGG_correct) PTS N-acetyl-D-glucosamine transporter MPNNNKELILSAPLSGPVLTLANVPDAVFASGAMGDGIAIDPLNDTLYAPCDAEVIHVARTGHAVTLRADNGAELLLHLGLDTVELQGEGFSMLVKEGARVSHGQPLLRYDVDKVALRCKSLVSLLVITNGEHFQARPITLKGVKVGEPLLHILAKAVGQAEHHDQDSGIEVFGQVRIAHRGGLHARPAALVRQTAQGFKSRSQLHFSGKSASCDSVMGMMGLAITEQAQVHVSCRGSDAEAALQALLTTLSTALVEEAHASAPPPEPPRANAEEGVLHGVCAAPGLVTGPLVRLSGIQLPEDIGGHAIEEQRQRLSDALAQVRGEIHLTLEHARARQHRDEEAIFSAHLALLEDPVLLDAADLFIEQGSAAPHAWSRSIDTQCQVLQQLGSTLLAERANDLRDLRQRVLRVLLGEAWQFDVAAGAIVAAQELTPSDLLQLSAQGVAGVCMVEGGATSHVAILARGKGLPCLVALGDELLAQEQGQAVVLDADGGRLELTPTVERLAQVRQAQTRRTALRAQQQSLAHTPARTVDGVEVEVAANVASSAEAGESLANGADGVGLLRTEFLFVDRHTAPDEEEQRQAYQAVLEAMGDKPVIIRTIDVGGDKQLDYLPLPSEANPVLGLRGIRLAQVRPDLLDQQLRALLQTRPLDRCRILLPMVTEVDELLHIRKRLDALGSELGLSERPQLGVMVEVPAAALLAEQLAEHADFLSIGTNDLSQYTLAMDRDHAGLAARVDALHPALLRLIAQTCAGAAKHGRWVGVCGALASDPLATPVLIGLGVRELSVSPPQIGEIKDRVRHLDAAQCARLSNELLNLGSALAVRRACHRHWPLG Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_17670 AO356_17670 L-alanine and D-alanine permease Specific phenotype on D-alanine and L-alanine D-alanine/D-serine/glycine permease MPVGNHLPHGETAQGGPLKRELGERHIRLMALGACIGVGLFLGSAKAIEMAGPAIMLSYIIGGLAILVIMRALGEMAVHNPVAGSFSRYAQDYLGPLAGFLTGWNYWFLWLVTCVAEITAVAVYMGIWFPDVPRWIWALAALVSMGSINLIAVKAFGEFEFWFALIKIVTIIAMVIGGVGIIAFGFGNDGVALGISNLWAHGGFMPNGVSGVLMSLQMVMFAYLGVEMIGLTAGEAKNPQKTIPNAIGSVFWRILLFYVGALFVILSIYPWNEIGTQGSPFVMTFERLGIKTAAGIINFVVITAALSSCNGGIFSTGRMLYSLAQNGQAPAGFAKTSTNGVPRRALLLSIAALLLGVLLNYLVPEKVFVWVTSIATFGAIWTWVMILLAQLKFRKSLSASERAALKYRMWLYPVSSYLALAFLVLVVGLMAYFPDTRVALYVGPAFLVLLTVLFYTFKLQPTGDVQRAVRSAS Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_17790 AO356_17790 alpha-ketoglutarate permease (MHS family) Specific phenotype on a-ketoglutarate. Not important for the utilization of other dicarboxylates (succinate or malate). 83% identical to PA5530, which is reported to transport a-ketoglutarate and also glutarate (PMC4097582). KEGG_correct MFS transporter MDNSNALPIGSAAVPARERTTASRIKSIFSGSVGNMVEWYDWYVYAAFSLYFAKVFFPKGDTTAQLLNTAAIFAVGFLMRPIGGWLMGLYADRAGRKRALMASVYLMCFGSLIIALSPSYETIGVGAPILLVFARLLQGLSVGGEYGTSATYLSEMATKERRGFFSSFQYVTLISGQLIALGVLIVLQQFLTTEQLYAWGWRIPFAIGALCAVVALYLRRGMEETESFTKKEKSKESAMRTLLRHPKELMTVVGLTMGGTLAFYTYTTYMQKYLVNTVGMSISDSTTISAATLFLFMCLQPVIGGLSDKIGRRPILIAFGILGTLFTVPILTTLHTIQTWWGAFFLIMAALIIVSGYTSINAVVKAELFPTEIRALGVGLPYALTVSIFGGTAEYIALWFKSIGMETGYYWYVTACIAVSLLVYITMKDTRKHSRIVTD Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_18450 AO356_18450 outer membrane component of uptake system, probably for ferrous iron PFam PF07433.7 (DUF1513). In a conserved cofit operon with an efeO-like gene (AO356_18455) and an efeB-like gene (AO356_18460). Another efeO-like gene (AO356_05015) is cofit but not nearby. hypothetical protein MFRRQVLALGSLLLGAVTLGGWTLFKQKDKHPLLLSARDDGDGKHYAVGYRLDGTRVFATQVGQRCHDIINHPTQPIALFVARRPGTESYLIDLRDGALLQTIASLPNRHFYGHAVIHNSGEWLYATENDTTDPGRGLLGVYRFEGERLVHSGEISTHGIGPHQVSWMPDGETLVVANGGIRTEAESRVEMNLDAMEPSLVLMQRDGTLLSKETLAQSMNSVRHLGIASDGTIVSGQQFMGAAHESSELVAIKRPGQPFQAFPVPEEQLQAMGHYTASVAVHSDLRLVALTAPRGNRFFIWDLDSGEVRLDAPLPDCAGVGAVADGFVVTSGQGRCRYYDCRQTQLVAKPLDLPAGLWDNHLHLV Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_18530 AO356_18530 L-tyrosine transporter Specific phenotype with tyrosine as the nitrogen source. Not important if phenylalanine is the nitrogen source. aromatic amino acid transporter MSGQNSHSGELKRGLKNRHIQLIALGGAIGTGLFLGSAGVLKSAGPSMILGYAICGFIAFMIMRQLGEMIVEEPVAGSFSHFAHKYWGGFAGFLSGWNCWILYILVGMSELTAVGKYIHYWAPDIPTWVSAAAFFILINAINLANVKVFGEAEFWFAIIKVVAIVGMIALGSYLLVSGHGGPQASVTNLWSHGGFFPNGVSGLVMAMAIIMFSFGGLEMLGFTAAEADKPKTVIPKAINQVIYRILIFYIGALVVLLSLTPWDSLLATLNASGDAYSGSPFVQVFSMLGSNTAAHILNFVVLTAALSVYNSGTYCNSRMLLGMAEQGDAPKALSRIDKRGVPVRSILASAAVTLVAVLLNYLVPQHALELLMSLVVATLVINWAMISYSHFKFRQHMNQTQQTPLFKALWYPYGNYICLAFVVFILGVMLLIPGIQISVYAIPVWVVFMWVCYVIKNKRSARQELAVAAAK Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_18700 AO356_18700 L-Arginine ABC transporter, periplasmic substrate-binding component Specific phenotype on L-Arginine. (SEED_correct) ABC transporter substrate-binding protein MKKLVLLGALALSVLSLPTFADEKPLKIGIEAAYPPFASKAPDGSIVGFDYDIGNALCEEMKVKCVWVEQEFDGLIPALKVRKIDAILSSMSITEDRKKSVDFTNKYYNTPARLVMKAGTQVSDNLAELKGKNIGVQRGSIHERFAREVLAPLGAEIKPYGSQNEIYLDVAAGRLDGTVADATLLDDGFLKTDAGKGFAFVGPAFTDEKYFGDGIGIAVRKGDALKDKINGAITALRENGKYKQIQDKYFAFDIYGK Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_18705 AO356_18705 L-Arginine ABC transporter, permease component 2 Specific phenotype on L-Arginine. (SEED_correct) ABC transporter MLKGYGAVILDGAWLTLELALSSMALAIVLGLIGVALRLSPVRWLAWLGDLYSTVIRGIPDLVLILLIFYGGQDLLNRVAPMLGYDDYIDLNPLAAGIGTLGFIFGAYLSETFRGAFMAIPKGQAEAGMAYGMSGFQVFFRVLVPQMIRLAIPGFTNNWLVLTKATALISVVGLQDMMFKAKQAADATREPFTFFLAVAAMYLVITSVSLLALRHLEKRYSVGVRAADL Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_18710 AO356_18710 L-Arginine ABC transporter, permease component 1 Specific phenotypes on L-Arginine; L-Arginine. (SEED_correct) amino acid ABC transporter permease MIFDYNVIYEALPLYFSGLLTTLKLLALSLFFGLLAALPLGLMRVSKQPIVNMTAWLYTYVIRGTPMLVQLFLIYYGLAQFAIVRESFLWPWLSSATFCACLAFAINTSAYTAEIIAGSLRATPNGEIEAAKAMGMSRYKLYRRILLPSALRRALPQYSNEVIMMLQTTSLASIVTLIDITGAARTVNAQYYLPFEAYITAGAFYLCLTFILVRLFKLAERRWLGYLAPRKH Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_18715 AO356_18715 L-Arginine ABC transporter, ATPase component Important for utiliizing L-arginine. Detrimental on L-lysine which might indicate that it leaks lysine. (SEED_correct) amino acid transporter MYKLEVQDLHKRYGSHEVLKGVSLKAAAGDVISIIGSSGSGKSTFLRCINLLEQPHAGKILLNNEELKLVAGKDGAMKAADPKQLQRMRSRLSMVFQHFNLWSHMTALENIMEAPVHVLGVAKAEAREKAEHYLNKVGVAHRKDAYPGHMSGGEQQRVAIARALAMEPEVMLFDEPTSALDPELVGDVLKVMQALAVEGRTMVVVTHEMGFAREVSNQLVFLHKGIVEESGNPREVLVNPQSERLQQFLSGSLK Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_18980 AO356_18980 sodium:C4-dicarboxylate symporter (dctA) Important for utilization of malate, succinate, or fumarate (all C4 dicarboxylates) as carbon sources. 81% identical to PA1183 from P. aeruginosa (PMC3165536), which is also involved in growth with these substrates. KEGG_correct C4-dicarboxylate transporter MTTRQPLYKSLYFQVIVAIAIGILLGHFYPQTGVALKPFGDGFIKLIKMVIAPIIFCTVVSGIGGMQNMKSVGKTGGYALLYFEIVSTIALLIGLVVVNVVQPGAGMHIDVSTLDTSKIAGFISAGKDQSIIAFILNVIPNTIVGAFANGDILQVLMFSVLFGFALHRLGAYGKPVLDFIDRFAHVMFIIINMIMKLAPLGAFGAMAFTIGAYGVGSLVQLGQLMICFYITCVVFVLVVLGAICRAHGFSVIKLIRYIREELLIVLGTSSSESALPRMLIKMERLGAKKSVVGLVIPTGYSFNLDGTSIYLTMAAVFIAQATDTPMDLTHQITLLLVLLLSSKGAAGVTGSGFIVLAATLSAVGHLPVAGLALILGIDRFMSEARALTNLVGNAVATIVVAKWVKELDEDQLQTELASGGRGISDVREDDEQIAAAQIAAAETSAPGTVK Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_19460 AO356_19460 allantoinase (EC 3.5.2.5) Specifically important for: Inosine. This protein is similar to hpxB from Klebsiella, which is allantoinase, an step in the degradation of purines such as adenine or hypoxanthine (inosine is the nucleoside of hypoxanthine). See PMID:19060149 allantoinase VSADYPRDLIGYGNNPPHPQWPGNARIALSFVLNYEEGGERNVLHGDKESEAFLSEMVAAQPLQGERNMSMESLYEYGSRAGVWRVLKLFKAFDIPLTIFAVAMAAQRHPDVIRAMVAAGHEICSHGYRWIDYQYMDEAQEREHMLEAIRILTEITGERPLGWYTGRTGPNTRRLVMEEGGFLYDSDTYDDDLPYWEPNTPNGKPHLVIPYTLDTNDMRFTQVQGFNKGDDFFQYLKDAFDVLYAEGAEAPKMLSIGLHCRLIGRPARLASLKRFLEYVKGHEHVWFSRRVDIARHWQQAHPYQGASNPGASK Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_19465 AO356_19465 5-hydroxyisourate hydrolase [EC: 3.5.2.17] Specifically important for: Inosine. 5-hydroxyisourate is an intermediate in purine degradation (KEGG_correct) 5-hydroxyisourate hydrolase MGRLTTHVLDAAHGCPGSAIKVELYRVEGSQLQLVASAQTNSDGRCDAPLLQGEDYRSGVYQLQFHAGDYYRARGVQLPEPAFLDVVVLRFGISAEQEHYHVPLLISPYAYSTYRGS Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_20235 AO356_20235 L-arabinolactonase (EC 3.1.1.15) / D-galactonolactonase (EC 3.1.1.25) Specifically important for: L-Arabinose; D-Galactose. The SEED prediction explains the phenotype on L-arabinose but not on D-galactose. L-arabinose and D-galactose are chemically similar and some dehydrogenases act on both substrates, so it is not surprising that a lactonase would hydrolase both of their products. The dehydrogenase is probably AO356_20240. (SEED_correct) gluconolaconase MKWTAVTEHRAKLGEGPFWDAPTQALYWVDIAGKQALRLIGANVEIWQMPEHVSAFIPTQSGDALVTLSSGVYRLDLDSPGLEPRLTLLCMADPQPGNRANEARCDPQGQLWLGTMQNNIGAEGEDLPIEHRSGGLFRVGSDGRVLPLLRGLGIPNTLLWSPDGTTVYFGDSLDGTVYRHFIYPEGNLAPAEVWFGPHPRGGPDGSAMDARGYIWNARWDGSCLLRLTPDGQVDRVIELPVSRPTSCVFGGEDLKTLYITSAASPLGHPLDGAVLSMRVDVPGVACTRFAG Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_20240 AO356_20240 L-arabinose 1-dehydrogenase (EC 1.1.1.46) This is specifically important for L-arabinose utilization. Some closely related proteins in other Pseudomonas are important for D-galactose utilization as well, so this is probably also a D-galactose 1-dehydrogenase. However mutants in this gene had little phenotype in D-galactose (two replicates). No other dehydrogenase was identified as specifically important on D-galactose. short-chain dehydrogenase MAEPLVLPPVPEPPKGERLKDKVVLLTGAAQGIGEAIVAAFASQQARLVISDIQAQKVEAVAAHWRERGADVHALQADVSKQQDLQAMARRAVELHGRIDVLVNCAGVNVFRDPLEMTEEDWRRCFAIDLDGAWYGCKAVLPQMIEQGVGSIINIASVHSSHIIPGCFPYPVAKHGLLGLTRALGIEYAPKGVRVNAIAPGYIETQLNVDYWNGFADPHAERQRALDLHPPRRVGQPIEVAMTAVFLASDEAPFINASCITIDGGRSVMYHD Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_21495 AO356_21495 gamma-glutamylputrescine oxidase (EC 1.4.3.-) Specifically important for: Putrescine Dihydrochloride. part of the pathway for oxidizing putrescine via gamma-glutamyl-putrescine (KEGG_correct) gamma-glutamylputrescine oxidoreductase MANTPYPESYYAASANPVPPRPALQDDVETDVCVIGAGYTGLSSALFLLENGFKVTVLEAAKVGFGASGRNGGQIVNSYSRDIDVIERSVGPQQAQLLGNMAFEGGRIIRERVAKYQIQCDLKDGGVFAALTAKQMGHLESQKRLWERFGHTQLELLDQRRIREVVACEEYVGGMLDMSGGHIHPLNLALGEAAAVESLGGVIYEQSPAVRIERGASPVVHTPQGKVRAKFIIVAGNAYLGNLVPELAAKSMPCGTQVIATEPLGDELAHSLLPQDYCVEDCNYLLDYYRLTGDKRLIFGGGVVYGARDPANIEAIIRPKMLKAFPQLKDVKIDYAWTGNFLLTLSRLPQVGRLGDNIYYSQGCSGHGVTYTHLAGKVLAEALRGQAERFDAFADLPHYPFPGGQLLRTPFAAMGAWYYGLRDKLGF Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_21640 AO356_21640 acetyl-CoA C-acetyltransferase [EC: 2.3.1.9] Specifically important for: L-Lysine; Carnitine Hydrochloride. acetyl-CoA acetyltransferase is required for the breakdown of acetoacetyl-CoA, which is an intermediate in lysine degradation (via glutaryl-CoA) and in carnitine degradation (from the beta cleavage enzyme, see PMID: 24240508) (KEGG_correct) acetyl-CoA acetyltransferase MQEVVIVAATRTAIGSFQGSLAAIPAPELGAAVIRRLLEQTGLSGEQVDEVILGQVLTAGSGQNPARQASILAGLPHAVPALTLNKVCGSGLKALHLGAQAIRCGDAEVIIAGGMENMSLAPYVLPAARTGLRMGHAKMIDSMITDGLWDAFNDYHMGITAENLVDKYGISREEQDAFAAASQQKAVAAIEGGRFADEITPILIPQRKGDPVAFATDEQPRAGTTAESLGKLKPAFKKDGSVTAGNASSLNDGAAAVILMSAEKAKALGLPVLAKISAYANAGVDPAIMGIGPVSATRRCLDKAGWSLEQLDLIEANEAFAAQSLAVARELKWDMDKVNVNGGAIALGHPIGASGCRVLVSLLHEMIKRDAKKGLATLCIGGGQGVALALERA Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_23175 AO356_23175 malonate-semialdehyde dehydrogenase (acetylating) (EC 1.2.1.18) Specifically important for: m-Inositol. 3-oxopropionate or malonate semialdehyde is an intermediate in myo-inositol catabolism methylmalonate-semialdehyde dehydrogenase MSDAPVVGHYIDGRIQASDNARLSNVFNPATGAVQARVALAEPSTVDAAVASALAAFPAWSEQSSLRRSRVMFKFKELLDRHHDELAQIISREHGKVLSDAHGEVTRGIEIVEYACGAPNLLKTDFSDNIGGGIDNWNLRQPLGVCAGVTPFNFPVMVPLWMIPLALVAGNCFILKPSERDPSASLLMARLLTEAGLPDGVFNVVQGDKVAVDALLQHPDIEAISFVGSTPIAEYIHQQGTAQGKRVQALGGAKNHMIVMPDADLDQAADALIGAAYGSAGERCMAISIAVAVGDVGDELIAKLLPRIDQLKIGNGQQPGTDMGPLVTAEHKAKVEGFIDAGVAEGARLIVDGRGFKVPGAEQGFFVGATLFDQVTAEMSIYQQEIFGPVLGIVRVPDFATAVALINAHEFGNGVSCFTRDGGIARAFARSIKVGMVGINVPIPVPMAWHSFGGWKRSLFGDHHAYGEEGLRFYSRYKSVMQRWPDSIAKGPEFSMPTAQ Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_24585 AO356_24585 L-arabonate dehydratase (EC 4.2.1.25) Specifically important for: L-Arabinose. L-arabonate is an intermediate in the oxidation of L-arabinose (SEED_correct) dihydroxy-acid dehydratase MSDKKPSLRSAQWFGTADKNGFMYRSWMKNQGIADHQFHGKPIIGICNTWSELTPCNAHFRQIAEHVKRGVIEAGGFPVEFPVFSNGESNLRPTAMLTRNLASMDVEEAIRGNPIDGVVLLTGCDKTTPALLMGAASCDVPAIVVTGGPMLNGKHKGQDIGSGTVVWQLSEQVKAGTITIDDFLAAEGGMSRSAGTCNTMGTASTMACMAEALGTSLPHNAAIPAVDARRYVLAHMSGMRAVEMVREDLKLSKILTKEAFENAIRVNAAIGGSTNAVIHLKAIAGRIGVQLDLDDWTRIGRGMPTIVDLQPSGRFLMEEFYYAGGLPAVLRRLGEANLIPNPNALTVNGKSLGENTKDAPIYGQDEVIRTLDNPIRADGGICVLRGNLAPLGAVLKPSAATAELMQHRGRAVVFENFDEYKARINDPELDVDANSILVMKNCGPKGYPGMAEVGNMGLPAKLLAQGVTDMVRISDARMSGTAYGTVVLHVAPEAAAGGPLAAVKEGDWIELDCASGRLHLDIPDAELAARLADLAPPQQLLVGGYRQLYIDHVLQADQGCDFDFLVGCRGAEVPRHSH Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_26995 AO356_26995 DNA damage response nuclease Conserved and specific phenotype: important for resisting cisplatin. Contains a VRR-NUC domain that is predicted to have nuclease activity. nuclease VATRSLDDPYYYLNNFQQVLAWLSQRYADVLSHEEQRFIDDFAALPRASQGLLVRMVMRKGLRFRHSKLSYPEIGDIGAAVAPLLALGWVEEQAPIGLVELFDVLLKAEILLCLGHLIEHPKAKKTEWLQALDNHPSPLQPFRTWCPQLDERLYSLTIMDLCDRLRLMFFGNLYQDWSEFVLADLGIFTYETVEFSAESRGLRSREDVDACLFLHDCQQRFEAGEPLEDIVAQVNELSLENPWLERRRGKLLFQIGQHGERIGDFALALCIYRDCTYPGARLRMVRVLERIGEYALALELGEAAAQTPQSAAETQALLRIVPRLRRKLGGPPVPRVMAREVERLELHLPRVDPGLSVEYHVQAHLHDETAPVHYVENSLINSLFGLLCWPAIFAPLPGAFFHPFQRGPVDLLNEDFHARRAELFAACLAELDDGRYRQTIGRRYVEKWGVQSPFVFWGALSEPLLEQALDCLPAEHLKHWFQRLLLDIKANRAGMPDLIQFWPQHKTYRMIEVKGPGDRLQDNQLRWLEFCHEHQMPVAVCYVQWAASAIASELAPAEDEPPQIIYGSELARDGRT Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_28020 AO356_28020 ethanol oxidation regulatory protein ercA Specifically important for: Ethanol. Similar to ercA (PA1991) which apparently has a regulatory role (PMCID: PMC3754586) rather than being directly involved in catabolism. AO356_28055 is probably the main ethanol dehydrogenase. (not an enzyme) alcohol dehydrogenase MSHVTEKMSLSPLRKFVSPEIMFGAGCRHNVGNYAKTFGARKVLIVTDPGVIAAGWVADVEASLQAQGIDYCIYSAVSPNPRVEEVMLGADLYRENHCDVIVAVGGGSPMDCGKGIGIVVAHGRSILEFEGVDTLNVPSPPLILIPTTAGTSADVSQFVIISNQQERMKFSIVSKAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREKIMLGSMQAGLAFSNAILGAVHAMSHSLGGFLDLPHGLCNAVLVEHVVAFNYNSAPERFKVIAETLGIDCRGLNHREIRTRLVEHLIALKHTIGFHETLGLHGVSTSDIPFLSQHAMHDPCILTNPRESSQRDVEVVYGEAL Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_1226 DNA damage response nuclease Conserved and specific phenotype: important for resisting cisplatin. Contains a VRR-NUC domain that is predicted to have nuclease activity. Hypothetical protein, restriction endonuclease-like VRR-NUC domain VAVRSLDDPFYYLNNFQQVLAWLTQRYADVLSTDEQRFIEHFAALPRGAQGLLVRMVMRKGLRFRHSKLHYPEIGDISAAVAPLLALGWVEEQAPIGLVELFEVLLKPEILLCLGHLIEHPKAKKTEWLHALDEHLNQPQPFDAWCPQLDDRLYSLTIMSLCDRLRLMFFGNLYQDWSEFVLADLGIFTYETVEFSAESRGLRSREDVDACLFLHDCQQRFEAGEPPEEIVAQVNELSLDNPWLERRRGKLLFQIGQHGERIGDFALALGIYRDCTYPGARLRMVRVLERIGEYGLALELGEVAMQAPQSAAETQALLRIVPRLRRKLGGPPVPRGLAREVERLELQLPRVDPTLSVEYHVQAHLHDDTAPVHYVENSLINSLFGLLCWPAIFAPLPGAFFHPFQRGPADLLNEDFHARRAELFAACLVELDDGRYRQTISRRYAEKWGVQSPFVFWGALSEPLLEQALDCLPAAHLKHWFDRLLLDIKANRAGMPDLIQFWPQHKTYRMIEVKGPGDRLQDNQLRWLEFCHEHQMPVAVCYVQWAESAIASDGAA Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_159 DNA damage resistance protein PFam PF07867.7 (DUF1654). Conserved specific phenotype for cisplatin resistance, in an operon with an endonuclease, and close homologs are regulated by LexA FIG00953874: hypothetical protein VATPSAATTPLDSYTRLGLRVSKIINAPTAQKAKAALIFRLPDEPVDEWERLLEEIDENDNVTLAYRDDGGVQVFWVVPKED Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2047 D-glucosaminate dehydratase (EC 4.3.1.9) Specifically important for: D-Glucosamine Hydrochloride. This enzyme had not previously been linked to a gene. This is the second step in catabolism of glucosamine, and the 'beta' form of the enzyme was expected to be PLP-dependent and about this size. Iwamoto et al (2003) purified a non-specific 'alpha' enzyme for this reaction (PMID: 12686150) D-serine deaminase (EC 4.3.1.18) MSSVIPNAGVEKGAATVGAHLLKDVSLPALVLHRAALEHNIRWMQAFVTDSGAELAPHGKTSMTPALFRRQLDAGAWGLTLASAVQTRAAYAHGVRRVLMANQLVGTPNMALIADLLADPAFEFHCMVDHPDNVADLGAFFASRGMKLNVMIEYGVVGGRCGCRTEAEVLALAEAIQAQPALALTGIEGYEGVIHGDHAISGIRAFAASLVRLAVQLQDNGAFAIDKPIITASGSAWYDLIAESFEAQNAHGRFLSVLRPGSYVAHDHGIYKEAQCCVLERRSDLHEGLRPALEVWAHVQSLPEPGFAVIALGKRDVAYDAGLPVPLKRYTPGSDSVTGDDVSGCKVTAVMDQHAFMNVAAGVELRVGDIISFGTSHPCLTFDKWRVGCLVDEQLRVVESMETCF Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2050 ABC transporter for D-Glucosamine, putative ATPase component Lacks fitness data but is in a conserved operon with confirmed glucosamine utilization genes ABC-type polar amino acid transport system, ATPase component MTDISTPSNTQPLLDIRGLRKQYGPLEVLKGVDLSMQRGNVVTLIGSSGSGKTTLLRCVNMLEEFQGGQIMLDGESIGYDDIDGKRVRHPEKVIARHRAMTGMAFQQFNLFPHLTALQNVTLGLLKVKKLPKDEAVALAEKWLERVGLLERRDHFPGQLSGGQQQRVAIARAIAMNPSLMLFDEVTSALDPELVGEVLNVIKGLAEDGMTMLLVTHEMRFAFEVSDKIVFMNQGRIEEQGPPKELFERPQSPRLAEFLKNTRF Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2051 ABC transporter for D-Glucosamine Hydrochloride, permease component 1 Specific phenotypes on D-Glucosamine Hydrochloride. Amino acid ABC transporter, permease protein MYESPSWLHELWVARDTLWAGFLTSVQCSLLAIVLGTLIGLVAGLVLTYGRTWMRAPFRFYVDLIRGTPVFVLVLACFYMAPALGWQIGAFQAGVLGLTLFCGSHVAEIVRGALQALPRGQMEASQAIGLTFYQSLGYVLLPQALRQILPTWVNSSTEIVKASTLLSVIGVAELLLSTQQIIARTFMTLEFYLFAGFLFFIINYAIELLGRHIEKRVALP Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2052 ABC transporter for D-Glucosamine Hydrochloride, permease component 2 Specific phenotypes on D-Glucosamine Hydrochloride; D-Glucosamine Hydrochloride. ko:K02029 : polar amino acid transport system permease protein amino acid ABC transporter, permease protein MNYQLNFAAVWRDFDTLLAGLGLGLSLALVSIAIGCVIGLAMAFALLSKHRVLRVLASVYVTVIRNTPILVLILLIYFALPSLGIRLDKLPSFVITLSLYAGAYLTEVFRGGLLSIHKGQREAGLAIGLGEWQVKAYVTVPVMLRNVLPALSNNFISLFKDTSLAAAIAVPELTYYARKINVESYRVIETWLVTTALYVAACYLIAMLLRYFEQRLAIRR Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2053 ABC transporter for D-Glucosamine, periplasmic substrate-binding component Specific phenotype on D-Glucosamine Hydrochloride. Glutamine ABC transporter, periplasmic glutamine-binding protein (TC 3.A.1.3.2) MQRRPSLFKTCVFLFAATVAAVGVAQAADSKLDSVLQRGKLIVGTGSTNAPWHFQGADGKLQGFDIDIARMVAKGLFNDPEKVEFVVQSSDARIPNLLTDKVDMSCQFITVTASRAQQVAFTLPYYREGVGLLLPANSKYKEIEDLKAAGDDVTVAVLQNVYAEELVHQALPKAKVDQYDSVDLMYQAVNSGRADAAATDQSSVKYLMVQNPGRYRSPAYAWSPQTYACAVKRGDQDWLNFVNTTLHEAMTGVEFPTYAASFKQWFGVELPSPAIGFPVEFK Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2074 required for sulfate utilization, putative electron transport protein for sulfite reductase PFam PF06073.8 (DUF934). conserved cofitness with sulfite reductase; auxotrophic Oxidoreductase probably involved in sulfite reduction MQRIIKNNEVIDETWHLLPKDATLDGISNCDDLIVPLALWRDHAHALKARDGGLGVWLDADEEAEEIGEDANQLQVIALNFPAFTDGRSYSNARLLRDRYGFKGELRAIGDVLRDQLFYMRRCGFDAFALRADKDPFEALESLKDFSVTYQAATDEPLPLFRRR Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2111 Dehydrocarnitine CoA-transferase and acetoacetate CoA-transferase, subunit A Very important on cartinine and also important on L-phenylalanine and L-leucine. Acts on dehydrocarnitine during carnitine catabolism to give dehydrocarnitine-CoA. Probably also acts on acetoacetate, which is an intermediate in the degradation of phenylalanine (via tyrosine and homogentistate) and leucine (from HMG-CoA lyase). Both substrates are 3-oxoacids, but not sure if succinyl-CoA is the source of the CoA as annotated. Note that acetoacetyl-CoA is probably cleaved to acetyl-CoA by _2113 (downstream). Similar to DhcA = PA1999. Succinyl-CoA:3-ketoacid-coenzyme A transferase subunit A (EC 2.8.3.5) MAGFDKRVSSYEEALEGLKDGMTVIAGGFGLCGIPENLIAEIKRKGIRDLTVVSNNCGVDGFGLGVLLEDRQIRKVVASYVGENALFEQQLLSGEIEVVLTPQGTLAEKMRAGGAGIPAFFTATGVGTPVAEGKEVREFHGRQYLMEESITGDFAIVKGWKADHFGNVIYRHTAQNFNPLAATAGKITVVEVEEIVEPGELDPTQIHTPGIYVDRVICGTFEKRIEQRTVRK Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2112 Dehydrocarnitine CoA-transferase and acetoacetate CoA-transferase, subunit B Specifically important for: Carnitine Hydrochloride; L-Phenylalanine. Also important on L-leucine. Converts dehydrocarnitine to dehydrocarnitine-CoA during carnitine catabolism. Probably also acts on acetoacetate, which is an intermediate in the degradation of phenylalanine (via tyrosine and homogentistate) and leucine (from HMG-CoA lyase). Both substrates are 3-oxoacids, but not sure if succinyl-CoA is the source of the CoA as annotated. Similar to DhcB = PA2000. Succinyl-CoA:3-ketoacid-coenzyme A transferase subunit B (EC 2.8.3.5) MALSREQMAQRVAREMQDGYYVNLGIGIPTLVANYIPEGMEVMLQSENGLLGMGAFPTEAEVDADMINAGKQTVTARIGASIFSSAESFAMIRGGHIDLTVLGAFEVDVEGNIASWMIPGKLVKGMGGAMDLVAGAENIIVTMTHASKDGESKLLPRCSLPLTGAGCIKRVLTDLAYLEIQDGAFILKERAPGVSVEEIVAKTAGKLIVPDHVPEMQFAAQ Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2427 DNA damage response gene with a putative DNA binding domain and often regulated by LexA (PA0922-like) Conserved and specific phenotype: important for resisting cisplatin. Transcriptional regulators LVNVEQLKSSVNRMSADVVREAVLELRLDGLVTEGKTPFNKLHFNTCFAEIEALFQRAGYHKQLDVVGYQGLLYALYDPGRWEAVEVLRWLKEFTEAAAKSTSVTT Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2632 tyrosine aminotransferase (EC 2.6.1.57) Specifically important for: L-Phenylalanine. Phenylalanine is first hydroxylated to tyrosine (Pf6N2E2_2630) and then transaminated. KEGG has same EC# but less specific. (KEGG_correct) Aspartate aminotransferase (EC 2.6.1.1) MHFDAIGRVPGDPILGLMEAYGADANPSKFDLGVGVYKDAQGLTPILQSVKQAEQRLVDRQTTKTYIGGHGDAAFGQLINELVLGADSPLISAKRAGATQTPGGTGALRLSADFIAQCLPGRGVWLSNPTWPIHETIFAAAGVKVGHYPYVGADNRLDFEAMLATLNQAPKGDVVLLHACCHNPTGFDLSHEQWRQVLEVVRDRDLLPLIDFAYQGFGDGLEQDAWAVRLFAQALPEVLVTSSCSKNFGLYRDRTGALIVCARDAEKLVDIRSQLANIARNLWSTPPDHGAAVVATILGNPELKSLWADEVQAMRLRIAQLRSGLLEALEPHGLRERFAHIGVQRGMFSYTGLTPEQVKHLRERHSVYMVGTGRANVAGIDATRLDLLAEAIADACK Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2878 required for 4-hydroxybenzoate and octanoate transport, together with MFP and FUSC proteins (Pf6N2E2_2877, Pf6N2E2_2879) PFam PF07869.8 (DUF1656). A conserved cofit operon. Important for utilization of octanoate and 4-hydroxybenzoate, which are probably toxic at the high concentrations used (5-20 mM), but it could also be for uptake rather than efflux. FIG00953813: hypothetical protein MGLREWSIGGVLLSPFLIYVVLALLVTGALRLLLSLMPAGRWIWHEALFDCALYVCVLTVITVVLGPL Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2958 ABC transporter for L-Lysine, periplasmic substrate-binding component Specific phenotype on L-Lysine; Gly-Glu. There is another dedicated transporter for the dipeptide gly-glu so the basis of that phenotype is unclear. Lysine-arginine-ornithine-binding periplasmic protein precursor (TC 3.A.1.3.1) MKKALLTLSALALCMAAGVATAKEYKELRFGVDPSYAPFESKAADGSLVGFDIDLGNAICAELKVKCKWVESDFDGMIPGLKANKFDGVISSMTVTPAREKAIDFSSELFSGPTAYVFKKGSGLSEDVASLKGKTVGYEQGTIQEAYAKAVLDKAGVKTQAYQNQDQVYADLTSGRLDAAIQDMLQAELGFLKSPKGEGYEVSKPVDSELLPSKTAIGIRKGNSELKALLNKGIKALHDDGKYAEIQKKHFGDLNLYSGK Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2959 ABC transporter for L-Lysine, permease component 1 Specific phenotypes on L-Lysine. Also important on gly-glu. There is another dedicated transporter for the dipeptide gly-glu so the basis of that phenotype is unclear. Histidine ABC transporter, permease protein HisQ (TC 3.A.1.3.1) MFEQLLQNLGLSAFSLQGFGPLLMQGTWMTIKLSALSLLLSVLLGLLGASAKLSSVKLLRIPAQLYTTLIRGVPDLVLMLLIFYSLQTWLTSLTDFMEWEYIEIDPFGAGVITLGFIYGAYFTETFRGAILSVPRGQVEAATAYGLKRGQRFRFVVFPQMMRFALPGIGNNWMVMLKATALVSIIGLADLVKAAQDAGKSTYQLFYFLVLAALIYLLITSASNFILRWLERRYAAGAREAVR Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2960 ABC transporter for L-Lysine, permease component 2 Specific phenotype on Gly-Glu; L-Lysine. There is another dedicated transporter for the dipeptide gly-glu so the basis of that phenotype is unclear. Histidine ABC transporter, permease protein HisM (TC 3.A.1.3.1) MIELLQEYWRPFLYSDGVNVTGLAMTLWLLSASLLIGFLVSIPLSIARVSPKFYVRWPVQFYTYLFRGTPLYIQLLICYTGIYSIAAVRAQPLLDSFFRDAMNCTILAFALNTCAYTTEIFAGAIRSMNHGEVEAAKAYGLTGWRLYTYVIMPSALRRSLPYYSNEVILMLHSTTVAFTATVPDVLKVARDANSATFLTFQSFGIAALIYLTVTFALVGLFRLAERRWLAFLGPTH Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2962 ABC transporter for L-Lysine, ATPase component Very important for L-lysine and gly-glu utilization. There is another dedicated transporter for the dipeptide gly-glu so the basis of that phenotype is unclear. Histidine ABC transporter, ATP-binding protein HisP (TC 3.A.1.3.1) MYKLTIEGLHKSYGEHEVLKGVSLKAKTGDVISLIGASGSGKSTFLRCINFLEQPNDGAMSLDGQPIQMIKDRHGMHVADADELQRIRTRLAMVFQHFNLWSHMTVLENITMAPRRVLGVSKQEADDRARRYLDKVGLPARVAEQYPAFLSGGQQQRVAIARALAMEPEVMLFDEPTSALDPELVGEVLKVIQGLAEEGRTMIMVTHEMSFARKVSNQVLFLHQGLVEEEGRPEDVLGNPTSERLKQFLSGNLK Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_3621 putative transporter, required for glycine utilization PFam PF03458.9 (UPF0126). conserved specific phenotype of UPF0126 putative membrane protein MLLMLYLIAITAEAMTGALSAGRRGMDWFGVVLIACVTALGGGSVRDVLLGHYPLTWVKHPEYLVLTTAAAMLTVFLARWMRHLRSLFLVLDAAGLVAFTLIGCMTALEMGHGMLVASVSGVITGVFGGILRDIFCNDIPLIFRRELYASVSFAAAWCYLLCVFLQLPSEQAILITLFGGFLLRLLAIRFHWEMPKFVYNDEV Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_3637 yqiA-like hydrolase, affects the cell envelope PFam PF05728.8 (UPF0227). conserved phenotypes: important for resisting doxycycline and for octanoate utilization (also a putative stress) Putative esterase, FIGfam005057 MSGSILYIHGFNSAPASTKASQLINVMAQLGLSDHLQVPALHHHPRQAIGQLEQAIAQLGRPLLVGSSLGGYYATHLAERHGLKALLINPAVSPHRMFDGYLGTQKNLYTDETWELTHDHVTALAELDVPAPRDPQRFQVWLQTGDETLDYRHAQQYYRACALRIQAGGDHSFQGFAQQLPALLSFAGIGADLYQAIDFTSL Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4509 Gamma-glutamyl-putrescine synthetase (EC 6.3.1.11) Specifically important for: Putrescine Dihydrochloride. This synthetase reaction is the first step in putrescine catabolism glutamine synthetase family protein VVRGKRIERTSLHKVYEKGINLPASLFALDINGSTVESTGLGLDIGDADRICYPIPDTLCNEPWQKRPTAQLLMTMHELEGEPFFADPREVLRQVVTKFDELGLTICAAFELEFYLIDQENVNGRPQPPRSPISGKRPHSTQVYLIDDLDEYVDCLQDILEGAKEQGIPADAIVKESAPAQFEVNLHHVADPIKACDYAVLLKRLIKNIAYDHEMDTTFMAKPYPGQAGNGLHVHISILDKDGKNIFASEDPEQNAALRHAIGGVLETLPAQMAFLCPNVNSYRRFGAQFYVPNSPTWGLDNRTVALRVPTGSADAVRLEHRVAGADANPYLLMASVLAGVHHGLVNKIEPGAPVEGNSYEQNEQSLPNNLRDALRELDDSEVMAKYIDPKYIDIFVACKESELEEFEHSISDLEYNWYLHTV Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4510 Gamma-glutamyl-GABA hydrolase (EC 3.5.1.94) Specifically important for: Putrescine Dihydrochloride. part of putrescine catabolism via gamma-glutamyl-putrescine (SEED_correct) Gamma-glutamyl-GABA hydrolase (EC 3.5.1.94) MSRLPLIGVTTCSRQIGLHAYHISGEKYSRAVATAAKGLPVLIPSLADLFPPSDILDALDGILLTGSPSNVEPFHYQGPASAPGTAHDPARDATTLPLIRAAVDAGIPVLGICRGFQEMNVAFGGSLHQKVHEVGTFIDHREDDTQAVDVQYGPAHAVHIQPGGVLAGLGLPQRIEVNSIHSQGIERLAPGLRAEAVAPDGLIEAVSVPGGKAFALGVQWHPEWEVSSNPHYLAIFQAFGDACRARAAQRDADASNNA Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4512 Gamma-aminobutyrate:alpha-ketoglutarate aminotransferase (EC 2.6.1.19) Specifically important for: Putrescine Dihydrochloride. KEGG annotates this as putrescine aminotransferase, probably based on similarity to spuC (PA0299) of P. aeruginosa, but it is believed that only the g-glutamyl- pathway operates in P. aeruginosa (X. Yao et al 2011, PMC3147493) Omega-amino acid--pyruvate aminotransferase (EC 2.6.1.18) MTRNNPQTREWQALSNDHHLAPFSDFKQLKEKGPRIITHAKGVYLWDSEGNKILDGMAGLWCVAVGYGREELADAASQQMRELPYYNLFFQTAHPPVLELSKAIADIAPEGMNHVFFTGSGSEGNDTMLRMVRHYWAIKGQPNKKVIISRKNGYHGSTVAGASLGGMTYMHEQGDLPIPGIVHIAQPYWFGEGGDMSPEEFGVWAANQLEEKILELGVDNVGAFIAEPIQGAGGVIVPPDSYWPRMKEILAKYDILFVADEVICGFGRTGEWFGTDHYELKPHMMTIAKGLTSGYIPMGGLIVRDDVVAVLNEGGDFNHGFTYSGHPVAAAVALENIRILRDEKIIERVHSETAPYLQKRLRELNDHPLVGEVRGVGLLGAIELVQDKATRKRYEGKGVGMICRQFCFDNGLIMRAVGDTMIIAPPLVISKAEIDELVAKARQCLDLTLSALQG Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4681 ABC transporter for Carnitine, ATPase component Specific phenotype on Carnitine Hydrochloride. This ABC transporter might also take up choline or glycine-betaine, in conjunction with another SBP, Pf6N2E2_4683 L-proline glycine betaine ABC transport system permease protein ProV (TC 3.A.1.12.1) MSIIRFEDVDVIFSNRPKAALDLLDKGLSRPEILQQTGLIVGVEKASLSIEKGEICVLMGLSGSGKSSLLRCINGLNTVSRGKLFVEHEGRQIDIASCSPAELKMMRTKRIAMVFQKFALMPWLTVRENISFGLEMQGRPEKERRKLVDEKLELVGLTQWRNKKPDELSGGMQQRVGLARALAMDADILLMDEPFSALDPLIRQGLQDELLELQRKLQKTIVFVSHDLDEALKLGTRIAIMKDGKIIQYSKPEEIVLNPADDYVRTFVAHTNPLNVLCGRSLMRTLDNCKRINGSVCLDPGGDSWLDLAEGNTIKGARQNGAALDLQNWVPGQAVEDLGRRPTLVDSNIGMRDALQIRYQTGNKLVLHDNQQVVGILGDSELYHALLGKNLG Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4682 ABC transporter for Carnitine, permease component Specific phenotypes on Carnitine Hydrochloride. This ABC transporter might also take up choline or glycine-betaine, in conjunction with another SBP, Pf6N2E2_4683 L-proline glycine betaine ABC transport system permease protein ProW (TC 3.A.1.12.1) MLIDQKIPLGQYIAGFVEWLTQNGANTFDAIALFLETMIHGVTFALTWFNPLALIGLIALLAHFIQRKWGLTIFVIASFLLILNLGYWQETMETLAQVLFATLVCVLIGVPLGIVAAHKPMFYTMMRPVLDLMQTVPTFVYLIPTLTLFGLGVVPGLISTVVFAIAAPIRLTYLGIRDVPDELMDAGKAFGCSRRQLLSRIELPHAMPSIAAGITQCIMLSLSMVVIAALVGADGLGKPVVNALNTADIALGFEAGLAIVLLAIMLDRICKQPDAKVGGDA Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4689 L-carnitine 3-dehydrogenase, B subunit (EC 1.1.1.108) Specifically important for: Carnitine Hydrochloride. Similar to CdhB = PA5385 FIG143042: Thioesterase-like protein MPTLTTYQTRILPEWVDYNGHLRDAFYLLIFSYATDALMDRLGMDSQNREASGHSLFTLELHLNYLHEVKLDAQVEVHTHIIGHDAKRLHLYHSLHLVGGDKELAGNEQMLLHVDLAGPRSAPFTEQTLDRLSALLDEQSDLPPPLYIGRIIALPLPR Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4690 L-carnitine 3-dehydrogenase, A subunit (EC 1.1.1.108) Specifically important for: Carnitine Hydrochloride. Similar to CdhA = PA5386 Carnitine 3-dehydrogenase (EC 1.1.1.108) @ 3-hydroxybutyryl-CoA dehydrogenase (EC 1.1.1.157) @ 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) MSFITDIKTFAALGSGVIGSGWISRALAHGLDVIAWDPAPGAEAALRKRVANAWGALEKQGLAPGASQDRLRFVATIEECVRDADFIQESAPERLELKLELHGQISAAAKPNALIGSSTSGLLPSEFYEGATHPERCVVGHPFNPVYLLPLVEVVGGKNTAPEAVQAAMQVYESLGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLAGGDAGMRHFMAQFGPALQLPWTYLPAPELTEKLIDDVVDGTSAQLGSHSISALERYRDDCLLAVLEAVKATKAKHGMAFSE Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4692 dehydrocarnitine cleavage enzyme (EC 2.3.1.-) Specifically important for: Carnitine Hydrochloride. Similar to CdhC = PA5387 FIG004891: hypothetical protein in carnitine cluster MNHDVIITCALTGAGDTTAKSPHVPVTPKQIADAAIEAAKAGATVVHCHVRDPQTGKFSRDVALYREVMERIREADVDIIVNLTAGMGGDLEIGAGEQPMEFGPNTDLVGPLTRLAHVEELLPEICTLDCGTLNFGDGDTIYVSTPAQLRAGAKRITELGVKAELEIFDTGHLWFAKQLIKEGLLDNPLFQLCLGIPWGAPADTTTMKAMVDNLPADAVWAGFGIGRMQMPMAAQAVLLGGNVRVGLEDNLWLDKGVLATNGQLVERAGEILSRLGARVLTPAEGRKKMGLTQRG Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4693 ABC transporter for Carnitine Hydrochloride, periplasmic substrate-binding component Specific phenotype on Carnitine Hydrochloride. Similar to CaiX. There might also be another SBP, Pf6N2E2_4683 (similar to CbcX) that is expected to be specific for choline and glycine-betaine. However _4683 is important for carnitine utilization as well and it does not appear to be a polar effect, so it could be another subunit. L-proline glycine betaine binding ABC transporter protein ProX (TC 3.A.1.12.1) MKRLISSCVLALCGTTFLNGTAMAAEPAACQNVRLGVVNWTDVIATSALTQVMLDGLGYKTKQTSASQQIIFAGIRDQRLDLFLGYWNPLMTQTITPFVEAKQVKVLEQPSLKDARATLAVPTYLADKGLKTFADIAKFEKELGGKIYGIEPGSGANTQIKAMIAKNQFGLGKFQLVESSEAGMLAAVDRAVRRKEAVVFFGWAPHPMNVNVQMTYLTGSDDALGPNEGMATVWTVTAPDYAQQCPNVGRLLSNLTFSAEDESRMMQPLLDHKDPLESARQWLKDHPQDKQRWLEGVTTFDGKPAADNLKLTSN Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4799 ycgB component of nitrogen-related signalling system (of yeaGH-ycgB) conserved cofitness; yeaG is a protein kinase FIG004684: SpoVR-like protein MTAKKEQKRQPISTGSEWTFELIKAYDREISRIADRYALDTYPNQIEVITAEQMMDAYASVGMPLGYHHWSYGKHFLSTEKSYSRGQMGLAYEIVINSDPCIAYLMEENTICMQALVVAHACYGHNSFFKGNYLFRTWTDASSIIDYLVFAKQYIMQCEERHGIDAVEDLLDSCHALMNYGVDRYKRPYPISAEEERRRQKDREEHLQKQINDLWRTIPKGADKYNEKDNARFPAEPQENILYFIEKHAPLLEPWQREIVRIVRKIAQYFYPQRQTQVMNEGWATFWHYTLMNDLYDEGLVTDGFMMEFLTSHTSVVFQPGFDSPYYSGINPYALGFAMYRDIRRMCENPTEEDRRWFPEIAGSDWLSAIKFAMSSFKDESFILQYLSPKVIRDLKLFSILDDDQKDDLLVPAIHDEGGYRIIRETLAAQYNLGNREPNVQIYSIDRRGDRSLTLRHQAHNRKPLGDSTDEVLKHLHRLWGFDIHLETLQGDQVMKTHHVPPRGEQAEGDYGRLDLAVIHL Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4800 yeaH component of nitrogen-related signalling system yeaH (of yeaGH-ycgB) PFam PF04285.8 (DUF444). conserved cofitness; yeaG is a protein kinase FIG002076: hypothetical protein MSYVIDRRLNGKNKSTVNRQRFLRRYRDHIKKAVEEAVSRRSITDMEHGEQISIPGRDIDEPVLHHGRGGKQTVVHPGNKEFTSGEHIPRPQGGGGGKGPGKAGNSGEGMDEFVFQITQEEFLEFMFEDLELPNLVKRNLTGTDTFKTVRAGISNEGNPSRINIIRTLRSAHARRIALSGSSRAKLREVKEELARLKREEPDNFGDIQDLEAEIEKLSARIHRVPFLDTFDLKYNLLVKQPNPSSKAVMFCLMDVSGSMTQATKDIAKRFFILLYLFLKRNYDKIDVVFIRHHTSAREVDEEEFFYSRETGGTIVSSALKLMQEIMAERYPANEWNIYAAQASDGDNWNDDSPICRDILINQIMPFVQYYTYVEITPREHQALWYEYERIAEAFSDTFAQQQLVSAGDIYPVFRELFQRRLVT Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4801 yeaG component of nitrogen-related signalling system (of yeaGH-ycgB) conserved cofitness; yeaG is a protein kinase Serine protein kinase (prkA protein), P-loop containing MSIFSHFQQRFESTRQEEYSLQEYLELCKQDRSAYASAAERLLLAIGEPELLDTSTNSRLSRIFSNKVIRRYPAFADFHGMEECIEQIVSYFRHAAQGLEEKKQILYLLGPVGGGKSSLAEKLKQLIEKVPFYAIKGSPVFESPLGLFNATEDGAILEEDFGIPRRYLNTIMSPWATKRLAEFGGDISQFKVVKLYPSILNQIAVAKTEPGDENNQDISALVGKVDIRKLEEFPQNDADAYSYSGALCRANQGLMEFVEMFKAPIKVLHPLLTATQEGNYNSTEGLGAIPFTGILLAHSNESEWHTFRNNKNNEAFIDRIYIVKVPYCLRVSDEVKIYDKLLFNSSLSKAHCAPDTLKMLAQFTVLSRLKEPENSNIYSKMRVYDGENLKDTDPKAKSIQEYRDNAGVDEGMNGLSTRFAFKILSKVFNFDPHEIAANPVHLLYVLEQQIEQEQFQAETRERYLRFLKEYLAPRYIEFIGKEIQTAYLESYSEYGQNIFDRYVLYADFWIQDQEYRDPETGEILNRVALNEELEKIEKPAGISNPKDFRNEIVNFVLRARANNNGKNPTWLSYEKLRVVIEKKMFSNTEDLLPVISFNAKASKEDQQKHNDFVTRMVERGYTDKQVRLLSEWYLRVRKSQ Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_515 malonate-semialdehyde dehydrogenase (acetylating) (EC 1.2.1.18) Specifically important for: m-Inositol. 3-oxopropionate or malonate semialdehyde is an intermediate in myo-inositol catabolism Methylmalonate-semialdehyde dehydrogenase [inositol] (EC 1.2.1.27) MSDAPVVGHYLNGHVQDHDSTRFSNVFNPATGAVQARVALAEPGTVDAAVASALAAFPAWSEQSSLRRSRVMFKFKELLDRHHDELAQIISREHGKVLSDAHGEVTRGIEIVEYACGAPNLLKTDFSDNIGGGIDNWNLRQPLGVCAGVTPFNFPVMVPLWMIPLALVAGNCFILKPSERDPSASLLMARLLTEAGLPDGVFNVVQGDKVAVDALLQHPDIEAISFVGSTPIAEYIHQQGTAHGKRVQALGGAKNHMIVMPDADLDQAADALIGAAYGSAGERCMAISIAVAVGDVGDELIAKLLPRIDQLKIGNGQQPGTDMGPLVTAEHKAKVEGFIDAGVAEGARLIVDGRSFKVPGAEQGFFVGATLFDQVTAEMSIYQQEIFGPVLGIVRVPDFATAVALINAHEFGNGVSCFTRDGGIARAFARSIKVGMVGINVPIPVPMAWHSFGGWKRSLFGDHHAYGEEGLRFYSRYKSVMQRWPDSIAKGPEFSMPTAQ Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5373 required for cephalothin efflux, together with NodT, MFP and FUSC proteins (Pf6N2E2_5371, Pf6N2E2_5374, Pf6N2E2_5372) PFam PF07869.8 (DUF1656). A conserved cofit operon. Specifically important for resisting cephalothin. Na+-dependent transporters of the SNF family MPREIAFHGVYMPTMTLMFFIAAGLAWALDRFLSGLDLYRFFWHPALLRLSLFTCLFGALALTVYR Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5402 ABC transporter for D-Alanine, periplasmic substrate-binding component Very important for D-alanine utilization. This transporter may also uptake L-histidine. Glutamate Aspartate periplasmic binding protein precursor GltI (TC 3.A.1.3.4) MKLLKSTLAVMTAAAVLGVSGFAQAGATLDAVQKKGFVQCGVSDGLPGFSVPDSTGKIVGIDADFCRAVAAAVFGDATKVKFSQLNAKERFTALQSGEIDMLSRNSTMTSSRDAGMGLKFPGFITYYDGIGFLANNKLGVKSAKELDGATICIQAGTTTELNVSDYFRANGLKYTPITFDTSDESAKSLESGRCDVLTSDKSQLFAQRSKLASPKDYVVLPETISKEPLGPVVRNGDDEWLAIVRWTGYALLNAEEAGVTSKNVEAEAKSTKNPDVARMLGADGEYGKDLKLPKDWVVQIVKQVGNYGEMFERNLGKGTPLEIDRGLNALWNAGGIQYAPPVR Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5403 ABC transporter for D-Alanine, permease component 2 Very important for D-alanine utilization. This transporter may also uptake L-histidine. Glutamate Aspartate transport system permease protein GltJ (TC 3.A.1.3.4) VRAWVFQVVTVVAVIALGWFLFDNTQTNLQHRGITSGFGFLERSAGFGIAQHLIDYTEADSYARVFLIGLLNTLLVTFIGVILATILGFIIGVARLSQNWIISKLATVYVEVFRNIPPLLQILFWYFAVFLSMPGPRAAHNFGDTFFVSSRGLNMPAALVAEGFWPFVISVVLAIVAIVLMTRWANKRFEATGEPFHKFWVGLALFLVIPALSALLFGAPVHWEMPELKGFNFVGGWVLIPELLALTLALTVYTAAFIAEIVRSGIKSVSHGQTEAARSLGLRNGPTLRKVIIPQALRVIIPPLTSQYLNLAKNSSLAAGIGYPEMVSLFAGTVLNQTGQAIEVIAITMSVYLAISISISLLMNWYNKRIALIER Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5404 ABC transporter for D-Alanine, permease component 1 Specific phenotypes on D-Alanine. Also important for histidine utilization, so this may also take up L-histidine Glutamate Aspartate transport system permease protein GltK (TC 3.A.1.3.4) MTTHTFKPDMPPPGSSIGVVAWMRANMFSSWINTLLTLFAFYLIYLIVPPLVQWAILDANWVGTTRADCTKEGACWVFIQQRFGQFMYGYYPADLRWRVDLTVWLAVIGVAPLFISRFPRKAIYGLSFLVLYPISAWCLLHGGVFGLDAVATSQWGGLMLTLVIATVGIVGALPLGIVLALGRRSNMPAIRVVCVTFIEFWRGVPLITVLFMSSVMLPLFLPEGMNFDKLLRALIGVILFQSAYIAEVVRGGLQAIPKGQYEAAAAMGLGYWRSMGLVILPQALKLVIPGIVNTFIALFKDTSLVIIIGLFDLLNSVKQAAADPKWLGMATEGYVFAALVFWIFCFGMSRYSMHLERKLDTGHKR Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5405 ABC transporter for D-Alanine, ATPase component Very important for D-alanine utilization. This transporter may also uptake L-histidine. ABC-type polar amino acid transport system, ATPase component MSEAIKQPVSPEGIIQMQGVNKWYGQFHVLKDINLNVKQGERIVLCGPSGSGKSTTIRCLNRLEEHQQGRIVVDGVELTNDLKQIEAIRREVGMVFQHFNLFPHLTILQNCTLAPMWVRKMPKRKAEEIAMHYLERVRIPEQAHKYPGQLSGGQQQRVAIARALCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAEDGMTMLCVTHEMGFARTVANRVIFMDKGEIVEQAAPNDFFDNPQNDRTKLFLSQILH Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5616 outer membrane component of uptake system, probably for ferrous iron PFam PF07433.7 (DUF1513). In a conserved cofit operon with an efeO-like gene (Pf6N2E2_5617) and an efeB-like gene (Pf6N2E2_5618). Another efeO-like gene (Pf6N2E2_2853) is cofit but not nearby. putative exported protein MFRRQVLALGSLLLGAVTLGGWTLFKQKDKHPLLLSARDDGDGKHYAVGYRLDGTRVFATQVGQRCHDIINHPTQPIALFVARRPGTESYLIDLRDGALLQTIASLPNRHFYGHAVIHNSGEWLYATENDTTDPGRGLLGVYRFEGERLVHSGEISTHGIGPHQVSWMPDGETLVVANGGIRTEAESRVEMNLDAMEPSLVLMQRDGTLLSKETLAQSMNSVRHLGIASDGTIVSGQQFMGAAHESSELLAIKRPGQPFQAFPLPEEQLQAMGHYTASVAVHSDLRLVALTAPRGNRFFIWDLDSGEVRLDAPLPDCAGVGAVADGFVVTSGQGRCRYYDCRQTQLVAKPLDLPAGLWDNHLHLA Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5660 L-Arginine ABC transporter, periplasmic substrate-binding component Specific phenotype on L-Arginine. (SEED_correct) Arginine/ornithine ABC transporter, periplasmic arginine/ornithine binding protein MKKLVLLGALALSVLSLPTFADEKPLKIGIEAAYPPFASKAPDGSIVGFDYDIGNALCEEMKVKCVWVEQEFDGLIPALKVRKIDAILSSMSITEDRKKSVDFTNKYYNTPARLVMKAGTQVSDNLAELKGKNIGVQRGSIHERFAREVLAPLGAEIKPYGSQNEIYLDVSAGRLDGTVADATLLDDGFLKTDAGKGFAFVGPAFTDEKYFGDGIGIAVRKGDALKDKINGAITAIRENGKYKQIQDKYFAFDIYGK Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5661 L-Arginine ABC transporter, permease protein AotQ Specific phenotypes on L-Arginine; L-Arginine. no data for ornithine (SEED_correct) Arginine/ornithine ABC transporter, permease protein AotQ MLKGYGAVILDGAWLTLELALSSMALAIVLGLIGVALRLSPVRWLAWLGDLYATVIRGIPDLVLILLIFYGGQDLLNRVAPMLGYDDYIDLNPLAAGIGTLGFIFGAYLSETFRGAFMAIPKGQAEAGMAYGMNGFQVFFRVLVPQMIRLAIPGFTNNWLVLTKATALISVVGLQDMMFKAKQAADATREPFTFFLAVAAMYLVITSVSLLALRHLEKRYSVGVRAADL Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5662 L-Arginine ABC transporter, permease protein AotM Specific phenotypes on L-Arginine; L-Arginine. (SEED_correct) Arginine/ornithine ABC transporter, permease protein AotM MIFDYNVIYEALPLYFSGLLTTLKLLALSLFFGLLAALPLGLMRVSKQPIVNMTAWLYTYVIRGTPMLVQLFLIYYGLAQFAIVRESFLWPWLSSATFCACLAFAINTSAYTAEIIAGSLRATSNGEIEAAKAMGMSRYKLYRRILLPSALRRALPQYSNEVIMMLQTTSLASIVTLIDITGAARTVNAQYYLPFEAYITAGVFYLCLTFILVRLFKLAERRWLGYLAPRKH Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5663 L-Arginine ABC transporter, ATPase component Very important for utilizing L-arginine. (SEED_correct) Arginine/ornithine ABC transporter, ATP-binding protein AotP MYKLEVQDLHKRYGSHEVLKGVSLKAAAGDVISIIGSSGSGKSTFLRCINLLEQPHAGKILLNNEELKLVAGKDGALKAADPKQLQRMRSRLSMVFQHFNLWSHMTALENIMEAPVHVLGVTKAQAREKAEHYLNKVGVAHRKDAYPGHMSGGEQQRVAIARALAMEPEVMLFDEPTSALDPELVGDVLKVMQGLALEGRTMVVVTHEMGFAREVSNQLVFLHKGIVEESGNPREVLVNPQSERLQQFLSGSLK Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5967 L-arabinose 1-dehydrogenase / D-galactose 1-dehydrogenase (EC 1.1.1.46; EC 1.1.1.48) Important for utilization of L-arabinose and D-galactose in several Pseudomonas. Both of these sugars are catabolized via a 1-dehydrogenase followed by lactonase and dehydratase reactions. This is the only dehydrogenase is specifically important for either of these carbon sources in several Pseudomonas, except for an alpha-ketoglutarate semialdehyde dehydrogenase that is expected to be the last dedicated step in L-arabinose catabolism (i.e., Pf6N2E2_612). L-arabinose and D-galactose are chemically similar and some dehydrogenases are already known to act on both substrates. This gene might also be involved in D-gluconate utilization. 3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100) MAEPLSLPPVPEPPKGERLKNKVVLLTGAAQGIGEAIVAAFASQQARLVISDIQAEKVETVAAHWRERGADVHALKADVSNQQDLHAMARHAVERHGRIDVLVNCAGVNVFRDPLEMTEEDWRRCFAIDLDGAWYGCKAVLPQMIEQGVGSIINIASTHSSHIIPGCFPYPVAKHGLLGLTRALGIEYAPKGVRVNAIAPGYIETQLNVDYWNGFADPYAERQRALDLHPPRRIGQPIEVAMTAVFLASDEAPFINASCITIDGGRSVMYHD Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_80 gamma-glutamylputrescine oxidase (EC 1.4.3.-) Specifically important for: Putrescine Dihydrochloride. This is part of the gamma-glutamyl-putrescine pathway. (KEGG_correct) Nucleoside-diphosphate-sugar epimerases VIGAGYTGLSSALFLLENGFKVTVLEAAKVGFGASGRNGGQIVNSYSRDIDVIERSVGPQQAQLLGNMAFEGGRIIRERVAKYQIQCDLKDGGVFAALTAKQMGHLESQKRLWERFGHTQLELLDQRRIREVVACEEYVGGMLDMSGGHIHPLNLALGEAAAVESLGGVIYEQSPAVRIERGASPVVHTPQGKVRAKFIIVAGNAYLGNLVPELAAKSMPCGTQVIATEPLGDELAHSLLPQDYCVEDCNYLLDYYRLTGDKRLIFGGGVVYGARDPANIEAIIRPKMLKAFPQLKDVKIDYAWTGNFLLTLSRLPQVGRLGDNIYYSQGCSGHGVTYTHLAGKVLAEALRGQAERFDAFADLPHYPFPGGQLLRTPFAAMGAWYYGLRDKLGF Pseudomonas stutzeri RCH2 psRCH2 GFF84 Psest_0084 alpha-ketoglutarate TRAP transporter, 4TM/12TM components specific phenotype on a-ketoglutarate and no other transporter for this substrate is apparent in the fitness data. (Mutants in another TRAP system, Psest_4268:Psest_4270, have a much milder defect in a-ketoglutarate utilization). TRAP transporter, 4TM/12TM fusion protein MSESQGLHASPSEWPRALFYVALLFSIYQIVTAAFHPVSSQVLRAGHVGFLLLLVFLCYPARGNGKPFQPVAWLLGLAGFATFFYQWYFEADLIQRSGDMTTADMVVGLTLIVLVFEAARRVMGIALPIICALFLAYGLLGEYLPGDLAHRGYYLDQIVNQLSFGTEGLYGTPTYVSATYIFLFILFGSFLEQAGMIKLFTDFAMGLFGHKLGGPAKVSVVSSALMGTITGSGVANVVTTGQFTIPLMKRFGYRPAFAGGVEATSSMGSQIMPPVMGAVAFIMAETINVPFVEIAKAALIPALLYFGSVFWMVHLEAKRAGLKGLPKDECPSAMAAVKERWYLLIPLVVLVWLLFSGRTPMFAGTIGLALTAIVILGSAIILKVSNFALRIAFWIALGLLCAGFFQLGIGVIFGVIAALVAVCWFIKGGRDTLVICLHALVEGARHAVPVGIACALVGVIIGVVSLTGVASTFAGYILAVGENNLFLSLLLTMLTCLVLGMGIPTIPNYIITSSIAAPALLDLGVPLIVSHMFVFYFGIMADLTPPVALACFAAAPIAKERGLKISMWAIRIAIAGFIVPFMAVYNPALMMQGGDWGATLYMLFKAAFAVGLWGAVFTGYLQRPMALWEKVLAFAAAASMVLAMPISDEIGFALGALFLIQHIWRARRAEPATA Pseudomonas stutzeri RCH2 psRCH2 GFF85 Psest_0085 alpha-ketoglutarate TRAP transporter, solute receptor component specific phenotype on a-ketoglutarate and no other transporter for this substrate is apparent in the fitness data. (Mutants in another TRAP system, Psest_4268:Psest_4270, have a much milder defect in a-ketoglutarate utilization). TRAP transporter solute receptor, TAXI family MRLTKRLGLLAAAAAFTASTAAVAAPTFINILTGGTSGVYYPIGVALSQQYNKIDGAKTSVQATKASVENLNLLQAGRGELAFSLGDSVEDAWNGVEDAGFKAPLKRLRAIAGTYNNYIQIVASAESGIKTLDDLKGKRISVGAPKSGTELNARAIFKAAGLDYKDMGRVEFLPYAESVELIKNRQLDATLQSSGLGMAAIRDLASTMPVTFVEIPAEVVEKIESDAYLAGVIPAGTYDGQDADVPTVAITNILVTHEKVSDEVAYQMTKLMFDNLAALGNAHSAAKDIKLENATKNLPIPLHPGAERFYKEAGVLK Pseudomonas stutzeri RCH2 psRCH2 GFF418 Psest_0419 Acyl-CoA dehydrogenase (EC 1.3.8.7) Specifically important for: L-tyrosine disodium salt; Sodium butyrate; Tween 20. tween 20 hydrolyzes to a mix of C12, C14, and C16 fatty acids; this is probably part of beta oxidation (SEED_correct) Acyl-CoA dehydrogenases MADYQAPLRDMRFVLNEVFDAPKLWQALPALAEVVDAETADAILEEAGKITANSIAPLNRSGDEEGCRWDAGAVSTPAGYREAYQLYAKGGWVGVGGDPAFGGMGMPKVISAQVEEMMNSASLAFGLYPMLTSGACLSIYAHASEELKQKYLPNMYAGVWSGSMCLTEPHAGTDLGIIRTKAEPQADGSYKVSGTKIFITGGEHDLTENIIHLVLAKLPDAPAGSRGISLFLVPKVMVNEDGSLGERNSLSCGSIEHKMGIQASATCVMNFDGAVGWMVGEPNKGLAAMFTMMNYERLGVGIQGLATGERSYQSAIEYARDRIQSRAPTGPVAQDKAADPIIVHPDVRRMLLTMKALNEGGRAFSSYVALQLDIAKFSDDDEARQRAEAQVALLTPVAKAFLTDMGLETTVHGQQVFGGHGFIREWGQEQLVRDCRITQIYEGTNGIQALDLVGRKIVGSGGTMYQAFVDEIRAFIADAGPELTEFAEPLKAAMDNLDELTAWVIDQAKANPNEIGAASVEYLHVFGYTAYAYMWARMAAVAVAKREEGDFYQSKLGTARFYFARLLPRIHSLSASVKAGSESLYLLDAAQF Pseudomonas stutzeri RCH2 psRCH2 GFF477 Psest_0482 yqiA-like hydrolase, affects the cell envelope PFam PF05728.8 (UPF0227). Conserved phenotypes: important for resisting carbenicillin and doxycycline Predicted esterase MSSDSPSILYIHGLNSSPLSQKASQLSAALEKLGLAERLRVPALHHHPRQAIAQLEACISELGRPLLVGSSLGGYYATHLAERHGLKALLINPAVTPHRRFDGYLGPQTNLYSGEVWELTEDHVAALAELETAPPQDAERYQVWLQTADETLDYRDAAQFYRGCALRIQAGGDHGFQGFSERLPALLAFAGVAPQIWLEQL Pseudomonas stutzeri RCH2 psRCH2 GFF765 Psest_0779 tyrosine aminotransferase (EC 2.6.1.57) Specifically important for: L-tyrosine disodium salt. This is cofit with 4-hydroxyphenylpyruvate dioxygenase (Psest_0779) which would be the second step in tyrosine catabolism (KEGG_correct) Aspartate/tyrosine/aromatic aminotransferase MHFGQIPRVPGDPILGLMDLYRADPNPAKLDLGVGVYKDAQGLTPIPRAVKLAEQRLVDGEQSKSYIGGHGDAQFGALLLRQALGSRAIALGEQRAGCTQAPGGTGALRLAGEFIAKCLPGRSIWLSDPTWPIHETLFAAAGLRVQHYPYVGADNRLDVEGMLAALQQVPPGDVVLLHACCHNPTGFDLNHDDWLRVLEVVRARELLPLFDFAYQGFGDGLEEDAWAVRLFAETLPEMLITTSCSKNFGLYRERTGALIAVTSDAERLLDVRSQLASLARNLWSTPPAHGAAVVATILADEPLRQIWQGEVERMRRRIASLRQGLVEALMPYGLAERFAHIAQQRGMFSYTGLTAEQVRRLRAEDSVYLVESGRANVAGLDAERLDALAKAIARVVSN Pseudomonas stutzeri RCH2 psRCH2 GFF1044 Psest_1077 acetyl-CoA:acetoacetate CoA transferase, B subunit (EC 2.8.3.8) Specifically important for: L-tyrosine disodium salt; L-Leucine. This role makes sense because of its involvement in acetoacetate catabolism (from tyrosine or leucine). It had been annotated as succinyl-CoA:3-ketoacid-coenzyme A transferase (a broader range of substrates and with succinyl-CoA not acetyl-CoA as donor). Similar to E. coli atoA (52% identical), which has this activity. 3-oxoacid CoA-transferase, B subunit MAWTREQMAQRAAQELQDGFYVNLGIGLPTLVANYIPEGMDVWLQSENGLLGIGPFPTEEEIDPDLINAGKQTVTALPGSSFFDNAQSFAMIRGGHINLAILGAMQVSEKGDLANWMIPGKMVKGMGGAMDLVAGVKRVVVLMEHTAKGGAHKILPACDLPLTGLGVVDRIITDLGVLDVTEQGLKLVELAEGVSFDELQEATGSPIQR Pseudomonas stutzeri RCH2 psRCH2 GFF1045 Psest_1078 acetyl-CoA:acetoacetate CoA transferase, A subunit (EC 2.8.3.8) Specifically important for: L-Leucine. Important on tyrosine as well. This role makes sense because of its involvement in acetoacetate catabolism (from tyrosine or leucine). It had been annotated as succinyl-CoA:3-ketoacid-coenzyme A transferase (a broader range of substrates and with succinyl-CoA not acetyl-CoA as donor). Similar to E. coli atoD (46% identical), which has the same activity. 3-oxoacid CoA-transferase, A subunit MNKIYPSAAHALEGLVEDGMTIAVGGFGLCGIPEQLIAALRDSGKKDLTAISNNAGVDGFGLGLLLETRQISKMVSSYVGENKEFERQYLAGELALEFTPQGTLAEKLRAGGAGIPAFYTKTGYGTLVAEGKETRQFNGEWYVMEESLTADLALVKAWKADKAGNLLFRKTARNFNPLAAMAGEVCVVEVEEIVETGELDPDQIHLPGIYVHRIVHNPNPEKRIEKRTVRS Pseudomonas stutzeri RCH2 psRCH2 GFF1123 Psest_1156 outer membrane component of uptake system, probably for ferrous iron PFam PF07433.7 (DUF1513). In a conserved cofit operon with two efeO-like genes (Psest_1159,Psest_1157) and a efeB-like gene (Psest_1158) Uncharacterized protein conserved in bacteria MRRRTLLGLTGAMFAAGGIAGWTLTRQGDQPVLLSARNDKDGKHYAVGYRLDGSQVFATPVAERCHDVYPHPYLPLAVFVGRRPSRESYLIDSRDGRLLQVLASPPHRHFYGHGVFHQDGEWFYTTENDTADAGRGVLGVYRLEDRQLVRVGEHATHGIGPHQLLWMPDNETLVIANGGIRTEADSRAMMNLDAMEPSLVLLRRDGRLISKEQLPERMNSVRHLAIAADGTIVSGQQYEGDAMDRVPLLAIKRPGQAFQHFPLGERQRQIMNQYTASLAIHDELRLLAVTAPRGNKVFIWDLDSTELRQEAHLPDCAGVAAVAEGFVVSSGQGRCRLFDCRGKGIASTPLELPAGLWDNHLRIV Pseudomonas stutzeri RCH2 psRCH2 GFF1145 Psest_1178 D-glycerate 2-kinase (EC 2.7.1.-) Specifically important for: Glycolic Acid. Either glycerate kinase or hydroxypyruvate reductase could be involved in glycolate utilization (via glyoxylate and tartronate-semialdehyde, which can be converted to glycerate, perhaps via hydroxypyruvate). However this protein is similar to TM1585 (also PDB:2b8nA or GCK_THEMA), which is a glycerate kinase. We were not able to find a rationale for KEGG's annotation as hydroxypyruvate reductase. (SEED_correct) Putative glycerate kinase MTLDPQALLRQLFDSAIEAAHPRHVLADHLPEDRSGRAIVIGAGKAAAAMAEAIEKVWEGELSGLVVTRYEHHADCKRIEVVEAAHPVPDDAGERVARRVLELVSNLEESDRVIFLLSGGGSSLLALPAEGISLADKQAINKALLRSGAHIGEMNCVRKHLSAIKGGRLAKACWPASVYTYAISDVPGDEATVIASGPTVADPTTSEQALEILERYHIEVPANVRAWLEDPRSETLKPGDPMLSRSHFRLIATPQQSLDAAAEVARAAGITPLILGDLEGEAREVAKVHAGIARQVVLHGQPIAAPCVILSGGETTVTVRGNGRGGRNAEFLLALTENLQGLPNVYALAGDTDGIDGSEDNAGALMMPDSYARAETLGLRAADALANNDGYGYFAALDDLIVTGPTRTNVNDFRAILILPPSA Pseudomonas stutzeri RCH2 psRCH2 GFF1599 Psest_1636 putative transporter, required for glycine utilization PFam PF03458.9 (UPF0126). conserved specific phenotype of UPF0126 Predicted membrane protein MELLHTIYLIAITAEAMSGAIMGMRRGMDLFGICLLGTVTALGGGTARDVLLGHYPVGWIAHPEYLTFTIGAAIVTGFIARHLHHLRMVFLLVDGLGLVAFTVIGCDVAMGMGAHPSIVVLAGVITGIFGGLMRDVLCNQVPMVLQRELYATVALFTGVFYVGMLWLEINTTLATLAALGSGFLFRVLAMTFHWKLPDFNGKEIRGLD Pseudomonas stutzeri RCH2 psRCH2 GFF2081 Psest_2124 D-gluconate TRAP transporter, large permease component specific phenotype on D-gluconate and no other transporter is apparent in the fitness data. TRAP transporter, DctM subunit MTVVVFLSSLLGFMTLGMPIAFALLLTGSVLMWYLDFWDVQLLAQNLQAGADSFPLLAVPFFILAGELMNAGGISRRIIAMAQAYFGHKRGGLGYVAIAASVLLASMSGSALADTAALATLLLPMMRERGYPLSSSSGLVAAGGIIAPIIPPSMPFVIYGVVTGTSISQLFLAGMVPGLIMGMGLIVAWTLIARRIDEPKQEKASAAERRRVLVDGAAALMLPVIIVGGLRGGLFTPTEAAVVAAVYALAVSTLLYRELNWAGLVEVLTRASRTTASVMFLCAAATVSAYMITLAQLPDEIAAMLGPLAQDPKLLMVAIMLLMIAVGMVLDLTPTILILGPVLAPIAIKAGIDPVYFGVMFVLIGSIGLITPPVGTVLNVVGGIGRLRMETLVRGVMPFFLIYLVIVGLLIAVPSIITVPLAWLR Pseudomonas stutzeri RCH2 psRCH2 GFF2082 Psest_2125 D-gluconate TRAP transporter, periplasmic component specific phenotype on D-gluconate and no other transporter is apparent in the fitness data tripartite ATP-independent periplasmic transporter solute receptor, DctP family MKRLLISTLAAALLGSTLSLGYAQAADDIRPRMIRFGYGLNEDSNQGRAAKLLAEEVAKASGGKLKVRTFASASLGSDDQMQNALIGGAQEMMVGSTATLVGISKEMAVWDTPFLFTDPRQADQVLDGPVGRQVMDKLEEKGLVGLVYWENGFRNVTNSARPIEKLEDFNGVKLRVMPNPVFIDTFKRMGANAVPLPFSELFTALETKAVDGQENPFNTILSSKFYEVQKYLSVTNHVYSPWIVTVSKRWWDGLSATEQGILMEAAEKARDAEREDTRREASQALAALKERGMQINEVSPDEIQRMREKAQPAIQTVIDAVGQELFDQVQAEVEKAAP Pseudomonas stutzeri RCH2 psRCH2 GFF2190 Psest_2235 DNA damage response nuclease Conserved and specific phenotype: important for resisting cisplatin. Contains a VRR-NUC domain that is predicted to have nuclease activity. VRR-NUC domain. MRQALENPFYYLDNFQQVLAWVGRHHGDLLDETERVFIERFAVLPQPSQALLVRMVMRKGALFRASKLRYGEIGCPRQAAAPLIEHGWIDAGRELTLEQLFSLLTKSELLQLFGAANAAGLRKAELLERLHAVHDLAKPFGAWWAGSEDAVFALCIDELCERLRLLFFGNIHQDWSEFVLADLGVYRYEQVPFSPASRAFSSRAELDAYLHLHRCRERFDAGEPLAEILAAVPAAPFGNAWLESRRGKLLLRIGQQFERLGELDEALRVHASNHYPGARERAIRVLERCGQPAAAMDLLLQARAVPESEHEAQQLQRILPRLQRNLGIPTERARSRKPEQLDLVLPRPTCSVEQAVREHLTTPDAPVYYVENALVGSLFGLLCWDAIFAPLPGAFFHPFHWAPADLNRADFHQRRADLFAACLACLDSDDYRDCIWRTFQAKLGIHNAFVAWGLLDEQLLAQALDCIPAAHLKLLFQRILVDVTGNRTGLPDLIQLWPEERRYRMIEVKGPGDRLQDNQKRWIDYAHQHGLPIAVCHVQWAEVMA Pseudomonas stutzeri RCH2 psRCH2 GFF3447 Psest_3512 fumarylacetoacetate (FAA) hydrolase (EC 3.7.1.2) Specifically important for: L-tyrosine disodium salt; casamino acids. The annotation of psa:PST_0871 has been updated to fumarylacetoacetate (FAA) hydrolase [EC:3.7.1.2], which is a step in tyrosine catabolism (KEGG_correct) 2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) MKLATLNQGRDGVLVVVSRDLAQAVKVPQIAATLQAALDDWNYCKPKLEAVYQRLNDGLEEGAFAFDQTACHSPLPRAYHWADGSAYVNHVELVRKARGAEMPESFWHDPLMYQGGADAFIPPHSPIRLADEAWGIDLEGELAVITDDVPMGATPAEAASHIQLLMLVNDVSLRNLIPGELAKGFGFYQSKPSSSFSPVAVTPDELGETWRDGKVHRPLVSHINGELFGQPDAGTDMTFNFPTLVAHAARTRPLGAGTIIGSGTVSNYDRSAGSSCLAEKRMLEVVEHGEAKTPFLKFGDRVRIEMFDAAGQSIFGAIDQQVERYGH Pseudomonas stutzeri RCH2 psRCH2 GFF3452 Psest_3517 branched-chain ketoacid ferredoxin reductase (EC 1.2.7.7) active on 4-methyl-2-oxopentanoate, (S)-3-methyl-2-oxopentanoate, or 3-methyl-2-oxobutanoate Specifically important for: L-Leucine; L-Isoleucine. This oxidizes and decarboxylates the alpha-keto acid that is produced by a branched chain amino acid dehydrogenase (4-methyl-2-oxopentanoate or (S)-3-methyl-2-oxopentanoate). This is also improtant for utilization of valine as a nitrogen source implying a third substrate (3-methyl-2-oxobutanoate). Indolepyruvate ferredoxin oxidoreductase, alpha and beta subunits MSLAEIRLDDKYRLATGHLYLTGTQALTRLPMLQHQRDQARGLNTGGFISGYRGSPLGGLDKSLWEARDYLKQHAIHFQPGVNEELAATAVWGSQQTNLFPGAKYDGVFAMWYGKGPGVDRAGDVFKHANAAGVSPQGGVLLLAGDDHGCKSSTLPHQSEHAFIAASIPVLNPANVQEILDYGIIGWELSRYSGCWVALKTIAENVDSSAVVEVDPLRVQTRIPEDFELPEDGVHIRWPDPPLAQEKRLNLYKIYAARAFARANNLNRVMLDSPNPRLGIITTGKSYLDVRQALDDLGLDEALCASVGLRVLKVGMSWPLEPVSVHEFAQGLDEILVVEEKRSIIEDQLTGQLYNWPVSKRPRVVGEFDEQGNSLLPNLSELTPAMIARVIAKRLAPIYTSDSIQARLAFLAAKEKALAARSYSTVRTPHYCSGCPHNSSTKVPEGSRASAGIGCHYMVQWMDRRTETFTQMGGEGVNWIGQAPFTDTPHMFQNLGDGTYFHSGSLAVRAAVAAGVNVTYKILYNDAVAMTGGQPIDGELRVDQLSRQIFHEGVKRIALVSDEPDKYPSRDTFAPITSFHHRRELDAVQRELREFKGVSVIIYDQTCATEKRRRRKRGKMEDPAKRAFINPAVCEGCGDCGEKSNCLAVLPLETELGRKREIDQNACNKDFSCVEGFCPSFVTVHGGGLRKPEAVAGGIEAATLPEPQHPTLDRPWNVLIPGVGGSGVTTLGALLGMAAHLEGKGCTVLDQAGLAQKFGPVTTHVRIAAKQSDIYAVRIAAGEADLLLGCDLIVAAGDESLTRLNEQISNAVVNSHESATAEFTRNPDAQVPGAAMRQAISDAVGADKTHFVDATRLATRLLGDSIATNLFLLGFAYQQGLLPISAEAIEKAIELNGVSAKLNLQAFRWGRRAVLEREAVEQLARPVDMVEPICKTLEEIVDWRVDFLTRYQSAGLARRYRQLVERVRDADSADDLALSKAVARYYFKLLAYKDEYEVARLYSEPEFRQQLEAQFEGDYKLQFHLAPAWLAKRDPVTGEPRKRELGPWVLNLFGVLAKFRFLRGTPLDPFGYGHDRRVERQLISEYEKTVDELLAQLKPTNYRTAVAIAALPEQIRGYGPVKERSIAKARQQEKLLREQLAKGDEVQSVRLFQPAA Pseudomonas stutzeri RCH2 psRCH2 GFF3795 Psest_3864 Histidinol-phosphatase (EC:3.1.3.15) Annotated as HAD-superfamily IB hydrolase or sometimes as phosphoserine phosphatase (serB). However Psest_0489 seems to be serB and has auxotrophic phenotypes, so this is more likely the missing phosphatase for histidine synthesis. Fitness data for close homologs in other pseudomonads is consistent with this interpretation. (auxotroph) HAD-superfamily subfamily IB hydrolase, TIGR01490 MRLALFDLDNTLLAGDSDHAWGEYLCQRGIVDASQYKARNDAFYQDYLAGNLDVHAYQNFCQELLGRSEMPQLQQWHDEFMRDFIEPIVLSKGEALLRQHLEAGDKVVIITATNRFITGPIAARLGVDTLLATECEMRDGRYTGRLTDIPCFQEGKVQRIERWLAETEQSLEDSYFYSDSRNDLPLLQRVTHPVAVDPDPLLRQIATERGWQIISLR Pseudomonas stutzeri RCH2 psRCH2 GFF4058 Psest_4131 alpha-ketoglutarate sensor protein (mifS) Specific phenotype on a-ketoglutarate and 56% identical to PA5512 (mifS), which regulates a-ketoglutarate transport in P. aeruginosa (PMC4482717). The transporter in this organism is Psest_0084:0085. Signal transduction histidine kinase regulating C4-dicarboxylate transport system MPALPNRLRVTLIVALILVGLLLSMHWAGRLAEQRAWAERSQESQGQLELYAQAIHTQVERFRSVPALLALDSDIQGLLADPGNRALRRELNQRLEQQNHAAGSSVLYLLDRNGETIAASNWRDWSSFVGNNYAFRPYFRDAVAHDSGRYFAVGVTTGIPGYFLSSSVKSATGEVLGVLVVKLELEDMQRDWVGQPGILLIADSLDIVILTNRPAWRFRYLRPLSDEVRSRLIDVRRYAEQTLQPLQSSRVQQLSESSERRLVDGPDGRREYLWQRLALPEEDWTLHLLHDPQMVVASVRSYRLAAAGVWMTLAFLLLYLAQRRKTRRVEMRSRSELEHLVHERTRELHTAQDELVHAARMAALGQMSAALAHEINQPLTALRMQLASLRLLLDSGRDGEVREGLGHVEGLLERMAALTGHLKTFARKSPAGLRQRLSLAEVLEQALQLLSPRIRSEQVEVFRQVPAEAMVSGDAIRLEQVLINLLHNALDAMAGRPQRRLRILCQLNGDSWQLSVGDNGGGIASEHLDQVFEPFFTTKPVGQGLGLGLAVSYGIVRDMGGTLEVSNDAHGAVFTLTLLAVEGHAAE Pseudomonas stutzeri RCH2 psRCH2 GFF4059 Psest_4132 alpha-ketoglutarate DNA-binding response regulator (mifR) Specific phenotype on a-ketoglutarate and 75% identical to PA5511 (mifR), which regulates a-ketoglutarate transport in P. aeruginosa (PMC4482717). The transporter in this organism is Psest_0084:0085. Response regulator containing CheY-like receiver, AAA-type ATPase, and DNA-binding domains MSGQVIFIDDEAAIRQAVQQWLELSGFQVRTFSRAREALTALDRDFPGVLISDVRMPDLDGLGLLEQLVALDADLPVIMVTGHGDVPMAVQALRQGAYDFIEKPFTPERLLDSVRRAMDKRRLVCENRQLREQFARKGRIESQLLGVSRAMDNLRRQVLELAGTDVNVLIRGETGSGKEQVARCLHDFSPRAGGPFVALNCAAIPETIFESELFGHESGAFTGAQGKRIGRIEHAAGGTLFLDEIESMPLAQQVKLLRVLQEKTLERLGSNRSIEVDLRVISAAKPDLLEEVRGGRFREDLLYRLNVAELHIPPLRERREDIPLLFEHFASQAAQRHGRAAPPVTPGELTQLLAHDWPGNVRELINAAERHALGLSAPAPASSGGQSLAEQMEAFEAQCLHNALQQCKGNITEVMTQLQLPRRTLNEKMQRHGLSRSDYLPAGSADS Pseudomonas stutzeri RCH2 psRCH2 GFF4196 Psest_4269 C4-dicarboxylate transporter, DctQ subunit Important for succinate and fumarate utilization (KEGG_correct). The other components (Psest_4268 and Psest_4270) were already annotated correctly TRAP-type C4-dicarboxylate transport system, small permease component MNALWRVWDHFEEGFIAFLLAAMTLVTFVYVILNNLYTLFYNLGDRFEGSADFWFAIGDFIIGLAQAMTWSTALTKALFAWLIFSGLAYGVRTAGHIGVDALVKLAPRHIQRIIGIIACLLCLGYAGLLTVASFEWIQTLFIANIGAEDLGHIGVKQWHIGMIVPFGFAMVFIRFAEIFVRILRNEQTGLGLADEAADALKHGEEEPK Shewanella loihica PV-4 PV4 5208032 Shew_0548 yqiA-like hydrolase, affects the cell envelope PFam PF05728.8 (UPF0227). conserved phenotypes: important in most defined media conditions hypothetical protein (RefSeq) MLLYIHGFNSSPHSDKGVVTAQYIAKHFPDINFVQPQLPATPKAAMALLTDLVEQALEMGESLSFIGSSLGGYFASYLAERYGGRAVLVNPAVKPFELFDEFLGPQYNPYTEEDYQILPEHKLEVAKYDTPAISHPDRFLVLLQSGDEVLDYRQAVNKYQCCQMLIEAGGDHSFVGYQQQMPGICDFLFLDK Shewanella loihica PV-4 PV4 5208605 Shew_1116 N-acetylglucosamine kinase (EC 2.7.1.59) Specifically important for: N-Acetyl-D-Glucosamine. The first step in NAG utilization (SEED_correct) ATPase, BadF/BadG/BcrA/BcrD type (RefSeq) MGFNQTEEQALVIGIDGGGSKCRATIYAADDSVLGTGVAGRANPLYGLTHTFDSISRATELALQDAGLKAGDGKTMVAGVGLAGVNVAHLYQAIKAWQHPFAEMYVTTDLHTACIGAHKGGDGAVIITGTGSCGYAHVGEQSLSLGGHGFALGDKGSGAWLGLQAAQQVLLDLDGFGPATQLTERLLEHFKVNDAMGIVEHLAGKSSGCYATLARTVLSCAQAQDEVAKAIVVEGAEYISALAHKLFEIHPPRFSMIGGLAEPLAPWLDKRVVDKISPILAPPELGAAYFARQQLGFSS Shewanella loihica PV-4 PV4 5208943 Shew_1444 dicarboxylate TRAP transporter (succinate, fumarate, L-malate, and alpha-ketoglutarate), large permease component Important for utilizing succinate, fumarate, and L-malate, as expected, and also for utilizing a-ketoglutarate TRAP dicarboxylate transporter, DctM subunit (RefSeq) MTIATLFISLFLCMLLGMPIAIALGFSSMLTILLFSDDSLASVALKLYESTSEHYTLLAIPFFILSSAFLSTGGVARRIIDFAMDSVGHIRGGLAMASVMACMLFAAVSGSSPATVAAIGSIVIVGMVRAGYPEKFAAGVITTSGTLGILIPPSIVMLVYAAATEVSAARMFMAGLIPGLMMGLLLMLAIYIVARIKKLPSRPFPGFRPLAISSAKAMGGLALIVIVLGSIYGGIASPTEAAAVACVYAYFIAVFGYRDIGPLKNVSWRDSGEPLIRAILRNLGFMVLAVFKTPADKEIRHVVRDGAKVSIMLLFIIANAMLFAHVLTTERIPHLIAETIVGMGLPVWGFLIIVNLLLLAAGNFMEPSAILLIMAPILFPIATQLGIDPIHLGIIMVVNMEIGMLTPPVGLNLFVTAGITGRSMGWVIHSCIPWLALLLFFLALITYIPQISLFLPEYIDKLNGY Shewanella loihica PV-4 PV4 5208944 Shew_1445 dicarboxylate TRAP transporter (succinate, fumarate, L-malate, and alpha-ketoglutarate), small permease component Important for utilizing succinate, fumarate, and L-malate, as expected, and also for utilizing a-ketoglutarate tripartite ATP-independent periplasmic transporter DctQ (RefSeq) MMSRFFSHIEEVVLNALITAMTLLVFVEVIARFFFNTGFLWIQELTLTICGWFVLFGMSYGVKVGAHIGVDAFVKKLPAQGRKYTAILAVAICLIYCGMFLVGSWDYLAKMYQIGVPMEDIDLPHFLIGGLDGDFAWEYLRIDVEEPAVPLWTSQSILLIGFILLTWRFLQLALAIITNKTDGFAFADEAKESMHLIDQEAQADDKQPGDKK Shewanella loihica PV-4 PV4 5208945 Shew_1446 dicarboxylate TRAP transporter (succinate, fumarate, L-malate, and alpha-ketoglutarate), solute receptor component Important for utilizing succinate, fumarate, and L-malate, as expected, and also for utilizing a-ketoglutarate TRAP dicarboxylate transporter, DctP subunit (RefSeq) MTRLNTCTFIKQIVKMTSIAALLGASLNSWAAPTEIKFSHVVAENTPKGQMALKFKQLVEERLPGEYQVNVFPNSQLFGDNNELSALLLNDVQFVAPSLSKFERYTKKLQLFDLPFLFKDMDAVNRFQQSDAGQQLLNSMKRKGVVGLGYLHNGMKQFSASSPLVLPEDAQGKKFRIMASDVLAAQFQAVEAIPVKKPFSEVFTLLQTRAIDGQENTWSNIYSKKFYEVQSNITESNHGVLDYMVVTSNTFWKSLPADKRKVIKASLDEAIAYGNEIAAAKVNKDKQAIIDSKRSEVTYLTPEQRAAWVNAMKPVWAQFEDKIGKDLIDAAVASNE Shewanella loihica PV-4 PV4 5209923 Shew_2371 actP-like component of L-lactate and L-malate uptake system annotated as an acetate transporter, but important for L-lactate and L-malate utilization; see Sama_2372 (DUF4212) Na+/solute symporter (RefSeq) MDVQTLTYLIVGFTFALYIGIAIWSRAGSTKEFYVAGGGVHPVMNGMATAADWMSAASFISLAGIVSFVGYDGSVYLMGWTGGYVLLALCMAPYLRKFGKFTVPDFIGDRYYSQAARTVAVVCAIFICFTYIAGQMRGVGVVFSRFLEVEVDTGVYIGMAVVFFYAVLGGMKGITYTQVAQYCVLIFAFMVPAIFISVMMTGHILPQLGFGAELVDAAGNNTGVYLLEKLDGLSAQLGFSQYTEGSKGMIDVFFITGALMFGTAGLPHVIVRFFTVPKVKDARVSAGWALVFIAIMYTTIPALAAFSRVNMIETINGPESTGVAYETAPDWIKNWEKTGLIKWDDKNNDGKIYYAKGETNEMKIDRDIMVLATPEIANLPAWVIALVAAGGLAAALSTSAGLLLVISTSVSHDLLKKNFMPDISDKQELLYARIAAALGIVMAGYFGINPPGFVAAVVAIAFGLAASSLFPAIIMGIFSRTMNKEGAIAGMVIGLLFSASYIIYFKFVNPGDNNASNWLFGISPEGIGMLGMIINFAVAFIVSKVTAAVPQNVVDMVESIRFPKGAGEAHDH Shewanella loihica PV-4 PV4 5209924 Shew_2372 small component of L-lactate and L-malate uptake system PFam PF13937.2 (DUF4212). conserved cofit with Shew_2371 hypothetical protein (RefSeq) MAFENNEKAEGYWRENLRLVLGLLAIWAAVSFGCGILLVDVLNEIHFMGFKLGFWFAQQGAMYVFVALIFVYVAKANALDKKYNVHED Shewanella amazonensis SB2B SB2B 6936240 Sama_0429 predicted FeS cluster maintenance protein PFam PF06155.8 (DUF971). conserved cofitness with mrp/apbC (Sama_2048) hypothetical protein (RefSeq) MSHPQVVSLKLKRKSRLLEVGFDDGSQYQLSCEFLRVYSPSAEVHGHGNPVLVTHKKDVNITAIEPVGNYAVKLVFDDGHDTGLYSWQVLHQLATNQLNLWEQYLARLRAEKGSREPMIPMNISYR Shewanella amazonensis SB2B SB2B 6936757 Sama_0944 N-acetylglucosamine kinase (EC 2.7.1.59) Specifically important for: N-Acetyl-D-Glucosamine. This is the first step in NAG utilization (SEED_correct) hypothetical protein (RefSeq) MAFDQTLEGQLYLGIDGGGSKCRATLYNNKLDVLGTGVAGRANPLFGLEQTFESILASTEMALRDAGLSLNDASLLVAGLGLAGVNVPRLLADVQAWQHPFKTMYVTSDLHTACIGAHQGGDGAVIITGTGSCGYVHVGDESLSLGGHGFALGDKGSGAWLGLRAAEHVLLQLDGFAEPTALTERLFANLGVSDALGIVENLAGRSSSCYATLAREVFAAADEGDKVAVGILREGAAYISEMARKLFTLEPARFSMIGGLAEPLQKWLDADVVARLEPSLAAPETGAVLFAIQQHNKQSAA Shewanella amazonensis SB2B SB2B 6937134 Sama_1304 component of chlorite stress sensing system with DUF692 specific phenotype; this gene seems to replace DUF2063 hypothetical protein (RefSeq) MNSIKKTAAAVALGSVVVGAAFAAEAQANPFGFNEMQAGYQLVGDEGKCGEGKCGEGKKAKEGKCGEGKCGEGMKAKEGKCGEGKCGEGMKKGHETAEKAKEGKCGEGKCGEGMKKGQETAEKAKEGKCGEAKGTEKAKEGKCGGAH Shewanella amazonensis SB2B SB2B 6937135 Sama_1305 component of chlorite stress sensing system with Sama_1304 PFam PF05114.9 (DUF692). conserved specific phenotype, and Sama_1304 seems to replace DUF2063 hypothetical protein (RefSeq) MAVSSLAGLGLRREMLAEFSQSVPAQIDFFEVAPENWMALGGKYGKQFRALTERHAFFCHGLSLSIGSSAPLDIDFIKGIKAFLDLHGIAVYSEHLSYCSGSGHLYDLMPMPFTPEAVRHIAGRVKQVEDIIERPLILENISFYAAPGAQMTELEFVLAVLEEADCQLLLDVNNIYVNSINHNYDAAAYLAAMPTERIRYLHVAGHYVEAPDLIVDTHGADIVDPVWQLLCDCYALHGPLPTLLERDFNIPPIGELLQEIDRIRDYQAAAIRTSRRAG Shewanella amazonensis SB2B SB2B 6937231 Sama_1401 D-cellobiose transporter (MFS superfamily) Specific phenotype on cellobiose and no other transporter for this compound was apparent in the fitness data. Also, this protein is 70% identical to bglT from S. fridgimarina, which is a cellobiose transporter (PMC2996990). sugar (glycoside-Pentoside-hexuronide) transporter (RefSeq) MLSVREKIAYGLGDTASNIVFQTVMLFLTFFYTDIFGISAAYVGTMFLAVRIMDAVTDPLMGYLADRTNTRWGRYRPYLLWFAFPFAAISVLAFTTPDLSESGKEWYAFATYALLMLAYTAINIPYCALGAALTTNPAERVSVQSYRFVFAMLGGVMVSALTLPLVDFFGQGDKAKGYQLTILAMSIVGTVMFLLCFIGTKERDFSSDDNSGNFKAASKALWANDQWRVLSAAAIFLLTGLVLKSTLAIYYVKYFLGREDMISVFVTSGVVGNIFGVALAKKLADKMCKVKAYIRLQLIAAALCMAAWFVPADQYVLALVFYIAWNFTINMGTPLLWAKMADTVDYGQFKTGVRTTGLVYSSVIFFIKLGLAIGGALGGWLLAAYGYQPDVAQTEETRAGILLCFTLYPALASIAVAFVMRHYTLDSQRVAEISVSLQQKHSGT Shewanella amazonensis SB2B SB2B 6937235 Sama_1405 glucokinase (EC 2.7.1.2) Specifically important for: D-Cellobiose. After cellobiose is cleaved to 2 glucose (by Sama_1404), it would be phosphorylated to enter glycolysis (SEED_correct) fructokinase (RefSeq) MYRSGIDLGGTKIELVTLNEKGEEVFRKRVPTPKDYRATLEAVAGLVHDSEKETGQVSSVGIGIPGVVSAVTGRVKNSNAVWLNGQPMDKDLGAMLGREVRIANDANCFAVSESVDGGGAGKTLVFGAILGTGCGAGIAINHKVHGGGNGIGGEWGHNPLPWMTADEFNSTRCFCGNADCIETFVSGTGFVRDFRAHGGEAASGIEIVALMGKGEPLAEAAFGRFIDRLARALAHVINLLDPDVIVLGGGVSNIDEIYEYLPALLPKYVLGGECATKVVKNHHGASSGVRGAAWLWAPGEQAALPGLQEL Shewanella amazonensis SB2B SB2B 6937352 Sama_1522 small component of lactate uptake system PFam PF13937.2 (DUF4212). conserved cofit with Sama_1523 hypothetical protein (RefSeq) MAFESNEKAQGYWRENLRLVISLLAVWFVVSYGFGILLVDVLNQITFMGFKLGFWFAQQGSMYVFVALIFIYAAKANALDKKYNVHED Shewanella amazonensis SB2B SB2B 6937353 Sama_1523 actP-like component of lactate uptake system annotated as an acetate transporter, but important for lactate utilization; see Sama_1522 (DUF4212) sodium/solute symporter family protein (RefSeq) MDVKTLTYLIVGLSFALYIGIAIWSRAGSTKEFYVAGGGVPPVMNGMATAADWMSAASFISLAGIVSFVGYDGSVYLMGWTGGYVLLALCMAPYLRKFGKFTVPDFIGERYYSQAARTVAVVCAIFICFTYIAGQMRGVGVVFSRFLEVDVDTGVYIGMAVVFFYAVLGGMKGITYTQVAQYCVLIFAFMVPAIFISVMMTGHIIPQLGFGAELIDAAGNGTGVYLLDKLDGLSTELGFSQYTEGSKSMIDVFAITAALMVGTAGLPHVIVRFFTVPRVKDARSSAGWALVFIAIMYTTVPALAAFSRVNMIETINGPDSTGVAYETAPGWIKNWEKTGLIKWDDKNGDGKMYYTKGDANEMNIDRDIMVLATPEIANLPAWVIALVAAGGLAAALSTSAGLLLVISTSVSHDLMKKGFAPNISDKQELLYARIAAAVGIVIAGYFGINPPGFVAAVVAFAFGLAASSLFPAIVMGIFSKKMNKEGAIAGMVVGLGFTAAYIVYFKFVNPAANVPANWLFGISPEGIGMIGMLINFAVAVIVAKLTSAVPAHVEEMVEGIRFPKGAGGAQDH Shewanella amazonensis SB2B SB2B 6937780 Sama_1921 yeaG component of nitrogen-related signalling system (of yeaGH-ycgB) conserved cofitness; yeaG is a protein kinase putative serine protein kinase, PrkA (RefSeq) MGIFEHYQQRYEKKLEEEYSLQEFLEICKQDKSAYATAAERLLLAIGEPELIDTSKNSVLSRIFSNRLISRYPAFKDFFGMEDAIEQIVAYLKHSAQGLEESKQILYLLGPVGGGKSSLAEKLKALMQKVPVYVLSADGVRSPVNDHPFCLFDADEDGKLLQEEYDIPTRYLRTIMSPWAVKRLHDYGGDISRFKVVKVFPSVLDQIAVAKTEPGDENNQDISSLVGKVDIRQLEHFAQNDADAYSYSGALCRANQGLMEFVEMFKAPIKVLHPLLTATQEGNYNGTEGLSALPFSGIILAHSNESEWSSFKNNKNNEAFLDRVYIVKVPYCLRVSEEIQIYKKLIINSELSEAPCAPGTLETLAQFSVLSRLKVPENSSIYSKMRVYDGESLKDTDPKAKSYQEYRDYAGVDEGMNGLSTRFAFKILSKVFNFDHTEIAANPVHLFYVLERQIEAEQFPGETAERYLEFLKGYLIPKYVEFIGKEIQTAYLESYSEYGQNIFDRYVTYADFWIQDQEYRDPETGQLFDRAALNAELEKIEKPAGISNPKDFRNEIVNFVLRARANNEGKNPTWTSYEKLRTVIEKKMFSNTEDLLPVISFNAKTSTDDQRKHDDFVNRMMEKGYTKKQVRLLSEWYLRVRKSS Shewanella amazonensis SB2B SB2B 6937781 Sama_1922 yeaH component of nitrogen-related signalling system yeaH (of yeaGH-ycgB) PFam PF04285.8 (DUF444). conserved cofitness; yeaG is a protein kinase hypothetical protein (RefSeq) MANFIDRRLNAKGKSTVNRQRFINRYKKQIKKAVSDAVTRRSVTDVDKGEQISIPTRDITEPMFHQGRGGFRERVHPGNDQFTRGDRIDRPPQGGGGQGSGQGDASDSGDGQDDFVFQISKDEYLELLFEDLELPNLQRNRLNKLVEYQVQRAGYTNDGVPANISIVRSLRSSLARRTAMTAAKKRHLKTLEAELEELENTPGANADRILALKTEIEALRKKIDAVPFIDTFDLRYNNFTKREVPSSQAVMFCLMDVSGSMDQATKDMAKRFYILLYLFLTRTYKNLEVVYIRHHTQAKEVDEHEFFYSQETGGTIVSSALKLMVEIQKERYPAEEWNIYAAQASDGDNWADDSPTCRQILEKQILPTVRYFSYIEITNRAHQTLWREYDSLRQVYDNMAVQHIRQAEDIYPVFRELFKKQAV Shewanella amazonensis SB2B SB2B 6937782 Sama_1923 ycgB component of nitrogen-related signalling system (of yeaGH-ycgB) conserved cofitness; yeaG is a protein kinase SpoVR family protein (RefSeq) MGKRTPLSDGPDWTFELLEEYQREIERVAAHYRLNTYPNQIEVITAEQMMDAYAGIGMPIGYTHWSFGKRFIQTEQSYKRGQMGLAYEIVINSNPCIAYLMEENTITMQALVMAHACYGHNSFFKGNYLFKTWTDASSIIDYLVFAKNYIAECEQRHGVDAVENVIDSCHALMNYGVDRYKRPSEISFREEKARQKEREEYLQSQVNDLWRTIPVSQVEKVQPKKRFPAEPQENILYFIEKHAPLLEPWQREIVRIVRKMGQYFYPQKQTQVMNEGWATFWHYTILNHLYDEGLVTDRFMLEFLQSHTGVVAQPAYNSRYYSGINPYALGFNMFTDIRRICENPTEEDRAWFPEIAGSNWLDTLHFAMENFKDESFISQYLSPAMIRQFKLFGIVDDERKNYLSISAIHDEVGYREIRQTMSQQYNLSNLEPNIQVHRVEVMGDRSMTLRYVPFNNIPLADDYREVLKHLHRLWGFTVVLEQEESDGTIKELARCPPRDEEGHSVKI Shewanella amazonensis SB2B SB2B 6937939 Sama_2080 DNA damage response helicase (yejH or radD) Conserved and specific phenotype: important for resisting cisplatin. Also important for resisting ionizing radiationa and UV radiation in E. coli (PMID:25425430) helicase (RefSeq) MQHDRRRQPTMTIKLRDYQQDAIEATLAHFRTSRESALLVLPTGAGKSLVIAELARLAKGRVLVLTHVKELVAQNAQKVDALAGNASIFSAGLGEKDSGGKTVVAGIQSAAVNVAAFDEPFSLVIIDECHRVSLDENSQYRQVFSQLREKNPDLLLLGLTATPYRLGEGAIYKRHVRGHVGNPDKGVFDVCIFELPIRSLIKQGYLTEPLLLDGLAAQYNFAALKASEDADYQEAEVQAILDTSTRATTTIMGQLKALAQQRLGVIIFAATVRHAKEIMALLDESAALITADTPGPERDNIITAFKAQELKFLVNVAVLTTGFDAPHVDLIAILRPTASVSLFQQMVGRGLRLFPGKAECLILDYAANGFSLYHPDVGKPRPDSKSVPVQVPCPACGFANLFWGKADTDGDIIEHYGRRCQGLLDDGNQCDFRFRARICPDCGAENDIAARVCRGCDSALVDPDKHLKAVLAHKHHHLFKVTDMLLGATDAGLEVTYLDMDGNSFIERFKMQTPGQRKALYALFLLRHQRAPGLALPKYPDAKALIKDSAKFRAPELLLLKKSKFGWQLVDKFFDYRGKYQTRARFED Shewanella amazonensis SB2B SB2B 6937966 Sama_2099 UMP phosphatase (EC 3.1.3.5) Specifically important for: Thymidine. Probably required for thymidine utilization because it allows overflow metabolism of pyrimidine intermediates, as with umpH from E. coli (which is 72% identical), see PMID 23903661 UMP phosphatase (RefSeq) MKNIICDIDGVLLHDNKLVPGSDKFIHRVLEQGNPLVILTNYPVQTGKDLQNRLDAAGINVPEECFYTAAMATADFLKHQEGSKAFVIGEGALTHELYKAGFTITDINPDFVIVGETRSYNWDMIHKAARFVADGARFIATNPDTHGPAFSPACGALCAPIERITGRKPFYVGKPSSWIVRSALNHINGHSENTVIIGDNMRTDILAGFQAGLETILVLTGVSRLEDIEKEPFRPNHVFNCAGDIDIF Shewanella amazonensis SB2B SB2B 6938088 Sama_2209 alpha-ketoglutarate TRAP transporter, solute receptor component specific phenotype on a-ketoglutarate. A putrescine ABC transporter (Sama_2642:Sama_2638) is also important in this condition, which is not explained. This organism can also utilize succinate or fumarate (but not L-malate), which we do not have fitness data for these under aerobic conditions. This could also transport some C4 compounds. C4-dicarboxylate-binding periplasmic protein (RefSeq) MKVSKPATLQSLFTLGKASLLATVLGFSFGAVAEPVEIKFSHVVAENTPKGQMALKFKELVESRLPGEYKVSVFPNSQLFGDNNELAALLLNDVQLVAPSLSKFERYTKKLQVFDLPFLFEDMDAVDRFQQSEAGQQLLNSMSRKGLVGLGYLHNGMKQFSANNALSLPGDAAGKKFRIMPSDVIAAQFEAVGAIPVKKPFSEVFTLLQTRAIDGQENTWSNIYSKKFYEVQTHITESNHGVLDYMLVTSETFWKSLPKDKREIIKQSMDEAVALGNKLALEKANEDRQLILDSKRVELVTLTPEQRQAWVNAMRPVWSQFEDKIGKDLIEAAESANKP Shewanella amazonensis SB2B SB2B 6938089 Sama_2210 alpha-ketoglutarate TRAP transporter, small permease component specific phenotype on a-ketoglutarate. A putrescine ABC transporter (Sama_2642:Sama_2638) is also important in this condition, which is not explained. This organism can also utilize succinate or fumarate (but not L-malate), which we do not have fitness data for these under aerobic conditions. This could also transport some C4 compounds. C4-dicarboxylate transporter, putative (RefSeq) MISRIFGYFEEGVLNLLITLMTLLVFMEVIARFFFNTGFLWIQELTLTFCGWFVLFGMSYGIKVGAHIGVDAFVKKLKPGARRISALLAVSICLIYCAMFLKGTWDYLSQIYHIGIGMEDLDVPSVLMKQMSEDFAWDVMRIDPEDPAIPLWISQSILLLGFVMLTWRFLELAVAIFRGTSNGFSFHDEAKESMHLADEQSGANDNNNDGAKS Shewanella amazonensis SB2B SB2B 6938090 Sama_2211 alpha-ketoglutarate TRAP transporter, large permease component specific phenotype on a-ketoglutarate. A putrescine ABC transporter (Sama_2642:Sama_2638) is also important in this condition, which is not explained. This organism can also utilize succinate or fumarate (but not L-malate), which we do not have fitness data for these under aerobic conditions. This could also transport some C4 compounds. C4-dicarboxylate transport protein (RefSeq) MTIATLFLTLFLCMLLGMPIAIALGFSSMLTILLFSNDSLASVALKLYEATSEHYTLLAIPFFILSSAFLSTGGVARRIIDFAMDSVGHIRGGLAMASVMACMLFAAVSGSSPATVAAIGSIVIVGMVRAGYPQKFAAGVITTSGTLGILIPPSIVMLVYAAATEVSAARMFMAGLIPGLLMGVLLMVAIYIVARIKNLPSRPFPGVKALSLSSAKAMGGLALIFIVLGSIYGGVASPTEAAAVACVYAYLVAVFGYRDIGPLKEVPWRKEGEAILAAIVRNLLHVGLGLIKTPTDKEIRNVVRDGAKVSIMLLFIIANAMLFAHVLTTERIPHIIAETIVGWGLPPWGFLIIVNLLLLAAGNFMEPSAILLIMAPILFPIAVQLGIDPIHLGIIMVVNMEIGMLTPPVGLNLFVTAGITGRSIGWVIHACLPWLLLLLGFLVLITYVPQISLFLPEYLDSLRGFK Shewanella amazonensis SB2B SB2B 6938110 Sama_2231 glucokinase (EC 2.7.1.2) Specifically important for: D-Maltose monohydrate. Maltose is presumably cleaved to glucose, so the annotation as glucokinase (but not as fructokinase) fits. The other glucokinase (Sama_1405) is not important on maltose. (SEED_correct) fructokinase (RefSeq) MMRMGVDLGGTKIELVALGEDGSELFRKRIATPREYQGTLNAVVTLVNEAEATLGTQGSLGIGIPGVISPYTGLVKNANSTWINGHPLDRDLGALLNREVRVANDANCFAVSEAVDGAAAGKRVVFGAILGTGCGAGLAFDGRVHEGGNGIGGEWGHNPLPWMRPDEFNTTECFCGNKDCIETFVSGTGFVRDFRNSGGTAQNGAEIMSLVDAGDELANLVFDRYLDRLARSLAHVINMLDPDAIVLGGGMSNVQAIYARLPAILPKYVVGRECRTPVVQNLYGCSSGVRGAAWLWEKR Shewanella amazonensis SB2B SB2B 6938540 Sama_2643 Gamma-aminobutyrate:alpha-ketoglutarate aminotransferase (EC 2.6.1.19) Specifically important for: Putrescine Dihydrochloride. Putrescine is catabolized via gamma-aminobutyrate (SEED_correct) putative aminotransferase (RefSeq) MQQQQQDTISALQAMDAAHHLHPFTDSADLAKRGTRVIERAEGVYIWDAKGNKLLDAMAGLWCVNVGYGRKSIADAAYAQLQTLPFYNNFFQCTHEPAIRLASKIASLAPGHMNRVFFTGSGSEANDTNLRMVRRYWDLKGMPSKKTIISRKNAYHGSTVAGASLGGMGFMHQQGDLPIPGIVHIDQPYWFGEGRDMSPEAFGIKTAQALEAKILELGEDKVAAFIAEPFQGAGGVIIPPDSYWNEIKRILEKYNILFILDEVISGFGRTGNWFAAQTLGLKPDLITIAKGMTSGYIPMGGVIVSDRVADVLISDGGEFAHGFTYSGHPVAAAVALENIRILEEERLVDKVRTDTGPYLQDRLQTLSAHPLVGEVRGMGMVGAIELVADKHSMVRFGSEISAGMLCREACIESGLVMRAVGDTMIISPPLCITRDEIDELIFKASQALSLTLEKIAARGN Shewanella amazonensis SB2B SB2B 6938542 Sama_2645 Gamma-glutamyl-GABA hydrolase (EC 3.5.1.94) Specifically important for: Putrescine Dihydrochloride. Part of the gamma-glutamyl-putrescine pathway for putrescine catabolism (SEED_correct) glutamine amidotransferase (RefSeq) MSDATIPLIGVSACNTPIGLQTFNTVGEKYLLGVINGTGGWPLIIPSIGDGMPTELLLERLDGILFTGSPSNVEPHHYSGPASEPGTHHDPRRDATTLPLIKAAIAAGVPVLGICRGFQEMNVAFGGSLHQKLHETGVFEEHREDRTAPLEVQYGLAHTVTLEPGGVIFEAWGRSSAEVNSVHTQGVERLGNGLRPEAYAPDGLIEAFSVTDAKNFALGVQFHPEWKVADNAFYLSIFNAFGDACRRRAQERAR Shewanella amazonensis SB2B SB2B 6938946 Sama_3044 yqiA-like hydrolase, affects the cell envelope PFam PF05728.8 (UPF0227). conserved phenotypes: important in most defined media conditions hypothetical protein (RefSeq) MLLYIHGFNSSPQSDKGLQSANFIAANHPGVRLVQPQLPTDIERAVALLCEITEEAKARGEPLRFIGSSLGGFFATYLAETYGGKAALINPAVSPYDLFEAFLGPQHNPYTGEDYLVLPSHREALKRYDVAAIANPDRFFVLLQTGDEVLDYRLALGKYYCCRMLIEPGGDHSFVGFERQLPDIAAFLELP Sinorhizobium meliloti 1021 Smeli SM_b20002 SM_b20002 ABC transporter for Lactose, ATPase component Specific phenotype on Beta-Lactose. (KEGG_correct) sugar ABC transporter ATP-binding protein MSELQLSDVRKSYGGLEVIKGVDLDIKSGEFVVFVGPSGCGKSTLLRMIAGLEEISSGDLTIDDVRMNDVDPSKRGIAMVFQSYALYPHMTVRENMGFALRFAGVPRAEIEKRVNEAAHILELGALLDRKPKQLSGGQRQRVAIGRAIVRHPKIFLFDEPLSNLDAELRVHMRIEIARLHKQLATTIVYVTHDQVEAMTLADKIVVMRAGVVEQVGSPLDLYDDPANLFVAGFIGSPKMNFLKGVIEIDEDQAYARLPDYGDAKIPVTLQAAAGTAVTIGIRPEHFDEAGPAALDLAIDMLEHLGGETFAYARHHGNGELIVVETKNGRGLKTGDRLTARFDPVSVLVFDGEGKRLRS Sinorhizobium meliloti 1021 Smeli SM_b20329 SM_b20329 required for glucoside 3-dehydrogenase activity on raffinose or trehalose (thuA) (EC 1.1.99.13) Specifically important for: D-Raffinose pentahydrate; D-Trehalose dihydrate. a close homolog is described by PMID 23772075; (SEED_correct) ThuA protein, function MPQITRRMTLSINAIVWGENIHEQTNAVVREIYPDGMHNTIAAALNSDPGIDATTATLQEPEHGLSETRLAAADVLLWWGHKDHGAVDDAIVERVAKRVWEGMGLIVLHSGHFSKVFKRLMGTPCALKWREAGERERVWVVNPRHPIAEGLGENFVIENEEMYGEQFSVPEPLETVFISWFAGGEVFRSGLTWRRGAGNIFYFRPGHETYPTYHDATVHKVLRNAVKWAYNPQGTYKAIHDAPNVPVEKALEPIVERGPRLHRAGEAGYR Sinorhizobium meliloti 1021 Smeli SM_b20330 SM_b20330 glucoside 3-dehydrogenase; active on raffinose or trehalose (thuB) (EC 1.1.99.13) Specifically important for: D-Raffinose pentahydrate; D-Trehalose dihydrate. a close homolog is described by PMID 23772075 trehalosemaltose utilization protein, function MKGTPMRLLILGTGGMANSHAKAFAEIEGVEMVGAVDVDPSRAKAFAVTHGIENTFTSLDDAIAWGEFDAATNVTPDKAHHPTTLALIAAGKHVLCEKPLAENYEKAAEMAAAAERAGLVTMVNLTYRNVAPLQKARELVVAGEIGRVRHLEASYLQSWLVSRAWGDWASESKWLWRLSTKHGSNGVLGDVGIHILDFAGYGANSSVERVFARLKAFDKAPDNRIGEYDLDANDSFAMTAEFENGAMAVIHASRWATGHLNELRLRLHGDRGALEVIHTPDGSSLRGCMGPDVEKAVWRTVDAGTVPTNYQRFVEAVKAGRTVEPGFRHAADLQRVLDLAIETERSRRELGVPDIDAVVQERAVG Sinorhizobium meliloti 1021 Smeli SM_b20890 SM_b20890 L-arabonate dehydratase (EC 4.2.1.25) Specifically important for: L-Arabinose. L-arabonate is an intermediate in the oxidation of L-arabinose (SEED_correct) dihydroxy-acid dehydratase MKKKAEWPRKLRSQEWFGGTGKNAIMHRSWMKNQGLPADTFDGRPIIGICNTWSELTPCNAHLRDLAERVKRGVYEAGGFPVEFPVFSTGESTLRPTAMMFRNLAAMDVEESIRGNPVDGVVLLGGCDKTTPSLLMGAASVDIPAIVVSGGPMLNGKWRGKDVGSGTAIWQFSEMVKSGEMSLEEFMDAEQGMARSAGSCMTMGTASTMASMAEALGMTLSGNAAIPAVDARRRVISQLTGRRIVEMVKEDLKPSDILTKEAFENAIRVNGAVGGSTNAVLHLLALAGRVGVDLSLDDWDRLGRDVPTIVNLQPSGKYLMEEFYYAGGLPVVIKAVAEMGLLHNDAITVSGDTIWNDVKGVVNYNEDVILPREKALTKSGGIAVLRGNLAPRGAVLKPSAASPHLMQHKGRAVVFESIEDYHARINREDLDIDETCIMVLKYCGPKGYPGMAEVGNMGLPPKVLKKGITDMIRISDARMSGTAYGTVILHTAPEAAEGGPLALVENGDLIEVDIPNRTLHLHVSDEELARRRAAWVSPVKPLTGGYGGLYIKTVMQADAGADLDFLVGARGSVVERDSH Sinorhizobium meliloti 1021 Smeli SM_b20891 SM_b20891 Ketoglutarate semialdehyde dehydrogenase (EC 1.2.1.26) Specifically important for: L-Arabinose. The only dehydrogenase steps in the arabinose catabolism pathway are L-arabinose 1-dehydrogenase (which is SMc00588) and a-ketoglutarate semialdehyde dehydrogenase (EC 1.2.1.26). So, this is the semialdehyde dehydrogenase. dehydrogenase MTLHQNLIAGEWVGGDGVANINPSNTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKLAPALCYGNTIVFKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLSVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHVPFGGRKASSYGPREQGKYAAEFYTNVKTAYTLA Sinorhizobium meliloti 1021 Smeli SM_b21103 SM_b21103 ABC transporter for L-Fucose, periplasmic substrate-binding protein Specific phenotype on L-Fucose. sugar ABC transporter substrate-binding protein MNRLLSGVSAGVIMLACAMGAAKAADLPGKFEGVTIDAKLIGGQQYEKLYERIGEWEKATGAKVNILSKKNHFELDKEIKSDIATGGLTWCVGSNHSSFAPQYPDIYADLFGLIPSEEVAKFVPAVIDASTLEGKLVMLPRAQFDVSALYFQKSLYQDEAKKTEFKAKYGYDLAPPDTWAQVSDQAEFFAAPPNFYGTQFAGKEEAINGRFYEMLVAEGGEYLDKDGRPAFNSDAGVRALEWFVKLYKDKAVPPGTTNYLWDDLGQGFASGSIAVNLDWPGWASFFNDPKSSKVAGNVGVKVQPAGSSGKRTGWSGHHGFSVTESCADKEAAASLVWWLTNEDSQKLESAAGPLPTRSAVWDFNIKAAEGDAYKTEVLQAFQEAAKHAFPVPQTAEWIEISNAVYPELQAAILGDKTSKEALDAAAEKATGILEDAGKL Sinorhizobium meliloti 1021 Smeli SM_b21104 SM_b21104 ABC transporter for L-Fucose, permease component 1 Specific phenotypes on L-Fucose. sugar ABC transporter permease MKLSKLSAPTLLLLPAFIVLAVFIVLPLIFSLYSSFTPFRLTKPDSLWVFIGFRNYVNVLTNAEFWVAFGRTVLLLTVALNAEMFLGLGLALLVNKATYGQRALRTAMMFPMMFSPVLVGFQFKFLFNDNIGFVNNALQSLGLTDRAIPWLIDGNLALFSIIVAEVWSSTAVFAILILAGLLAMPKDPVEAAHVDGCTPWQTFRYVTWPYLMPFAFIAMTIRSLDVARAYDIVKIMTDGGPAKRTELLWTLIGRTAYGDARMGMANAMAYVAILLSIFFTVYFFRKLAAARQQIGAEW Sinorhizobium meliloti 1021 Smeli SM_b21105 SM_b21105 ABC transporter for L-Fucose, permease component 2 Specific phenotypes on L-Fucose. sugar ABC transporter permease MDTNASHRLRRRLLKVAHLAGLFLAMLVICLPGLWIVLSSLRPTVEIMAKPPVWIPETLSLDAYRAMFSGAGQGGVPVWDYFRNSLIVSVTSTVIALAIGLSGGYAFARYRFKAKSAIFLGFMLTRAVPGIALSLPLFMLYARTGIIDTHFSLILTYVALNVPFTIWLIDGFFRQVPKDLAEAAQIDGCTPWQAFWQVEFPLAGPGIASAGIFAFLTSWNEYALASQITRSVNSKTLPVGLLDYTAEFTIDWRGMCALAVVMIVPALTLTFIIQKHLVSGLTFGAVKG Sinorhizobium meliloti 1021 Smeli SM_b21106 SM_b21106 ABC transporter for L-Fucose, ATPase component Specific phenotype on L-Fucose. sugar ABC transporter ATP-binding protein MAPVTLKKLVKRYGALEVVHGIDLEVKDREFIALVGPSGCGKSTTLRMIAGLEEVSGGAIEIGGRKVNDLPPRARNISMVFQSYALYPHMTVAENMGFSLKIAGRPAEEIKTRVAEAAAILDLAHLLERRPSQLSGGQRQRVAMGRAIVRQPDVFLFDEPLSNLDAKLRTQVRTEIKKLHARMQATMIYVTHDQVEAMTLSDRIVIMRDGHIEQVGTPEDVFRRPATKFVAGFIGSPPMNMEEAVLTDGKLAFASGATLPLPPRFRSLVREGQKVTFGLRPDDVYPSGHGLHAGDADAVHEIELPVTITEPLGNETLVFTQFNGRDWVSRMLNPRPLRPGEAVPMSFDLARAHLFDGETGRALAS Sinorhizobium meliloti 1021 Smeli SM_b21108 SM_b21108 L-fucose mutarotase (EC 5.1.3.29) Specifically important for: L-Fucose. The first step in fucose catabolism. This protein is related to XCC4070 (FUCM_XANCP) hypothetical protein MQRMGMVIGLEPSKIAEYKRLHAAVWPEILALISECNITNYSIFLKEPENLLFGYWEYVGEDFEADMTKMAAHPKNQEWWSVCMPCQKPLESRRQGEWWAMMEEVFHHD Sinorhizobium meliloti 1021 Smeli SM_b21109 SM_b21109 L-fucose dehydrogenase (EC 1.1.1.122) Specifically important for: L-Fucose. The second step in fucose catabolism. oxidoreductase MTETFDPSSLRQWWPKPVAPRPIVIFGAGSIVGDAHLPAYRNAGFPVAGIFDPDAGKAAALARASDVMAFTSEEEALSAENAIFDLATPPAAHASILSKLPKGSFALIQKPLGSDLAAATGILEICRERNIRAAANFQLRFAPMMLALKDAIATGYLGEVVDFDAWLALATPWGLWPFLKGLPRIEIAMHSIHYLDLVRSLLGDPRGVHAKTIGHPNHDVAQTRTAAILDYGDAVRCVLSVNHDHDFGRRFQACEFRICGTRGAAYVKLGVNLDYPRGEPDELWIRPAGGADWIQVPLEGSWFPDAFANRMANLQRHAGGEDDELIGSVEDAWRTMALVEAAYQSSARPATPIAALPLEN Sinorhizobium meliloti 1021 Smeli SM_b21164 SM_b21164 N-formylglutamate deformylase (EC 3.5.1.68) Specifically important for: L-Histidine. KEGG suggests formimidoyl-L-glutamate as the substrate, while SEED suggests N-formylglutamate. This gene is cofit with a deiminase or iminohydrolase (which produces N-formylglutamate) which suggests that the SEED annotation is correct. (SEED_correct) formiminoglutamase MAVFEVRQGSSPVILGFPHTGTDVPASIRERLNDNGRILADTDWHIHDLYQGLLPDATAVRATFHRYVIDANRDPAGVSLYPGQNTTGLVPETDFDGLPIWKEGEGPTEVDITERLRDFHAPYHAALSAEIARVKAIHGVVVLYDCHSIRSHIPFLFEGRLPDFNIGTDMGKTCATEIERAAAEIAAGAECYSHILNGRFKGGWTTRHYGRPEQGVHAIQMELAQSTHLATEAPPFALDRAKADRLRRPLKAILERIETVAKELKRTGSEA Sinorhizobium meliloti 1021 Smeli SM_b21216 SM_b21216 ABC transporter for D-Glucosamine, ATPase component Specific phenotype on D-Glucosamine Hydrochloride. sugar ABC transporter ATP-binding protein MSALEIRNIRKRYGEVETLKGIDIALESGEFLVLLGSSGCGKSTLLNIIAGLAEPSGGDILIGERSVLGVHPKDRDIAMVFQSYALYPNLSVARNIGFGLEMRRVPQAEHDKAVRDTARLLQIENLLDRKPSQLSGGQRQRVAIGRALVRNPQVFLFDEPLSNLDAKLRMEMRTELKRLHQMLRTTVVYVTHDQIEAMTLATRIAVMRDGRIEQLAAPDEVYDRPATLYVAGFVGSPPMNILDAEMTANGLKIEGCEEVLPLPAAFNGAAWAGRRVKVGIRPEALRLAAGSEAQRLTASVEVVELTGPELVTTATVGSQRITACLPPRTAVGMGSAHAFTFDGTALHLFDPESGRSLRME Sinorhizobium meliloti 1021 Smeli SM_b21219 SM_b21219 ABC transporter for D-Glucosamine, permease component 1 Specific phenotypes on D-Glucosamine Hydrochloride. sugar ABC transporter permease MERQSPLFSVFIHASALLLAVVILAPVAWLLIMSISPAADLSAKPLAWWPSDIDLSRYRTLLSAVENSAGAAFIASLLNSIKVAGMATLAAVVVAVPAAWAVSRTPAVAWSLYAVIATYMLPPVALAVPLYMGLAYFGLLNSVFGLALVYLTILAPFTTWLLKSGFDSIPREIESAAMIDGARLDQILRILTLPLAAPVMATSALFAFLLAWDEFFYALLFTSDQRAKTLTVAIADLAGGRVSDYGLIATAGVLAALPPVLIGLIMQRALISGLTSGGVKG Sinorhizobium meliloti 1021 Smeli SM_b21220 SM_b21220 ABC transporter for D-Glucosamine, permease component 2 Specific phenotypes on D-Glucosamine Hydrochloride. sugar ABC transporter permease MTGTWISTRAWLLMLPLLVVMTAVIGWPLVDTVRLSFTDAKLVGTEGGFVGTANYIKMLGGSNFQRALVTTTWFAVISVAAEMVLGVLAALLLNQQFRGRTALRALMILPWALPTVVNATLWRLIYNPEYGALNAALTQLGLLDSYRSWLGEPGTALAALIVADCWKNFPLVALIALAALQAVPRDITAASLVDGAGPFNRFRFVIMPYLAGPLLVALVLRTIEAFKVFDIIWVMTRGGPANSTRTLSILVYQEAFSFQRAGSGASLALIVTLLVTILAAAYAALLRKAAGAS Sinorhizobium meliloti 1021 Smeli SM_b21221 SM_b21221 ABC transporter for D-Glucosamine, periplasmic substrate-binding protein Specific phenotype on D-Glucosamine Hydrochloride. (SEED_correct) sugar uptake ABC transporter substrate-binding protein precursor MLKSTRNALIGATLIGAGFTGHAQAETTLNALFMAQAAYSEADVRAMTDAFAKANPDIKVNLEFVPYEGLHDKTVLAQGSGGGYDVVLFDVIWPAEYAANNVLLDVTDRVTDEMNKGVLPGAWTTVEYDGKRYGMPWILDTKYLFYNKEILEKAGIKQPPKTWEELSEQATAIKDKGLLESPIAWSWSQAEAAICDYTTLVSAYGGKFLDGGKPAFTTGGGLDALNYMVTSYTSGLTNPNSKEFLEEDVRKVFQNGEAAFALNWTYMYNLANDPKESKVAGKVGVVPAPGAAGKSEVSAVNGSMGLGITATSKHPEEAWKYIVHMTSQETQNAYAKLSLPIWASSYENPNVTKGQEELIAAAKRGLAAMYPRPTTPKYQELSTALQQAIQEALLGQSSAEDALKSAAENSGL Sinorhizobium meliloti 1021 Smeli SM_b21374 SM_b21374 tagatose kinase (EC 2.7.1.101) Important on tagatose. This is the first step in tagatose catabolism. sugar kinase MHKILTIGEILVEIIATEKGDGFRKATPLIGPFPSGAPAIFIDQAGKLGQPCAIISRVGGDDFGTVNLERLKRDGVDISGIEVDPLATTGSAFVRYRPDGSRAFVFNIRDSACGKITLDERMTRLVGECSHVHVMGSSLYAPSVVESILAAIGIVKAGGGTVSFDPNLRPEILKSPGMREALLTVLAETDLFLPSGDELFLFTEAKTESQAVAELLASGIKAVVVKRGAAGASYFDAGAALSLPGFPVEEIDPTGAGDCFGATFVSFWLNGASPREALEFAAASGARAVMHFGPMEGASTRAELERFISEQQA Sinorhizobium meliloti 1021 Smeli SM_b21644 SM_b21644 ABC transporter for D-Raffinose, ATPase component Specific phenotype on D-Raffinose pentahydrate. ABC transporter ATP-binding protein MVTIESIVPAPEERRDRDMKDERPVIDARKVAVSFKVENGTVQAVKDVSFQLYRGETVAIVGESGSGKSVTARTVMGLLSKRATIAPQARIEYDGRDVLKFSKRERRALRGDRISMIFQEPMSSLNPVYTIGSQIIEAIRAHRRVSRRAAAERALELLRHVQIPDPEARLNQYPHQLSGGQRQRVMIAMALANDPDVLIADEPTTALDVTVQAQILNLIRKLQQELGMAVILITHDLTVVRQFSDYVYVMQLGEVKEHNTTEALFADPQHAYTRRLLSSEPSGSANPLPDDAPILLDGRNVRVSFTLKKGGFFRPEFKELVAVDGLSLNLRRHETLGLVGESGSGKTTFGQALIRLLNTDGGEIYFEGEPIHDKDRKGMRPLRSKIQIVFQDPFSSLNPRMSVGQIIEEGLIVNGMGENRKDRLKRVEDALVSAGMPSNILSRFPHEFSGGQRQRIAIARAVALEPEFILLDEPTSALDLSVQAQIIELLRRLQDERGLSYLVISHDLKVVRALCHRVVVMQDGKIVEEGPVSEVLNNPKTAYTERLVKAAFEVAA Sinorhizobium meliloti 1021 Smeli SM_b21645 SM_b21645 ABC transporter for D-Raffinose, permease component 1 Specific phenotypes on D-Raffinose pentahydrate. ABC transporter permease MTIEAESTLPVAIEPEEKHHHESYSALVWRRLKRSWTGLLGLVLVCLLILMAVFAEFLSPVDPKATDVAFAQPQTISFRDKEGNFVFPPRSYPVRETEELDPVTFQPIIGPDYDNPQVLGFFVKGAPYRLFGLIPAERHLFGAVDGTPVHLLGTDKFGRDVLSRILYGSRISLMIALTVVFIVTVVGTTVGMVSGYFGGRFDAWVQRFVELVLAFPQLPLYLALASLIPVTAPTNVFLAFVIIVMSALGWAQMSREVRGKTLALARIEYVRAAIAIGATDRRIIFQHIFPNVMSHVIVAVTLAIPHVVLLESFLGFLGFAVKPPLISWGLMLQDTANYSAIGSYPWILSPVAFVLVTVFAFNALGDGLRDAIDPY Sinorhizobium meliloti 1021 Smeli SM_b21646 SM_b21646 ABC transporter for D-Raffinose, permease component 2 Specific phenotypes on D-Raffinose pentahydrate. ABC transporter permease MFRFLLVRIASAIPVLLVLSVVTFGIIQAPPGDYSDYIRSQLINQGGASFEEADAQAQAYRKEHGLDKPLPIQYVNWITGIVTRGDFGHSLYYNKPVADVVGERLPRTLALALVCHILASVIGIAFGIIAATRQYSWIDSLLSTVSFLGMTVPRFLMALIIVYILVFHFNVSEINSFHSARYGGAPWSWDKFVDLIKHVWPVVAIATFGGLAYNMRVMRGNLLDTLNAQYVETARAKGLSEGAVVMRHAVPNALHPLIMYQGVVLPYMLTGEIETAIIFALPTVGPAIVGSMWVGDVYVTATFMLVLSATLIVGNIIADMMLAALDPRVRMGGGVYA Sinorhizobium meliloti 1021 Smeli SM_b21647 SM_b21647 ABC transporter for D-Raffinose, periplasmic substrate-binding protein Specific phenotype on D-Raffinose pentahydrate. alpha-galactoside ABC transporter substrate-binding protein precursor MKTHRLNMTASLLIGISAFAVQAFASEPTVVPEQPPFPAQGKITYVSRDSILEFKALREYREPEWVTEKFVKAGKLPPVAERLPKEPMVFKAGNMPDGMGVYGDVMRHVIGGRPEGWNYSAGQTQGWGGIDIGMFECLTRTAPLFQVEADDMEPLPNLAKSWDWSEDGRKLTMHLIEGAKWSDGDPFDADDVMFYWEDNVLDSSVSPLNGATPETFGEGTTLKKIDQYTVEWTFKEAFPRQHLFAMAYGTFCPGPSHILKTKHPKYAGTTYNEYKNGFPAEYMNLPVMGAWVPVAYRPDDIIVLRRNPYYWKVDEAGNQLPYLNELHYKLSTWADRDVQAIAGSGDISNLEQPENFVESLKRAANESAPARLAFGPRVIGYNMHMNFSGNGWGDPDERAKAVRELNRNLDFRKAVTMAVDRKKLGEALVKGPFTAIYPGGLSSGTSFYDRNSTIYYPHDLEGAKVLLEKVGLKDTDGNGFVNFPAGKLGGRDVEIVLLVNSDYSTDRNLAEGMVGQMEKLGLRVVLNALDGKQRDAANYAGRFDWMIHRNTAEFASVVQNTPQLAPTGPRTSWHHRAPEGGEVDVMPHEQELVDIVNKFIASNDNDERTELMKQYQKVATTNVDTVGLTEYPGALIINKRFSNIPPGAPIFMFNWAEDTIIRERVFVAADKQGDYELYPEQLPGKPGESGPIN Sinorhizobium meliloti 1021 Smeli SM_b21652 SM_b21652 ABC transporter for Lactose, periplasmic substrate-binding component Specific phenotype on Beta-Lactose. (KEGG_correct) lactose ABC transporter substrate-binding protein MDIQTRAYLPRIAGLALAGASFLGVTAAQAKEITIWCWDPNFNVAIMKEAGARYTKTHPDVTFNIVDFAKLDVEQKLQTGLSSGTADALPDIVLIEDYGAQKYLQSFPGAFAPLSGTVDYSGFAPYKVELMTLDGQVYGMPFDSGVTGLYYRKDYLEAAGFKPEDMQDLTWDRFIEIGKQVEEKTGKKMMGLDPNDAGLVRIIMQSAGQWYFDKEGKPNIAGNAALKAALETIGKIMQANIYKPANGWSDWVGTFTSGDVATVVTGVWITGTVKAQPDQSGNWGVAPIPALSIEGATHASNLGGSSWYVLESSEEKAEAIDFLNEIYAKDIDFYQKILQDRGAVGSLLAARGGAAYEAADPFFGGEKVWQNFSDWLAKVPSVNYGIFTNEADLAVTAQLPAVTQGTPVDEVLQAIEAEVSAQIQ Sinorhizobium meliloti 1021 Smeli SM_b21653 SM_b21653 ABC transporter for Lactose, permease component 1 Specific phenotypes on Beta-Lactose. Not important for arabinose utilization but there is no other clear arabinose tranpsorter so who knows (KEGG_correct) lactose ABC transporter permease MVRARRGIGRYYDVNGWLFVAPALGLITLFMVYPIAWSLWMSFQSGRGMTLKFAGFANIVRLWNDPVFIKALTNTMTYFVVQVPIMILLALILASLLNNPRLVGRGVFRTAIFLPCVSSLVAYSVLFKGMFATDGIVNSTLQAIGLAASPIPWLTHPFWAKVLVILAITWRWTGYNMIFYLAALQNIDKSIYEVARIDGVPAWARLTHLTIPLLKPVILFTTVISTIGTLQLFDEVYNLTEGKGGPSNATLTLSLYIYNLTFRFMPNLGYAATVSYVIVVLVALLAFVQFFAARERDR Sinorhizobium meliloti 1021 Smeli SM_b21654 SM_b21654 ABC transporter for Lactose, permease component 2 Specific phenotypes on Beta-Lactose. Not important for arabinose utilization but there is no other clear arabinose tranpsorter so who knows (KEGG_correct) lactose ABC transporter permease MNGFGRFAAMAATYGFLGLMAFLSVFPFIWMVLGATNSSIDIIKGKLLPGAAFATNVANFFTLVNVPLVFWNSAKIAIVATVLTLAVSSLAGYGFEMFRSRRRERVYRAMLLTLMIPFAALMIPLFVMMGKAGLINTHLAVVLPSIGSAFVIFYFRQSTKAFPSELRDAAKVDGLKEWQIFLFIYVPVMRSTYAAAFVIVFMTAWNNYLWPLIVLQTNETKTITLVISSLASAYYPDYGVVMVGTILATLPTLAVFFFMQRQFVQGMLGSVK Sinorhizobium meliloti 1021 Smeli SMc00588 SMc00588 L-arabinose 1-dehydrogenase; D-galactose 1-dehydrogenase (EC 1.1.1.46; EC 1.1.1.48) Important on L-arabinose and D-galactose; may also act on D-glucose, given phenotype with some N sources with glucose as C source; 55% identical to ARAA_AZOBR, which has L-arabinose and D-galactose 1-dehydrogenase activity in vitro D-galactose 1-dehydrogenase MSPINIAIVGVGKIVRDQHLPALAKNADYRLIAAASRHGTVDGIDNFKSIEAMIDAVPAVEAVSLCMPPQYRYEAARTALAAGKHVFLEKPPGATLSEVADLEALAEEKGVSLFASWHSRYAPAVEAAKTFLASAAIRNVRIIWKEDVRHWHPNQEWIWAAGGLGVFDPGINALSIMTHILPRPVFITSATLEFPENRDAPIAATIAFSDAEKLDVAAEFDWRQTGKQSWDIVAETDAGGMVLSEGGAKLAIDGKIVHEEPEQEYPMLYRRFAEIIKAGRSDVDLAPLRHVADAFMLGRRKFVEAFHD Sinorhizobium meliloti 1021 Smeli SMc00781 SMc00781 malonate-semialdehyde dehydrogenase (acetylating) (EC 1.2.1.18) Specifically important for: m-Inositol; Uridine. 3-oxopropionate or malonate semialdehyde is an intermediate in myo-inositol catabolism and also in pyrimidine catabolism malonic semialdehyde oxidative decarboxylase MYELGHFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYHSFGGWKSSSFGDLNQHGTDSIKFWTRTKTITSRWPSGIKDGAEFSIPTMR Sinorhizobium meliloti 1021 Smeli SMc01054 SMc01054 required for sulfate utilization, putative electron source for sulfite reductase CysI PFam PF11011.4 (DUF2849). conserved cofit with sulfite reductase and has a complementary pattern of gene presence as cysJ hypothetical protein MVEKVLTANRLADGISVWLDASGNWVESLQDAFVARHAEAVAALEATGKRSFDENKVVDVNVIDVEEVDGTLRPLRMRERIRAEGPSIPYAPGYSGLAGPKNVAA Sinorhizobium meliloti 1021 Smeli SMc01105 SMc01105 uridine nucleosidase (EC 3.2.2.3) Specifically important for: Uridine. annotated by SEED as acting on uridine and inosine nucleoside hydrolase MSSARKIIIDTDPGQDDAAAIMLALGSPEEIEVLGITAVAGNVPLTLTARNARIVCELCNRTDVKIFAGAERPVARPLVTAEHVHGKTGLDGPALDEPTMPLQEQHAVDFIVETLRAEAPGAVTLCTLGPLTNIALALTKAPEIAPSVRELVMMGGGFFEGGNITPAAEFNIYVDPEAAEIVFRSGIPIVMMPLDVTHRVLTRKTRVEKIRAIGSPAAVALAEMLEFFERFDIEKYGTDGGPLHDPTVIAYILRPELFTGRDCNVEIETASPLTTGMTVVDWWQVTGRAHNAKVMRHIDDEGFFELLAERLARI Sinorhizobium meliloti 1021 Smeli SMc02118 SMc02118 ABC transporter for L-Glutamine, L-Histidine, and other L-amino acids, periplasmic substrate-binding component Specific phenotype on L-Histidine; L-Glutamine. general L-amino acid-binding periplasmic ABC transporter protein MARRILTALVGAAVVGIGTHAASAATLDDVKAKGFVQCGVNTGLAGFAAPDASGNWSGFDVDYCKAIAAAIFGDGSKVKYTPLSAKERFPALQSGEVDVLARNTTWSINRDTALGFNFRPVNYYDGQGFMVRKELDVKSALELSGAAVCVQTGTTTELNLADYFKANNLQYNPVVFEKLEEVNAAYDAGRCDVYTTDQSGLYSLRLTLSKPDDHIVLPEIISKEPLAPAVRQGDDQWFDIVSWVHYALVQAEEFGVTQANLEEMKKSTNPDVQRFLGVEADSKIGTDLGLTNEWAVNIVKAVGNYGEVFDRNIGAGSPLKIERGLNALWNKGGLQYAPPVR Sinorhizobium meliloti 1021 Smeli SMc02119 SMc02119 ABC transporter for L-Glutamine, L-Histidine, and other L-amino acids, permease component 1 Specific phenotypes on L-Glutamine; L-Histidine. Mild phenotypes on proline or lysine (KEGG_correct) general L-amino acid transport permease ABC transporter protein MAIGVTNAPERSRSSGSIINDPQVRGIFYQAITIIILAALIYWIVDNTVDNLRRANIASGYDFVRSRAGFDVGQSLISFTSDSTYGRALLVGFINTLLVAITGIITATIIGFIVGIGRLSHNWIIAKLSLAYVEVFRNIPPLLVIFFWYSGVLSILPQARDALALPFDIFLSNRGVAFPRPIAEEGAEYTLLAFVIAVAASVFFARYARKRQLATGERLPVLWTVLGLIIGLPLVTFLVTGAPITFDIPVAGKFNLTGGSVVGPEFMSLFLALSFYTAAFIAEIVRAGIRGVSKGQTEAAHALGIRPALTTRLVVVPQAMRIIIPPLTSQYLNLTKNSSLAVAIGYADLVAVGGTILNQTGQSIEIVSIWLIVYLSLSLATSLFMNWYNARMALVER Sinorhizobium meliloti 1021 Smeli SMc02120 SMc02120 ABC transporter for L-Glutamine, L-Histidine, and other L-amino acids, permease component 2 Specific phenotypes on L-Glutamine; L-Histidine. Mild phenotypes on proline or lysine (KEGG_correct) general L-amino acid transport permease ABC transporter protein MSTNQASFVRASMIEASPAPSLESGAVSWLRKNLFATPKDTALTIISLLILAWLVPPAIQWLFIDAAWSGGGRGVCATLSQGGSQPEGWSGACWAFVNAKFAQFLFGRYPLDERWRPALVGILFVLLLVPMLIPRIPYKGLNALLLLVALPILSAILLPGGWFGLTYVETPLWGGLMVTLVLSFVGIAVSLPLGILLALGRRSNMPVIKMLCTVFIEVIRGVPLITVLFMASVMLPLFLPQGVTFDKFLRALIGVSLFASAYMAEVVRGGLQAIPKGQYEGADSLGLSFWQKMGFIVLPQALKLVIPGIVNTFIGLFKDTSLVSIIGMFDLLGIVRLNFSDTNWATAVTPLTGLIFAGFVFWLFCFGMSRYSGFMERLLDRSQR Sinorhizobium meliloti 1021 Smeli SMc02121 SMc02121 ABC transporter for L-Glutamine, L-Histidine, and other L-amino acids, ATPase component Very important for histidine and glutamine utilization and also for lysine utilization. It could be the ATPase component for lysine transport by Smc00140:Smc00138 as well (as there is no ATPase component in that gene cluster or other ATPase component identified in the fitness data) general L-amino acid transport ATP-binding ABC transporter protein MANTATAPKLAVSTTDVAIEITNMNKWYGDFHVLRDINLRVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEVRREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKEAEQVAMHFLERVKIPEQALKYPGQLSGGQQQRVAIARSLCMRPKILLFDEPTSALDPEMVKEVLDTMVGLAEEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFLSQILH Sinorhizobium meliloti 1021 Smeli SMc02123 SMc02123 required for sulfate utilization, putative electron transport protein for sulfite reductase PFam PF06073.8 (DUF934). conserved cofitness with sulfite reductase (SMc02124, sometimes misannotated as nitrite reductase); auxotrophic hypothetical protein MTKIWKETGFVNDDPWVIETDETKAGSNEKAILNIDGFLAAVAESDASELGVLINPADDVMRLQPYLERIALVAVAFPAFSDGRSFSHASLLRSRLGYQGEIRAVGDVLIDPIPLMLRCGVDSFAVTNATAIKRLSEGRLPGISNHYQPTAKPSANINSYSWRRVS Sinorhizobium meliloti 1021 Smeli SMc02237 SMc02237 DNA damage response helicase, ligase-associated Conserved and specific phenotype: important for resisting cisplatin. Related to Lhr, which is either a DNA:DNA or DNA:RNA helicase, but lacks the long C-terminal extension that might have a regulatory role (see putative winged helix domain in E. coli lhr). This is also related to the archael protein saci_1500, which has also been linked to DNA damage response, as a mutant is sensitive to UV (PMID: 26148716) ATP-dependent helicase MFSVDRIDSPSPEGDALTLPAPFLRWFAEKGWRPRAHQLELLSRAEAGESTLLIAPTGAGKTLAGFLPSLVDITRRGRIPPGAPFTGIHTLYISPLKALAVDIERNLMKPVGEMGLPVSIENRTGDTPQGKRQRQKLNPPDILLTTPEQLALLLANGEAERFFKDLRYVVLDELHSLVMSKRGHLLSLGLARLRRLAPRLQTMGLSATVADPMDLQRWLVAQFLAKENHAGLITVSGGAKPEISILRTENQVPWAGHSARYAIPDVYAAIKEHRTTLLFVNTRSQAEMLFQELWKINDDDLPIALHHGSLDVAQRRRVEAAMAENRLRAVVATSTLDLGIDWGDVDLVVHVGAPKGASRLAQRIGRANHRMDEPSRAILVPANRFEVMECQAALDANYVGAQDTPSIGKGALDVLAQHILGMACAQPFDALELYEEVISAAPYARLAWETFERAVDLVATGGYALRTYERYARIRKTKDGLWRVSNPMVAQQYRLNVGTIVESPMLNIRMVKRNQRGSLGRGGMSLGKVEESFLEMLSPGDTFLFSGKVLRFEGIRENECLVSQAFSFDPKVPSYAGGKFPLSTYLAAQVRKMLADPARRAGLPDQVRDWLALQGDVSMLPRDDELLIETFPRGSRHYMVIYAFEGRLAHQTLGMLLTRRLDRAGLKPLGFVATDYSLAVWALDDMGAAFRARAPSLGQLFDEDMLGDDLEAWLNESFLLKRTFRNCAVIAGLIEQRHPGREKTGRQITVSADLIYDVLRAHEPDHILLEATRNDAATGLLDIGRLGSMLKRIKGHITHRRLDQISPLAIPVMLEIGRESVHGEAQDFLLTEAADDLINEAMGGHGTDG Sinorhizobium meliloti 1021 Smeli SMc02321 SMc02321 L-rhamnose isomerase (EC 5.3.1.14) Specifically important for: L-Rhamnose monohydrate. KEGG now annotates it as L-rhamnose isomerase, which is correct. The gene is cofit with SMc03003 (rhaK), which is probably rhamnulose kinase. It had been suggested that rhaK might be rhamnose kinase and that the isomerase might act on L-rhamnose 1-phosphate, but the S. meliloti rhaK is not a rhamnose kinase. See the PhD thesis of Damien M. R. Rivers (2015). (KEGG_correct) sugar isomerase MTLMISTSVLDAENASRRDALTRDYESLGDRLARRGIDIDAVKAKVAAYGVAVPSWGVGTGGTRFARFPGPGEPRNIFDKLEDCAVIQQLTRATPAVSLHIPWDKVSDLGALKEKGSALGLSFDAMNSNTFSDAPGQAHSYKFGSLSHTDSATRRQAIEHNLECVEIGKALGSKALTVWVGDGSNFPGQSNFTRAFERYLDSMKAVYAALPDDWRIFTEHKMFEPAFYSTVVQDWGTNYLIAQELGPKAFCLVDLGHHAPNVNIEMIVARLIQFKKLGGFHFNDSKYGDDDLDTGSIDPYRLFLVFNELVDAETRAANGFDPAHMLDQSHNVTDPIESLMTSAMEVGRAYAQALIVDRKALAGYQEENDALMASETLKTAFRTDVEPILATARLENDGAIAPVAAYRASGYRARVAAERPAVAGGGGGIV Sinorhizobium meliloti 1021 Smeli SMc02322 SMc02322 rhamnulose-1-phosphate aldolase (EC 4.1.2.19) / lactaldehyde dehydrogenase (EC 1.2.1.22) Specifically important for: L-Rhamnose monohydrate. These are the steps after the L-rhamnose 1-phosphate isomerase (SEED_correct) short chain dehydrogenase MLDKHQGARLANLWDDGKAAGMTEPEKLLYRSNLLGSDKRITNYGGGNTSAKVMEKDPLTGEIVEVLWVKGSGGDVGTIKMDGFSTLYMDKLRALKGIYRGVEFEDEMVGYLPHCTFNLNPRAASIDTPLHAYVPKPHVDHMHPDAIIAIAASKNSRELTSKIFGDEIGWLPWKRPGYELGLWLEKFCQENPDARGVVLESHGLFTWGDTAKEAYETTIEIINRAIAWFETENTGPAFGGRSKPVLAAADRAAIAKKLMPVIRGLISAGESKVGHFDDSQAVLDFVTSTSLEPLAALGTSCPDHFLRTKIRPLVVDFDPAQPDVGNTLAGLPEAIATYRADYAAYYERCKRADSPAMRDPNAVVYLVPGVGMITFAKDKATARISAEFYVNAINVMRGASGVSTYVGLPEQEAFDIEYWLLEEAKLQRMPKPKSLAGRIALVTGGAGGIGKATANRLMQEGACVVLADIDETALEAAQTELSTRYGKDFVRSVNMNVTSEAAVESGFGDALLAFGGLDILVSNAGLATSAAVEDTTLALWNKNMDILATGYFLVSREAFRIFRNQKAGGNVVFVASKNGLAASPGASAYCTAKAAEIHLARCLALEGASAQIRVNVVNPDAVLRGSKIWTGEWKEQRAAAYKMDVDELEAHYRERSMLKLSVFPEDIAEAIYFLASDMSAKSTGNIVNVDAGNAQSFTR Sinorhizobium meliloti 1021 Smeli SMc02869 SMc02869 N-Acetyl-D-glucosamine ABC transport system, ATPase component Specific phenotype on N-Acetyl-D-Glucosamine. (SEED_correct) ABC transporter ATP-binding protein MCAPASRSSFNPRGRHVGSLQLKTIRKAFGSHEVLKGIDLDVKDGEFVIFVGPSGCGKSTLLRTIAGLEDATSGSVQIDGVEVGHVAPAKRGIAMVFQSYALYPHLTVKDNMGLGLKQAGVPKAEIEEKVAKAAGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPKLFLFDEPLSNLDAALRVNTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVLNAGRIEQVGSPMELYNRPANLFVAGFIGSPQMNFIEAAKLGDGEAKTIGIRPEHIGLSRESGDWKGKVIHVEHLGADTIIYIESETVGLLTVRLFGEHRYATDDIVHATPVIGSMHRFDADGRVIKSGQ Sinorhizobium meliloti 1021 Smeli SMc02871 SMc02871 ABC transporter for N-Acetyl-D-glucosamine, permease protein 2 Specific phenotypes on N-Acetyl-D-Glucosamine; N-Acetyl-D-Glucosamine. (SEED_correct) ABC transporter permease MSKARASFMRTGAVHAALIAYTLIALFPVFLTIVNSFKSRNAIFREPLAVPTPETFSLIGYETVLKQGDFIGYFQNSIIVTVVSIALVLLFGAMAAFALSEYRFRGNTLMGLYLALGIMIPIRLGTVAILQGMVATGLVNTLTALILVYTAQGLPLAVFILSEFMRTVSDDLKNAGRIDGLSEYAIFLRLVLPLIRPAMATVAVFTMIPIWNDLWFPLILAPAEATKTVTLGSQIFIGQFVTNWNAVLSALSLAIFPVLVLYVIFSRQLIRGITAGAVK Sinorhizobium meliloti 1021 Smeli SMc02872 SMc02872 ABC transporter for N-Acetyl-D-glucosamine, permease protein 1 Specific phenotypes on N-Acetyl-D-Glucosamine; N-Acetyl-D-Glucosamine. (SEED_correct) ABC transporter permease MNPREITTYVTEIKRPRRWHILVFLLPALVVYTAVMILPLFETLRQSFYNTVDGQLTFVGLGNFKVLFGDPRWAADFWNALKNNFVFFLIHMAVQNPIGIALAAMLSVPKLRFGAFYRTAIFLPTLLSFVIVGFIWKLILSPIWGVAPYLLDTVGLRSLFGPWLGKPDTALIAVSLISVWQYIGIPMMLIYAALLNIPDEVTEAAELDGVTGWSQFWKIKLPLILPAIGIVSILTFVGNFNAFDLIYTVQGALAGPDKSTDILGTLLYRTFFGFQLQLGDRSMGATIAAIMFLIILAGVALYLFGIQRRMRRYQF Sinorhizobium meliloti 1021 Smeli SMc02873 SMc02873 N-Acetyl-D-glucosamine ABC transport system, periplasmic substrate-binding component Specific phenotype on N-Acetyl-D-Glucosamine. (SEED_correct) periplasmic binding (signal peptide) ABC transporter protein MTRTTMKGLLLASSILGSAGLAQAQDATLTIESWRNDDLAIWQEKLIPAFEAKNPGIKVVFAPSAPTEYNAALNAKLDAGSAGDLITCRPFDASLELYNKKHLADLTGLSGMENFSDVAKSAWTTDDGKATFCVPMASVIHGFIYNKDAFDQLGLSVPATEEEFFAVLEKIKADGNYIPMAMGTKDLWEAATMGYQNIGPNYWKGEEGRLALLKGEQKLTDEPWVEPFRVLAKWKDYLGDGFEAQTYPDSQNLFTLGRAAIYPAGSWEISGFNTQAEFKMGAFPPPVKKAGDTCYISDHNDIGIGLNAKSKNADAAKTFLTWVASPEFAEIYANALPGFFSLNSTAVKMSDPLAQEFVSWREKCKPTIRSTYQILSRGTPNLENETWVMSANVINGTDTPEAAAKKLQDGLDSWFKPVK Sinorhizobium meliloti 1021 Smeli SMc02875 SMc02875 N-acetylglucosamine kinase (EC 2.7.1.59) Specifically important for: N-Acetyl-D-Glucosamine. The first step in NAG catabolism (SEED_correct) hypothetical protein MTFYLIGIDGGGTSCRAAVAALDGRILGRGKAGAANILTDPETALQNITDAARDAFGDAGLDPAGIGASRAIVGVAGHNVGDAVHYVKRRLPFAQADIESDGLIALQGALGDGDGAVAILGTGTIYIARRGDEVSYVGGWGFTIGDHGSGARIGHALLQESLLAYDGIHQGSGVTDAVLAEFNDDPRDIVDFARLAKPGEFGRYAPRVFEFAERGDPVAISLLKAAAATVDEALDVVVSRGSEKLCLLGGLAPLYRRWLADRHQPRFVEARADALTGAVALAAARFGSHSGVSA Sinorhizobium meliloti 1021 Smeli SMc03003 SMc03003 Rhamnulokinase RhaK in alpha-proteobacteria (EC 2.7.1.5) Specifically important for: L-Rhamnose monohydrate. Also see comment on SMc02321; this is the first step in L-rhamnose degradation. (SEED_correct) hypothetical protein MMMKTVAVIDIGKTNAKVALVDLERFEEIAVRKSGNGVSDDGPYPHFDTERLWRFVLDSLAALHREHPVDAISVTTHGATAVLLDEAGELALPVLDYEFTGPDALAEEYEKARPPFTETGSARLPMGLNVGAQLFWQQRMFPEHFARVATILTYAQYWSYRLTGVRTNELTSLGCHTDLWNPKAATFSSMVDEQGWRHLFAPVRRAGDVLGPLLRQVADETGLPPETPVHCGIHDSNASLLPHLITRQAPFSVASTGTWVVMLAVGAEPVKLDERRDTLINVNALGDPVPSARFMGGRAYSLLIGDDPPTASPEAEASVLEQGHMLLPSLPGGSGPFPAARPHWTADEDKLAPAERLAVVSFHLALMTATCLDLIGARGEILVEGPFALNDAYLRMLAAATGRPVLANRLNSTGTSLGAACLVAGARVRTGAEAIPAAKPDAYAAYAEAWRRRTAAHVRSDP Sinorhizobium meliloti 1021 Smeli SMc03162 SMc03162 epimerase involved in beta-glucoside degradation Specifically important for: D-Salicin; D-Cellobiose. The SEED prediction (for a step in myo-inositol degradation) is not consistent with the phenotypes on D-salicin and D-cellobiose (which are both beta-glucosides). Because it is cofit with a beta-mannosidase (SMc04255), we suspect that it converts beta-glucosides to beta-mannosides. However this pathway also seems to involve two oxidoreductases (SMc03161, SMc04253) so its exact role is uncertain. hypothetical protein MKTIKGPGLFLAQFAGDAAPFNSWDSITKWAADCGYKGVQVPSWDGRLFDLKKAAESKTYCDEVAGKARDNGVEITELATHLQGQLVAAHPAYDEAFDGFAVPQVRGNPRARQEWAVEQVKLALTASKNLGLGAMASFSGALAWPFVYPWPQRPAGLVETAFDELARRWKPILDHAEDCGVDVCYEIHPGEDLHDGITYEMFLERTGNHARACMLYDPSHYVLQCLDYLENIDIYKDRIRMFHVKDAEFNPTGRQGVYGGYQSWVNRAGRFRSLGDGQVDFGAVFSKMAANDFAGWAVVEWECCLKHPEDGAREGSEFVKAHIIRVTEKAFDDFADSGTDEAANRRMLGI Sinorhizobium meliloti 1021 Smeli SMc04256 SMc04256 ABC transporter for D-Cellobiose and D-Salicin, ATPase component Specific phenotype on D-Salicin; D-Cellobiose. ABC transporter ATP-binding protein MTSVSVRDLSLNFGAVTVLDRLNLDIDHGEFLVLLGSSGCGKSTLLNCIAGLLDVSDGQIFIKDRNVTWEEPKDRGIGMVFQSYALYPQMTVEKNLSFGLKVAKIPPAEIEKRVKRASEILQIQPLLKRKPSELSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQSLKNTMIYVTHDQIEALTLADRIAVMKSGVIQQLADPMTIYNAPENLFVAGFIGSPSMNFFRGEVEPKDGRSFVRAGGIAFDVTAYPAHTRLQPGQKVVLGLRPEHVKVDEARDGEPTHQAVVDIEEPMGADNLLWLTFAGQSMSVRIAGQRRYPPGSTVRLSFDMGVASIFDAESENRL Sinorhizobium meliloti 1021 Smeli SMc04257 SMc04257 ABC transporter for D-Cellobiose and D-Salicin, permease component 1 Specific phenotypes on D-Cellobiose; D-Salicin. ABC transporter permease MAAAYETAPGGPMAGPRGRKPRRTLSRRNIIVYGTLIVVALYYLLPLYVMIVTSLKGMPEIRVGNIFAPPLEITFEPWVKAWAEACTGLNCDGLSRGFWNSVRITVPSVIISIAIASVNGYALANWRFKGADLFFTILIVGAFIPYQVMIYPIVIVLREMGVYGTLTGLIIVHTIFGMPILTLLFRNYFAGLPEELFKAARVDGAGFWTIYFKIMLPMSLPIFVVAMILQVTGIWNDFLFGVVFTRPEYYPMTVQLNNIVNSVQGVKEYNVNMAATILTGLVPLTVYFVSGRLFVRGIAAGAVKG Sinorhizobium meliloti 1021 Smeli SMc04258 SMc04258 ABC transporter for D-Cellobiose and D-Salicin, permease component 2 Specific phenotypes on D-Cellobiose; D-Salicin. ABC transporter permease MTGLTRGSARPNQWLRNLNAKIASIPMILTAMVIFVGGTAWTVVYSFTNSKLLPRLAFVGFDQYERLWAAPRWLVSIQNLAVFGCLSLVFSLVIGFVLAALMDQKIRFENTFRTIMLYPFALSFIVTGLVWQWLLNPQYGIQSIVRSLGWTSFSFDPLYNSNIVIYGILIAALWQGTGLVMCLMLAGLRGIDEDIWKAARVDGIPMWKTYVLIIIPMMRGVFITTLVIIASGIVKVYDLVVAQTSGGPGIASEVPAKYVYDYMFQAQNLGQGFAASTMMLVTVAIIIVPWAYLEFGGGRKRG Sinorhizobium meliloti 1021 Smeli SMc04259 SMc04259 ABC transporter for D-Cellobiose and D-Salicin, periplasmic substrate-binding protein Specific phenotype on D-Salicin; D-Cellobiose. periplasmic binding ABC transporter signal peptide protein MNLRFLAAALGATAALPFGAASATDLEVTHWWTSGGEAAAVAELAKAFDATGNKWVDGAIAGSGGTARPIMISRITGGDPMAATQFNHGRQAEELVQAGLMRDLTDIATKENWKEIVKPSSLLDSCTIEGKIYCAPVNIHSWQWLWLSNAAFKQAGVEVPKNWDEFVAAAPALEKAGIVPLAVGGQPWQANGAFDVLMVAIAGKENFEKVFAQKDEEVAAGPEIAKVFKAADDARRMSKGTNVQDWNQATNMVITGKAGGQIMGDWAQGEFQLAGQKAGVDYTCLPGLGVNEVISTGGDAFYFPLLEDEEKSKAQEVLASTLLKPETQVAFNLKKGSLPVRGDVDLAAANDCMKKGLDILAKGNVIQGTDQLLSADSQKQKEDLFSEFFANHSMTPEDAQKRFADIIAAAD Sinorhizobium meliloti 1021 Smeli SMc04383 SMc04383 putative hydrolase, required for lysine catabolism PFam PF07063.9 (DUF1338). This gene is specifically important for utilizing lysine, and this phenotype is conserved. It might be the decarboxylating 2-oxoadipate hydrolase of the D-lysine oxidase pathway, which has not been linked to a gene, or the crotonyl-CoA hydratase in the glutaryl-CoA degradation pathway. hypothetical protein MKENSFVSADDIRSAFSAAMSLMYREEVPAYGTLMELVARVNGETLSADATLKGRLEATDSLERISEERHGAIRLGTPAELSMMRRVFAVMGMYPVGYYDLSTAGVPVHSTAFRPVGDAALKHNPFRVFTSLLRLDLISDEALRAEAEAILKERRIFTSGAVELTEKAERDGGLDKADAERFVAEVLETFRWHDEANVSAGMYERLHDAHRLIADVVSFKGPHINHLTPRTLDIDRVQALMPEYGIAPKAVVEGPPTRKCPVLLRQTSFKALEEPVSFRDSDGSWKTGSHTARFGEIEQRGIALTPKGRGLYDRLLDESRKIVRPAADGSNAREYEAALAQVFEAFPDSWAELREAGLGYFSYSLTDKGRRTKLPGRRDLNSLIADGLVQFDPIVYEDFLPVSAAGIFQSNLGDGAQQEFEASPNQKRFETDLGVAVLNEFDHYAGIEQASIEGCLKALTAAMAAE Sinorhizobium meliloti 1021 Smeli SMc04386 SMc04386 2-aminoadipate:2-oxoglutarate aminotransferase (EC 2.6.1.39) Specifically important for: L-Lysine. This is required for catabolism of lysine on the way to glutarate. The amino group donor is uncertain aspartate aminotransferase B protein MTINATVKEAGFQPASRISSIGVSEILKIGARAAAMKREGKPVIILGAGEPDFDTPEHVKQAASDAIHRGETKYTALDGTPELKKAIREKFQRENGLAYELDEITVATGAKQILFNAMMASLDPGDEVIIPTPYWTSYSDIVHICEGKPVLIACDASSGFRLTAEKLEAAITPRTRWVLLNSPSNPSGAAYSAADYRPLLEVLLRHPHVWLLVDDMYEHIVYDGFRFVTPAQLEPGLKNRTLTVNGVSKAYAMTGWRIGYAGGPRELIKAMAVVQSQATSCPSSISQAASVAALNGPQDFLKERTESFQRRRDLVVNGLNAIDGLDCRVPEGAFYTFSGCAGVLGKVTPSGKRIKTDTDFCAYLLEDAHVAVVPGSAFGLSPFFRISYATSEAELKEALERIAAACDRLS Pseudomonas simiae WCS417 WCS417 GFF142 PS417_00715 required for octanoate transport, together with NodT, MFP, and FUSC proteins (PS417_00725, PS417_00720, PS417_00710) PFam PF07869.8 (DUF1656). A conserved cofit operon. This and orthologous operons are important for growth in 20 mM octanoate (as the carbon source), which is probably toxic. This operon could also be for uptake rather than efflux. membrane protein MIGDLDISGVFLPTLLVLMGITYVLFLVVHGLLTRLHFYRLVWHRALFNVGLYALLLGAVDSLSRYLMT Pseudomonas simiae WCS417 WCS417 GFF481 PS417_02455 putative transporter, required for glycine utilization PFam PF03458.9 (UPF0126). Substrate is a conserved specific phenotype of UPF0126 membrane protein MLLMLYLIAITAEAMTGALSAGRRGMDWFGVVLIACVTALGGGSVRDVLLGHYPLTWVKHPEYLVLTSIAALVTIFIAPLMRRLRSLFLALDAVGLVAFTLIGCMTALEMGHGMLVASVSGVITGVFGGILRDIFCNDIPLIFRRELYASVSFLAAWFYMLCLYLELPSEQAILLTLFSGFLLRLLAIRFHWEMPKFVYNDDVH Pseudomonas simiae WCS417 WCS417 GFF827 PS417_04200 2-ketoglutaric semialdehyde dehydrogenase (EC 1.2.1.26) Specifically important for: D-Galacturonic Acid monohydrate. alpha-ketoglutarate semialdehyde is an intermediate in the oxidation of galacturonate (SEED_correct) aldehyde dehydrogenase MSQAQRFDNYINGQWVAGADYCVNLNPSELSDVIGEYAKADVTQVNAAIDAARAAFPAWSTSGIQARHDALDKVGSEILARREELGTLLAREEGKTLPEAIGEVTRAGNIFKFFAGECLRLSGDYVPSVRPGVNVEVTREALGVVGLITPWNFPIAIPAWKIAPALAYGNCVVIKPAELVPGCAWALAEIISRAGFPAGVFNLVMGSGRVVGDVLVNSPKVDGISFTGSVGVGRQIAVSCVSRQAKVQLEMGGKNPQIILDDADLKQAVELSVQSAFYSTGQRCTASSRLIVTAGIHDQFVAAMAERMKSIKVGHALKSGTDIGPVVSQAQLDQDLKYIDIGQSEGARLVSGGGLVTCDTEGYYLAPTLFADSEAAMRISREEIFGPVANVVRVADYEAALAMANDTEFGLSAGIATTSLKYANHFKRHSQAGMVMVNLPTAGVDYHVPFGGRKGSSYGSREQGRYAQEFYTVVKTSYIGS Pseudomonas simiae WCS417 WCS417 GFF828 PS417_04205 D-galacturonate transporter (MFS superfamily) Specific phenotype on galacturonate. This phenotype is conserved. There is also another putative hexuronate transporter that has a weaker phenotype on galacturonate (PS417_14775). glucarate transporter MQATKPTHVRYLILLMLFLVTTINYADRATIAIAGSSLQKDLGIDAVTLGYIFSAFGWAYVAGQIPGGWLLDRFGSKKVYALSIFTWSLFTVLQGYVGEFGVSTAVVALFMLRFMVGLAEAPSFPGNARIVAAWFPTAERGTASAIFNSAQYFATVLFAPLMGWIVYSFGWQHVFIVMGVIGIIFSLIWLKVIHSPRQHPMINEAEFNHIAANGAMVDMDQDKGKGKKTDGPKWDYIRQLLTNRMMLGVYLGQYCINGITYFFLTWFPVYLVQDRGMTILKAGFIASLPAICGFIGGVLGGVISDYLLRKGHSLTFARKAPIIGGLLISSSIVACNYVDIEWMVVGFMALAFFGKGVGALGWAVVSDTSPKQIAGLSGGLFNTFGNLASITTPIVIGYIISTTGSFKWALVFVGANALVAVFSYLVIVGPIKRVVLKEPPTQGPELTRLTEAHS Pseudomonas simiae WCS417 WCS417 GFF1004 PS417_05090 ferric citrate outer membrane transporter (fecA) Specific phenotype on citrate; 63% identical to E. coli fecA; SEED_correct transporter MPQQPTLLARTLRQLLLGASLSLTALPPVMAADAKPYHIAPTSLEAALNQFGREAGVLISFGSEVTAGMQSRGLSGNYGAADGLQKLLEGTGLQARAEGDNAYSLQPATAPASIELGTSSVVGDWLGDAAQTHVFEHPGARDVIRREEFERQGATQAKDVLNRIPGVNAPDNNGTGSHDMALNFGIRGLNPRLASRSTVLMDGIPVPFAPYGQPQLSFAPISMGNMDAVDVVRGGGAVRYGPQNVGGVVNFVTRAIPDAPTVKGGLQTETSPSSSHDGFKTTGNLLAGGTADNGLGGAILYSGTRGGDWRENSNTRIDDLILKGKYQLDDANSFNAMAQYYEGQADMPGGLNVADYKADPYQSTRPYDKFWGRRTMFNVGYRYEQDRREFTVNSFFTKTLRSGYLDQGTFLSLSPREYWVRGIETRFAQGFDLGPTSHEVGVGYRYINEAGHELRYRTPIAANQQIPTTNSRNDRDTRGGTEANAFFVDDRIDIGKWTITPGIRYEIIESQQTNNLTNVKYKGDYNTALPALNVLYHLTDNWNLYANTEGSFGSVQYSQMPNRVTSGEVKPEKARTWELGTRYDDGTLRAEIGAFLINFDNQYESNQTNDSVIARGETRHQGIETSINYALDGLSPALAGFDVYATYAYVDATIREDGPNKGNRVPFSSKHKGTLGVGYTEGRWKLNLDSSYQSSQFADNANTEKETANGANGRIPGYMLFSSRAAYDFGPQLSDLNVAVGVKNIFNTQYFTRSFDDNNKGKYVGEPRTVYVQTSIAF Pseudomonas simiae WCS417 WCS417 GFF1065 PS417_05405 L-alanine and D-alanine permease Important for utilizing both isomers of alanine, and no other transporter is apparent. Both phenotypes are conserved. D-alanine/D-serine/glycine permease MPVGNHLPHGETAQGGPLKRELGERHIRLMALGACIGVGLFLGSAKAIEMAGPAIMLSYIIGGLAILVIMRALGEMAVHNPVAGSFSRYAQDYLGPLAGFLTGWNYWFLWLVTCVAEITAVAVYMGVWFPDTPRWIWALAALISMGSINLIAVKAFGEFEFWFALIKIVTIIAMVIGGVGIIAFGFGNDGVALGISNLWAHGGFMPNGVQGVLMSLQMVMFAYLGVEMIGLTAGEAKNPQKTIPSAIGSVFWRILLFYVGALFVILSIYPWNEIGTQGSPFVMTFERLGIKTAAGIINFVVITAALSSCNGGIFSTGRMLYSLAQNGQAPATFAKTSSNGVPRKALLLSIFALLLGVLLNYLVPEKVFVWVTSIATFGAIWTWLMILLAQLKFRKSLSPAEQAGLKYRMWLYPVSSYLALAFLLLVVGLMAYFPDTRIALYVGPVFLVLLTVLFYVFKLQPTQVAQGEARPV Pseudomonas simiae WCS417 WCS417 GFF1579 PS417_08035 adenine transporter (MFS superfamily) specific phenotype on adenine and no other transporter was identified by the fitness data. Also mildly important on adenosine, which could reflect extracellular conversion to adenine transporter MKNSFGFTWYLAGLSMLGYLAMDMYLPAFGAMGEQLQIGAGAVGASLSIFLAGFAVGQLLWGPLSDRLGRKPILLAGLSLFVLGCAGMFWVETAPQLLALRFIQAIGVCSAAVSWQALVIDRYPADKAHRVFASIMPLMSLSPALAPLLGAMVLNHFGWQAIFGVLLGVSVLLLLPTVFLRGMPKRPTEGREPVRLGYGQLLTSRVFTGNVMIFAACSASFFAWLTASPFILGGMGYSPNDIGLSYVLPTLAFLVGGYSCRSALQRFQGKTLLPWLLLAYCISMVALYLVATLTVPTLTTLLIPFCLMALCNGASYPIVVANALMPFSENSGKAAALQNTLQLGLCFLSSLVVSSMLDQPLLITAIVMLATAPLAVLGYWLARPKADNSVLAPNLK Pseudomonas simiae WCS417 WCS417 GFF2142 PS417_10925 malonate-semialdehyde dehydrogenase (acetylating) (EC 1.2.1.18) Specifically important for: m-Inositol. 3-oxopropionate or malonate semialdehyde is an intermediate in myo-inositol catabolism methylmalonate-semialdehyde dehydrogenase MTTTIEHYINDQRVSRDDRYQDVFNPATGEKTGRVALASRQTVSEAVAAAQAAFAGWADTPPIRRARVLFEYLHLLRERKDDLARIIVAEHGKVFTDAQGEVDRGIDILEFACGIPNLLKGEHSDQVSRGMDNWTMRQPLGVVAGVTPFNFPVMVPMWMYPIAIAAGNTFILKPSPTDPSASLFMAELLREAGLPKGVFNVVQGDKESVDALIEHPDVKAVSFVGSTPIAQYIYETGARNGKRVQGLGGAKNHMVVMPDADIEKTVDALMGAAYGSAGERCMAISVAVLVGDVGDKVIAALTERAKHLRITDGRDLKAEMGPIVSRAALERISGYIEQGVQAGAQLLLDGRDYVPTEPGLENGFWLGATLFDHVTEEMSIYREEIFGPVLACVRVNDFAEAIKLVNAHEFGNGVSCFTRDGNIAREFARRIEVGMVGINVPISVPMAWHGFGGWKKSLFGDMHAYGTEGVRFYTKQKSIMQRWSESIEQGAEFAMPVSK Pseudomonas simiae WCS417 WCS417 GFF2156 PS417_11000 L-arabonate dehydratase (EC 4.2.1.25) Specifically important for: L-Arabinose. L-arabonate is an intermediate in the oxidation of L-arabinose (SEED_correct) dihydroxy-acid dehydratase MPDKKPGLRSAQWFGTADKNGFMYRSWMKNQGIADHQFHGKPIIGICNTWSELTPCNAHFRQIAEHVKRGVIEAGGFPVEFPVFSNGESNLRPTAMLTRNLASMDVEEAIRGNPIDGVVLLTGCDKTTPALLMGAASCDVPAIVVTGGPMLNGKHKGQDIGSGTVVWQLSEQVKAGTITLDDFLAAEGGMSRSAGTCNTMGTASTMACMAEALGTSLPHNAAIPAVDARRYVLAHMSGMRAVEMVREDLKLSKILTKEAFENAIRVNAAIGGSTNAVIHLKAIAGRIGVELDLDDWTRIGRGMPTIVDLQPSGRFLMEEFYYAGGLPAVLRRLGEANLIPHPNALTVNGKSLGENTQDSPIYGQDEVIRTLDNPIRADGGICVLRGNLAPLGAVLKPSAASPALMQHRGRAVVFENFDMYKARINDPELDVDANSILVMKNCGPKGYPGMAEVGNMGLPAKLLAQGVTDMVRISDARMSGTAYGTVVLHVAPEAAAGGPLATVKEGDWIELDCANGRLHLDIPDAELAARMADLAPPQKLIVGGYRQLYIDHVLQADQGCDFDFLVGCRGAEVPRHSH Pseudomonas simiae WCS417 WCS417 GFF2159 PS417_11015 Ketoglutarate semialdehyde dehydrogenase (EC 1.2.1.26) Specifically important for: L-Arabinose. alpha-ketoglutarate semialdehyde is an intermediate in the oxidation of L-arabinose (SEED_correct) ketoglutarate semialdehyde dehydrogenase MTSFLGHNYIGGQRSANGSVTLQSVDATSGEALPQHFYQATPQEVDAAAKAAAQAYPAYRALSAARRAQFLDAVADELDALGDEFVELVCRETALPAARIKGERGRTSGQMRLFATVLRRGDFYGARIDKALPDRQPMPRPDLRQYRIGLGPVAVFGASNFPLAFSTAGGDTAAALAAGCPVVFKAHSGHMATAERVADAIIRAAEATEMPAGVFNMIFGGGVGEALVKHPAIQAVGFTGSLKGGRALCDMAAARPQPIPVFAEMSSINPVIVLPQALKARAESVARDLTASVVQGCGQFCTNPGLVIGVASPEFTAFTQQVAQLIGDQPAQTMLNAGTLSSYGKGLEKLLAHPGIQHLAGSQQAGNQAQPQLFKADVRLLIDGDEVLQEEVFGPTTVFVEVADQAQLSAALHGLHGQLTATIIGEPADLQQFAELTPLLEQKVGRILLNGYPTGVEVCDSMVHGGPYPATSDARGTSVGTLAIDRFLRPVCFQNYPDSLLPDALKNANPLRIQRLVDGTPSRDPL Pseudomonas simiae WCS417 WCS417 GFF2160 PS417_11020 L-arabinolactonase (EC 3.1.1.15) Specifically important for: L-Arabinose. a step in L-arabinose oxidation (SEED_correct) gluconolaconase MSCIAVTPHRAQLGEGPFWDAPTQALYWVNIAGKQALRLMGGQLQVWQLPEHVSAFIPCESGDALVTLSSGVYRLDLATEALTLLCVADPQPGNRGNEARCDASGRLWLGTMQNNIGEQGEDLPITRRSGGLFRIDADAQVTPLLSGLGIPNTLLWSDDGRHVHFGDSLDGTLYRHAIQPDGQLDPAQTWFGPHERGGPDGSAMDVDGYIWNARWDGSCLLRLTPDGEVDRIVELPVSRPTSCVLGGPNLTTLYITSAASPLDHPLDGAVLAMEVDVPGKPCHRFAG Pseudomonas simiae WCS417 WCS417 GFF2259 PS417_11520 Sorbitol dehydrogenase (EC 1.1.1.14) Specifically important for: D-Sorbitol. The first step in sorbitol degradation (SEED_correct) sorbitol dehydrogenase MKRLEGKSALITGSARGIGRAFAQAYIAEGATVAIADIDLQRAQATAAELGPQAYAVAMDVTDQASIDGAITAVVAQAGKLDILINNAALFDLAPIVDITRDSYDRLFSINVAGTLFTLQAAARQMIRQGHGGKIINMASQAGRRGEPLVAIYCATKAAVISLTQSAGLNLIKQGINVNAIAPGVVDGEHWDGVDALFAKHEGLAPGEKKQRVGAEVPFGRMGTAEDLTGMAIFLASKEADYVVAQTYNVDGGNWMN Pseudomonas simiae WCS417 WCS417 GFF2331 PS417_11885 Inositol transport system sugar-binding protein specific phenotype on inositol. SEED_correct rhizopine-binding protein MKTPIRFTALALSMLLASGVASAADLKIGVSMSAFDDTFLTYLREDMDKQAKSYPKGDGVQLQFEDARADVVKQLSQVENFISQKVDAIIVNPVDTASTANIIKAATAAKIPLVFVNRRPDSQTLAPGVAAVTSDDVEAGKLQMQYIAEKLGGKGNIVILLGDLANNSTTNRTKGVKEVLTKYPGIKIEQEQTGIWLRDRGMTLVNDWLTQGRDFQAVLSNNDEMAIGAAMALKSAGKKGVLIAGVDGTPDGLNAITKGDMTVSAFQDAKGQADKSVETARKMAKNEPIEQNVVIPFQLITPDNVKDFK Pseudomonas simiae WCS417 WCS417 GFF2332 PS417_11890 Inositol transport system ATP-binding protein specific phenotype on inositol. SEED_correct D-ribose transporter ATP-binding protein MLAQATVSQPPSLQPQTLEEPYLLEIVNISKGFPGVVALADVQLRVRPGTVLALMGENGAGKSTLMKIIAGIYQPDAGEIRLRGKPIVFETPLAAQKAGIAMIHQELNLMPHMSIAENIWIGREQLNSLHMVNHREMHRCTAELLARLRINLDPEEQVGNLSIAERQMVEIAKAVSYDSDILIMDEPTSAITEKEVAHLFSIIADLKSQGKGIVYITHKMNEVFAIADEVAVFRDGHYIGLQRADSMNSDSLISMMVGRELSQLFPLRETPIGDLLLTVRDLTLDGVFKDVSFDLHAGEILGIAGLMGSGRTNVAETIFGITPSSSGQITLDGKAVRISDPHMAIEKGFALLTEDRKLSGLFPCLSVLENMEMAVLPHYTGNGFIQQKALRALCEDMCKKLRVKTPSLEQCIDTLSGGNQQKALLARWLMTNPRLLILDEPTRGIDVGAKAEIYRLIAFLASEGMAVIMISSELPEVLGMSDRVMVMHEGELMGTLDRSEATQEKVMQLASGMTAVH Pseudomonas simiae WCS417 WCS417 GFF2333 PS417_11895 Inositol transport system permease protein specific phenotype on inositol. SEED_correct ABC transporter MNAITDNKPATVPTKSRRRLPTELSIFLVLIGIGLVFELFGWIVRDQSFLMNSQRLVLMILQVSIIGLLAIGVTQVIITTGIDLSSGSVLALSAMIAASLAQTSDFSRAVFPSLTDLPVWIPVAMGLGVGLLAGAINGSIIAVTGIPPFIATLGMMVSARGLARYYTEGQPVSMLSDSYTAIGHGAMPVIIFLVVAVIFHIALRYTKYGKYTYAIGGNMQAARTSGINVKRHLIIVYSIAGLLAGLAGVVASARAATGQAGMGMSYELDAIAAAVIGGTSLAGGVGRITGTVIGALILGVMASGFTFVGVDAYIQDIIKGLIIVVAVVIDQYRNKRKLKR Pseudomonas simiae WCS417 WCS417 GFF2378 PS417_12125 D-glucosaminate dehydratase (EC 4.3.1.9) Specifically important for: D-Glucosamine Hydrochloride. This enzyme had not previously been linked to a gene. This is the second step in catabolism of glucosamine, and the 'beta' form of the enzyme was expected to be PLP-dependent and about this size. Iwamoto et al (2003) purified a non-specific 'alpha' enzyme for this reaction (PMID: 12686150) amino acid deaminase MSAINAVEKGAAAVGAHLVRDVSLPALVLHRDALEHNIRWMQDFVSNSGAELAPHGKTSMMPALFQRQIEAGAWGITLANAVQTRAAYAGGVRRVLMANQLVGAPNMALIADLLADKDFDFHCMVDHPDNVADLGLFFAARGLRLNVMIEYGVVGGRCGCRTEQEVRDLARAIKAQPALALTGIEGYEGVIHGEHAISGIRDFAASLVRLAVDLQNNGSFDLPKPIVTASGSAWYDLIAESFEQQNAAGRFLSVLRPGSYVAHDHGIYKEAQCCVLDRRSDLNEGLRPALEVWAHVQSLPEPGFAVIALGKRDVAYDAGLPVPLKRYKAGILPAEGDDVTACKVTAVMDQHAFMTVAPGVELRIGDIISFGTSHPCLTFDKWQVGCLVDEQLQVIESLETRF Pseudomonas simiae WCS417 WCS417 GFF2712 PS417_13835 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) Specifically important for: L-Valine. KEGG no longer makes any prediction (see pfo:Pfl01_2864). 3-hydroxy-isobutanoyl-CoA is an intermediate in valine degradation. (SEED_correct) crotonase MTAQVSSEASHAETLQDEVLAEVRNHIGHLTLNRPAGLNAITLNMVRRLASQLKAWADDPQVYAVVLRGAGEKAFCAGGDIRSLYDSFKNGDTLHQDFFVEEYALDLAIHHYRKPVLALMDGFVLGGGMGLVQGADLRVVTERSRLAMPEVAIGYFPDVGGSYFLPRIPGELGIYLGVTGVQIRAADALYCGLADWYLESSKLADLDNKLDRLQWHDSPLKDLQGVLAKLAVQQLPDAPLAVLRPAIDHFFALPDVPSIVEQLQQVTVADSHEWALTTAHLMQTRSPLAMAVTLEMLRRGRRLPLEQCFALELHLDRQWFERGDLIEGVRALIIDKDKAPRWNPPTLHGLALSHVESFFHNFKKVAN Pseudomonas simiae WCS417 WCS417 GFF3392 PS417_17360 D-galacturonate dehydrogenase (EC 1.1.1.203) Specifically important for: D-Galacturonic Acid monohydrate. KEGG now annotates it as uronate dehydrogenase which is correct (although less specific) (KEGG_correct) NAD-dependent dehydratase MTTTPTTPVPFNRLLLTGAAGGLGKVLRERLRPYAQVLRLSDIANMAPAADASEEVQPCDLADKQAVHHLVEGVDAILHFGGVSVERSFEEVLGANISGIFHIYEAARRHGVKRVIFASSNHVIGFYKQGEKLDAHSPRRPDSYYGLSKSYGEDMASFYFDRYGIETVSIRIGSSFPEPQNRRMMHTWLSFDDLTQLLERALYTPNVGHTVVYGMSDNLDTWWDNRYAAHLGFAPKDSSEVFRAQVETQPPVSDNDPAKVYQGGAFCAAGPFGD Pseudomonas simiae WCS417 WCS417 GFF3404 PS417_17420 ethanol oxidation regulatory protein ercA Strongest phenotype is on ethanol. Similar to ercA (PA1991) which apparently has a regulatory role (PMCID: PMC3754586) rather than being directly involved in catabolism. Consistent with a regulatory role, this gene has pleiotropic phenotypes. The main ethanol dehydrogenase is probably PS417_17460. alcohol dehydrogenase MSPNLSLLRKFVSPEIIFGAGCRHNVGNYAKTFGARKVLVVSDPGVIAAGWVADVEASLQAIGIDYCLYSAVSPNPRVEEVMLGAEVYRENHCDVIVAIGGGSPMDCGKAIGIVVAHGRCILEFEGVDTIRVPSPPLILIPTTAGTSADVSQFVIISNQQERMKFSIVSKAVVPDVSLIDPETTASMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPGDIALREKIMLGSMQAGLAFSNAILGAVHAMSHSLGGFLDLPHGLCNAVLVEHVVAFNYNSAPERFKVIAETFGIDCRGLSHRQVCARLVEHLIALKHAIGFHETLGLHGVRVADIPFLSRHAMHDPCILTNPRESSQRDVEVVYGEAL Pseudomonas simiae WCS417 WCS417 GFF3461 PS417_17720 xylitol 2-dehydrogenase (EC 1.1.1.9) Specifically important for: Xylitol. This is the first step in xylitol degradation (SEED_correct) iditol 2-dehydrogenase MDKHTEMQAVVCHGPKDYRLERIGKPQARANELVIRIAACGICASDCKCHSGAAMFWGGDNPWVKAPVVPGHEFFGYVVEAGEGAEEHFEVAVGDKVIAEQIVPCGKCRFCKSGKYWMCEVHNIFGFQREVAEGGMAQYMRIPKTAIVHKIPESVSLEDSALVEPMACSIHTVNRGDIQLDDVVVIAGAGTLGLCMVQVAALKTPKKLVVIDMVDERLELAKKFGADVVINPSRDNAREIINGLTDNYGCDVYIETTGVPAGVTQGLDLIRKLGRFVEFSVFGAETSVDWSIIGDRKELDVRGAHLGPYCYPIAIDLFERGLVTSKGIVTHDFPLDDWAEAFELANSTKSIKVLLKPVV Pseudomonas simiae WCS417 WCS417 GFF4091 PS417_20960 Nitrate-binding regulatory protein (nasS) This protein is specifically important for the utilization of nitrate as a nitrogen source, but this may be a polar effect. It is74% identical to the nasS/PA1786 protein from P. aeruginosa (PMID:22493305) and to nasS from Azotobacter vinelandii (PMID:8748040), which binds nitrate and suppresses the activity of the transcriptional activator nasT. It is also more distantly related to the periplasmic substrate-binding components of nitrate ABC transporters (i.e., 37% identity to the N terminal part of ntrC/sll1452 and 36% identity to ntrA/sll1450), hence the misannotation as a transporter. nitrate transporter MNDSDGNSPMNDPLAWVNGSDAPEKSSLDLGFMALSDCASMVVAATQGFAQPYGLTLNLKRQTSWANLRDKLVSGELDAAHSLYGLIYAVHLGIGGVAPTDMAVLMGLNQNGQSINLSRGLQQQGVITPEALDRHVHQSRTKLTFAQTFPTGTHAMWLYYWLASQGIHPLQDVDSVVVPPPQMVAHLQAGRIDGFCVGEPWCASAVKQNQGFTLATTQAIWPDHPEKVLGCTQAFVDQYPNTARVLVMAILEASRFIEESSENRRSTAQLLSGREYLDAPLDCIEPRLLGTYDDGLGNHWQDPHALRFFADGEVNLPYLSDGMWFMTQFRRWGLLREDPDYLGVARQVQQLPLYRQAAAALGIATKHPDMRSSQLIDGKVWDGSDPADYARSFRLHALADTTHRQALR Pseudomonas simiae WCS417 WCS417 GFF4238 PS417_21710 Succinylornithine transaminase (EC 2.6.1.81) Specifically important for: L-Arginine. succinylornithine transaminase is involved in L-arginine degradation via N-succinylarginine. Also this gene is cofit with other putative steps in that pathway (N-succinylarginine dihydrolase, succinylglutamate-semialdehyde dehydrogenase, succinylglutamate desuccinylase). In contrast, neither of the functions proposed by KEGG have an obvious relationship to arginine catabolism. (SEED_correct) acetylornithine aminotransferase MSVEQAPVQRADFDQVMVPNYAPAAFIPVRGEGSRVWDQAGRELIDFAGGIAVNVLGHAHPALVGALTEQAHKLWHVSNVFTNEPALRLAHKLIDATFAERVFFCNSGAEANEAAFKLARRVAFDRFGSEKYEIIAALNSFHGRTLFTVNVGGQSKYSDGFGPKITGITHVPYNDLDALKAAVSDKTCAVVLEPIQGEGGVLPAELAYLQGARDLCDANNALLVFDEVQTGMGRSGHLFAYQHYGVTPDILTSAKSLGGGFPIAAMLTTEALAKHLVVGTHGTTYGGNPLACAVAEAVIDVINTPEVLAGVNAKHDLFKARLEQIGKQYGIFTEVRGMGLLLGCVLSDAFKGKAKDVFNAAEKENLMILQAGPDVVRFAPSLVVEDADIKEGLDRFERAVKALTQA Pseudomonas simiae WCS417 WCS417 GFF4243 PS417_21735 ABC transporter for L-Arginine, permease component 2 Specific phenotype on L-Arginine. This gene is listed because other components of the arginine transporter are misannotated. (SEED_correct) (KEGG_correct) amino acid ABC transporter permease MIFDYNVIWEAMPLYLGGLLTTLKLLAISLFFGLLAALPLGLMRVSKQPIVNGAAWLYTYVIRGTPMLVQLFLIYYGLAQFEAVRESFLWPLLSSATFCACLAFAINTSAYTAEIIAGSLKATPNGEIEAAKAMGMSRYKLYRRILLPSALRRALPQYSNEVIMMLQTTSLASIVTLIDITGAARTVNAQFYLPFEAYITAGVFYLCLTFILVRLFKLAERRWLSYLAPRKH Pseudomonas simiae WCS417 WCS417 GFF4244 PS417_21740 ABC transporter for L-Arginine, permease component 1 Specific phenotypes on L-Arginine; L-Arginine. KEGG annotation has been updated since the last public release (KEGG_correct) ABC transporter MLKGYGAVILDGAWLTLQLALSSMALAIVLGLIGVALRLSPVRWLAWLGDLYSTVIRGIPDLVLILLIFYGGQDLLNRVAPMLGYDDYIDLNPLAAGIGTLGFIFGAYLSETFRGAFMAIPKGQAEAGLAYGMSSFQVFFRVMVPQMIRLAIPGFTNNWLVLTKATALISVVGLQDMMFKAKQAADATREPFTFFLAVAAMYLVITSVSLLALRHLEKRYSVGVRAADL Pseudomonas simiae WCS417 WCS417 GFF4245 PS417_21745 ABC transporter for L-Arginine, substrate-binding component Specific phenotype on L-Arginine. The ATPase component of this system is not clear. PS417_21725 is nearby and similar to aotP, but has no phenotype on arginine. It might be redundant with another ATPase? (SEED_correct) (KEGG_correct) ABC transporter substrate-binding protein MKKLVLLGALALSVLSMQAFAEGKPLKIGIEAAYPPFASKAPDGSIVGFDYDIGNALCEEMKVKCTWVEQEFDGLIPALKVRKIDAILSSMSITDDRKKSVDFTNRYYLTPARLVLKEGTAVSDSLDELKGKKIGVQRGSIHDRFAKEVLAPKGATIVPYSSQNEIYLDVEAGRLDGTVADATLLQEGFLDTPAGKGYAFTGPAFTDAKYFGDGIGIAVRKGDKENLDRINAAIAAIRANGKYKEIEKKYFNFDIYGPEAQ Pseudomonas simiae WCS417 WCS417 GFF4500 PS417_23035 D-trehalose PTS system, I, HPr, and IIA components Specific phenotype for trehalose and no other trehalose transporter is apparent in the fitness data. The IIB and IIC components are provided by PS417_23050 PTS mannose transporter subunit IIC MTTTQPLELLAPLSGVLLALDKVPDPVFSSRLIGDGLCIDPTSQTLCAPLAGVISNIQDSGHAVSITDDNGVQVLMHIGLDTVNLAGQGFTRLVQEGQRVEAGQPLIEFDADYVALNARSLLTLMLVVSGEPFSLLADGLVETGQPLLQLSPSGAVEAVDEEEGDALFSKPLTLPNANGLHARPAAVFAQAAKGFNASIYLHKQTQSANAKSLVAIMALQTVQGDTLQVSAAGEDAEAAIKALVALLAEGCGEAVVNVAEPVATQSSATLLRGVCASPGSAFGQVVQVTDPELVITEQGTGGATERAALTRGLLAANEALQVLQDKAAGSAQAEIFRAHQELLEDPTLLEHAHRLLGEGKSAAFAWNSATLATVTLFQGLGNALIAERAADLADVGQRVLKLILGIQDSAWDLPERAILIAEQLTPSQTASLDTRKVLGFVTVAGGATSHVAILARALGLPAICGVPAQVLALANGKQVLLDADKGELHLEPNLAEIEQLEAARKHQVLRHQRDVAQASLPATTRDGHHVEVTANVASLQEVEHALTLGGEGVGLLRSEFLYLDRNRAPSPEEQAGTYTAIARALGTERNLVVRTLDVGGDKPLAYVPMDAETNPFLGLRGIRLCLERPQLLREQFRAILASAGFARLHIMLPMVSLLSELHLARKILEEEALALGLTELPKLGIMIEVPSAALMADVFAPHVDFFSIGTNDLTQYTLAMDRDHPRLANQADSFHPAVLRLIATTVKAAHAHGKWVGVCGALASEALAVPVLIGLGVDELSVSVPLIPTIKATVRELDLADCQIIARQVLGLEEAAEVREALRQYHAATVESSPVVEH Pseudomonas simiae WCS417 WCS417 GFF4501 PS417_23040 D-trehalose outer membrane porin Specific phenotype for trehalose (and conserved) maltoporin MKTTIKLGLVASCLGLPFGAQALEFAGYLRSGAGTSTGSGPQQCFQLPGAQTKYRLGNECEQYAELELRQDLLTLDDGSVLSVDAMASLYNKYDRALKFQGENNGSARMPQMYAQWSNLPSLNGGSLWAGRRYYKRNDIHISDFYYWNQSATGGGIEDVLIGDLKYSYAISRKDNLYQKEYATRHDFNVAGFKTNPGGELELGLSYIEKAGGRDTNSGWALTAQHVQKPFLGGKNKFALQYGEGPGTGLGYTGNTFLDKSSKSYRAVEFFDWQVTPRFGGQIEAVYQKDIRPGSQDQTWMSLGVRPAYAISEQFKLVTELGHDQVDATGGTRKLSKFTFAPTWSPKGPEFWARPEVRLYYTYATWNKAAKRAANELAAGSALSDTGSYGTARHGSNVGVQVEYWWK Pseudomonas simiae WCS417 WCS417 GFF4629 PS417_23685 anthranilate 1,2-dioxygenase (deaminating, decarboxylating) large subunit [EC: 1.14.12.1] Specifically important for: L-Tryptophan. anthranilate is an intermediate in the breakdown of tryptophan (via kynurenine) (KEGG_correct) anthranilate 1,2-dioxygenase MSGARSVEQWKTFIEGCLDFRPADEVFRIARDMFTEPQLFDLEMELIFEKNWIYACHESELANNHDFVTMRAGRQPMIITRDGEGQLNALINACQHRGTTLTRVGKGNQSTFTCPFHAWCYKSDGRLVKVKAPGEYPDGFDKATRGLKKARIESYKGFVFISLDVAGTDSLEDFLGDAKVFFDMMVAQSATGELEVLPGKSAYTYDGNWKLQNENGLDGYHVSTVHYNYVATVQHRQQVNTENGAGAGSTLDYSKLGAGDANTDDGWFAFNNGHSVLFSDMPNPSVRSGYATIMPRLVEEHGQQKAEWMMHRLRNLNIYPSLFFLDQISSQLRIIRPVAWNKTEIISQCLGVKGESDADRENRIRQFEDFFNVSGMGTPDDLVEFREAQRGFQGRLERWSDISRGSHRWETGPTPNSEAIGIQPAMTGTEFTHEGLYVNQHRNWQQFLLNGLDRQALTLREVK Pseudomonas simiae WCS417 WCS417 GFF4712 PS417_24105 D-lactate transporter (lctP family) specific phenotype for D-lactate and no other transporter for D-lactate was apparent in the fitness data. Also important for utilization of D,L-lactate. Not clear if it transports L-lactate as well or not, but since it is in an apparent operon with a D-lactate dehydrogenase (PS417_24110), its main role is probably for transport of D-lactate. L-lactate permease MQTWQQLYSPLGSLGLSAMAAVIPIVFFFLALAVFRLKGHVAGSITLALSILVAIFAFQMPVDMALAAAGYGFAYGLWPIAWIIVAAVFLYKLTVKSGQFEIIRSSVLSITDDQRLQVLLIGFCFGAFLEGAAGFGAPVAITAALLVGLGFNPLYAAGLCLIANTAPVAFGALGIPIIVAGQVTGIDAFKIGAMTGRQLPLLSLFVPFWLVFMMDGVRGVRETWPAALVAGLSFAITQYFTSNFIGPELPDITSALASLISLTLFLKVWQPKRTAGAQIAGATSSAAVTASAGGFGLPRNTIVSPYSLGQIFKAWSPFLILTVLVTIWTLKPFKAMFAAGGSMYSWVFNFAIPHLDQLVIKVAPIVTNPTAIPAVFKLDPISATGTAIFFSALISMLVLKIDIKTGLTTLKETFYELRWPILSIGMVLAFAFVTNYSGMSSTMALVLAGTGAAFPFFSPFLGWLGVFLTGSDTSSNALFSSLQATTAHQIGVNDTLLVAANTSGGVTGKMISPQSIAVACAATGLVGKESDLFRFTLKHSLFFATIVGLITLAQAYWFTGMLVH Pseudomonas simiae WCS417 WCS417 GFF5067 PS417_25960 Acyl-CoA dehydrogenase (EC 1.3.8.7) Specifically important for: Sodium octanoate. presumably part of beta oxidation, but not sure why 2 different ones are required (could relate to different chain lengths) (SEED_correct) acyl-CoA dehydrogenase MADYKAPLRDMRFVLNEVFEVATTWAQLPALADTVDAETVEAILEEAGKVTAKSIAPLSRGGDEQGCRWDNTAVFTPDGFPQAYATYAQGGWVGVGGDPIFGGMGMPKAVSAQVEEMINSSSLAFGLYPMLTSGACVSINTHASEALKATYLPKMYSGEWSGSMCLTEAHAGTDLGIIRTKAEPQADGSYKVSGTKIFITGGEHDLTDNIIHLVLAKLPDAPAGPKGISLFLVPKFMVNADGSLGARNTVSCGSIEHKMGIQASATCVMNFDEAVGYLVGEPNRGLAAMFTMMNYERLGVGIQGLASGERSYQNAIEYARDRLQSRAPTGAQAQDKMADPIIVHPDVRRMLLTMKAANEGGRAFSTYVATQLDIAKFSDDAAARERADNLVALLTPVAKAFLSDLGLETTVLGQQVFGGHGYIREWGQEQLVRDVRITQIYEGTNGIQALDLMGRKIVGSGGAFYTLFADEIRGFIASSGTELAEFTKPLSAAVDNLDELTAWVLDRAKTNPNEIGAASVEYLHAFGYMAYAYMWARMAKAALGKESEEDFYASKLGTARFYFARLLPRIHSLSASVKAGSESLFLLDEALF Pseudomonas simiae WCS417 WCS417 GFF5070 PS417_25975 Acyl-CoA dehydrogenase (EC 1.3.8.7) Specifically important for: Sodium octanoate. presumably part of beta oxidation, but not sure why 2 different ones are required (could relate to different chain lengths) (SEED_correct) acyl-CoA dehydrogenase MPDYKAPLRDIRFVRDELLGYEAHYQSLPACQDATPDMVDAILEEGAKFCEQVLAPLNRVGDIEGCTWSESGVKTPTGFKEAYKQFVEGGWPSLAHDVEHGGQGLPESLGLAVSEMVGEANWSWGMYPGLSHGAMNTISEHGTPEQQEAYLTKLVSGEWTGTMCLTEPHCGTDLGMLRTKAEPQADGTYKVSGTKIFISAGEHDMADNIVHIVLARLPDAPAGTKGISLFIVPKFLPNADGSIGARNAVTCGSLEHKMGIHGNATCVMNFDAATGFLIGPANKGLNCMFTFMNTARLGTALQGLAHAEIGFQGGLKYARDRLQMRSLTGPKAPDKAADPIIVHPDVRRMLLTMKAFAEGNRAMVYFTAKQVDIVKYGTDDEAKKQADGLLAFMTPIAKAFMTEVGFESANHGVQIYGGHGFIAEWGMEQNVRDSRISMLYEGTTGIQALDLLGRKVLMTQGEALKGFTKIVHKFCQANEGNEAVKEFVAPLAALNKEWGELTMKVGMAAMKDREEVGAASVDYLMYSGYACLAYFWADMARLAAEKLAAGTTEEAFYTAKLQTARFYFQRILPRTRTHVATMLSGANNLMDMKEEDFGLAY Pseudomonas simiae WCS417 WCS417 GFF5299 PS417_27130 Gamma-aminobutyrate:alpha-ketoglutarate aminotransferase (EC 2.6.1.19) Specifically important for: Putrescine Dihydrochloride. KEGG annotates this as putrescine aminotransferase, probably based on similarity to spuC (PA0299) of P. aeruginosa, but it is believed that only the g-glutamyl- pathway operates in P. aeruginosa (X. Yao et al 2011, PMC3147493) aminotransferase MSSNNPQTREWQALSSDHHLAPFSDFKQLKEKGPRIITKAHGVYLWDSEGNKILDGMAGLWCVAIGYGRDELADAAAKQMKELPYYNLFFQTAHPPVLELAKAISDIAPAGMNHVFFTGSGSEGNDTMLRMVRHYWAIKGQPNKKTIISRKNGYHGSTVAGASLGGMTYMHEQGDLPIPGITHIAQPYWFGEGGDMSPEEFGVWAANQLEEKILELGVDNVGAFIAEPIQGAGGVIVPPATYWPRIKEILAKYDILFIADEVICGFGRTGEWFGSDFYDLKPHMMTIAKGLTSGYIPMGGLIVRDEVVEVLNEGGDFNHGFTYSGHPVAAAVALENIRIMRDEKIVNRVHDETAPYLQKRLRELADHPLVGEVRGVGMLGAIELVQDKATRKRYEGKGVGMICRTFCFENGLIMRAVGDTMIISPPLVISKAEIDELVTKARQCLDLTLAALQG Pseudomonas simiae WCS417 WCS417 GFF5301 PS417_27140 Gamma-glutamyl-putrescine synthetase (EC 6.3.1.11) Specifically important for: Putrescine Dihydrochloride; L-Arginine. The first step in the gamma-glutamyl-putrescine pathway gamma-glutamylputrescine synthetase MSVPPRAVQLNEANAFLKDHPEVLYVDLLIADMNGVVRGKRIERTSLHKVYEKGINLPASLFALDINGSTVESTGLGLDIGDADRICYPIPDTLCNEPWQKRPTAQLLMTMHELEGEPFFADPREVLRQVVSKFDDLGLTICAAFELEFYLIDQENVNGRPQPPRSPISGKRPHSTQVYLIDDLDEYVDCLQDILEGAKEQGIPADAIVKESAPAQFEVNLHHVADPIKACDYAVLLKRLIKNIAYDHEMDTTFMAKPYPGQAGNGLHVHISILDKDGKNIFASEDPEQNAALRHAIGGVLETLPAQMAFLCPNVNSYRRFGAQFYVPNSPCWGLDNRTVAIRVPTGSSDAVRIEHRVAGADANPYLLMASVLAGVHHGLTNKIEPNAPVEGNSYEQNEQSLPNNLRDALRELDDSEVMAKYIDPKYIDIFVACKESELEEFEHSISDLEYNWYLHTV Pseudomonas simiae WCS417 WCS417 GFF5490 PS417_28100 glucose-6-phosphate 1-epimerase [EC: 5.1.3.15] Specifically important for: D-Trehalose dihydrate; N-Acetyl-D-Glucosamine. NAG is phosphorylated by a PTS system, deacetylated (PS417_22985), and converted to fructose-6-phosphate by an aminotranferase (PS417_22990). One might expect the fructose-6-P to be converted to fructose-1,6-bisphosphate, but no gene for that is apparent in this organism or many other Pseudomonas (nor did the fitness data highlight any kinase). Instead, the fructose-6-phosphate is apparently converted to glucose-6-phosphate by the glucose-6-phosphate isomerase (PS417_23920) and oxidized by G6P dehydrogenase (PS417_22110). (Both of these genes are essential so we cannot confirm this.) G6P dehydrogenase is reportedly specific for the beta form, while G6P isomerase produces the alpha form of G6P, so it makes sense for a glucose-6-P epimerase to be involved (even though the reaction can occur spontaneously). This gene is also mildly important for trehalose utilization, which involves the hydrolysis of trehalose 6-phosphate to glucose-6-phosphate. Because trehalose has an alpha 1->1 linkage, the product is probably alpha-G6P. Thus, this gene's phenotypes are consistent with KEGG's annotation as glucose-6-phosphate 1-epimerase. (KEGG_correct) aldose epimerase MPTPHVETVKIDELDCWRIRHNGAELIVAQQGAHLFSYGRDGEQPLIWPNPEAVFKKGKGIRTGVPVCWPWFGVFDRNPQSVKAMRQSEQPAGAHGFVRTALWELAATELEGEALRVDLVLPVPAGGFPGWPHQVDLTLSLLLDEQLHIRLTSHNRGTDTVTLSQALHTYFAVSDVRNAQVEGLDGRAYIDTADGWTEKTQSGLLHFTAETDRIYLDTPSQLTIVDKDWQRRIQLTSEGSKSTVIWNPWTERAKAFDDMADDGWTGMLCIETANVLDDVVSLAPGESHTLGVSIAAIAL Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_603 L-2-keto-3-deoxyarabonate dehydratase (EC 4.2.1.43) Specifically important for L-arabinose utilization and 80% similar to araD from A. brasilense (KDADA_AZOBR, PMID:16950779). This gene is also important for D-galactose utilization, which might be due to polar effects. SEED_correct L-2-keto-3-deoxyarabonate dehydratase (EC 4.2.1.43) VPTTFHEDGTLDLDSQKRCLDFMIDAGVDGVCILANFSEQFSLSDAEREVLTRTSLEHVAGRVPVIVTTTHYGTRVCAERSRAAQDMGAAMVMVMPPYHGATFRVPEAQIYEFYARVSDAIRIPIMVQDAPASGTVLSAPFLARMAQEIENLAYFKIEVPGAASKLRELIRLGGDAIEGPWDGEEAITLLADLDAGATGAMTGGAFPDGIRPIIEAHRQGDMDQAFALYQRWLPLINHENRQGGILTAKALMKEGGVIACEAGRHPFPAMHPEVRRGLVDIARRLDPLVLRWAR Burkholderia phytofirmans PsJN BFirm BPHYT_RS22715 BPHYT_RS22715 L-2-keto-3-deoxyarabonate dehydratase (EC 4.2.1.43) important for L-arabinose utilization and 70% similar to araD from A. brasilense (KDADA_AZOBR, PMID:16950779). SEED_correct cytochrome C biogenesis protein CcdA MTQSSHPAAMRGVFPVAPTIFDDAGRLDLEGQKRCIDFMIDAGSNGLCILANFSEQFALSDDERNTLMHVVLEHVAGRVPVIVTTTHFSSYQCAERSRSAQAAGAAMVMVMPPYHGATIRIGERGIYEFYRTVSDAIGIPIMIQDAPVSGTPLSAPFLARMAREIDNVSYFKIEVPQAANKLRELIELGGDAIVGPWDGEEAITLMADLDAGATGSMTGGGYADGIRLIVDAYAAGDTEAAAAHYQQWLPLINYENRQGGLASCKALMKEGGVIRSDAVRHPLPQMHPATREGLLKVARRLDPLVLRWGR Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_4623 2-dehydro-3-deoxy-L-arabinonate dehydratase (EC 4.2.1.43) # Specifically important in carbon source L-Arabinose. Similar to PA2216 from Pseudomonas aeruginosa (see PMC:PMC4038344) and to gguC or araD1 (Atu2345) from Agrobacterium tumefaciens (see PMC: PMC3232879), which also have this activity. In Agrobacterium, this reaction is proposed to be a step in L-arabinose oxidation. (Note that 2-keto-3-deoxy-L-lyxonate and 2-keto-3-deoxy-L-arabinonate are the same compound.) SUGAR TRANSPORTER MRLVQFELSHGERRVGVVEDGLVREVRDARSVRDLALAAIEAGVNLEQQVQTLGLGISHDYSALLANLQILPPLDHPDPAHMLVSGTGLTHLGSASARDKMHQQAGDETAMTDTMRIFKWGVEGGKPATGQVGVQPEWFYKGDGSIVVRPGKPFPLPPFAEDAGEEPELSGLYVIGHDGKPYRLGFAVGNEFSDHVMERKNYLYLAHSKLRSCSYGPELRVGELPQHLAGTSRILRDGEVLWQNEFLSGEANMCHSLENLEYHHFKYSQFLRPGDVHIHFFGTATLSFADGIRTQPGDVFEISQAEFGAPLINGIEPVEAAFEPGTVGTL Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_611 2-dehydro-3-deoxy-L-arabinonate dehydratase (EC 4.2.1.43) # Specifically important in carbon source L-Arabinose. Similar to PA2216 from Pseudomonas aeruginosa (see PMC:PMC4038344) and to gguC or araD1 (Atu2345) from Agrobacterium tumefaciens (see PMC: PMC3232879), which also have this activity. In Agrobacterium, this reaction is proposed to be a step in L-arabinose oxidation. (Note that 2-keto-3-deoxy-L-lyxonate and 2-keto-3-deoxy-L-arabinonate are the same compound.) SUGAR TRANSPORTER MRLVQFELPNGERRVGVVDGDQVREVQGAASVRDLALAAIEAGVKLEEQVNSLGLGAGHDYARLLSELRILPPLDHPDPAHLLVSGTGLTHLGSASARDKMHQQAGDESAMTDTMRIFKWGVEGGKPQAGQAGVQPEWFYKGDGSIVVRPGHPFPLPPFAEDAGEEPEISGLYVIGHDGKPYRLGFAVGNEFSDHVMERKNYLYLAHSKLRSCSFGPELRVGELPQHLSGTSRILRNGEVLWQNEFLSGEANMCHSLENLEFHHFKYSQFLRPGDVHVHFFGTATLSFADGIRTQPGDVFEISQAEFGAPLVNGIAPVDAVFNPGTIGTL Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_24595 AO356_24595 2-dehydro-3-deoxy-L-arabinonate dehydratase (EC 4.2.1.43) # Specifically important in carbon source L-Arabinose. Similar to PA2216 from Pseudomonas aeruginosa (see PMC:PMC4038344) and to gguC or araD1 (Atu2345) from Agrobacterium tumefaciens (see PMC: PMC3232879), which also have this activity. In Agrobacterium, this reaction is proposed to be a step in L-arabinose oxidation. (Note that 2-keto-3-deoxy-L-lyxonate and 2-keto-3-deoxy-L-arabinonate are the same compound.) FAH family protein MRLVQFELSNGERRVGVVDGDQVREVQGAGSVRELALAAIEAGVKLEQQVDSLGLGTGHDYARLLGELRILPPLDHPDPAHLLVSGTGLTHLGSASARDKMHQQAGDEATMTDTMRIFKWGVEGGKPQAGQTGVQPEWFYKGDGSIVVRPGHPFPLPPFAEDAGEEPEISGLYVIGHDGKPYRLGFAVGNEFSDHVMERKNYLYLAHSKLRSCSFGPELRVGELPQHLSGTSRILRNGEVLWQNEFLSGEANMCHSLENLEFHHFKYSQFLRPGDVHVHFFGTATLSFADGIRTQPGDVFEISQAEFGAPLVNGIAPVDAVFNPGTIGTL Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_3317 2-dehydro-3-deoxy-L-arabinonate dehydratase (EC 4.2.1.43) # Specifically important in carbon source L-Arabinose. Similar to PA2216 from Pseudomonas aeruginosa (see PMC:PMC4038344) and to gguC or araD1 (Atu2345) from Agrobacterium tumefaciens (see PMC: PMC3232879), which also have this activity. In Agrobacterium, this reaction is proposed to be a step in L-arabinose oxidation. (Note that 2-keto-3-deoxy-L-lyxonate and 2-keto-3-deoxy-L-arabinonate are the same compound.) SUGAR TRANSPORTER MRLVQFELSNGERRVGVVEAGLVREVQDTRTVRDLALAAIEASASLEQQVQSLGLGISHDYAELLTQRRILPPLDHADPAHMLVSGTGLTHLGSASARDKMHQQSGDETAMTDTMRIFKWGVEGGKPAVDEAGVQPEWFYKGDGGIVVRPGQPFPLPPFAEDAGEEPEIAGLYVIGHDGKPYRLGFAVGNEFSDHVMERKNYLYLAHSKLRSCSYGPELRVGELPQHLAGTSRILRDGEVLWQNEFLSGEANMCHSLANLEFHHFKYSQFLRPGDVHIHFFGTATLSFADGIRTQPGDVFEITQAEFGAPLINGIAPVAAAFEPGTVGTL Sinorhizobium meliloti 1021 Smeli SM_b20892 SM_b20892 2-dehydro-3-deoxy-L-arabinonate dehydratase (EC 4.2.1.43) # Specifically important in carbon source L-Arabinose. Similar to PA2216 from Pseudomonas aeruginosa (see PMC:PMC4038344) and to gguC or araD1 (Atu2345) from Agrobacterium tumefaciens (see PMC: PMC3232879), which also have this activity. In Agrobacterium, this reaction is proposed to be a step in L-arabinose oxidation. (Note that 2-keto-3-deoxy-L-lyxonate and 2-keto-3-deoxy-L-arabinonate are the same compound.) hypothetical protein MLISQVRKEDGSVIVAVRAPGETARAVRGAESVYALAMEAANSRRSLRDVVDAKGFGETIDLEEAYSQGRLLSPITHPDPAHLHLTGTGLTHLGSAATRDAMHKKATEATEETLTDSMKMFRMGLEGGKPKSGEKGVQPEWFYKGNGTTAVAPGEPLVSPSFAEDGGEEPEMAGIYVISDKGVPFRLGFAVANEFSDHKTERVNYLWLAHSKLRQASFGPEIRIGAAPEDIRGASRILRGGKVLWEKPFLSGEANMSHSFANLEYHHFKYGLFRAPGDIHVHMFGTATLSFGDGIRTEEGDVFEIEAKEFGLPLRNPLAIAAEEEVAVHQL Sinorhizobium meliloti 1021 Smeli SMc02775 SMc02775 D-arabinose 1-dehydrogenase # Specifically important in carbon source D-Arabinose. This is the first step in the oxidation of D-arabinose. (The fucose dehydrogenase is SM_b21109.) The product is probably the 1,5-lactone, not the 1,4-lactone, see SM_b21101. L-fucose dehydrogenase (D-threo aldose 1-dehydrogenase) protein MQTRRIGRTALAVTEYSFGTAGLGGLYRECTREAAMATLDAAWEAGIRYFDTAPFYGLGLAERRVGDFLRDKPRDSFVLSTKVGRLLHPVPENQVPDYSYVKPLNFDVTYDYGYDAIMRSVEMSYARLGLNRIDILYVHDIGGYTHGAAKNAVYLRQLLDSGLKALDELKSSGVISAYGLGVNEVPVCLDVMRQADIDCILLAGRYTLLDRSAVAELLPLCAKKDTSLVVGGVFNSGILATGPVEGAHFDYMPATGEVRAKVAAMERIAGERGMPLAAPALQFPLANPHVASVLLGTAKPSSLTRNMELTRYGIAPEDYAAFEPHTLVAPELGPEAVRA Sinorhizobium meliloti 1021 Smeli SM_b21101 SM_b21101 L-fucono-1,5-lactonase; D-arabinolactonase # Specifically important in carbon source D-Arabinose; carbon source L-Fucose. A related protein (29% identical) was shown by Hobbs et al (2013) to be a L-fucono-1,5-lactonase. Note that D-arabinolactone is chemically similar to L-fuconolactone, with one methyl group replaced with a hydrogen. hypothetical protein MIIDTHLHLIDKSALNYPWLAGVPALDRDFLYATYAAEAKRVGVAASLHMEVDVDPAEIELETREVARLAGEPGSLLKGAIAACRPEDEGFAAYLERQEENAFVKGFRRVLHVVTDDLSEQPLFRENVKRLSGTRFTFDLCVLPHQIPKAIALADLAPDVQFILDHCGVPDIKGHAEHPWRDHMTEIARHPNVVAKISGVVAYAEEDWALDSIRPYVEHTISVFGWDRVVWGSDWPVCTLGGNLSTWVAATQALIEGCSPQERRKLLSGNAQRIWNLI Sinorhizobium meliloti 1021 Smeli SMc02776 SMc02776 D-arabinoate dehydratase (EC 4.2.1.5); also involved in L-fucose catabolism # Specifically important in carbon source D-Arabinose; carbon source L-Fucose. SMc02776 is 36% identical to D-galactarate dehydratase (garD) from E. coli, which is a similar reaction. The product (2-dehydro-3-deoxy-D-arabinonate) is consumed by SMa0247. The role of SMc02776 role in L-fucose catabolism is unclear because two other dehydratases (SM_b21107 and SM_b21110) are also required but the pathway requires only one dehydratase reaction (PMID:17144652). Probably two of these dehydratases act together (with one of them in reverse) to switch the stereochemistry of a chiral center. altronate hydrolase MPAPSSILLSPDDNVVVATAAIAPGDRLAGGVSAVARIEPGHKAAIRRIDVGEPVVKYGQAIGRATSPIAPGEHVHSHNLAFDQGRLAVGAAVPPEAASEADKARTFLGYRRADGRAATRNYIGIVASVNCSTTVCRAIADEANRRILPKYEGIDGFVPIVHDQGCGMSSTGDGMKNLHRTLAGYARHANFGGVLMVGLGCEVNQLTLYGQSGAGAEKRHFNIQEAGGSRRSVERALGILDEIAKEVAAARRVPIPVSEIIVGLQCGGSDGLSGITANPALGAAVDILAAAGGTAILSETSEIYGAEHLLRSRAVNETVAVKLDGLIAWWEDYVAMHGASLDNNPSPGNKRGGLTTILEKSLGAVAKGGRSPLTAVYNYAERVTEPGLVFMDTPGYDPVSATGQVAGGANVIAFTTGRGSCFGCRPAPSIKLTSNTALYRAMEEDMDIDCGVIASGETTIADLGRGIFELIIETASGRKTKSELFGYGDNEFVPWHLGATL Sinorhizobium meliloti 1021 Smeli SMa0247 SMa0247 2-dehydro-3-deoxy-D-arabinonate dehydratase, 2,4-dioxopentanoate forming # Specifically important in carbon source D-Arabinose. SMa0247 is related to 2-keto-3-deoxyxylonate dehydratase (xylX), which acts on the same substrate. Furthermore, a close homolog (HSERO_RS19360, 59% identical) is important for D-xylose utilization. However, the product of XylX is 2,5-dioxopentanoate, but in S. meliloti the pathway probably proceeds via 2,4-dioxopentanoate (see SM_b21112). hypothetical protein MSGGFLVSFEQALSAESIQPADASSAMLVGRVWSKTAGGPCPVLISEGEVFDLTPLAATISALLEIDGLVDALRDPSRFASLGSLDAFLRGEAGDLLAPADLQAVKAAGVTFADSMLERVIEEQAKGDPLRAQEIRGRLAPVLGDNLKGLVAGSDKAAEVKKLLQELGLWSQYLEVGIGPDAEIFTKAQPMSSVGCGAYIGIHPKSDWNNPEPEVVLAVTSKGKIVGATLGNDVNLRDFEGRSALLLSKAKDNNASCSIGPFIRLFDGAFTIEDVKQAEVSLVVDGKEGFKMTGISPMSAISRSPEDLVSQLLNDNHQYPDGVVFFLGTMFAPVKDRRGTGLGFTHEIGDRVEISTPRLGRLVNWVDHSDRCPKWSFGLGALMKNLAERGLLQAKREG Sinorhizobium meliloti 1021 Smeli SM_b21112 SM_b21112 L-2,4-diketo-3-deoxyrhamnonate hydrolase; 2,4-dioxopentanoate hydrolase # Specifically important in carbon source L-Fucose; carbon source D-Arabinose. SM_b21112 is 58% identical to LRA6, which is L-2,4-diketo-3-deoxyrhamnonate hydrolase (PMID:19187228). This reaction is also proposed to be involved in L-fucose catabolism (PMID:17144652), which explains the phenotype on L-fucose. Its role in D-arabinose catabolism suggests that it also acts on a five-carbon substrate such as 2,4-dioxopentanoate. This protein belongs to the fumarylacetoacetate hydrolase family, which hydrolyses substrates of the form R-CO-CH2-CO-R'. Both keto groups are involved in the catalytic mechanism (Bateman et al 2001) so we propose that 2,4-dioxopentanoate is the intermediate in D-arabinose catabolism. This would be formed from D-arabinoate by two successive dehydratase reactions (see SMa0247 and SM_b21112). bifunctional 2-hydroxyhepta-2,4-diene-1, 7-dioatesomerase/5-carboxymethyl-2-oxo-hex-3-ene-1, 7-dioatedecarboxylase MKLLRYGEPGQEKPGLLGSDGIIRDLSGHVSDLAAGALDPSKLDELANLDVETLPAVSGNPRLGPCVAGTGKFICIGLNYSDHAAETGATVPPEPIIFMKATSAIVGPNDDLVLPRGSEKTDWEVELGIVIGKTAKYVSEAEALDYVAGYCTVHDVSERAFQTERHGQWTKGKSCDTFGPTGPWLVTKDEVADPQDLAMWLKVNGETMQDGSTKTMVYGAAHLVSYLSQFMSLRPGDIISTGTPPGVGMGMKPPRYLKAGDVVELGIEGLGSQKQRVRADA Sinorhizobium meliloti 1021 Smeli SM_b21107 SM_b21107 dehydratase involved in L-fucose catabolism # Specifically important in carbon source L-Fucose. T. Lukk's 2009 thesis reported that this protein had weak activity as a L-fuconate dehydratase, which was the expected substrate. The fitness data shows that two other dehydratases are involved in fucose catabolism as well (see SMc02776 and SM_b21110), so the pathway is probably more complicated. mandelate racemase or evolutionary related enzyme of the mandelate racemase muconate lactonizing enzyme family protein MARIEKTELRMVDLPPKNKRTDAIQSFVSQETPIVTITDADGATGTGYSYTIGTGGSSVMRLLSDHLVPILLGEDADCIEALWQKMEFATHATTIGAITALALAAVDTALWDLRAKKQKLPLWKLAGGAKESCPLYTTEGGWLHIEKQALVDDALQAKANGFSGSKVKIGKPSGAEDYDRLSAMRAALGDGFEIMTDCNQGFTVDEAIRRAARLRELDLAWIEEPLPADDLDGHIRLTRSTPTPIAVGESIYSIRHFREYMQKGACSIVQVDVARIGGITPWLKVAHAAEAFDIPVCPHFLMELHVSLVCAVPNGKYVEYIPQLDDLTQMGMEIREGRAIAPSNPGIGIAWDWEAVKARSVAEFTREFRR Sinorhizobium meliloti 1021 Smeli SM_b21110 SM_b21110 dehydratase involved in L-fucose catabolism # Specifically important in carbon source L-Fucose. This protein is similar to the (R)-enoyl-CoA hydratase portion of E. coli maoC (36% identical). It is one of three dehydratases involved in L-fucose catabolism (see SMc02776 and SM_b21107) MaoC-like (monoamine oxidase-like) protein, NodN MSEQTIYYEDYEQGHVRLTSGRTITETDFVVHAGHTGDFFPHHMDAEFAKTLPGGQRIAHGTMIFSIGVGLTASLINPVAFSYGYDRLRFVRPVHIGDTIRTRVTIAAKEDDPKRPGAGRVVERCEVINQRGEVVLAADHILIVERKPEGTIQ Burkholderia phytofirmans PsJN BFirm BPHYT_RS16920 BPHYT_RS16920 L-arabinose 1-dehydrogenase; D-galactose 1-dehydrogenase (EC 1.1.1.46; EC 1.1.1.48) # Specifically important in carbon source L-Arabinose; carbon source D-Galactose. Some other dehydrogenases are known to act on both of these substrates. 3-oxoacyl-ACP reductase MSSPANANVRLADSAFARYPSLVDRTVLITGGATGIGASFVEHFAAQGARVAFFDIDASAGEALADELGDSKHKPLFLSCDLTDIDALQKAIADVKAALGPIQVLVNNAANDKRHTIGEVTRESFDAGIAVNIRHQFFAAQAVMEDMKAANSGSIINLGSISWMLKNGGYPVYVMSKSAVQGLTRGLARDLGHFNIRVNTLVPGWVMTEKQKRLWLDDAGRRSIKEGQCIDAELEPADLARMALFLAADDSRMITAQDIVVDGGWA Pseudomonas simiae WCS417 WCS417 GFF3393 PS417_17365 galactaro-1,5-lactonase # Specifically important in carbon source D-Galacturonic Acid monohydrate. This is the second step after D-galacturonate dehydrogenase (PS417_17360) and forms meso-galactarate, which is the substrate of PS417_04210. The substrate is probably the 1,5-lactone, not the 1,4-lactone, given the characterization of the D-galacturonate dehydrogenase from Agrobacterium tumefaciens (PMID:24450804), which is 51% identical to PS417_17360. gluconolactonase MNAELIVDARNAVGECPVWVPGENALYWVDIPKGGLQRWSAATGHVAAWTAPQMLACIARTDAGNWVAGMETGFFQLTPHNDGSLDTTLLAAVEHPRQDMRLNDGRCDRQGRFWAGSMVLNMGLNAAEGTLYRYTSGAAPHAQLDGFITLNGLAFSPDGRTMYASDSHPLVQQIWAFDYDIDTGTPSNRRVFVDMHKHLGRPDGAAVDADGCYWICANDAGLIHRFSPDGRLDRSLTVPVKKPTMCAFGGSRLDTLFVTSIRDDQSEQSLSGGVFALNPGVVGLPEPTFTL Caulobacter crescentus NA1000 Caulo CCNA_02122 CCNA_02122 DNA repair nuclease, ligase-associated (TIGR04123) # Very important for resisting cisplatin. This family was previously annotated as a DNA ligase-associated metallophosphoesterase (TIGR04123). A member of this family (PdeM) has been studied biochemically and found to have nuclease activity, but it was not known if DNA was the physiological substrate (see PMC4320098). DNA ligase-associated metallophosphoesterase MTRFQSSPCGGLRVALANVEVMLRWSGALWLERERTLIVADLHFEKGSSYAARFGQMLPPYDTRETLDRLDREITQLAPRRLIFLGDSFHDAAGEARLASDDYRRLEGLASGRELVWAVGNHDADGPRALPGDVIDEASLAGLTLRHEPLPGAQPGEVAGHLHPAAKVSSGRATVRRRCFVTDGARLVLPAFGAYAGGLNILDEAFSGLFDGPVLAGALGPQRVHAVGLKSLRPD Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS09085 CA265_RS09085 DNA repair nuclease, ligase-associated (TIGR04123) # Specifically important in stress Cisplatin. This family was previously annotated as a DNA ligase-associated metallophosphoesterase (TIGR04123). A member of this family (PdeM) has been studied biochemically and found to have nuclease activity, but it was not known if DNA was the physiological substrate (see PMC4320098). phosphoesterase MTITSQGEELILDKERALFLPKHQLLAISDLHLGKTAHFRQAGLQVPATLAQTDLQRLSLLIKQYHPKTLLINGDMFHHGLNTDIDEFSAWRKQYQELNFLLVKGNHDRLSATNYAAMDIEIHEPSFCLGPFCFIHDAPNCTEEELYPISGHVHPGVTIVGKAKQRLKFPCFYFGKDYAVLPAFSLFTGLYTIYPKMNERIFAVTPKSVVEV Phaeobacter inhibens BS107 Phaeo GFF589 PGA1_c06030 DNA repair nuclease, ligase-associated (TIGR04123) # Very important for resisting cisplatin. This family was previously annotated as a DNA ligase-associated metallophosphoesterase (TIGR04123). A member of this family (PdeM) has been studied biochemically and found to have nuclease activity, but it was not known if DNA was the physiological substrate (see PMC4320098). Predicted ICC-like phosphoesterases MTGYDFSLAGQQLTALGSGALWWQARGLLCVADLHLGKSERQLRRGGTALPPYETRDTLERLAAVIDQTRPETVICLGDSFDDNAATAALSDADQTRVDQLITAHRWIWITGNHDPAPTGLAGEAHDSLPLGPLLFRHIADPAFTSESATDVTAEISGHYHPKARLRGNARPAFLADHQRLILPAFGTYTGGLCTTHDALRDLMSPRALAILTGPRPLPCPMPR Sinorhizobium meliloti 1021 Smeli SMc02236 SMc02236 DNA repair nuclease, ligase-associated (TIGR04123) # Specifically important in stress Cisplatin. This family was previously annotated as a DNA ligase-associated metallophosphoesterase (TIGR04123). A member of this family (PdeM) has been studied biochemically and found to have nuclease activity, but it was not known if DNA was the physiological substrate (see PMC4320098). hypothetical protein MTMHRLIYATSPAVNPSLHARTSINGVAAICDPLGGLYFPESRTLVVSDLHLEKGSAFARRGMMLPPYDTLATLRILDAVIARHEPATVISLGDNFHDRKGSAAMPETFRQMIAAMACGREWIWINGNHDPDGAQGLPGASMDELRHAGLVFRHEPSRRDGIGEIAGHLHPSATVRRRERSVRRACFATDGKRLVMPAFGVTTGGLDLRHREMSGLFDRQQLVAHMLGRDRIYSVRFANLLG Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_3186 N515DRAFT_3186 DNA repair helicase Lhr # Specifically important in stress Cisplatin. Similar to the full length of Lhr from Mycobacterium smegmatis, which is a helicase that is suspected to be involved in DNA repair (see PMC3656269) (SEED_correct) ATP-dependent helicase Lhr and Lhr-like helicase MSLQAFHPAVRQWFEGTFPAPTAAQLAAWPSIREGRHTLVAAPTGSGKTLTAFLAAIDGLVREGLAHGGALPDATTVVYVSPLKALSNDIHINLEAPLEGIRAELAALGLPDVAIRTAVRTGDTPQAERTLMRRQPPHILVTTPESLYILLGSASGREMLGGTRTVIVDEIHAMASTKRGSHLALSLERLEALCQRPLLRIGLSATQKPIEEVAKFLVGEGNDATLAAAFTPSPQRGEGWGEGDRRSVEAGTEKRAMLGRSAIASPGPSSAPPAHTCNIVDVGHTRERDLAIEVTPVPLEAVMSNDAWELVYNRLAELAQAHRTTLVFVNTRRMAERVARHLSERMGKQAVAAHHGSLAREQRLDAEQRLKRGELKVLVATASLELGIDIGDVDLVCQLSSPRSIAAFLQRAGRSGHAVSGTPKARLFPTSRDDLIECAALLDCVRRGELDTLAIPPQPLDVLAQQIVAEVACTEWNEDALFALVRRAYPYRELPREQFDAIVRMLADGFTTRRGARAAYVHRDAVHKQLRARRGARLTAVTSGGAIPDTADYLVVLEPQATVIGSVHEDFAVESLAGDIFQLGNTSYRIIRVERDRLRVEDAHGVPPSIPFWLGEAPGRSDELSHGVSRLREEISARLDEGGVPEVLSWLRNTLGLSEPAAQQLADYLARAKAALGVLPTQHTLVFERFFDESGGTQLVIHTPWGSRINRAWGLALRKRFCRQFNFELQAAATEDAIVLSLSTSHSFPLIEVARYLHSNTAEQVLVQALLDAPLFPVRWRWNATTSLALPRFQGGRKVAPQIQRMRSEDLLATVFPDQVACLENIAGERQIPDHPLVGQTLYDCLREAMDVDGLLHILRGLEGGQITVVARDLTTASPLAAEVLTAAPYAYLDDAPLEERRTQAVQTRRWSDGDSAEDLGQLDPDAIEAVRGEAWPQVRGADEMHEALSVLGFVSAEEAAGDAWDHWLEALAQARRATALSLPGHANWQVWVAAEKLPLWQAIHADAAMQPPIEAPAEFLAQPWTREDALLEMVRGRLVGLGPVTVATLAASLAVDSGDVELALLRLQSEGYVMQGRFTPAASETEWCERHLLARIHRYTIGRLRREIEPVSRRDFMRFQFDWQHVAPGARLSGPDALPAAIAQLEGYEAAAGAWEAELLPARIDDYSITWLDDLCRAGRVGWNRLRGATGGSSPVRATPIVLLPRKEMALWSSVAGTGQPQDVLLSSRAQAVADALREHGALFFDELMSVAHLLRTELEDALGELVAAGRVTADSFAGLRALLLPAAKRDAQRHRRVRRHMLSGIEDAGRWSLVRAPREQDGARAESVEHIARTLLRRYGVVFWKLLEREAAWLPTWRELLRVYHRLEARGEIRGGRFVEGLVGEQFALPEAIGKLRQVRQQPNEGQHVCLSGCDPLNLVGTVLSGNRLPAVIGTRVLYEDGVAVAALVANKPQWLVESDTAQQQRWKNALLRRAEHEPVHF Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_06780 AO353_06780 DNA repair helicase Lhr # Specifically important in stress Cisplatin. Similar to the full length of Lhr from Mycobacterium smegmatis, which is a helicase that is suspected to be involved in DNA repair (see PMC3656269) (SEED_correct) ATP-dependent DNA helicase MNLPVSAESALAGFHPAVRAWFNSTFPAVTAAQAGAWPLIRQRRSTLVAAPTGSGKTLTAFLAVIDDLVHQGLAHGGELPDETLVVYVSPLKALSNDIQINLQTPLAGITEQLRELGFPELQINTAVRTGDTPQKDRSAMRKSAPHILVTTPESLYVLLGSDSGRRMLASTRTVIVDEIHAIAGSKRGSHLALSLERLQALCCEPLMRIGLSATQKPIEAVSRFLVGTGRPCEIIDIGHARRRDLGIEVPPVPLSAVMANDVWELVYDRIAELAREHRTTLIFVNTRRLAERLSRHLSERLGKDAVAAHHGSLAKEFRLDAEQRLKRGDLQVLIATASLELGIDIGDVDLVCQIASPRSIAGFLQRVGRSGHQVGGTPKGRLFATTRDDLIECAALLDCVRRGELDTLLIPHAPLDVLAQQIVAEVSCQEWQERALLEMVRRASPYTELDDTHYQALLQMLAEGYNGRQGIRSAYLHRDAVTRTLRGRRGAKLTAVTSGGTIPDNADYSVLLEPQGLNIGSVNEDFAVESIAGDVFQLGNTSYRILRVETGKIRVEDAQGQPPTIPFWLGEAPGRSAELSLAVARLHAHLDELLGATPGDVQPSIDWLTETLGLNLASAEQLVDYLARARLTLGALPSQNTLLMERFFDESGGTQLIIHSLFGSRINRAWGLALRKRFCRTFNFELQAAASEDAIVLSLSTSHSFELDEVWRYLHSNTAEQILIQAVLDAPLFGVRWRWNAGVALALPRYSGGRKVPPQIQRMKSEDLIASVFPDQIACLENLVGEREIPDHPLVEQTLDDCLHEAMDCEGWLALLRRMESGEVRLISRDLPAPSPLAAEILSARPYTFLDDAPLEERRTQAVLNRRWSDPQSTDDLGALDAEAIQSVRDEAWPQPTSVDEMHEALMSLAAISNAEALANPQWSHWLQTLADSGRASRLQINAEHSLWLALERLTCLQAIYPHATLLPPLQALPGFDEPWDVDEALVELIRARLSAFGPLPIHAIAQPLGLSTAQVTQALAQLEREGYVLRGRFSPAAPQEEWCERHLLARIHRYTVKRLRREIEPVALQDFMRFLFDWQHLSPATQGQGSAVLPAIVSQFEGYPAAASAWDSDLLPARLKNYSSTWLDELCRSGKLVWTRLTVRNKATSAALRSTPIVLLPRAQVPLWSSLTEPPEVSELSPKTQKVHQALSQHGALFFDELLHEAHLLRSELEIALQELVGAGLVNADSFAGLRALITPASKRQARSSRRGRGAFVGGMDDAGRWALLRRQSTPPVVDNRGTPSETLEHIALTLLRRYGVVFWRLLEREAEWLPSWRELLRTFHRLEARGEIRGGRFVSGLAGEQFALPEAIPLLREVRRRQHDGSLISVCGVDPLNLAGTLLPGHKVPALASNRLVYRDGLPAAAEIAGTQHYWLELDQPNTAELHKKLTQYRTL Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_2220 Echvi_2220 pif1-like DNA repair helicase # Specifically important in stress Cisplatin; stress Nalidixic acid sodium salt; stress Lomefloxacin hydrochloride. Contains a pif1-like helicase domain and probably part of the RecD superfamily (see CDD). (SEED_correct) PIF1 helicase. MNKDKQDIPNPSALIRQNFPYEPTHGQGSFFRLMNTFLDEDFDRKPTFVLRGYAGTGKTSVIAAVVKSLPKLNFRSLLLAPTGRAAKVMAAYSGRMGFTIHKIIYRPKDQEGMAGSGFDLQKNYYKNTVFIVDEASMLSDDALGGSNLLRDLLQYVFQHPSNRLILIGDTAQLPPVGSENSPALDGNYLVHHYGLDVLEAELTEVMRQQLDSGILYNATELRKEVVKEAPVISFRIKGFPDFYKMTSERLEDGLRYAYDKYGVENTIIITRSNKTAVQYNQYIRRTIHFYEEEISAGDMLMIVRNNYTYMAESDKVSFLANGDFVEVVKIRSFEEMYGLRFATLELRLIDYPEEPFFEAKVILDTLYTSSTSLSTEDAKELYRQVTEDYAGVENKKERREYIKKDPYLNALQVKFAYALTCHKSQGGQWSAVFVDQGYVSEDQLDTAYIRWLYTALTRATAEVFLVNFHANFFVG Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS12710 CA265_RS12710 pif1-like DNA repair helicase # Specifically important in stress Cisplatin; stress Nalidixic acid sodium salt; stress Lomefloxacin hydrochloride. Contains a pif1-like helicase domain and probably part of the RecD superfamily (see CDD). (SEED_correct) ATP-dependent endonuclease MIPDKSQLIASAYEHTPTREQLLFCERMSVFLQQDDEYRCFVLKGYAGTGKTTSVAALVKVLKQFNLRSELLAPTGRAAKVMSQYSYRKALTIHKRIYRKRSAASPEMQFQLAPNLSENTLFIIDEASMIADEFNETGSSILRDLLEFVYNTKNCFLLFVGDTAQLPPVGSLDSPALNEQYLKDKFALTVSSVELKEVVRQGKKSGILANATMLRNQIAKNPENPLPKFLTKSYTDIYNMPGARLVEGLEYAYRKFGMENTLVVCRSNKSANVYNQQIRARLLYREEELTGGDQIMVVRNNYFWLPDNEDTAFIANGDMAKVIRVRGEEERYGFRFADATLEFMDFPAAGQISCKVMLDTLNLESANLPYEQNKKLFDGLNEDYEHIANKRQRMLAIKADPFYNALQIKFAYAVTCHKAQGGQWDAVFADQGYLTEEMIDLDFLRWLYTAVTRAKKELYLVNFAPQLFAKTALEDYF Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_2564 Echvi_2564 DNA repair nuclease with dnaQ and GIY-YIG domains # Specifically important in stress Cisplatin. Contains a domain that is similar to DnaQ (the epsilon subunit of replicative DNA polymerase which is the exonuclease for proofreading) as well as a GIY-YIG nuclease domain.This protein is often misannotated as DnaQ, but the proofreading activity of the replicative DNA polymerase seems to reside in the same polypeptide as the catalytic subunit (see Echvi_2020 or discussion in PMC3919608). exonuclease, DNA polymerase III, epsilon subunit family MIYAIVDIETTGGYGKRHRITEVAAVAHNGSQILDSFQTLINPDCEIPGFITGLTGIDQSMVEGAPYFEDIADELYAFLEDKIFVAHNVNFDYQFIRSEFERIGKSFDRPKLCTVRLSRKIFPGLRSYSLGRICEHKNIEIKSRHRAFGDAEATAELFTKLLLADQEGIVEQLLKRNSGEAFLPPNITKEQFLSLPESIGVYYFHDANGKVIYVGKALNIRHRFKGHFSGAGKGKQGMKSAIYDVSFQLTGSEFLALLVEALEIKQHWPKYNRAQKAKNAPWGIYRYQDGQGFERFQVAKINRFTKPLLAFHSHHEAWSYLLEKIEKHQLCAKLCGVQKSASACFDHQAGACLGACCGEEEPSSYNTRVEDWLQEIQREKSRLLIREKGRHPNEQAAIYFEDGVLKAYGFIDSEAEFDTDEAVIDQLEMVKPVGDTSSILAQYLSKNLMKKVVVLPS Pontibacter actiniarum KMM 6156, DSM 19842 Ponti CA264_07430 CA264_07430 DNA repair nuclease with dnaQ and GIY-YIG domains # Specifically important in stress Cisplatin. Contains a domain that is similar to DnaQ (the epsilon subunit of replicative DNA polymerase which is the exonuclease for proofreading) as well as a GIY-YIG nuclease domain.This protein is often misannotated as DnaQ, but the proofreading activity of the replicative DNA polymerase seems to reside in the same polypeptide as the catalytic subunit (see discussion in PMC3919608). DNA polymerase III subunit epsilon MYAIVDIETTGGQPHQDKITEIAIFIHDGEKIVDKYHTLINPERPIPYFITQLTGIKDDMVLEAPKFYEVAKEIVEFTEGKVFVAHNVRFDYSFMKKEFADLGFTFQRKTLCTVRLSRSLIPGLPSYSLGKLCNSIDIPLSQRHRAIGDAEATALLFDKLIKINRPVVDGNMNMAADNTTQVLKKEIKTSLLPPAISKEQVDALPMVPGVYYFHNEEGEVIYVGKSINIKKRIIQHFNIDYKSRKSLDFKNNITDITYELMGNELVALLFESAEIKRMKPQYNRQQRRSVFNTGIFVYEDNNGYKRLSYDTINKADNESLTPIIALSNHFKAKGFLFHKVAKYNLCQKLCDLYKTNGACFDYQVHQCNGACIGKESPEEYNLRVEEAIESFTYEHNSFVIIGKGREPGEKSVVVVEHGTYLGFGFVDDTFSAHNLEDFKGAIQRYNDNKDIQQIIRNHMRGKHKDKVIVFE Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_0867 Echvi_0867 uvrA paralog in Bacteroidetes # Specifically important in stress Cisplatin; stress D-Cycloserine. Both the "standard" uvrA and this gene were important for cisplatin resistance. (SEED_correct) excinuclease ABC, A subunit MNETTALNPSSIENLDPKSYIIIKNARVNNLKNLSVAIPRNKLVVVTGLSGSGKSSLAFDTLFAEGQRMYVESLSSYARQFLGRMEKPDVEYIKGVSPAIAIQQKVSTKNPRSTVGTTTEIYDYLKLLFSRIGRTISPVSGEEVKHHTVTDVVDFIHGFEEGEKVMISCPLQANASRTMQKELEVLLQKGFTRIIIEGEVYYVEDLLEEKTIPDGDIEILIDRAVVRKDDEDNHFRIADSVQTAFFEGHGDCFVVIPGKETRKFSDRFELDGLSFELPSVNFFSFNNPYGACKTCEGFGSVLGIDPDLVIPDKSLSIYEGAIAPWRGETTKKWAAPLIKNGIHFDFPIHRPYEELDEAHKDLIWKGNSYFKGLDAFFEHLQSKTHKIQYRVMLSRFRGRTTCPDCKGTRLRKDAAYVKVNGHSITDIVLMPIDRALAFFQNIQLTEAEEKTANRLLKEILNRLEYIDKVGLGYLTLNRLTSSLSGGEYQRIKLATSLGSALVGSMYILDEPSIGLHPRDSDRLISVLKSLRDMGNTVIVVEHEEKIMKAADEIVDIGPEAGVNGGKLVFQGKLDELLAHGETYTAKYLKGEEKIDIKQGNRKWKDKILINGARENNLKNINVQIPLNTLTVITGVSGSGKSTLIKKVLYPALGKILGTVIDETGKFDKLEGDYKSISQVEFVDQNPIGKSSRSNPVTYVKAYDAIRSLFADQPVAKQRGYKPAFFSFNVDGGRCEACQGEGTQKIEMQFMADIFLTCESCKGKRFKNEILDITYKDKNIADVLEMTIDEAMEFFQGKNAIISRLQPLQEVGLGYIGLGQSSNTLSGGEAQRVKLASFLGKGGNKAKDHVLFIFDEPTTGLHFHDIKKLLYSINALIEEGHSVIIIEHNTEVIKSADWVIDLGPEGGERGGNVTFEGTPEALREVKDNYTAKYLRESFS Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS00660 CA265_RS00660 uvrA paralog in Bacteroidetes # Very important for resisting cisplatin. Both the "standard" uvrA and this gene were important for cisplatin resistance. (SEED_correct) excinuclease ABC subunit A MSKKEAEKDPHKNIIIKGARVHNLKNIDVAIPKNKLVVVTGMSGSGKSSLAFDTLYAEGQRRYVESLSSYARQFMGRMNKPDVDYIKGIAPAIAIEQKVITSNPRSTVGTSTEIYDYLKLLFSRIGKTISPVSGKEVKKDSVSTVVDYVNAMPEDTTVTIFCPLYPHNNRTIKEELAILLQKGFLRVLINDKIEKIETVLDDADFKDAELTDDKTVQILIDRIVTNQEEETLSRLADSAQTAFFEGKGDCYVEAQGTTKHFSDRFELDGIKFEEPTPNFFSFNNPYGACKRCEGYGNVIGIDEDLVIPDKSKSVYDNAIAPWRGEKMNVWLQNFIKAAPKFEFPIHRPYSALTETEQQLLWTGNKYFAGLDAFFKELEEQTYKIQYRVMLSRYRGKTTCPDCKGSRLRKDASYVKIAEKSIIDVVLMPLAKALVFFNELKLNTNDTKIAKRLLAEIDNRFLYLNNVGLGYLTLNRLSNTLSGGESQRINLATSLGSSLVGSIYVLDEPSIGLHPRDTNKLIEVLISLRNVGNTVLVVEHEEEMMRAADYIIDIGPEAGTHGGNLVFSGNYEEILKDKNSLTGRYLSGLEKIAIPDKRRKWKDHILIKGARENNLQNIDVKFPLGVFTAVSGVSGSGKTSLVKKILYPALQKAIGNYAGEQTGAYDGIFGNYDLVSAVEMVDQNPIGRSSRSNPVTYVKAWDDIRALFSGLASAKAAGLKPAAFSFNVEGGRCDVCQGEGEVKIEMQFMADIYLPCEACNGKRFKQQVLDVTYKEKNVSEILDMTIEEAVEFFKDEQKILNKLNPLVDVGLGYVHLGQSSNTLSGGEAQRIKLASFLIKGNNANKTLFIFDEPTTGLHFHDIKKLLKALNTLIEQGNTILVIEHNMDMIKCADWVIDIGPEGGDGGGQVVFEGIPEDLVQVEKSYTGKYLASHLNLNP Pontibacter actiniarum KMM 6156, DSM 19842 Ponti CA264_14900 CA264_14900 uvrA paralog in Bacteroidetes # Very important for resisting cisplatin. Both the "standard" uvrA and this gene were important for cisplatin resistance. (SEED_correct) excinuclease ABC subunit A MANTSADKLDELDARQNIIIKGARVHNLKNLSVALPRNKFIVITGLSGSGKSSLAFDTLYAEGQRMYVESLSSYARQFLGRMDKPDVDYIKGISPAIAIEQKVSIKNNRSTVGTSTEIYDYLKLLYARIGKTYSPVSGEVVKKDSVTDVVNFIFSLEDEARVMILAPLHQHQERTLAKELDLLLQKGYSRIYANEQVYFIEELLEEKKPKLGKEVFILVDRAVIYKSDEDLAFRISDSVQTAFFEGHGECRVLYGNGEERVFSDRFELDGMVFEEPSVNFFSFNNPYGACQTCEGFGSVLGIDPDLVIPDKSLTVYEGAIAPWRTDKMNEWLQPLLKNGIRFDFPIHRPYNELTEAEQELLWTGNKYFSGLNAFFKEIQSQTHKIQYRVMLSRYRGRTTCPECRGSRLRKDASYVKVGGKSITDLVLMPITQVLPFFQNLELTEHEHNVAERLVTEVSNRLGYLQRVGLGYLTLNRLSNTLSGGESQRINLATSLGSALVGSMYILDEPSIGLHPKDSEQLIGVLRSLQQIGNTVIVVEHEEEMMKAADQLIDIGPEAGSGGGNLMFQGSFEEMTQRADTYTSKYLSGKMEVPVPAQRRKWRNAIEIIGARENNLKNLSVKVPLGVMTVVTGVSGSGKSTLIKKILAPAMQKLHGSTAEATGKFDKLAGDYNKIEHVEFVDQNPIGKSSRSNPVTYVKAYDAIRTLYADQPLAKSRGFKPSHFSFNIEGGRCEVCQGEGQVKIEMQFMADIYLTCESCHGQRFKQDVLDIKYKDKSISDVLEMTIADSIDFFADQPKIIEKLKPLNDVGLGYIRLGQSSNTLSGGEAQRVKLASFLTKGAQPHQENILFIFDEPSTGLHFHDISKLLTSINALIENGNTVVIIEHNMDIVKCADWIIDLGPEGGTNGGHLLFEGTPEEMAKLEDNDTARFLKEKL Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_2275 Echvi_2275 translesion DNA polymerase (imuC-like) # Specifically important in stress Cisplatin. Distantly related (less than 30% identity) to imuC (also known as dnaE2), which is a translesion DNA polymerase that is involved in DNA repair in Pseudomonas and Mycobacteria (see PMC3090020). DNA polymerase III, alpha subunit MYVNCHSYFSFRYGTMPVQEMVDQAKKLGVKAMALTDINCTAAVYPFLKATKAANIHGVIGIDFRNGIDQQYIGLALNHHGFFEMNRHLSDHKGKKRPFPQKAPQWQNTAVIYPFPQPYFKLGPREYLGIPADQLKKALRSPWIAEKDRWILLQSVTFHSQQSFNIHRLLRCIELNILLSKLPTSEQGNLSDRFYSTLELAERCAPHYWLLQQTHALLSRCRFEQDYQPVANKKSVYGSEQEDLAQLTALTYQGAKNRYGTPLSERQETRILKELDIIRQKDFVSYFLINYEIVKFARERGFYYVGRGSGANSIVAYCLNITDVDPIELDLYFERFINLYRSTPPDFDIDFSWRDRDEVIQHIFHKHNTEDHEHVCLLATHNTFQINSSIRELGKVFGLPKTDIEALINHVVKPGNYIPDRIGALVLKYSQLIHGMPSHLSIHAGGILISQQPIHYYTATDLPPKGFPISHFDMVTAEEIGFAKFDILSQRGLGHIRDSLEIIEKNQGKKVDIHRIKDFKHDEKIKQHLRKGHTIGAFYVESPAMRMLLAKLEVDEYLGLVAASSIIRPGVARSGMMREYILRHRKPEMRKSRAHPILHDLMPETYGIMVYQEDVIKVAHYFAGLSFDEADVLRRGMSGKFRSRAAFLKVKESFFKKSMEKGHAPKITSEIWFQVESFAGYSFAKGHSASFAVESYQSLYLKAHFPLEFMVGVINNFGGFYKTEFYIRELQGYHADVQLPHLNESDYLTVIKGTTVYLGFIHLKYLQKDITNTILQNRETEGPFTGLRDFINRIAISLEQLLILIRIDAFRFTAKRKQELLWEAHFLTNKQKNKPSTNHLFRQINLRELSIPHLETNDPRQDILDQLEIMEFSIADPFLLLKAPPHDTLKAQDIPSYAGKEIRLMGYLVTVKYTRTVKGDIMNFGTFLDRDGQWIDTVHFPPVIRQYPLTGRGIYLLEGKVSEEFNFYTIEISSCKKLAYWNAADDHPNPVTNQSPKTSIDN Sinorhizobium meliloti 1021 Smeli SMc03165 SMc03165 Novel Xylose regulator from LacI family # Specifically important in carbon source D-Xylose. Also see expression evidence for the putative ortholog from Phaeobacter, PGA1_c13990, which is 41% identical (PMC4148808). (SEED_correct) transcriptional regulator MRPTVHDIAAEAGVSLATVDRVLNNRPGVRSVTRGKVERAIATLGYVRDVAAANLAKSRSYPLIFILPAGENSFMRGLEAEVRSAMSRSATERLDITILSVPVFDAPALAAALHDARERRPAGVAVVAVDAPEVTEAVKRLREDGIAVVTLVSDLPGSGRDHFAGVDNVAAGRTAGSLMGRFLGGGEGPVAVLAGSMLVRDHRDRLEGFQAVMSEDFAWRRILPVIEGQDNPSLVETLVGALLGQHPDLAGIYSLGAGNRGLVAALEKAGKGRAVCTIAHELTPHSRAGLLSGTIDALLNQNAGHEVRSAIRVLKAKADGLPVIAAQERIRIDIFLKDNLPLEQE Phaeobacter inhibens BS107 Phaeo GFF1382 PGA1_c13990 Novel Xylose regulator from LacI family # Specifically important in carbon source D-Xylose. Also see expression evidence (PMC4148808). (SEED_correct) putative transcriptional regulator, iacl family MGKPTLHDVAAAAGVSYATADRVLNNRGGVAKKSQDRVRAAIADLGYQRDITAANLSRRRRYRFAVLMPAAQEGFFATLHADLEQEVAARSQARQQITLTQVPPFDAAALTCALEACAAEGYDGVCLVAVQDPSVDAALTGLRAQGVAVVTLVADSAAQARDTYVGIDNRRAGRTAGDLMRLAHRGSAASLGQILPITGSLNARDHADRYAGFCDVVSADLHILPPLETGDDPEILEQALRRTLRANPNITGIYNLGAGIPGLISALAAIQPDDRPVVISHELCPATRDAVAHGLIDAVIDQKPAQEITAALAALVALSDGQSVDPLAGQITPAVHFKHNMPPQSAVGPEEGA Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_772 ABC transporter for L-asparagine and L-glutamate, permease component 1 # Specifically important in carbon source L-Asparagine. Also important for glutamate utilization. We do not have fitness data for aspartate utilization - it may well transport aspartate as well. Also note that the aspariganase (Pf1N1B4_2023) is predicted to be cytoplasmic and is important for asparagine utilization, so we do not think that asparagine is converted to aspartate before uptake. Glutamate Aspartate transport system permease protein GltJ (TC 3.A.1.3.4) MNYNWDWGVFFKSTGVGSEIYFDWYLSGLGWTIAIAVAAWIIALLLGSILGVMRTVPNRIVSGIATCYVELFRNVPLLVQLFIWYFLVPDLLPADIQEWYKQDLNPTTSAFLSVVVCLGLFTTARVCEQVRTGIQALPRGQEAAARAMGFKLPQIYWNVLLPQAYRIIIPPLTSEFLNVFKNSSVASLIGLMELLAQTKQTAEFSANLFEAFTLATLIYFTLNMSLMLLMRSVEKKVAVPGLISVGGK Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_16280 AO353_16280 ABC transporter for L-aspartate, L-asparagine, L-glutamate, and L-glutamine, permease component 1 # Specifically important in carbon source L-Aspartic Acid; pH ; carbon source L-Asparagine; carbon source L-Glutamic acid monopotassium salt monohydrate; carbon source L-Glutamine amino acid ABC transporter permease MDLDFSGVVQAVPGMWNGMVMTLQLTVLGVVGGIILGTLLALMRLSHSKLLSNIAGAYVNYFRSIPLLLVITWFYLAVPFVLRWITGEDTPIGAFTSCIVAFMMFEAAYFCEIVRAGVQSIPKGQMGAAKALGMGYGQMMRLIILPQAFRKMTPLLLQQSIILFQDTSLVYTVGLVDFLNATRASGDIIGRANEFLIIAGLVYFTISFAASRLVKRLQKRFAV Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_16285 AO353_16285 ABC transporter for L-aspartate, L-asparagine, L-glutamate, and L-glutamine, permease component 2 # Specifically important in carbon source L-Aspartic Acid; pH ; carbon source L-Asparagine; carbon source L-Glutamic acid monopotassium salt monohydrate; carbon source L-Glutamine amino acid ABC transporter permease MNYNWDWGVFFKSTGVGSETYLDWFITGLGWTIAIAIVAWIIALMLGSVLGVMRTVPNRLVSGIATCYVELFRNVPLLVQLFIWYFLVPDLLPQNLQDWYKQDLNPTTSAYLSVVVCLGLFTAARVCEQVRTGIQALPRGQESAARAMGFKLPQIYWNVLLPQAYRIVIPPLTSEFLNVFKNSSVASLIGLMELLAQTKQTAEFSANLFEAFTLATLIYFTLNMSLMLLMRMVEKKVAVPGLISVGGK Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_21715 AO353_21715 ABC transporter for D-glucosamine, permease component 1 # Specifically important in nitrogen source D-Glucosamine Hydrochloride; carbon source D-Glucosamine Hydrochloride amino acid ABC transporter permease MNYQLNFAAVWRDFDTLLAGLGLGLELALVSIAIGCVIGLLMAFALLSKHRALRVLASVYVTVIRNTPILVLILLIYFALPSLGIRLDKLPSFIITLSLYAGAYLTEVFRGGLLSIPKGLREAGLAIGLGEWQVKAYVTVPVMLRNVLPALSNNFISLFKDTSLAAAIAVPELTYYARKINVESYRVIETWLVTTALYVAACYLIAMLLRYLEQRLAIRR Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_21720 AO353_21720 ABC transporter for D-glucosamine, permease component 2 # Specifically important in nitrogen source D-Glucosamine Hydrochloride; carbon source D-Glucosamine Hydrochloride ABC transporter permease MYESPSWLHELWVARDTLWSGFLTSVQCSVLAIMLGTLIGIVAGLVLTYGTLWMRAPFRFYVDLIRGTPVFVLVLACFYMAPALGWQIDAFQAGVLGLTLFCGSHVAEIVRGALQALPRGQMEASKAIGLTFYQALAYVLLPQALRQILPTWVNSSTEIVKASTLLSVIGVAELLLSTQQIIARTFMTLEFYLFAGFLFFIINYAIELLGRHIEKRVALP Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_1961 ABC transporter for D-sorbitol, permease component 2 # Specifically important in carbon source D-Sorbitol. We do not have fitness data for the putative first subunit Pf6N2E2_1962. Various polyols ABC transporter, permease component 2 MMTLKQSRSLQSLLLGTLAWVAALLLFFPIFWMVLTSFKTEIDAFATPPQFIFMPTLENYLHIQERSDYFHFAWNSVLISFSATALCMLIAVPAAYSMAFYETKRTKQTLLWMLSTKMLPPVGVLMPIYLLAKGAGLLDTRIALIVIYTLINLPIVVWMIYTYFKDIPREILEAARLDGATLGQEMLRVLLPISKGGLASTMLLSMILCWNEAFWSLNLTSSSAAPLTALIASYSSPEGLFWAKLSAVSTLACAPILIFGWISQKQLVRGLSFGAVK Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_771 ABC transporter for L-asparagine and L-glutamate, periplasmic substrate-binding component # Specifically important in carbon source L-Asparagine. Also important for glutamate utilization. Glutamate Aspartate periplasmic binding protein precursor GltI (TC 3.A.1.3.4) MRIVPHILGAAIAAALISTPVFAAELTGTLKKIKESGTITLGHRDASIPFSYIADASGKPVGYSHDIQLKIVEAIKKDLDMPNLQVKYNLVTSQTRIPLVQNGTVDVECGSTTNNVERQQQVDFSVGIFEIGTKLLSKKDSAYKDFADLKGKNVVTTAGTTSERILKSMNADKQMGMNVISAKDHGESFQMLETGRAVAFMMDDALLAGEMAKAKKPTDWAVTGTAQSNEIYGCMVRKGDAPFKKAVDDAIIATYKSGEINKIYEKWFMQPIPPKGLNLMFPMSEELKALIANPTDKAADEKKS Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_773 ABC transporter for L-asparagine and L-glutamate, permease subunit 2 # Important for glutamate and asparagine utilization and cofit with other components Glutamate Aspartate transport system permease protein GltK (TC 3.A.1.3.4) MEFDFSGIIPSLPGLWNGMIMTLKLMALGVIGGIILGTILALMRLSHNKLLSNIAGAYVNYFRSIPLLLVITWFYLAVPFVLRWITGEDTPIGAFASCIVAFMMFEAAYFCEIVRAGVQSIPKGQMGAAQALGMEYGQMMRLIILPQAFRKMTPLLLQQSIILFQDTSLVYAVGLVDFLNASRASGDIIGRSNEFLIFAGLTYFTISFAASLLVKRLQKRFAV Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_774 ABC transporter for L-asparagine and L-glutamate, ATPase component # Reannotated based on fitness data for other genes in the operon. We have no fitness data for this gene. Glutamate Aspartate transport ATP-binding protein GltL (TC 3.A.1.3.4) MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLPKLRSRVGMVFQHFELFPHLSIMDNLTIAQVKVLGRSKEEASKKALQLLERVGLSAHAKKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAHEGMTMMCVTHEMGFARKVADRVIFMDQGKIIEDCKKEEFFGDITARSDRAQHFLEKILQH Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_16275 AO353_16275 ABC transporter for L-aspartate, L-asparagine, L-glutamate, and L-glutamine, ATPase component # Reannotated based on fitness data for other genes in the operon. We have no fitness data for this gene. amino acid ABC transporter ATP-binding protein MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVVVDGTSIADPKTDLPKLRSRVGMVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLERVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLANEGMTMMCVTHEMGFARKVADRVIFMDQGKIIEDCKKEEFFGDINARSDRAQHFLDKILQH Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_16290 AO353_16290 ABC transporter for L-aspartate, L-asparagine, L-glutamate, and L-glutamine, periplasmic substrate-binding component # Specifically important in carbon source L-Aspartic Acid; carbon source L-Asparagine; pH ; carbon source L-Glutamic acid monopotassium salt monohydrate; carbon source L-Glutamine ABC transporter MRIVPHILGAAITAALISTPVFAAELTGTLKKIKESGTITLGHRDASIPFSYIADASGVPVGYSHDIQLKIVEAIKKDLDMPNLKVKYNLVTSQTRIPLVQNGTVDVECGSTTNNTERQQQVDFSVGIFEIGTKLLSKKDSTYKDFADLKGKNVVTTAGTTSERILKSMNADKQMGMNVISAKDHGESFQMLESGRAVAFMMDDALLAGEMAKAKSPTDWAVTGTAQSYEIYGCMVRKGDAPFKKAVDDAIVATYKSGEINTIYGKWFTQPIPPKNLNLMFPMSDELKALISNPTDKAAEEKKS Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_21710 AO353_21710 ABC transporter for D-glucosamine, periplasmic substrate-binding component # Specifically important in nitrogen source D-Glucosamine Hydrochloride; carbon source D-Glucosamine Hydrochloride ABC transporter substrate-binding protein MQRRLSLFTACVFLFAATASAVGIAQAADSRLDNVLKRGHLIVGTGSTNAPWHFQGADGKLQGFDIDIGRMVAKGLFNDPSKVEFVVQSSDARIPNLLTDKVDMSCQFITVTASRAQQVAFTLPYYREGVGLLLPANSKYKEIEDLKAAGDSVTVAVLQNVYAEELVHQALPKAKVDQYDSVDLMYQAVNSGRADTAATDQSSVKYLMVQNPGRYRSPTYAWSPQTYACAVKRGDQDWLNFVNTVLHEAMTGVEFPTYAASFKQWFGVDLPSPAIGFPVEFK Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_21725 AO353_21725 ABC transporter for D-glucosamine, ATPase component # Reannotated based on fitness data for other genes in the operon. We have no fitness data for this gene. ATP-binding protein MTQAQVSTQNASQALLEIRDLHKQYGPLEVLKGVDLTMQRGNVVTLIGSSGSGKTTLLRCVNMLEEFQGGQILLDGESIGYHEVNGKRVRHSEKVIAQHRAMTGMAFQQFNLFPHLTALQNVTLGLLKVKKLHKDEAVVLAEKWLERVGLLERRDHYPGQLSGGQQQRVAIARAIAMNPSLMLFDEVTSALDPELVGEVLSVIKGLAEDGMTMLLVTHEMRFAFEVSDKIVFMNQGRIEEQGPPKELFERPQSPRLAEFLKNTRF Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_1962 ABC transporter for D-sorbitol, permease component 1 # Reannotated based on fitness data for other genes in the operon. We have no fitness data for this gene. Various polyols ABC transporter, permease component 1 VSPSVALLLLWMIVPLAMTVYFSVIRYNLLNPGENEFVGLENFAYFVTDSGFLPGALNTLILVGSVLLISVIFGVLIAALLEASEFFGRGIVRVLLISPFFIMPTVGSLIFKNLIFHPVSGILAAVWKFFGAQPVDWLAHYPLFSIIVIVSWQWLPFAILLLMTAMQSLDQEQKEAARLDGAGALAIFWHLTLPHLARPIAVVVMIETIFLLSVFAEIFTTTNGGPGFASTNLAYLIYNQALVQFDVGMASAGGLIAVVIANIAAIVLVRMIGKNLTDKA Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_1963 ABC transporter for D-sorbitol, periplasmic substrate-binding component # Specifically important in carbon source D-Sorbitol Various polyols ABC transporter, periplasmic substrate-binding protein MKITNALILSTGLSFALASHAAETLTIATVNNGDMIRMQRLSKVFEQQHPDIKLSWVVLEENVLRQRLTTDIATQGGQFDVLTIGTYETPMWGAKNWLEPMKDLPAGYDVDDIFPAVRQGLSVNDTLYALPFYGESTITYYRTDLFKAAGLTMPAQPTWSQLGEFAAKLNDPSKDQYGMCLRGKAGWGENMALLTTMANAFGARWFDEKWQPELNGPEWKAAATFYVDTLKKYGPPGVSSNGFNETLALFNSGKCAIWVDASVAGSFTTDKEQSRVVDSVGFAPAPTEVTDKGSSWLYAWSLAIPATSKHKEAAKSFVTWATSKEYIQLVTDKDGITNVPPGTRISTYSDAYLKAAPFAQVTLQMMKHADPSQPSAKPVPYVGIQYVVIPEFQSIGTSVGKLFSAALTGQMSVEQALASAQSTTEREMKRAGYPKK Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_1960 ABC transporter for D-sorbitol, ATPase component # Specifically important in carbon source D-Sorbitol Various polyols ABC transporter, ATP-binding component MATLKIENLKKGFEGLSIIKGIDLEVKDKEFVVFVGPSGCGKSTLLRLIAGLEDVTSGTIELDGRDITEVTPAKRDLAMVFQTYALYPHMTVRKNLSFALDLAGEKKPDVERKVAEAARILELGSLLDRKPKQLSGGQRQRVAIGRAIVRNPKIFLFDEPLSNLDAALRVQTRLELSRLHKELQATMIYVTHDQVEAMTLATKVVVLNAGRIEQIGSPLELYHHPANLFVAGFLGTPKMGFLQATVHAVHASGVEVRFASGTTLLIPRDSSALSVGQSVTIGIRPEHLTLSAEGQVPVTTDVTERLGSDTFCHVNVDSGESLTVRVQGDCEVPYAARRYLTLDVAHCHLFDESGLSVSPAASRAA Pseudomonas simiae WCS417 WCS417 GFF2134 PS417_10885 Deoxyribose 1-dehydrogenase, beta subunit # Specifically important in carbon source 2-Deoxy-D-Ribose; not required for deoxyribonoate utilization; related to iorB isoquinoline 1-oxidoreductase MNLINELLDAPVNLSRRRFLASTAVGALVIGFGLPLGAGRVQAATSAERGTQVPAFLEIRPDGTVRLLSPFMEGGQGTHTAMAQIVGEELDADPATFIVEAAPPGEAYVVMENGLRITGGSMSVRMSYPTMRRLGALARAMLLQAGAKQWGVPVGELTTQPGRVVHAASGRSLGYGELASSALDMPVPDPASITLRDPSQFRWIGKPVKRLDAYDKSTGKALYSIDLKVDNMLHAAVQHAPRLGMTVGSLRNQSQVEGMKGVHSVHVLPGAVAVVAERWWHAKRAVEAIQVDWQEAAADSALRVMPADFSSDKHREFLAAQQGPTRDDENEGDVAGALKGAKTQVEATYHNQYLNHAQLEPPSALARFNPDGTLEIWLPNQAPDMFRADIAKRTGLDPAQITLHSPLLGGFFGRHFLYDSANPYPQAIALAKAVSRPIKLIWSREEEFLRDVLRPLAVVKFRAALDDKGLPVAIEAVSATEGPTEALAGKQGDKIDPTAVEGLSGKSYAIPNKRIAQIYVKGAPMLGYWRSVGNSLNDFFYESFLDELADKGGHDPYELRLHLLRDNPRLTTLLQAAGELSGGWKRGPFTAEDGTRRARGVAMASPFGSHTAAIAEVSIENGKVKVHDIWQAIDPGSIVNPAIVEAQVNGAVALGLSQTLLEEAVYVDGKPRARNYDLYPILAPAQMARVHVRVVESGEKMGGIGEPPLPAVAPAVANAVAQLTGQRVRSLPLSRHTFS Pseudomonas simiae WCS417 WCS417 GFF2135 PS417_10890 Deoxyribose 1-dehydrogenase, alpha subunit # Specifically important in carbon source 2-Deoxy-D-Ribose; not required for deoxyribonoate utilization; related to iorA (2Fe-2S)-binding protein MELRINQKAYQVDADADTPLLWVIRDDLGLTGTKYGCGLAQCGACSVLVDGNVVRSCVTPVAGVVGREITTIEAIETDEVGKRVVATWVEHQVAQCGYCQSGQVMAATALLKHTPAPSKAQIDAAMINLCRCGTYNAIHAAVDDLAKQGGV Pseudomonas simiae WCS417 WCS417 GFF1427 PS417_07255 Deoxyribonolactonase # Specifically important in carbon source 2-Deoxy-D-Ribose; a putative lactonase calcium-binding protein MRIEVLVDVKTTLGEGPVWDVEQQRLYWIDSADGRILRCTDDGRELRAWEVGQKIGSMALRQDGESAIVALQNGVHTLDLKSGELNLIADPEPHLPDNRLNDGKVDRQGRFIFGSMDTQEDNASAKLYRLDADLSLHTLDEGIIVSNGPCWSPSGDTFYFCDTWSGEIWAYDYDLATGNVSNRRTFAKVDTRGGGAADGCTVDAEGCLWQALVYAGKLVRYTPEGVVDRIIQMPVKKVTSLTFGGPNLDTLFVTSMAKPPLPRFPADGQQRGALFAITGLGVQGIAERRFAS Pseudomonas simiae WCS417 WCS417 GFF1426 PS417_07250 2-deoxy-3-keto-D-ribonoate cleavage enzyme # Specifically important in carbon source 2-Deoxy-D-Ribose; carbon source 2-Deoxy-D-ribonic acid lithium salt; this is a beta keto acid cleavage enzyme, see PMID:24240508 hypothetical protein MSKNRPVIITCAVTGAIHTPSMSPHLPITAQEIADAAIGAAEAGAAIVHLHARDPNDGRPSQDPALFAEFLPQIKAASDVVINITTGGAPTMGVEERLQPVMQFKPELASLNMGSMNFGLYEMLNRFTDFKHDWERPYLEESDDRIFRNTFRDITHILNACAENRTRFEIECYDIGHLYTAAHFLERGLLKPPLFIQSVFGLRGGIGGHPEDLAHMRRTADRLFGSDYVWSILGAGRGQIPLATMGLSMGSNARVGLEDSLWDGPGKLAASNADQVRRIRTVIEALGHRVATPDEAREILGLKGRDQVNF Pseudomonas simiae WCS417 WCS417 GFF1424 PS417_07240 Transcriptional regulator of deoxyribose catabolism # Specifically important in carbon source 2-Deoxy-D-Ribose. Conserved synteny (in an apparent operon) with the SDR and the beta-keto acid cleavage enzyme suggested that it might regulate the operon. Motif analysis found a conserved palindrome GTGATCAC upstream of the operon that matches the motif for AkgR from Rhodobacter sphaeroides (PMCID: GTGATCAC), which is 32% identical to PS417_07240. GntR family transcriptional regulator MTDGPLLLPTLRQVSRDTLQDQVYRQIREALMSGRFQPGQKLTIRGLAEALGSSPMPVREALQRLSAENAFEVTETSRLRVRLMTVERLREIRDARVALEGLLAEKAVLLLQKADLDEITDLCQQMQHAADEVDVSRYLWTNFAFHRRIYAVAQAELTMAAVENFWLHMGPCFALVAPDKAHLQRSMEAHTRIVEALAARDGGGARAAVTDDIMQAADSLARLLVKNDRSRSSVSGGKRA Sinorhizobium meliloti 1021 Smeli SM_b21373 SM_b21373 D-tagatose 6-phosphate 4-epimerase [EC:5.1.3.40] Specifically important for: D-Tagatose. This protein is >50% identical to Atu3167, which converts D-tagatose 6-phosphate to D-fructose 6-phosphate (see PMC4661409). This information is in the recent releases of KEGG and MetaCyc. sugar kinase MQENHLIDIARWSERPGPRGIPSICSAHPLVIEAAMLRAHREKAPVLIEATCNQVNQDGGYTGMTPEDFTRFVGAIADRIEFPREKILLGGDHLGPNPWKHLPADEAMAKAEAMITAYAKAGFTKLHLDTSMGCAGEPTALPDATTAARAARLAAVAEDAVGGRGGVLPVYIIGTEVPIPGGALEELDTLEVTAPEAAIETVRVHRAAFEEAGAAGAFSRVVGAVVQPGVEFGNENVIAYDRARAEKLSATLGQLHGMVFEAHSTDYQTPDALRELVADGFAILKVGPGLTFALREALYGLDQIAAFLFPAARERTLAEVTEAVMREEPANWAKYYHGSAEEQRLQRHFSYSDRIRYYWPHPKAAAAVDELMSLLDGVAIPETLISQFLAGSYARVRNGEVAPQAKPLALAAVDAVLQDYFAACRV Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS23040 HSERO_RS23040 D-galacturonate dehydrogenase (EC 1.1.1.203) # Specifically important in carbon source D-Galacturonic Acid monohydrate. Also see related proteins URODH_PSESM and URODH_PSEPK in Swiss-Prot. NAD-dependent dehydratase MSQDQDVAAWQTARFSRLLLTGAAGGVGKQLRARLASFAEVVRVADLASAMAAVDPAAAHEEALGCDLADRAAVDAMVAGCEAIIHLGGVSVERPFEEILEANIKGVFHIYEAARRHGVKRVIFASSNHVTGFYGQDERIDARDMKRPDGYYGLSKSYGEDMAQFYFDRYGVETVSIRIGSIFPEATNRRMLASWMSMDDFEQLLRRSLFIPDVGHTIVYGMSANAKTWWDNRYAAHLGYAPKDSSEIFRAKVEAQPMPAPDDPVLTLQGGAFTTAGPFDPLAD Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS15795 HSERO_RS15795 galactaro-1,5-lactonase # Specifically important in carbon source D-Galacturonic Acid monohydrate. The lactone is probably formed by HSERO_RS23040 and the product (meso-galactarate) is probably consumed by HSERO_RS15800 6-phosphogluconolactonase LIATSALSLATSHAGAATIAYVSHADSQDIYVLRLNNDGSVNLIDKVDTGSTVMPLAISPDRKYLYASLRREPYAVASYAIDPASGKLKALSKAPLADNMANIATDRSGRYLLAASYFGNKISVNAIGSDGAVQTPPLAVIPTGKNAHSVQVDPANAFVFASNLGSDVILQYRFDPASGAVTPNTPPSVASKAGAGPRHFVFSPDQRFLYCANELDATVSTYAYDRQAGTLTLLGSDSALPEGFQSSEQLAAADLHLTPDGRFLYATERTSNTLTGYRVDRASGKLTRILNIPTETQPRAFNIDPQGRYLLAVGQKAGLTSYAIDAASGTLTPLFRYTLGRNPNWVEIIDLP Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS00735 HSERO_RS00735 Ketoglutarate semialdehyde dehydrogenase (EC 1.2.1.26) # Important for utilization of D-Galacturonate, L-Arabinose, and D-Xylose. These are all catabolized by oxidative pathways leading to alpha-ketoglutarate semialdehyde (also known as 2,5-dioxopentanoate) 2,5-dioxovalerate dehydrogenase VSFNILGHNYIGGQRSGQGDVALHSVDATTGALFETPFLTATDKEVAAAVHAAEQAYPLYRATTSEQRAQFLEAIADEIDALGDDFLAAVARETALPATPRLAGERARTSGQMRLFAKVVRRGDFYGARIDTALPQRQPLPRPDIRQYKIGVGPVAVFGASNFPLAFSVAGGDTAAALAAGCPVVFKAHSGHLVTSELVADAIERAVKKTGMPAGTFNMIYGDRVGAQLVKSAGIQAVGFTGSLRGGRALCDMAAARPQPIPVFAEMSSINPIILMPEALKLRGDAIAKDLAGSVTVGVGQLCTSPGLLLGVRSPELTSFIEKLSAAFGGTNPATMLNSGGLTHYNGGVARLTQLPGVKVIATGGTSYTQAVPHLFKADAALLFSKEAPLEEEVFGPSTVIVELESREQLLDFAAKMNGQLTATLQAEIGDLQGNQDLIAILEQKAGRLLLNGFPTGVEVCDAMVHGGPYPATSDARGTSVGSLAIERFLRPVCYQNYPDAMLPAALQNANPLGLMRLVDGEQTRATVG Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_1358 L-leucine transaminase; L-isoleucine transaminase (EC 2.6.1.42) # Specifically important in nitrogen source L-Isoleucine; nitrogen source L-Leucine. Similarity to A0A060PQX5 suggests that glutamate is probably the physiological amino group donor (not alanine), see PMID:24687296 Valine--pyruvate aminotransferase (EC 2.6.1.66) VKLNDLPQNSTWTLARRAERMNPSVIREILKVTEKPGIISLAGGLPSPKTFPVSAFAAASAAVLANDGPAALQYAASEGYAPLRQAIADFLPWDVDADQILITTGSQQALDLIAKVLIDENSRVLVETPTYLGALQAFTPMEPSVVAVASDDEGVLIDDLKAKVGTGADKARFLYVLPNFQNPTGRTMTEARRAALVKAAAELNLPLVEDNPYGDLWFDNPPPAPLTARNPEGCIYMGSFSKVLAPGLRLGFVVAPKAVYPKLLQAKQAADLHTPGYNQRLVAEVMKGNFLDRHVPTIRALYKQQCEAMLAALTQEMAGLGVEWNRPDGGMFLWVRLPEGMSAIELLPQAVERNVAFVPGAAFYADNADPRTLRLSFVTSTVEQIATGIAALAAAIRSHKG Shewanella oneidensis MR-1 MR1 200835 SO1670 fumarylacetoacetate hydrolase (EC 3.7.1.2) # Important for utilization of phenylalanine (which is catabolized via tyrosine due to phenylalanine-4-hydroxylase SO1666) , gelatin, or CASamino acids. This protein encodes the missing fumarylacetaectate hydrolase. fumarylacetoacetate hydrolase family protein (NCBI ptt file) MKLASYNNGRRDGQLMLVSRDLTQTVAVPAIAHTMQQLLDGWELLKPQLQELYDALNEGKLPNTQTFDETKCLSPLPRAYQWADGSAYVNHVELVRKARGAEMPETFWTDPLFYQGGSDSFIAPKADIPLASEDWGIDFESEIAVITDDVPMGVSAENAAKHIKLLMLVNDVSLRNLIPAELAKGFGFFQSKPSSSFSPVAITPDELGHRWEDSKVHLPLITYLNGELFGRPNAGVDMTFNFSQLVSHVAKTRPLGAGAIIGSGTISNYDRSAGSSCLAEKRMLEVIADGKASTPFMRFGDTVRIEMLDDNGVSIFGSIDQKVVEYKA Burkholderia phytofirmans PsJN BFirm BPHYT_RS13545 BPHYT_RS13545 3-hydroxyadipyl-CoA dehydrogenase (EC 1.1.1.35) # Specifically important in carbon source L-Phenylalanine. Phenylalanine is catabolized via phenylacetyl-CoA. This protein contains both a 3-hydroxyacyl-CoA dehydrogenase domain, which fits with the requirement for 3-hydroxyadipyl-CoA dehydrogenase in the phenylacetate pathway, and a enoyl-CoA hydratase domain, whose role is uncertain. (BPHYT_RS17335 is probably the trans-2,3-dehydroadipyl-CoA hydratase) 3-hydroxyacyl-CoA dehydrogenase MTPNPSADVVSRELRGKVLLVTIDHAPVNALSADVRRGLLAAIEAADADKAVEAVLIVGAGRNFIAGADIREFGKPPVPPSLPDVCNRIEACTKPVVAAIHGAALGGGLEVALAAHYRIAVDGAKLGLPEVQLGLLPGAGGTQRTPRLIGAQAALDLILSGRHASAKEALAFGLIDRLGSSDDILAEGLAYVHELLAAHAPVRRTRDAAALSDRAASLAAVATARAETAKKSRGLFSPLKIVDAVEAAIEQPFDEGLRVERKLFLECIDSPQRAGLIHAFFAEREVLKAPETRAAKPRTLNTIGVVGGGTMGAGIAVAVLDAGLPVTMIERDDASLARGRAHIEKVYDGLIAKGRLSAEKKAALMSRWSGSTSYDALAGADLVIEAVFEDLAVKQAVFAELDRVCKAGAVLATNTSYLDIDALASSVSRPADVIGLHFFSPANIMKLLEVVVPKQVSADVVATAFELAKKLRKTPVRAGVCDGFIGNRVLAVYRSAADAMMEDGASPYQIDAAVRAFGFPMGPFQVVDLAGGDIGWAARKRRAATRNPAARYVQIADRLCERGWFGQKSGRGFYLYPEGSRSGTPDPEVEAIIDAERARAGITPRSFTDEEIIRRYMAAMINEGANVVHERIALRPLDVDVTFLYGYGFPRYRGGPMKYADMVGLPKILADIREFAKEDPLFWKPSPLLIELVERGADFASLNQSV Burkholderia phytofirmans PsJN BFirm BPHYT_RS28235 BPHYT_RS28235 L-rhamnose-1-dehydrogenase ( EC 1.1.1.173) # Specifically important in carbon source L-Rhamnose monohydrate. This is the first step in its catabolism. short-chain dehydrogenase MLLKDKVVIVTGGSRGIGRAIAVACAAEGADVAINYWGDNDVSYGRRSAVAEVVAEIEALGRRVIAIEGNVAARETGQQLVRHTVEAFGKVDVLASNAGICPFHAFLDMPPEVLESTVAVNLNGAFYVTQAAAQQMKLQGTGGAIVATSSISALVGGGMQTHYTPTKAGVHSLMQSCAVALGPYGIRCNSVMPGTIATDLNAQDLADEAKKAYFEKRIPLGRLGRPEDVADCVTFLASDRARYVTGAALLVDGGLFVNLQ Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_2738 electron transfer component of the anthranilate 1,2-dioxygenase system (EC 1.14.12.1) # Specifically important in carbon source L-Tryptophan. Tryptophan is catabolized via kynurenine and anthranilate, so this system acts on anthranilate, not benzoate. The subunits of the other component are PfGW456L13_2739 and PfGW456L13_2740. benzoate dioxygenase, ferredoxin reductase component; Anthranilate dioxygenase reductase MNHKVAFSFADGKTSFFEVKPNELLLDAALRNGVNIPLDCREGVCGTCQGRCESGRYTQDYVDDEALSEQDLAQRKMLSCQTRVQSDASFYFDFDSSLCNAGATQLLQAVITGVEQVSATTAILHLDACSHPRQLDFLPGQYARLHVPGTDEWRSYSFANRPNPDNQLQFLIRLLPDGVMSNFIREHCRPGEVLEFEAPLGSFYLRQVSKPLVLVAGGTGLSAFLGMLDTIAEQGGCGHPIQLFYGVTQDNDLCETQRLADYRDKIANFDYHLVVSKPSEHWKGKTGWIPDHFDRQSFEANPFDIYLCGPPPMVEAVKTWFSDQKIERFQMYYEKFIESNSKH Pseudomonas simiae WCS417 WCS417 GFF4631 PS417_23695 electron transfer component of the anthranilate 1,2-dioxygenase system (EC 1.14.12.1) # Specifically important in carbon source L-Tryptophan. Tryptophan is catabolized via kynurenine and anthranilate, so this system acts on anthranilate, not benzoate. The subunits of the other component are PS417_23685 and PS417_23690. anthranilate dioxygenase reductase MNHKVAFSFADGKTLFFPVGANEILLDAALRNGIKIPLDCREGVCGTCQGRCESGDYSQDYVDEEALSSLDLQQRKMLSCQTRVKSDATFYFDFDSSLCNAPGPVQVKGTVSAVEQVSASTAILQVQLDQALDFLPGQYARLSVPGTDSWRSYSFANLPGNHLQFLVRLLPDGVMSNYLRERCQVGDELLMEAPLGAFYLRHVTQPLVLVAGGTGLSALLGMLDQLAANGCEQPVHLYYGVRGAEDLCEAARIRAYAAKIPNLRYTEVLSAPSEEWSGKRGYLTEHFDLAELRDGSADMYLCGPPPMVESIQQWLADQALDGVQLYYEKFTQSNI Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_25665 AO353_25665 3-hydroxy-isobutyryl-CoA hydrolase (EC 3.1.2.4) # Specifically important for: L-Valine. Hydroxyisobutyryl-CoA is an intermediate in valine degradation. But is this the hydrolase (forming 3-hydroxyisobutyrate) as suggested by SEED, or is it the hydratase (or hydro-lyase in reverse) converting methylacrylyl-CoA to (S)-3-hydroxy-isobutanoyl-CoA, as suggested by KEGG? Characterized homologs are hydrolases (Q81DR3; Q5XIE6) crotonase MTAQVSSQATHGIDASANDVLAEVRNHIGHLTLNRPAGLNAITLDMVRSLHRQLDAWSKDPHIHAVVLRGAGEKAFCAGGDIRSLYDSFKSGGTLHEDFFVEEYALDLAIHHYRKPVLALMDGFVLGGGMGLVQGADLRVVTERSRLAMPEVAIGYFPDVGGSYFLPRIPGELGIYLGVSGVQIRAADALYCGLADWYLESQKLAELDQHLDSLEWHDTPLKDLQGLLAKLALQQLPDAPLQALRPTIDHFFALPDVPSIVEQLRTVTVADSHDWAMTTADLLDSRSPLAMGVTLEMLRRGRQLSLENCFALELHLDRQWFERGDLIEGVRALLIDKDKSPRWNPPTVQALDAKHVASFFSGFDQSGS Burkholderia phytofirmans PsJN BFirm BPHYT_RS13910 BPHYT_RS13910 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92); possible 5-dehydro-2-deoxyphosphogluconate aldolase DUF2090 (EC 4.1.2.29) # Specifically important in carbon source m-Inositol. This protein is a fusion of 5-keto-deoxygluconate kinase and DUF2090. As DUF2090 has distant similarity to aldolases, it may provide the missing 5-dehydro-2-deoxyphosphogluconate aldolase activity. 5-dehydro-2-deoxygluconokinase MDQSITSSGVTSASAPATGSRFAPGRSRDIVCLGRLAVDLYAQQVGARLEDVSSFAKYLGGSSANIAFGCARLGLASSMLARVGNDHMGRFLTETLTKEGCDVSHVRIDQERLTALVLLGLKDRDTFPLIFYRENCADMAVDEADFDEAYIASSKALLITGTHFSTEQVNRTSRRALDYARRNQVRTVLDIDYRPVLWGLTGKADGETRFVASEGVTAHLQRILPLFDLVIGTEEEFRIAGGKTELVDALAMVRAVTPATLVLKRGPMGCQIIDGAVPASLDDLPIHGGVEVEVLNVLGAGDAFASGFLSGWLRDQPLEACARIANASGALVVSRHGCAPAMPTPAELDYFLREAKADPQRMRRPDRDATLARLHRVSPARKQWDEVLGFAFDHRNQFFELAQQTGADDARIARLKGLFVEAVAQTESALGLQNRIGVLIDDRYGQDALNAATGRGWWIGRPVELPGSVPLVFDHGRSIGTTLIPWPQEHIVKCLVQFHPDEPIEQRLEQEAQLRALYDATQASGHELLLEVIPPKHAHLPQAPDTVYRALKRLYNIGIYPEWWKLEPMDAAQWRNVDALIAERDPYCRGVVLLGLSAAVEQLDEGFRAAAQSATCRGFTVGRTIFHEPSHAWLAGEIGDDELIGRVRRTFETLIASWRATRGASAAQSSAPKPVHQEQAA Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_512 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92); possible 5-dehydro-2-deoxyphosphogluconate aldolase DUF2090 (EC 4.1.2.29) # Specifically important in carbon source m-Inositol. This protein is a fusion of 5-keto-deoxygluconate kinase and DUF2090. As DUF2090 has distant similarity to aldolases, it may provide the missing 5-dehydro-2-deoxyphosphogluconate aldolase activity. 5-keto-2-deoxygluconokinase (EC 2.7.1.92) / uncharacterized domain MGQTRFASGRQLDVICLGRLGVDLYAQQVGARLEDVASFAKYLGGSSANIAFGTARLGLRSAMLSRVGDDHMGRFLVESLAREGCDVSGIKVDPERLTAMVLLGIKDRETFPLVFYRENCADMALRVEDIDETFIASSKALLITGTHFSTDGVYKASTQALDYAEKHNVKCVLDIDYRPVLWGLAGKADGETRFVADQKVSQHVQGILPRFDLIVGTEEEFLIAGGSEDLLSALRTVRSLTAATLVVKLGAQGCTVIHGAIPARLEDGALYPGVRVEVLNVLGAGDAFMSGFLAGWLEDASDERCCQLANACGGLVVSRHACAPAMPTRAELDYLFKSPVPITRPDQDAVLQRLHQVSVPRKTWKQLFIFAFDHRWQLVELAQKGGRDLNCIGDLKQLFIQAVERVEADLQRQGIEADVGLLADQRFGQDSLNAATGRGWWVARPVEVQNSRPLAFEHGRSIGSNLIAWPQEQIIKCLVQFHPDDEPLLRLEQEAQLMGLYKASQVSGHELLLEVIPPKDHPSPHPDVLYRALKRLYNLGIFPAWWKIEAQSAQEWKQLDELIQQRDPYCRGVVLLGLNAPAAALAEGFRQASQSTTCRGFAVGRTIFQEPSRAWLAGEIDDETLIRQVQGRFVELIEAWRSARA Klebsiella michiganensis M5al Koxy BWI76_RS03085 BWI76_RS03085 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92); possible 5-dehydro-2-deoxyphosphogluconate aldolase DUF2090 (EC 4.1.2.29) # Specifically important in carbon source m-Inositol. This protein is a fusion of 5-keto-deoxygluconate kinase and DUF2090. As DUF2090 has distant similarity to aldolases, it may provide the missing 5-dehydro-2-deoxyphosphogluconate aldolase activity. 5-dehydro-2-deoxygluconokinase MNAAVKRLDVICIGRVAVDLYAQQIGARLEDVASFSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDTEYLITDKQRLTALVMLGIKDQETFPLIFYRDNCADMALSPEDIKEEYIASSRALAVTGTHLSHANTREAVLKALEYARRHGLRTALDIDYRPVLWGLTSLGDGETRFIESGQVTSQLQEVLHLFDLVVGTEEEFHIAGGSTDTLTALKNVRNATKATLVCKRGPMGCVVLEGAIPDNWDSVPLQQGVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGCAPAMPTKAELDDYLSRAESVPRPDIDDRLNHLHRVTSRRQAWPELCIFAFDHRKQLADLALETGRDESCIPQLKLLLLAAAEAAADEAGLDGRSGILADGTYGQRSLNAITGKGWWIGRPIEMPSSRPLRLEHGNIGSQLIDWPLEHVVKCLVFYHPADPAELRAEQDALLLEVWQACNKSGHELLLEIILPENGPDKDERHYHDMLEHFYQLGIQPDWWKLPPLSSAEWERIGKLIAREDSWCRGILILGLDAPSDRLRAGFAEAAKHPMIKGFAVGRTIFGQPSRRWMQGELSDEALINEVKRNYLTLIGYWREARG Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_21335 AO353_21335 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92); possible 5-dehydro-2-deoxyphosphogluconate aldolase DUF2090 (EC 4.1.2.29) # Specifically important in carbon source m-Inositol. This protein is a fusion of 5-keto-deoxygluconate kinase and DUF2090. As DUF2090 has distant similarity to aldolases, it may provide the missing 5-dehydro-2-deoxyphosphogluconate aldolase activity. 5-dehydro-2-deoxygluconokinase MGQTRFASGRQLDLICLGRLGVDLYAQQVGARLEDVSSFAKYLGGSSANIAFGTARLGLKSAMLSRVGDDHMGRFLVESLAREGCDVSGIKVDPERLTAMVLLGLKDRETFPLVFYRENCADMALRAEDISEAFIASSKALLITGTHFSTDGVYKASIQALEYAEKHNVKRILDIDYRPVLWGLAGKADGETRFVADQQVSQHVQKILPRFDLIVGTEEEFLIAGGSEDLLSALRNVRRLTAATLVVKLGPQGCTVIHGVIPVRLEDGAIYPGVRVEVLNVLGAGDAFMSGFLSGWLEDASDERCCQLANACGGLVVSRHACAPAMPTRAELDYLFNSPVPITRPDQDAVLQRLHQVSVPRKTWKQLFIFAFDHRGQLVELAQKGGRELSSIGELKQLFIKAVERVEADLRRQGIEADVGLLADQRFGQDSLNAATGRGWWVARPVEVQGSRPLAFEHGRSIGSNLIAWPQEQIIKCLVQFHPDDEPLLRLEQEAQIKGLYQAAQVSGHELLLEIIPPKDHPSAHPDVLYRAIKRLYNLGIFPAWWKIEAQSSEEWKQLDDLIQERDPYCRGVVLLGLNAPAATLAEGFAQASQSKTCRGFAVGRTIFQEPSRAWLAGEIDDEALIQRVQGTFVELINAWRTARA Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_23160 AO356_23160 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92); possible 5-dehydro-2-deoxyphosphogluconate aldolase DUF2090 (EC 4.1.2.29) # Specifically important in carbon source m-Inositol. This protein is a fusion of 5-keto-deoxygluconate kinase and DUF2090. As DUF2090 has distant similarity to aldolases, it may provide the missing 5-dehydro-2-deoxyphosphogluconate aldolase activity. 5-dehydro-2-deoxygluconokinase MGQTRFASGRQLDVICLGRLGVDLYAQQVGARLEDVSSFAKYLGGSSANIAFGTARLGLRSAMLSRVGDDHMGRFLVESLAREGCDVSGIKVDPERLTAMVLLGIKDRETFPLVFYRENCADMALRAEDIDETFIASSKALLITGTHFSTDGVYKASIQALDYAQKHQVKRVLDIDYRPVLWGLASKADGETRFVADQKVSQHVQSILPRFDLIVGTEEEFLIAGGSEDLLTALRTVRSLTAATLVVKLGPQGCTVIHGAIPARLEDGAIYPGVRVEVLNVLGAGDAFMSGFLAGWLEDASDERCCQLANACGGLVVSRHACAPAMPTRAELDYLFDSPVPITRPDQDVVLQRLHQVSVPRKTWKQLFIFAFDHRGQLVELAQKGGRELSSIGELKQLFIQAVARVEADLRHQGIEADVGLLADQRFGQDSLNAATGRGWWVARPVEVQGSRPLAFEHGRSIGSNLIAWPQEQIIKCLVQFHPDDEPLLRLEQEAQLMGLYKASEASGHELLLEVIPPKDHPSPHPDVLYRALKRLYNLGIFPAWWKIEAQGADEWQQLDELIQQRDPYCRGVVLLGLNAPAAALAEGFRQASQSSTCRGFAVGRTIFQEPSRAWLAGEIDDETLIQQVQGRFVELIEAWRAARS Sinorhizobium meliloti 1021 Smeli SMc01165 SMc01165 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92); possible 5-dehydro-2-deoxyphosphogluconate aldolase DUF2090 (EC 4.1.2.29) # Specifically important in carbon source m-Inositol. This protein is a fusion of 5-keto-deoxygluconate kinase and DUF2090. As DUF2090 has distant similarity to aldolases, it may provide the missing 5-dehydro-2-deoxyphosphogluconate aldolase activity. sugar kinase MSQIPSAQVPSGAGAKPLDLITIGRASVDLYGQQIGTRLEDVASFAKSVGGCPCNISVGTARLGLKSALLTRVGDEQMGRFIREQLQREGVETRGIVTDPERLTALAILSVENDKSFPLLFYRDNCADNALCEDDISEDFIRSARAVLVTGTHFAKPNADAAQRKAIRIAKESGARIVFDIDYRPNLWGLAGHDAGESRYIASDRVSAHLKTVLGDCDLIVGTEEEVLIASGESDLLAALKTIRSLSKATIVLKRGPMGCIVYDGPISDDLEDGIVGKGFPIEVYNVLGAGDAFMSGFLRGWLTGEPHATSATWANACGAFAVSRLLCAPEIPTWTELQYFLEHGSKEKALRKDEAINHVHWATTRRRDIPLLMALAVDHRSQLEDIAEGNPELLSRIPAFKVLAVKAAAEVAQGRSGFGMLIDDKYGRDALYAAGAHRDFWIGKPIELPGSRPLTFEFSQDLGSRLVDWPVDHCIKVLSFYHPDDPAELKAAQVAKLRSAFEAARKVGREILIEIIAGKHGKLDDRTIPRALEELYDAGLKPDWWKLEPQASRAAWAAIDAVIETRDPLCRGVVLLGLEAPYEVLKDGFAAARTSKTVKGFAVGRTIFADAAKAWLAGRMTDEQAVSDMAAKFKALVDLWLQLGETKAA Burkholderia phytofirmans PsJN BFirm BPHYT_RS34225 BPHYT_RS34225 L-fucose dehydrogenase (EC 1.1.1.122) Specifically important for: L-Rhamnose monohydrate; L-Fucose. This is the only good candidate for the L-fucose dehydrogenase, but there is another putative rhamnose dehydrogenase (BPHYT_RS28235) that also seems to be required for rhamnose utilization. So the phenotype of this gene (BPHYT_RS34225) on rhamnose could be due to polar effects. aldo/keto reductase MTATIGSKIGQRRRIGRGPLQVTGLGLGTAPLGGLYRDLSDEEAHATIAAAWDAGVRYFDTAPHYGNTKAEHRLGDALRRYPRADYVLSTKVGRRFVPRTTPFDDKEGWQNPLPFEAIYDYTHDGILRSFEDSQQRLGIVDIDILLVHDIGRVTHGDNHPHYWRQLTEGGGFRALDALRSSGAIKAVGLGVNEGAAILDAMAEFDIDCALLAGRYTLLEQTTLDDLLPACEKRGVSILLGGAFNSGILARGVQGDLKFNYGEAPPEVIERVARLEAVCRTHGVPLAAAALQFPYAHPTVATVLTGARSADELRENAASFELPIPAALWFALREEGLLDSRAPAPED Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_1959 D-sorbitol dehydrogenase (EC 1.1.1.14) # Specifically important in carbon source D-Sorbitol. This is the first step in sorbitol degradation. Multiple polyol-specific dehydrogenase (EC 1.1.1.-) MKRLEGKSALITGSARGIGRSFAQAYIGEGATVAIADINLERAQATASELGPQAYAVEMDVTRQASIDAAIAEVVARAGKLDILVNNAALFDLAPITEITRESYDKLFAINVSGTLFTLQAAAKQMISQGHGGKIINMASQAGRRGEALVGVYCATKAAVISLTQSAGLNLIKHKINVNAIAPGVVDGEHWDGVDALFAKHENRPLGEKKRLVGLEVPYGRMGTAEDLVGMAIFLAGSESDYIVAQTYNVDGGNWMS Pseudomonas putida KT2440 Putida PP_0154 PP_0154 Succinyl-CoA:acetate CoA-transferase (EC 2.8.3.18) # Specifically important in carbon source Sodium acetate; carbon source Potassium acetate. 48% identical to B3EY95 from Acetobacter, which uses succinyl-CoA to form acetyl-CoA and aids growth on acetate, see PMID:18502856 propionyl-CoA:succinate CoA transferase MYRDRIRLSSLHSKVMSAADAAGLIEDGMTVGMSGFTRAGEAKAVPHALAERAKQSPLKISLMTGASLGNDLDKQLTEAGVLARRMPFQVDSTLRKAINDGQVMFIDQHLSETVEQLRNQQLKLPDIAVIEAVAITEQGHIVPTTSVGNSASFAIFAKQVIVEINLSHNTNLEGLHDIYIPTYRPTRTPIPLVKVDDRIGSTAIPIDPAKIVGIVISDQPDSPSTVLPPDDETQGIADHLINFLKKEVDAGRMTNKLGPLQAGIGSIANAVMCGLIESPFEDLTMYSEVLQDSTFDLIDAGKLSFASGSSITLSTRRNADVFGNLERYKDKLVLRPQEISNHPEVVRRLGIIGINTALEFDIYGNVNSTHVCGTRMMNGIGGSGDFARNAHLAVFVTKSIAKGGAISSVVPMVSHVDHTEHDVDILVTEQGLADLRGLAPRERARAIIDNCVHPDYRAALNDYFDRACQRGGHTPHILREALSWHENLEETGRMLAS Shewanella sp. ANA-3 ANA3 7022768 Shewana3_0023 fadA Acetyl-CoA C-acyltransferase (EC 2.3.1.16) Specifically important for utilizing Tween 20. Automated validation from mutant phenotype: the predicted function (KETOACYLCOATHIOL-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 3-ketoacyl-CoA thiolase (RefSeq) MKQAVIVDCIRTPMGRSKAGVFRNVRAETLSAELMKGLLLRNPQLDPNTIEDVIWGCVQQTLEQGFNIARNASLLAGIPKTAGAVTVNRLCGSSMEAIHQAARAIMTGMGDTFIIGGVEHMGHVPMNHGVDFHPGLANNVAKASGMMGLTAEMLGKLHGITREQQDAFAVRSHQRAHAATVEGRFAKEIYGIEGHDANGALIKVLHDEVIRPETSMESLAALRPVFDPANGTVTAGTSSALSDGASAMLVMEESKARALGLPIRARIRSMAVAGCDAAIMGYGPVPATQKALARAGITVNDLDVIELNEAFAAQSLPCVKDLGLLDVVEDKINLNGGAIALGHPLGCSGARISTTLINLMEHKDATLGLATMCIGLGQGIATVFERV Shewanella sp. ANA-3 ANA3 7022769 Shewana3_0024 fadB Enoyl-CoA hydratase (EC 4.2.1.17); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) Specifically important for utilizing Tween 20. Automated validation from mutant phenotype: the predicted function (ENOYL-COA-HYDRAT-RXN, OHACYL-COA-DEHYDROG-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. multifunctional fatty acid oxidation complex subunit alpha (RefSeq) MIYQSPTIQVELLEDNIAKLCFNAPGSVNKFDRETLASLDAALDSIKQQSNIQALVLTSGKDTFIVGADITEFLGLFAQDDAVLLSWIEQANAVFNKLEDLPFPTASAIKGFALGGGCETILATDFRIADTTAKIGLPETKLGIIPGFGGTVRLPRVIGADNALEWITTGKDQRPEDALKVGAVDAVVAPEALEAAAIQMLKDAVAEKLDWQARRQRKMSPLTLPKLEAMMSFTTAKGMVFAVAGKHYPAPMAAVSVVEQAATKGRSDALQIEHQAFIKLAKTDVAKALIGIFLNDQLVKGKAKKAGKLAKDVKSAAVLGAGIMGGGIAYQSASKGTPIVMKDIAQPALDLGLGEAAKLLSAQVARGRSTPEKMAKVLNNITPALDYAPVKHADVVVEAVVEHPKVKAQVLAEVEQYVSEDAIIASNTSTISINLLAKSMKKPERFCGMHFFNPVHKMPLVEVIRGEHSSEETIASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFNGLLAEGGDFAAIDKVMEKQFGWPMGPAYLLDVVGLDTGHHAQAVMAEGFPDRMGKSGNDAIDVMFENKRLGQKNGKGFYAYSVDSRGKPKKDVDPTSYELLKAAFGEQKAFDADEIIARTMIPMIIETVRCLEEGIVASPAEADMGLVYGLGFPPFRGGVFRYLDTMGVANFVALADKYAHLGGLYQVTDAMRALAANNGSYYQA Shewanella sp. ANA-3 ANA3 7022818 Shewana3_0069 Fructokinase (EC 2.7.1.4) Specifically important for utilizing Sucrose. Automated validation from mutant phenotype: the predicted function (FRUCTOKINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. ribokinase-like domain-containing protein (RefSeq) MTVLLSFGEVLVDLLPTDISGKSHQAIAGGAPANVAVGYAKLGGKSYFAGGISTDDYGAMLKQALANEGVVTDYLTQVPEAPTATVVVNLDEHGERTFEFNRQGTADLCYSPRHFDAIPWQQMDIFHLCSNTFTEASIFNASLYGACCANSFNKIVSFDVNLRLSLWPDTALLAERVEQCFRYTQVLKMSREEAEYLALTRNKSFEDYLQFCLAHGVEVILITDGANPVQCITVNERFSVPVPQIKAVDTTAAGDSFMAGFLFALGFELAFDLEHLTLKHRLACQAQLRKAIEFAVRCGAVTCGQKGAFPALPTLSQVS Shewanella sp. ANA-3 ANA3 7023381 Shewana3_0611 Arginine N-succinyltransferase (EC 2.3.1.109) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (ARGININE-N-SUCCINYLTRANSFERASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. arginine succinyltransferase (RefSeq) MLIIRPIQAGDFESLYQIAEESGHGFTSLPVNADLLRHKIARAEASFVKVIDKPFDEGYLMVLEDTATREVVGTCAIEAAVGMEDAFYHYRLGTEVYHSEQIEVRNEVETLTLCHDYTGAAELCTLFLREGYRKGNNGRMLSRSRFLFLAQHAKRFGETVIAEMRGVSDSDGNSPFYCWLQKNFLGIDFIQADYLSGLGKKAFMAEMMPRNPVYVCLLPEEAQKVIGEVHTNTRPALSLLQAEGFRCRGYVDIFDGGPTVECRLTDIRAVRESRLLTVDIGEMPESDKQFIVSNTQLANYRATSACLAVDDKTEQVVISPELAEGLLLAKGDQIRILAM Shewanella sp. ANA-3 ANA3 7023590 Shewana3_0819 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) Specifically important for utilizing L-Proline. Automated validation from mutant phenotype: the predicted function (1.2.1.88, 1.5.5.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase (RefSeq) MEAITMFKASEVLAGRYDSANLDELFKAVTDNYIVDEEQYLSELIKLVPSSDEAIERVTRRAHELVNKVRQFDKKGLMVGIDAFLQQYSLETQEGIILMCLAEALLRIPDAATADALIEDKLSGAKWDEHLSKSDSVLVNASTWGLMLTGKIVKLDKKIDGTPSNLLSRLVNRLGEPVIRQAMMAAMKIMGKQFVLGRTMKEALKNSEDKRKLGYTHSYDMLGEAALTRKDAEKYFNDYANAITELGAQSYNENESPRPTISIKLSALHPRYEVANEDRVLTELYDTVIRLIKLARGLNIGISIDAEEVDRLELSLKLFQKLFNADATKGWGLLGIVVQAYSKRALPVLVWLTRLAKEQGDEIPVRLVKGAYWDSELKWAQQAGEAAYPLYTRKAGTDVSYLACARYLLSDATRGAIYPQFASHNAQTVAAISDMAGDRNHEFQRLHGMGQELYDTILSEAGAKAVRIYAPIGAHKDLLPYLVRRLLENGANTSFVHKLVDPKTPIESLVVHPLKTLTGYKTLANNKIVLPTDIFGSDRKNSKGLNMNIISEAEPFFAALDKFKSTQWQAGPLVNGQTLTGEHKTVVSPFDTTQTVGQVAFADKAAIEQAVASADAAFATWTRTPVEVRASALQKLADLLEENREELIALCTREAGKSIQDGIDEVREAVDFCRYYAVQAKKLMSKPELLPGPTGELNELFLQGRGVFVCISPWNFPLAIFLGQVSAALAAGNTVVAKPAEQTSIIGYRAVQLAHQAGIPTDVLQYLPGTGATVGNALTADERIGGVCFTGSTGTAKLINRTLANREGAIIPLIAETGGQNAMVVDSTSQPEQVVNDVVSSSFTSAGQRCSALRVLFLQEDIADRVIDVLQGAMDELVIGNPSSVKTDVGPVIDATAKANLDAHIDHIKQVGKLIKQMSLPAGTENGHFVSPTAVEIDSIKVLEKEHFGPILHVIRYKASELAHVIDEINSTGFGLTLGIHSRNEGHALEVADKVNVGNVYINRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLTRFVTEKTRTNNITAIGGNATLLSLGDSDA Shewanella sp. ANA-3 ANA3 7023976 Shewana3_1184 Glutaminase (EC 3.5.1.2) Specifically important for utilizing L-Glutamine. Automated validation from mutant phenotype: the predicted function (GLUTAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glutaminase (RefSeq) MPEQALLEEVVDKVRPLLGQGKVANYIPALANVDAGKLGIAVTTIDGETIGAGDYLEPFSIQSISKVFSLTLALTLYEETEIWSRVGKEPSGHSFNSLVQVELERGKPRNPFINAGALVIADLLQSRLGAPKHRMLELVRALSQNDKVCFDKQVADSEYQHSARNAAIAYLMKSFGNFQGDVDTVLRTYFHYCALKMNCADLSRAMLYLANRGKTLDGTELISQVQTRQLNALLATSGLYDGAGEFAYRVGMPGKSGVGGGIIAVIPGELSVCVWSPELDNQGNSLAGTAMLEHLSQRLGRSIF Shewanella sp. ANA-3 ANA3 7024494 Shewana3_1672 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (RXN0-2301) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. isovaleryl-CoA dehydrogenase (RefSeq) MNSLYTSLNFGLGEEVDMLRDAVQDFAKHEIAPIAAKVDHDNAFPNEIWPVLGGMGLLGVTVPEEYGGANMGYLAHVVAMEEISRASASIGLSYGAHSNLCVNQINRNGNAEQKAKYLPKLVSGEHIGALAMSEPNAGSDVVSMKLHARKEGDRYILNGNKMWITNGPDANTYVIYAKTDLTKGAHGITAFIVERGFKGFSQAQKLDKLGMRGSNTCELVFEDVEVPEENILGGLNNGVKVLMSGLDYERVVLSGGPLGIMNACMDIVVPYIHEREQFGKSIGEFQLVQGKLADMYTGMNAAKAYVYSVAKSCDRGETTRKDAAGAILYSAELATKMALDAIQLLGGNGYVNEYATGRLLRDAKLYEIGAGTSEIRRMLIGRELFNESK Shewanella sp. ANA-3 ANA3 7024550 Shewana3_1728 Succinylarginine dihydrolase (EC 3.5.3.23) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (SUCCARGDIHYDRO-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. succinylarginine dihydrolase (RefSeq) MKHFEANFDGLVGPTHNYAGLSFGNVASLNNAALVSNPKAAAKQGLQKAKALADLGMIQGMLAPQERPDLNTLRRIGFSGSDAQVLQQAAKTAPALLNACCSASSMWTANAATVSPSADTRDGKLHFTPANLVDKLHRSIEPTTTGRILTATFNDPHYFHHHNHLPEHNSFGDEGAANHTRLCQEYGHAGVELFVYGQEATNPNAPRPQKYPARQTLEASMAIARLHQLEEDNCVFIQQNPDVIDQGVFHNDVIAVGNQNVLFYHEQAFLNTQAKLDEIRRKLDTELFFIEVPTTKVAINNAVKSYLFNTQIITLPSGEMAIIAPTDCQENPAVYAYLNELLTLNTPIKQVLYFDVKQSMQNGGGPACLRLRVAMNEREVAAANQHTLLNDALFARLNTWVDKHYRDRLSTQDLADPQLVVESRTALDELTQIMKLGSVYPFQR Shewanella sp. ANA-3 ANA3 7024891 Shewana3_2065 araD L-ribulose-5-phosphate 4-epimerase (EC 5.1.3.4) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (RIBULPEPIM-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-ribulose-5-phosphate 4-epimerase (RefSeq) MSFLELKREVYEANMELEKRKLVTYTFGNVSQIDRQLGVIGIKPSGVPYEDLKVEDIVIVDLENQIVEGRMRPSSDTKTHTYLYRQWQSIGGITHTHSTYATAWAQAQIAIPCLGTTQADYVYGEIPCTAVMRNDQISRDYEEETGVQILDCFADRDPNESPMVIVAGHAPFTWGANAAKSVYHAVLLEEIARMAYLTKTLSPGISQLKQELIDKHYLRKHGKDAYYGQSK Shewanella sp. ANA-3 ANA3 7024892 Shewana3_2066 L-arabinose isomerase (EC 5.3.1.4) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (ARABISOM-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-arabinose isomerase (RefSeq) MKAFKQKQVWFITGSQDLYGPKVLEQVAKNSEQIVHGFNESSAISIEVVYKPTVKSPREIHAVCQAANSDENCVGVILWMHTFSPAKMWIAGLNELSKPFMHLHTQFNAELPWSEINMNYMNTHQSAHGCREFGFIGTRMRKERKVVVGHWQSSDVQAQIDDWCRAAAGWHESQNLRIARFGDNMRQVAVTEGDKVAAQIQFGYEVHAYSLGELNEAIADIAEGDVTAQLDRYASEYQVGNELFGDEYQLDRLRKEAKIELGLTQFLTQGGFGAFTNCFENLTGMTGLPGLATQRLMANGFGYGGEGDWKTAAMVRIMKVMGQGRAGGTSFMEDYTYNFGATDQVLGAHMLEVCPSIAAAKPRLEVHRHTIGVRCDVPRLLFTGKAGPAINVSTIDLGNRFRIILNELDTVTPPQDLPNLPVASALWEPRPNLAVAAAAWIHAGGAHHSAYSQAITTDQIVDFAEMAGAELVIIDADTKIREFKNELRQNSVYYGLARGL Shewanella sp. ANA-3 ANA3 7025148 Shewana3_2311 Alpha-glucosidase (EC 3.2.1.20) Specifically important for utilizing D-Maltose monohydrate. Automated validation from mutant phenotype: the predicted function (3.2.1.20) was linked to the condition via a SEED subsystem. This annotation was also checked manually. alpha amylase, catalytic region (RefSeq) MSELTWWRGAVIYQIYPRSLLDTNGDGVGDLRGIITKLDYIASLNVDAIWISPFFKSPMADFGYDISDYREVDPLFGTMQDFDELIEKAHQRGIKVIIDQVLSHTSDQHAWFCESRESRTNPKADWYVWAEPKEDGTAPNNWLAIFGGCAWEWEPRRQQYYLHNFLRSQPDINFHNPDVRQAVLDNVEFWLKKGVDGFRLDAITFCYHDEQLRDNPPKPKDKRQGRGFSEDNPYAYQYHYYNNDRPQTILFIEELRQLINRYPGAVTLGEVSAEDSLAVMAAYTKGEDRLHMAYSFELLTDDYSAAYIRQTVEALEASIGDGWPCWAIGNHDAQRVASRWGRGKQTSDMVKMLNAMVNSLRGSVCSYQGEELGLTEAPIEYHELQDPFGKTFWPMFKGRDGCRTPMPWEQNADFSGFSQVTPWLPIAQAHRALAVDVQEADSQSMLHGYRQFLAWRKGYPALVEGEIEFLDAPEPLLVFVRTSGEQKLLVCFNLQDTEQALSLDALSIQQEITGHGLKTAQRIADTLTFSAYACFYALLN Shewanella sp. ANA-3 ANA3 7025418 Shewana3_2573 Cytidine deaminase (EC 3.5.4.5) Specifically important for utilizing Cytidine. Automated validation from mutant phenotype: the predicted function (CYTIDEAM2-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. cytidine deaminase (RefSeq) MQDRFIKSITQLPTPLADALIPLLHQNFAGHIDAQQLAELVQSSKMTEAEVLLALLPIAAALAKPPISEFYVGAIAKGKSGDIYMGANLELLGEALFHSVHAEQSAISHAWLSGESQIVDMIVNASPCGHCRQFMNELVEGGQIKIHLPSQDSHLLSYYLPYAFGPKDLNVQSPLLVKQETEFALDSSDPMVIEALDHAGLSYAPYTQSYAAVVLETADGATYCGRYAENAAFNPSMLPMQMALSNLTRHNRDFGEIRRAVLVESSQGKISLVGATMDALHAVAAIELEHIVVDPV Shewanella sp. ANA-3 ANA3 7025964 Shewana3_3112 N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (NAG6PDEACET-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-acetylglucosamine 6-phosphate deacetylase (RefSeq) MKFTLIAEQLFDGEAFHRDVPVTIEDGLIASLDTASGAKEIRYPGTLVPGFIDVQVNGGGGALFNSSPTVACIETIGKAHARFGTTGFLPTLITDDVQVMAKAADAVASAVAQKSAGVLGVHFEGPHLSVPKKGVHPQGFIREITEAELAIFCRQDLGIRVVTLAPENVSPEVIRLLVESGVKVCLGHSNADYDTVVAALAAGATGFTHLYNAMSPLGSREPGVVGAAIESETAWCGLIVDGHHVHPAAARVALRAKPRGKVMLVTDAMPPVGMDDETSFELFGTQVLRVGDRLNAVTGELAGCVLDMATAVENSVKMLGLPLGEALRMASLYPAEFLGIAESVGRLAVGQRADLVLLDNQYKVLANYIAGNAVYVRP Shewanella sp. ANA-3 ANA3 7025965 Shewana3_3113 Glucosamine-6-phosphate deaminase [isomerizing], alternative (EC 3.5.99.6) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (GLUCOSAMINE-6-P-DEAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. sugar isomerase (SIS) (RefSeq) MTNTIMEQEARTAPQKIAGQLAANADLMQQLGEKLRAFDPRFVMIVGRGSSDHAGVFAKYLFEIEAGVPTFAAAPSVASVYGKTLKLEGGLVIVISQSGRSPDILAQARMAKNAGAFCVALVNDETAPIKDIVDVVVPLRAGEEKAVAATKSYLATLSAILQLASAWTQSESLAAAVNSLPQALQTAVDAEPQLTPASVENVKNLVVLGRGLGYAVSKEIALKLKEVCSIHAEAFSSAEFLHGPVTLVEKKLTIVDVCIGDESYASHIEQIENVSQRGADLVHLNQTSTDIHPRVAPLALLQRFYIDVAAVAIARGIDPDQPAGLKKVTQTL Shewanella sp. ANA-3 ANA3 7026437 Shewana3_3579 Aldose 1-epimerase (EC 5.1.3.3) Specifically important for utilizing D-Maltose monohydrate. Automated validation from mutant phenotype: the predicted function (5.1.3.3) was linked to the condition via a SEED subsystem. This annotation was also checked manually. aldose 1-epimerase (RefSeq) MVRFSVLDPWTDPRGGEIERVRIDNGIIALEVLSLGGIIRSLWTPDKQGQRANIVLGCDSAEDYLTQNAHLGAIAGRFANRIAMGKLQYQEQEYQLDINQASNCLHGGREGFNRKNWHLGQLPDGVRLSLVSPDGDMGFPGNCTVQLDYRLAANNLYVEILASVDKPCPVSLTQHSYFNLDGLPNNHQHRMQIDATRYLTMNEVGVPTGIAEVKNSIFDLTQGVTFGDKLQDPALVRTQGYDHCYLLDNPDGALRRFGCLSSPVSGRAMTVFTNQPGVQLYCANFLAGTLGRNQQSLAQYQGVCIEPQKLPDSPNQPQLGDDAWLVPGKIYHHISRYQFDIEG Shewanella sp. ANA-3 ANA3 7026537 Shewana3_3680 Uridine phosphorylase (EC 2.4.2.3) Specifically important for utilizing Cytidine and Uridine. Automated validation from mutant phenotype: the predicted function (URPHOS-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. uridine phosphorylase (RefSeq) MADVFHLGLTKAMLDGATLAIVPGDPERVKRIAELMDNATFLASHREYTSYLAYADGKPVVICSTGIGGPSTSIAVEELAQLGVNTFLRVGTTGAIQPHVNVGDVIVTQASVRLDGASLHFAPMEFPAVANFECTTAMVAACRDAGVEPHIGVTASSDTFYPGQERYDTVTGRVTRRFAGSMKEWQDMGVLNYEMESATLFTMCATQGWRAACVAGVIVNRTQQEIPNEATMKQTEVSAVSIVVAAAKKLLA Shewanella sp. ANA-3 ANA3 7026975 Shewana3_4104 2-amino-3-ketobutyrate coenzyme A ligase (EC 2.3.1.29) Specifically important for utilizing L-Threonine. Automated validation from mutant phenotype: the predicted function (AKBLIG-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 2-amino-3-ketobutyrate coenzyme A ligase (RefSeq) MASTSFYAQINQQLADVKAEGLYKSERVIASPQQTAIQVNHQEVVNFCANNYLGLANHPELIKAAQQGLDSHGFGMASVRFICGTQDIHKQLEASLSEFLGMEDTILYSSCFDANAGLFETLLDAEDAIISDALNHASIIDGVRLCKAKRFRYANNDMADLETQLIAAKAAGARNILIATDGVFSMDGVIANLQGVCDLADKYGALVMVDDSHAVGFVGLNGRGSHEHCGVMGRVDIITGTLGKALGGASGGFTSGKKEVIDWLRQRSRPYLFSNSLAPSIVTASIHVLEMLKSGQALREAVWENSRYFREKMSAAGFTLGGADHAIIPVMIGDAKLASDFANRLLAEHIYVIGFSFPVVPKGQARIRTQMSAAHTREQLDKAIEAFTRIAKEMAII Burkholderia phytofirmans PsJN BFirm BPHYT_RS02045 BPHYT_RS02045 Fructokinase (EC 2.7.1.4) Specifically important for utilizing D-Sorbitol. Automated validation from mutant phenotype: the predicted function (FRUCTOKINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. sugar kinase MSNQSANHEFPFFVSAGDILTDLVRTGASQWLSRPGGAGWNVARCVARLGLPTACAGSLGVDNFSDELWNASVAAGLDMRFMQRVERPPLLAIVHQTHPPAYFFMGENSADLAFDPAQLPAGWMGQVKWAHFGCISLVRQPIGNTLATLAAELRSQGVKISFDPNYRNLMEHGYEPTLRKMAALADLIKVSDEDLRLIFKTDDEAGALAQLRAMNPAATVLVTRGPETAVLIDGAMVTEARPPRVEVVDTVGAGDASIGGLLFSLMTAPQRAWPEHLAFALAAGAAACRHAGAHAPSLDEVVALL Burkholderia phytofirmans PsJN BFirm BPHYT_RS02730 BPHYT_RS02730 N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (NAG6PDEACET-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-acetylglucosamine-6-phosphate deacetylase MLTGNILTTDGWIHGTLEYENGRITALTGERADPSTNDAPYILPGFIDLHVHGGGGSDVMEGGSAIETITRTHARYGTTSLLATTMTAPRDELMAVVAELGNNARIRTPGGARVLGVHLEGPYINPGKLGAQPDAAVSAVMDEVLKYLSIAPIRVVTLAPEIAGHMEIISEMAARGVRVQLGHSLGTYDDAVAALKHGACGFTHLFNAMSPLHHRNPGLVGAALAHAEFAEIIPDLLHVHPGAIRAALRAIPRLYVVTDSTSATGMPDGEYRLGSQHVTKCLGGVRLADGTLAGSTLTMDQALRNLVSIGLPIADVSNRLSRYAADYLGIEDRGRIARGAWADVVVFDRELALSATYVEGEAIVEYA Burkholderia phytofirmans PsJN BFirm BPHYT_RS02735 BPHYT_RS02735 Glucosamine-6-phosphate deaminase [isomerizing], alternative (EC 3.5.99.6) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (GLUCOSAMINE-6-P-DEAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. iron dicitrate transport regulator FecR MLKEALASAETVAAQLTDTSRVEALAAKLAQQPRHVALTVARGSSDHAASYFASLTMSRLGVPVASLPMSVATLQQAPLQVRDQLALAFSQSGKSPDLVGTMEALRKAGALTVAAVNVSGSPLADACEFELPLVAGPELSVAATKSYIAMLSISAQLVAHWQKDAELLAALKTLPEALCTAGKLDWSVAVEELRGIERMIVIGRGLGLAIAQEAALKLKETSGIQAEAFSSAEVRHGPMELIDRDYPLLVFAPRGPEQAGLLQLARDMKARGARVLLAASVDVPEATLPLATTAHAALDPIAAILSFYVMAAGLAAARGRNPDAPRHLNKVTETH Burkholderia phytofirmans PsJN BFirm BPHYT_RS07555 BPHYT_RS07555 Histidine ammonia-lyase (EC 4.3.1.3) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (HISTIDINE-AMMONIA-LYASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. histidine ammonia-lyase MTLKPGYLTLPQLRQIAREHVALQLDPASHAAIDACAQAVADIAAKGEPAYGINTGFGRLASTHIPHDQLELLQRNLVLSHAVGVGEPMSRPVVRLLIALKLSSLGRGHSGIRREVMEALITLYNADVLPVIPVKGSVGASGDLAPLAHMSATLLGVGEVFAKGERMPATEGLALVGLKPLTLQAKEGLALLNGTQASTALALYNMFAIEDLYRTALVSGALSVDAAMGSVKPFDARIHELRGHQGQIDAAGAYRSLLQGSGINVSHADCDKVQDPYSLRCQPQVMGACLDQMRHAANVLLLEANAVSDNPLIFPDTGEVLSGGNFHAEPVAFAADNLALAAAEIGALAERRIALLIDATLSGLPPFLVRDGGVNSGFMIAHVTAAALASENKTLAHPASVDSLPTSANQEDHVSMATFAARKLGDIAENTANILSIELLAAAQGVDLRAPHKTSPSLQKVMDAVRKDVAHYELDHYFAPDIAAVTRLVQDGTIAKLSPLSFASEQ Burkholderia phytofirmans PsJN BFirm BPHYT_RS07585 BPHYT_RS07585 N-formylglutamate deformylase (EC 3.5.1.68) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (N-FORMYLGLUTAMATE-DEFORMYLASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-formylglutamate amidohydrolase MTASNTPPVFSLHRGSLPLLISIPHLGTQIPADIAATMTPAAQRTDDCDWHLDRLYAFAKRMGASILAPTYARYVIDLNRPPDGANLYPGQDTTGLLPVDTFDKEPLYLDGQLPDEAETTRRRDAYWKPYHEALQGELAALKAKHGKVLLWEAHSIRSHVPRFFEGRLPDFNFGTSNGASAVAGLAEEMAATVEQYDGGYTAVANGRFKGGYITREYGQPSQGVHALQLELSQITYMEEHMPYAYDETLAAKVEPLLEALVVKALERVKTA Burkholderia phytofirmans PsJN BFirm BPHYT_RS07720 BPHYT_RS07720 Succinylglutamate desuccinylase (EC 3.5.1.96) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (SUCCGLUDESUCC-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. succinylglutamate desuccinylase MPVPLLDDFLAYTLAGTRPAASETQGTCAGGVRWSWLDDGVLLMEPAAQDESVRSVLVSAGVHGDETAPIELLGFLVRDIAQGTAALTCRLLVILGNVDAMRDACRYRDDDLNRLFSGRHLQVPQSYEAPRAAALEQAATQFFAAASNKSGARWHIDMHTAIRASAFEQFALLPHTGKPFSRAMFEWLGEARISAVLLHTTKGNTYSHFTAQVCGAEACTLELGKVRPFGQNDLTRFAGADHAVRHLLAGMRGHVRADLPRAFTVIDQITKQSDAFELLVAADVANFTPFAKGTVLARDGEYRYVVQHDEERLVFPNATVKPGLRAGLMVVETTQDTLSKLV Burkholderia phytofirmans PsJN BFirm BPHYT_RS08815 BPHYT_RS08815 L-asparaginase (EC 3.5.1.1) Specifically important for utilizing L-Asparagine. Automated validation from mutant phenotype: the predicted function (ASPARAGHYD-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-asparaginase MNTSTSSSAMPSDEGAMPLLPRIVVLATGGTIAGAAASATNTSGYQAGVIGVEQLLAVVPALSTVARMEREQIASVDSKDMAMPLWTTLAQRINTLLADDEIDGVVVTHGTDTLEETAYLLHLTIKSDKPVVLTAAMRPASALSADGPLNLLNAVTVAAQASARGQGVLVAFNNRIHSARDVVKTSTYAVDAFHSPEIGALGWVQDGRVEFQRGVVRPHTLATEFVIGAQWPHVEIVLSYAGVSRIAVDALVAAGVRGIVVAGTGNGSIHASVQQALADAASQGVAVVRASRVGSGHVMRNGAAADDALGFVSAGSLNPYKARVLLMLALAAGATGPMALQKIFDTY Burkholderia phytofirmans PsJN BFirm BPHYT_RS12305 BPHYT_RS12305 Malate synthase (EC 2.3.3.9) Specifically important for utilizing Tween 20. Automated validation from mutant phenotype: the predicted function (MALSYN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. malate synthase MASPQSSHSSLQLPQGMEITAEIKPGYDAILSREALELVAALHRTFEPRRQQLLQARAERTKRLDAGERPDFLAETKSVRDGDWTIAPLPQDLQCRRVEITGPVERKMIINALNSGADSYMTDFEDSNAPSWDNQITGHINLKDAVRRTISLEQNGKSYTLNDKVATLIVRPRGWHLDEKHVKVDGKRVSGGIFDFALFMVHNAKELVARGSGPYFYLPKMESHLEARLWNDIFVAAQEAVGVPRGTIRATVLIETIVAAFEMDEILYELREHSSGLNAGRWDYIFSAIKKFKADRDFCLADRSQITMTSPFMRAYALLLLKTCHRRNAPAIGGMSALIPIKNDPAANDKAMSGVRSDKARDAGDGYDGGWVAHPGLVPIAMEEFVKVLGDKPNQIGKQRDDVLVTATDLTDFRPEAPITEGGLRNNINVGIHYLGAWLAGNGCVPIHNLMEDAATAEISRSQVWQWIRSPKGKLEDGRKVTAELVRELSAQELEKVKQAVGGDTKPYERAAQIFEEMSTSEQFTDFLTLPLYEEI Burkholderia phytofirmans PsJN BFirm BPHYT_RS13300 BPHYT_RS13300 Dihydropyrimidinase (EC 3.5.2.2) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (3.5.2.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. phenylhydantoinase MTTLIRGGTIIDAENTYRADVLCADPQDGGTILQIGADLEAPAGATIVDAGGQYVMPGGIDPHTHMELPFMGTTASDDFYTGTAAGLSGGTTSIIDFVIPSPKQPLMDAFKEWRGWAEKASSDYGFHVAVTWWDDSVYRDMGTLVHEHGVSSFKHFMAYKNAIMADDEVLVNSFSRSLELGALPTVHAENGELVFQLQRQLLAKGFTGPEAHPLSRPPEVEGEAANRAIRIAQVLGVPVYIVHVSSKDAVDAIARARSEGLRVFGEVLPGHLVIDEAVYRDPDWTRAAAHVMSPPFRSAEHREALWRGLQAGQLHTTATDHCVFCASQKAMGRDDFTKIPNGCGGVEDRMAVLWHHGVNSGRLTPNEFVRITSTNAAQIFNLYPRKGAVRVGADADLVVWDPNASKTISVKTHHQKVDFNVFEGMTVQGVAMHTLTRGALAWTDGELRAVRGAGRYLKRPPNGAYFDAIRVANKRKEPHPVER Burkholderia phytofirmans PsJN BFirm BPHYT_RS13920 BPHYT_RS13920 Myo-inosose-2 dehydratase (EC 4.2.1.44) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (MYO-INOSOSE-2-DEHYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. xylose isomerase MTAFDVRIGINPLSWMNDDLPSLGGETPLEVALTEGREIGYQGFELGNKFPREPQALKSLLAQYDLALVSGWYSGRLARRSVEEEIAEVGPHLELLAQNGATAMVYGEVADSIQGAAQPLYQRPRFFSEKQWADYAARVDEFARYTLSRGVRLAYHHHMGAYVETPADVDQLMARTSDAVGLLFDAGHITFAGGDPLAVLDKHIGRVCHVHCKDVRPAVMKLARNRNWSFLDAVIAGAFTVPGDGAVNFPAIIERLKRHGYCGWLVVEAEQDPVVAPSFEYAQKGYKTLRALVDAPLDGTEQEAA Burkholderia phytofirmans PsJN BFirm BPHYT_RS14905 BPHYT_RS14905 Aromatic-amino-acid transaminase (EC 2.6.1.57) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (2.6.1.57) was linked to the condition via a SEED subsystem. This annotation was also checked manually. histidinol-phosphate aminotransferase MTASFGPSYVRAIAPYIAGKPISEVAREFGLDEATIVKLASNENPLGMPESAQRAMAQAASELGRYPDANAFELKAALSERYGVPADWVTLGNGSNDILEIAAHAFVEKGQSIVYAQYSFAVYALATQGLGARAIVVPAVKYGHDLDAMLAAVSDDTRLIFVANPNNPTGTFIEGPKLEAFLDKVPRHVVVVLDEAYTEYLPQEKRYDSIAWVRRYPNLLVSRTFSKAFGLAGLRVGFAIAQPELTDLLNRVRQPFNVNTLAQAAAIAALNDKAFLEKSAALNAQGYRRLTEAFDKLGLEYVPSDGNFVLVRVGNDDAAGNRVNLELLKQGVIVRPVGNYGLPQWLRITIGLPEENEAFIAALERTLAAA Burkholderia phytofirmans PsJN BFirm BPHYT_RS16025 BPHYT_RS16025 Kynurenine formamidase, bacterial (EC 3.5.1.9) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (ARYLFORMAMIDASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. kynurenine formamidase MPTLWDITPAVDTATPVWPGDTPVGIERVWRMEAGSPVNVARLTLSPHTGAHTDAPLHYDAEGVAIGEVPLDAYLGRCRVIHCIGASPVVTPQHLSGSLDDLPPRVLLRTYRNAPTAAWDSAFCAVAPDTIDLLAARGVKLIGIDTPSLDPQESKTMDAHHRIRTHRMAILEGIVLDDVAPGDYELIALPLKLTTLDASPVRAILRALPESQ Burkholderia phytofirmans PsJN BFirm BPHYT_RS16030 BPHYT_RS16030 Kynureninase (EC 3.7.1.3) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (KYNURENINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. kynureninase MNHRDEALALDSADPLATLRDQFALSSTTIYLDGNSLGVPPAAAAQRAQTVIGAEWGEGLIRSWNTAGWFELPRRLGNKLAPLIGAAENEVVVTDTISINLFKLLSAAVRVANERDPKRRVIVSERSNFPTDLYIAQGLIEQLDRGYELRLVDDPSELPAAIGDDTAIAMITHVNYRTGYMHDMAALTKLIHDKGALALWDLAHSAGAVPVDLNGVGADYAVGCTYKYLNGGPGSPAFVWVPKRHQNEFAQPLSGWWGHRAPFKMDPAYQPDDGIGRFLCGTQPMVSMSLVECGLDVFLQTDMQAVRKKSLALTDLFIELVEARCSEFPLTLVTPREHAQRGSHASFEHPHGYEVMQALIARGVIGDYREPHVLRFGFTPLYTRFVDVWDAVETLREVLVKETWRAPEFAARGAVT Burkholderia phytofirmans PsJN BFirm BPHYT_RS16285 BPHYT_RS16285 Branched-chain amino acid aminotransferase (EC 2.6.1.42) Specifically important for utilizing L-Isoleucine. Automated validation from mutant phenotype: the predicted function (BRANCHED-CHAINAMINOTRANSFERILEU-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. branched-chain amino acid aminotransferase MSMADRDGKIWMDGKLIDWRDAKIHVLTHTLHYGMGVFEGVRAYKTADGGTAIFRLQEHTKRLLNSAKIFQMDVPFDHETLAAAQCEVVRENKLESCYLRPIIWVGSEKLGVSAKGNTIHVAIAAWPWGAYLGEDGIAKGIRVKTSSFTRHHVNVSMVRAKASGWYVNSILANQEAIADGYDEALLLDVDGYVSEGSGENFFLVNNGKLYTPDLSSCLDGITRDTVITLARDAGIQVIEKRITRDEVYTCDEAFFTGTAAEVTPIRELDNRTIGSGARGPITEKLQSGFFDIVNGKSDKYANWLTKI Burkholderia phytofirmans PsJN BFirm BPHYT_RS16720 BPHYT_RS16720 Gluconokinase (EC 2.7.1.12) Specifically important for utilizing D-Gluconic Acid sodium salt. Automated validation from mutant phenotype: the predicted function (GLUCONOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. gluconate kinase MILIAMGVSGAGKTRIGEMLAERLHCAFTDGDAFHSAANKEKMHHGIPLTDEDRWPWLQTIRVAIVEKQKAGETAVFTCSSLKRSYRDVLRDGDKDVCFVYLKGSREVLEQRLTTRTGHFFDPSLLQSQLDTLEEPGPDEAITVSIELSPEEIVVEVLKQVEARK Burkholderia phytofirmans PsJN BFirm BPHYT_RS19340 BPHYT_RS19340 L-serine ammonia-lyase (EC 4.3.1.17) Specifically important for utilizing L-Serine. Automated validation from mutant phenotype: the predicted function (4.3.1.17) was linked to the condition via a SEED subsystem. This annotation was also checked manually. serine dehydratase MAVSVFDLFKIGIGPSSSHTVGPMRAALMFAQGLERDGLLAATASVKVELYGSLGATGKGHGTDRGVMLGLMGDAPDTVDPDTIAQRLEGVRVSRKLALLGTHEVPFVQKDHISFYRQALPEHPNGLKLRALDAQGETLRESTYLSVGGGFVVTAGAPNTKVLSAVEQLPHAFRSGNELLALCESTGKSIAQLMWENERVWHTEEETRAGLLKIWDVMQSCVARGCGINNPDADGNLPGPFQVKRRAPQLYRALSGNPELALRDPLSMIDWINLYAIAVNEENAAGGRVVTAPTNGAAGIIPAVLHYYMRFMPGSNQQGVIDFLMTAAAIGILYKLNASISGAEVGCQGEVGVACSMAAGALAAVMGGTPRQVENAAEIGMEHNLGLTCDPVGGMVQIPCIERNAMASVKAVNAARMALRGDGSHYVSLDSVIKTMRETGADMKTKYKETSRGGLAVNIVEC Burkholderia phytofirmans PsJN BFirm BPHYT_RS22380 BPHYT_RS22380 Carnitine 3-dehydrogenase (EC 1.1.1.108) Specifically important for utilizing Carnitine Hydrochloride. Automated validation from mutant phenotype: the predicted function (CARNITINE-3-DEHYDROGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 3-hydroxybutyryl-CoA dehydrogenase MAVIVDIKTFAAIGVGVIGSGWVARALAHGLDVIAWDPAPGAEKQLRENVANAWSALQRVGLAAGASPERLRFVDTIQACVGQADFIQESAPEREELKLSLHEQISRAAKPDAIIASSTSGLLPSDFYARAVNPQRCIVGHPFNPVYLLPLVEVLGGESTAPETIDAALQVYRALSMRPLRVRKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAGIRWSFMGTFLTYTLAGGDAGMRHFMQQFGPALELPWTKLVAPKLTDELIDRVVDGTAEQVGPRSIKQLERYRDDCITSVLTAIAEAKARHGMQPAE Burkholderia phytofirmans PsJN BFirm BPHYT_RS24155 BPHYT_RS24155 5-dehydro-4-deoxyglucarate dehydratase (EC 4.2.1.41) Specifically important for utilizing D-Galacturonic Acid monohydrate. Automated validation from mutant phenotype: the predicted function (4.2.1.41) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 5-dehydro-4-deoxyglucarate dehydratase MTTPQELKQIVSEGLLSFPVTDFDEQGDFRADTYAERLEWLAPYGASALFVAGGTGEFFSLTHNDYSNVVKTATEVCKGKVPILAGAGGPTRVAIAYAQEAERHGANGILLMPHYLTEACQEGIAAHAEEVCKSVPNMGVIIYNRANSKLNADMLEGLAERCPNLIGFKDGVGEIENMVSIRRRLGDRFSYLGGLPTAEVYAAAYKALGVPVYSSAVFNFIPKTAMDFYRAIAADDHATVGKLIDEFFLPYLAIRNRRAGYAVSIVKAGAKLVGHSAGPVRAPLTDLTEEEMGKLDALIKTLGPQ Burkholderia phytofirmans PsJN BFirm BPHYT_RS32825 BPHYT_RS32825 Xylose isomerase (EC 5.3.1.5) Specifically important for utilizing D-Xylose. Automated validation from mutant phenotype: the predicted function (XYLISOM-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. xylose isomerase MSYFEHIPEIRYEGPQSDNPLAYRHYDKSKKVLGKTLEEHLRIAVCYWHTFVWPGVDIFGQGTFRRPWQQAGDAMERAQQKADSAFEFFSKLGTPYYTFHDTDVSPEGSNLKEYSENFLRITDYLARKQESTGIKLLWGTANLFSHPRYAAGAATSPDPEVFAFAATQVRHALDATQRLGGDNYVLWGGREGYDTLLNTDLVRERDQLARFLHMVVDHAHKIGFKGSLLIEPKPQEPTKHQYDYDVATVHGFLLQHGLDKEIRVNIEANHATLAGHSFHHEIATAYALGIFGSVDANRGDPQNGWDTDQFPNSVEELTLAFYEILKHGGFTTGGMNFDSKVRRQSVDPEDLFYGHIGAIDNLALAVERAAVLIENDRLDQFKRQRYSGWDAEFGRKISSGDYSLSALAEEAMARGLNPQHASGHQELMENIVNQAIYSGR Caulobacter crescentus NA1000 Caulo CCNA_00452 CCNA_00452 N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (NAG6PDEACET-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-acetylglucosamine-6-phosphate deacetylase MPAALINGRVLTESGVVEGKAVLVKDGLILDVIEAAQTPSDAKPRDLKGGLLVPGFIDTQVNGGGGVLFNDAPTVETIATIGAAHRRFGTTGFLPTLISDDLRVVDQAMRATEEAIARGVPGVLGLHIEGPFLNPKRKGIHDAGKFRVIDDEALALLTSLKRGKTLVTLAPERTTPQIIRRLADAGVIVAAGHTNALYATMRQALEHGLTGFTHLFNAMSPLTSREPGAVGAALESPDAWCGIIVDGRHVDPVVLKIALRTRALDRFMLVTDAMPTVGLPDKRFNLQGRDIRVVDGVCVDDHGTLAGSDLDMIGAVRNAIDLLDLSLDDAVMMASHAPASFLGLGHGRGLIAPGYAADLCLLNDRLEVAATWIDGQEG Caulobacter crescentus NA1000 Caulo CCNA_00453 CCNA_00453 Glucosamine-6-phosphate deaminase [isomerizing], alternative (EC 3.5.99.6) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (GLUCOSAMINE-6-P-DEAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glucosamine-6-phosphate deaminase MEATVLTRHETPAPTGASPPSLAPASTHMFREAGEAARVAAVQLTANAPKIQALAQRLRANPPRVVVTCARGSSDHAATFARYLIETKAGVLTSSAGPSVSSVYDASPNLEGALYLAISQSGKSPDLLAAVKAAKAAGAHAVALVNVVDSPLAALADEVIPLHAGPELSVAATKSYIAALVAVTQLIAAWTEDAELTAALQDLPTALAAAWTLDWSLAVERLKTASNLYVLGRGVGFGVALEAALKFKETCGLHAEAFSAAEVLHGPMALVKDGFPALVFAQNDESRASVDEMAAGLRARGASVLIAGGGGDAPDALPTLASHPVLEPILMIQSFYRMANALSVARGYDPDSPPHLNKVTETI Caulobacter crescentus NA1000 Caulo CCNA_00651 CCNA_00651 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrite reductase (NAD(P)H) catalytic subunit MTQATPKLRLVVIGNGMAGCRAVEEVLKRDPDRYAVTIFGAEPRVNYNRIMLSPVLAGEKAFEDIVINDEAWYRDNGITLHAGRAVTAIDLAARKVFAEGGLEIGYDKLILATGSDPFRLPLPGGDLKGVVTFRDLDDVNAMLAASAEPDARAVVIGGGLLGLEAAYGLARRGMAATVVHLMDVLMERQLDESAGYLLREALADRGVETVLGAHSEEIVGADGQVTGLKLKDGRVLPCDLLVMAVGIRPNTTLAKAAGLTVNRGVAVDDAMRTSDPDVFAVGECVEHRGQCYGLVAPIWEMCRALAQALTDGEGAYQGSVLSTRLKVSGVDVFSAGKFAGGEGCEDIVFRDAARGVYKRVVIEDGKVAGAVLFGDAADGGWYFDLMKAGADVAGIRETLIFGQAITEGLSGLDPSAAVAAMPDTQEICGCNGVCKGAITSAITAQGLTTLDDVRAVTKASASCGSCTPLVEQVLKLTLGDGFQAQTGPKPICKCSPKTHGDVRRAIVDQGLKSMPAVMQALEWSTPDGCASCRPALNYYLLCAWPGEYRDDKQSRYINERVHANIQKDGTYSVVPRMWGGMTSPAELRAIADVAEKFAIPAVKVTGGQRIDLLGVKKDDLPAVWADLNAAGMVSGHAYAKGLRTVKTCVGSDWCRFGTQDSTGLGMRLEKFLWGSWAPAKVKLAVSGCPRNCAEATCKDFGVVCVDSGYEIHIGGAAGLHIQGTQVLTRVATEDEAVWVIAAAMQLYREEGWYLERVYKWMDRVGLESIRAQVTDPDQRRALYDRFVYSQRFARIDPWAERVAGRHNEEFTPMSRRMEFVPA Caulobacter crescentus NA1000 Caulo CCNA_00653 CCNA_00653 Nitrate reductase (EC 1.7.99.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.99.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. assimilatory nitrate reductase catalytic subunit MADGSAALTATRTACPYCGVGCGVIGATAAGARAVAISGDEAHPANHGRLCSKGTALGATVSLAGRLLEPTIQGRSASWDEATALVARRFRETIARHGPDSVAFYVSGQLLTEDYYVANKLMKGFIGSGNIDTNSRLCMASAVVAHKQAFGADLVPGCYEDLDLANLVVFSGHNAAWTHPVLFRRMEAAKARGQKHVVIDPRRTDTAEGADLHLALAPQSDVRLWNGLLADLIRRGAVDMDFLRDHVDGYAAVITSLAEDDQSPAAVAADCGLALADLQTFFDLFAAHPRTVSLFSMGANQSAQGVAKGLAIINAHLATGRIGKPGACPFSITGQPNAMGGRETGGMANTLAGHMDFSPEERDRVARFWGAPNTARAPGLKAIDMFEAVRDGRIKALWVMATNPAVSLPASGAVREALERCPFVVVSDCVETDTTAFADVKLPALAWGEKDGTVTNSERRISRQRTLFPPPGQARADWRIIAEVARAMGFDGFGWPHAASVFREWARLTAYENKGRLLNLEGLTRLDPQAYDALEPVQWPVDTEGRGRARLFEDGRFQTANGRARLVPVRPRGPAEATSDKFPMALNTGRIRDQWHTMTRTGLAPDLCRHAPEPYVEVHPDDARAVGLTEGALARVMTTRAEAVAVAKLSDRQRRGSLFMPMHWTDAFAPAGRANALVAPMTDPSSGQPEFKHTPARIGAYRETWRGFFLAREPALIVDPGLVWRRIPRDACHQHEFAGRGDRAQRATLRKRLVRALTGEIVAYEDAATGALREAWIRDDRLVAVLYMTEAGRLPPRDWLADLFAAPLTPETRATLLHGFPPGAPVDKGPMVCACLKVGGKAIEAAIIGGASTADAVGAATGAGTNCGSCRPEISRMIRAFTDAKQETADVL Caulobacter crescentus NA1000 Caulo CCNA_00862 CCNA_00862 Xylonate dehydratase (EC 4.2.1.82) Specifically important for utilizing D-Xylose. Automated validation from mutant phenotype: the predicted function (XYLONATE-DEHYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. xylonate dehydratase xylD MSNRTPRRFRSRDWFDNPDHIDMTALYLERFMNYGITPEELRSGKPIIGIAQTGSDISPCNRIHLDLVQRVRDGIRDAGGIPMEFPVHPIFENCRRPTAALDRNLSYLGLVETLHGYPIDAVVLTTGCDKTTPAGIMAATTVNIPAIVLSGGPMLDGWHENELVGSGTVIWRSRRKLAAGEITEEEFIDRAASSAPSAGHCNTMGTASTMNAVAEALGLSLTGCAAIPAPYRERGQMAYKTGQRIVDLAYDDVKPLDILTKQAFENAIALVAAAGGSTNAQPHIVAMARHAGVEITADDWRAAYDIPLIVNMQPAGKYLGERFHRAGGAPAVLWELLQQGRLHGDVLTVTGKTMSENLQGRETSDREVIFPYHEPLAEKAGFLVLKGNLFDFAIMKSSVIGEEFRKRYLSQPGQEGVFEARAIVFDGSDDYHKRINDPALEIDERCILVIRGAGPIGWPGSAEVVNMQPPDHLLKKGIMSLPTLGDGRQSGTADSPSILNASPESAIGGGLSWLRTGDTIRIDLNTGRCDALVDEATIAARKQDGIPAVPATMTPWQEIYRAHASQLDTGGVLEFAVKYQDLAAKLPRHNH Caulobacter crescentus NA1000 Caulo CCNA_00864 CCNA_00864 D-xylose 1-dehydrogenase (EC 1.1.1.175) Specifically important for utilizing D-Xylose. Automated validation from mutant phenotype: the predicted function (1.1.1.175) was linked to the condition via a SEED subsystem. This annotation was also checked manually. xylose dehydrogenase xylB MSSAIYPSLKGKRVVITGGGSGIGAGLTAGFARQGAEVIFLDIADEDSRALEAELAGSPIPPVYKRCDLMNLEAIKAVFAEIGDVDVLVNNAGNDDRHKLADVTGAYWDERINVNLRHMLFCTQAVAPGMKKRGGGAVINFGSISWHLGLEDLVLYETAKAGIEGMTRALARELGPDDIRVTCVVPGNVKTKRQEKWYTPEGEAQIVAAQCLKGRIVPENVAALVLFLASDDASLCTGHEYWIDAGWR Caulobacter crescentus NA1000 Caulo CCNA_01019 CCNA_01019 Beta-glucosidase (EC 3.2.1.21) Specifically important for utilizing D-Salicin. Automated validation from mutant phenotype: the predicted function (3.2.1.21) was linked to the condition via a SEED subsystem. This annotation was also checked manually. beta-glucosidase MISTTLRSLSLALLISASASALSVVPALADAAKPAAALAHPWMDKSLDADKRADLVLKAMTNDEKFTLIFGYFGADMKPKYTRIPESLPGSAGYIAGVPRLGIPAQFQTDAGVGVATQGSAKEFRERTALPSGMATTATWNPELAFQGGAMIGKEARDSGFNVQLAGGVNLVREPRNGRNFEYGGEDPLLAGVMVAAQIRGIQSNNIISTIKHYALNAQETGRFVVSSNIDDTAARMSDLLAFQFAIEQSDPHSVMCAYNRVNSVYACESDWLLNTVLKKDWGYKGYVMSDWGAAHSSAKAANAGLDQESAGDAFDKQPFFAAPLKADLASGAVSQARIDDMARRVLRAMFASGVVDHPLTGAPLAMPAETLAAHAKITQADAEEGIVLLKNDGGLLPLAKTAKTIAVIGSYADVGVLSGGGSSQVYPVGGRAVQGLEPKTWPGPVIYYPSSPLKAIAARYPGAKVVYDDGTDPARAAKLAASSDLALVFADQWTTESVDVTTLNLPKNQDATIDAVASANKKTVVVLLTGGPLLMPWLDKVGAVVEAWFPGTAGGEAIARVLTGEVDASGRLPVTFPKSVAELPRPKLDGLGKPDGEMFDVDYTLEGAAVGYKWYDLKKIEPLFAFGHGLSYTQFAYSNLTASASGDTLTVSFEVKNVGRRPGKDVPQVYVGPKAGGWEAPKRLAGFQKVSLAPGASQRVTVTVDPRLLAVWDSKAHGWSIAAGQYDIALGASSRAISSTAQVTLAARSLPVSPAAK Caulobacter crescentus NA1000 Caulo CCNA_01360 CCNA_01360 Methylmalonate-semialdehyde dehydrogenase [inositol] (EC 1.2.1.27) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (RXN-2902) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. malonate-semialdehyde dehydrogenase IolA MMRDIPHFIGGQKVDGASGRFGEVFDPNTGKVQARVALASAGELNTAIANAKVAQAAWAATNPQRRARVMFEFKRLLEVHMDELAALLSSEHGKVIADSKGDIQRGLEVIEFACGVPHLLKGEYTQGAGPGIDVYSMRQPLGVVAGITPFNFPAMIPMWMFGPAIATGNAFILKPSERDPSVPVRLAELMIEAGLPPGVLNVVHGDKDCVEAILDHPDIKAVSFVGSSDIAQSVFQRAGAAGKRVQAMGGAKNHGLVMPDADLDQAVADIIGAAYGSAGERCMALPVVVPVGEKTATALREKLVAAIGGLRVGVSTDPDAHYGPVVSAAHKARIESYIQMGVDEGAELVVDGRGFSLQGHEEGFFVGPTLFDHVKPTSRSYHDEIFGPVLQMVRAESLEEGIALASRHQYGNGVAIFTRNGDAAREFADQVEVGMVGINVPIPVPVAYHSFGGWKRSGFGDLNQYGMDGVRFYTRTKTVTQRWPKGGAVLDQSFVIPTMR Caulobacter crescentus NA1000 Caulo CCNA_03284 CCNA_03284 Adenosine deaminase (EC 3.5.4.4) Specifically important for utilizing Adenosine. Automated validation from mutant phenotype: the predicted function (ADENODEAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. adenosine deaminase MTDASFAPSASAEFVRGLPKAELHMHIEGSLEPELMFELAQRNGITLPFASVEEIRAAYDFSNLQDFLDIYYQGAGVLITEADFKDLALAYFQRLAADGGAHAEIFFDPQTHTDRGIAFDTVMNGLLAGMDEAEKTLGVTSKLILCFLRHLSEEAAFETLEQAKPWLAKLAGVGLDSSEVGHPPAKFARVLQASRDLGLKVVAHAGEEGPPAYVWEAIDLVKVDRIDHGNRALEDEALTARLVKDGITLTVCPLSNLKLCGVPSLDVHPLKRMLDLGLKATVNSDDPAYFGGYLLENYLATADAVGLTRDDIVTLAKNSFAGSFLTDAEKAQRIAAVEAYAAAH Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_0119 Echvi_0119 Proline dehydrogenase (EC 1.5.5.2) Specifically important for utilizing L-Proline. Automated validation from mutant phenotype: the predicted function (1.5.5.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Proline dehydrogenase MNTKPNISFENTEIAFASRTDAELRKMYLFFAVMDKNWAVKIGTNLSAVAFKLKLPVKGIMKKTIFGHFCGGESVEDCSKSIQELQEFGIGTILDYSVEGTGTEKSYDFTRDEILRTIERSAGASEIPFSVFKVTGLGSYKIMTKVQAGQKLSAKEQEAFERLKDRVDTLCKAAYENDVRIMIDGEESWFQDVIDDMAYEAMEKYNKEKAIVYNTFQMYRKDMLGLLKKAHEEAELKGYHVGAKLVRGAYMEKERDRAEDRGYPSPIQDTKEDTDNAYNDALKFSMEHKDRIYLVSGSHNELSNIILTELMNLHGVAANDKRVYFSQLYGMSDNISYNLAFAGYNVAKYVPYGPVESVMPYLYRRASENTSVAGQSSREFELIKNEMARRASLKKTII Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_0503 Echvi_0503 L-ribulose-5-phosphate 4-epimerase (EC 5.1.3.4) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (RIBULPEPIM-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Ribulose-5-phosphate 4-epimerase and related epimerases and aldolases MSKFLELKRECYEANMQLPALDLVVYTFGNVSAVDRKEGVFAIKPSGVAYEALTPEDIVICDFDAKIVEGEMRPSSDTKTHAYLYKEWENIGGIVHTHSLYGVSWAQAQMDVPIFGTTHADHLTKDIPCAPPMADELIEGDYEHMTGKQILDCFAEKGLDYEEVEMILVGSHGPFTWGKTAAKAVYNSKVLEEVAKMAYLTLQINPNAPRLKDALIKKHYERKHGKDAYYGQGC Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_0515 Echvi_0515 Ribulokinase (EC 2.7.1.16) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (RXN0-5116) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-ribulokinase MNDKFVIGLDYGSDSVRAVIVNTGNGEVKGSHVFWYPRWKAGKYCDPVNNQFRQHPLDHLEGLEETIREVIKESGVPADQIKGICVDTTGSSPMAVDQQGKPLALSPEFAENPNAMMVLWKDHTAIKEADEINELARTWGGEDYTKYEGGIYSSEWFWAKILHVIREDDAVAQAAYSWMEHCDVITAELIGADNPLDVKRSRCAAGHKALWHESWDGLPPKEFLSKLDPRLADLRDRLYTETFTSDLPAGNLSAEWAKKLGLSTDTVIAVGTFDAHAGAVGGEVTENTLVKVMGTSTCDIMVATHEAIGDNLVKGICGQVDGSVIPGTVGLEAGQSGFGDVLAWFKHLVVKPTAALIRASNVLDEEKKEALIHEIDSQLLIKLSEEAIQIPLSETAPVALDWVNGRRTPDANQALKGAVMGLNMGTDAARVFKALVESICFGSKKIVDRFREEGVAIDTVIGMGGVAKKSKLVMQTMADVLNMPIKIATSDQAPALGAAMYASVAAGIHPTTEAAIAAMTNGFDKVYEPIPENVEVYKALYAKYAEFGAFVEGQTSPVLADQ Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_0577 Echvi_0577 Ornithine aminotransferase (EC 2.6.1.13) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (ORNITHINE-GLU-AMINOTRANSFERASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. ornithine aminotransferase MMQPITSSQQAIELENKHGAHNYHPLPVVLSRGEGVFMWDVEGEKYYDFLSSYSAVNQGHCHPRILQTLIDQAGTLTLTSRAFHNDVLGPFEKFLTEYFGYDKVLPMNTGAEGVETAIKIARKWGYEKKGIPENEGTIIVAKNNFHGRTTTVISFSNDETARKNFGPYTPGFVTIPHDDIDALKDVLSQSKNIIGYLVEPIQGEAGVYVPKEGYLKEVAAVCKDHGVLFMADEIQTGIARTGKLLACDHEGVKPDMLILGKAISGGFYPVSAVLADDHIMEVIQPGQHGSTFGGNPLGAKVAMTALNVVKDEKLAENADKLGKLFRERIQQLVDKSDLVELVRGKGLLNAIVINDTEDSDTAWRLCLALKENGLLAKPTHGNIIRFAPPLVITEEQLHDCCDIIEKTIQNFKK Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_0697 Echvi_0697 Aldose 1-epimerase (EC 5.1.3.3) Specifically important for utilizing D-Galactose. Automated validation from mutant phenotype: the predicted function (5.1.3.3) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Galactose mutarotase and related enzymes MSTAQTNHSKTTVERTVFGQTPTGSDIHLFTLRNANGAKACVTNYGATLTHLEVPDRDGQFRDVVLGFDSYEDYTSEAYLKAGAFMGCTVGRVCNRIDHGRFQLEGKPYQMAVNNGDHHLHGGLEGFDKKIWEASIIEDGVEFTYVSPDGEESYPGELTVTVAFTLSAANELKLAYRATTNKTTVVNLTNHSYFNLSGDLSSSILDHELQVNAPLYIPVKEGSIPTGEILSVKGTPLDFLQPKKVKKGVMADHPQTVIANGLDQTLVFDAHQPAAVLSSAASGIRMEVATSEPGIQLYTANYFDGTLQGKGRTYGKHGGIALETQHFPDSPNHPHFPTVVLQPGETFHSFTAFKFSVIK Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1572 Echvi_1572 Lactaldehyde dehydrogenase (EC 1.2.1.22); Rhamnulose-1-phosphate aldolase (EC 4.1.2.19) Specifically important for utilizing L-Rhamnose monohydrate. Automated validation from mutant phenotype: the predicted function (1.2.1.22, 4.1.2.19) was linked to the condition via a SEED subsystem. This annotation was also checked manually. rhamnulose-1-phosphate aldolase/alcohol dehydrogenase MSTAERTFKHVNYLWDEQKAQELEGDEVALLIYRSNILGADLRITNYGGGNTSCKTTEVDPLTKEETEVMWVKGSGGDIGTLKRSGLAGLYVEKLHSLKNVYRGLEFEDEMVGLFNHCIYDLDSKAPSIDTPLHAFLPFKHIDHLHPDAAIAIAASKDGEKITEELFEGQIAWVPWQRPGFDLALQLEKALNENPGIRGIMLGGHGLFTWGDTAYECYINSLEVIDKASEYLEQNYGKDRPVFGGQKIESLAPEQRQEQASIIAPVLRGLASGYNRMVGHFTDDERVLQFANSHDLEKLAPLGTSCPDHFLRTKIRPLVLDFPADVDLSKADEIKEKLDKDFEEYRAYYKKYYEDHKRDNSPAMRDPNPVVIIWPGVGMFSYAKNKQTARVASEFYINAINVMRGAEAVSEYVALPLQEAFDIEYWLLEEAKLQRMPKEQPLSRKVALVTGGAGGIGKAIADKLASEGACVFITDINQERLDGAVATYSKDVGGGAVMDVTKGDDIIKAYKAAALKFGGVDIIVNCAGLAISKPIEQTSEQDWDLLQDILVKGQFAVSKAGVETLRAQNLGGDIINIASKNALVSGPNNVGYGTAKAAQVHMSRLLAAELGKDKIRVNVVNPDAVIEGSKIWEGEWAKGRAKAYGITVEELPAFYAKRTILNEIIGVDDIANGVFAFVGGHLSKCTGNILNVDGGVAAAFVR Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1573 Echvi_1573 L-rhamnose isomerase (EC 5.3.1.14) Specifically important for utilizing L-Rhamnose monohydrate. Automated validation from mutant phenotype: the predicted function (5.3.1.14) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Predicted sugar isomerase MRIDKQKIKEVNDQALSEHRESFGHLSSVLGKKGIDVNVLVEKLKEFQVAVPSWALGTGGTRFGRFSGGGEPGTLEDKISDVGLLHQLSQSAGAISLHIPWDIPNDVQAIKELAASHGLIFDAVNSNTFQDQPDQELSYKFGSLCHADKKVRDQAVKHNLEVIKYGDALGSKSLTVWLADGSSFPGQLNFKKAFQRTLESLQEIYAGMPEDWKLFVEYKPYEPNFYSTVIQDWGTSHMLADKLGDRAYSLVDLGHHLPNTNIEQIVATLMMVGKLGGFHFNDSKYGDDDVTVGSLKPYQLFLIFNELVDGMEDPSSNNPYPAWMIDASHNLKDPLEDLLQSLEAIKLAYAQALLVDRDALEEARENNDPALAQEILQAAYRTDVRSLLAEARLQADGALDPIAAYRKLNVRKELIAQRGEKVISTGL Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1574 Echvi_1574 Rhamnulokinase (EC 2.7.1.5) Specifically important for utilizing L-Rhamnose monohydrate. Automated validation from mutant phenotype: the predicted function (2.7.1.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Sugar (pentulose and hexulose) kinases MTPIPVIAIFDIGKTNKKFFLFDEHSNEIKQEYNKIPLTEDEDGFECDDLVALSEWITSTVEEICQSPDYALKGINFSTYGASFVHIDADGNPLTPLYNYLKEIPQEIIDEFYRQYPEETNNLETASPSLGMLNSGLQLYWLKKTKPDLFSKIAYSLHFPQYLSYLFTKKAVSEPTSIGCHTRLWDFQKDQYHDWVKQEGIDRVLPDIVPTGQLYQVDLCGRKVDIGVGIHDSSSALASYLVRVKEPFLLISTGTWSISLNPFTTDPLTKDELHNDCLNFLSIEGKPVKASRFFMGYEFNYQIDRINKHFGKPDKFYKSVPANPAIIKAIKTGKVSNTFYPRHIAETPLVKALYEGNEWNPASFANFDEAYHHLIWGLTLLQVESLKLARGNSGIKKVFIDGGFVHNEVFMELLRYYLPESELEFSDFPLGSAYGAALVLEASEKKMA Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1587 Echvi_1587 Saccharopine dehydrogenase (NADP(+), L-lysine-forming) (EC 1.5.1.8); Saccharopine dehydrogenase (NAD(+), L-glutamate-forming) (EC 1.5.1.9) Specifically important for utilizing L-Lysine. Automated validation from mutant phenotype: the predicted function (1.5.1.8, 1.5.1.9) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Alanine dehydrogenase MKIGLIKEGKVPSDRRVAFSPQQLKTMNEAYAGRAVFVVEKSDIRAFKNEEYEEEGIEVVDDVSDCDVLMGIKEVPIASLMEGKTYFFFSHTIKAQPYNRGLLQAVLEKDIRLVDYEVLRNAGERVVAFGRWAGIVGGYNGLWTYGKKTGLFDMKRAKDCFDLMELHEEVKQIQLPPIKMVITGNGRVGNGVKEILQVAGIREVSPKELLQNYYDEPVFVQLAMEDYNRRKTDGGYDKAEFYSQPEKYESHFLKFAEVSDVLFAAAFWDPKAPKLFERKDVVSEDFNLSVIADITCDIDGSVPTTVKPSTIDAPVYDVDRESFEVLPAFGEQLSISVMAIDNLPCELPRDASEDFGSQLMETVIPALLEDESGIIEKATIAENGELTHYFDYLEDFVRERSDDS Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1876 Echvi_1876 Xylose isomerase (EC 5.3.1.5) Specifically important for utilizing D-Xylose. Automated validation from mutant phenotype: the predicted function (XYLISOM-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. xylose isomerase MSKTYFPGIEKIKYEGRDSKNPFAFKFYDENKVVAGKTMKEHFKFAIAYWHSFNATGDDPFGPGTKTFVWDQAEDALQRAKDKMDAAFEFITKIGAPYYCFHDVDLIDEGSTIEEYESRMKAITEYAKQKQVETGVKLLWGTANVFSNPRYMNGASTNPDFDVVSWAATQVKNSIDATIALGGENYVFWGGREGYMSLLNTDMKRETEHLAKFLTMARDYGRKQGFKGNFLIEPKPMEPTKHQYDYDSATVVGFLRHYGLDKDFKLNIEVNHATLAGHTFQHELQVAADAGLLGSIDANRGDYQNGWDTDQFALNLQELTESLLVILEAGGLQGGGVNFDAKLRRNSTDLDDLFHAHIGSMDAFARALLIANDILEQSEYKALRKKRYASFDGGKGKEFEEGKLTLEDLREHAIATGEPASTSGKQEMYENIINQYI Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1879 Echvi_1879 L-arabinose isomerase (EC 5.3.1.4) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (ARABISOM-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-arabinose isomerase MKNLKENEVWFITGSQHLYGPEALQQVAEHAQIIAEELNKSEKISVTTVFKPIVTTTEEIYAAIQEANNAPNCIGVITWMHTFSPAKMWINGLKILQKPMLHLHTQYNQDIPWNSIDMDFMNLNQSAHGDREFGFMTARMKVKRKVVVGHWKDEEVHSQIDVWARAASGWHDWQGAKFARFGDNMRFVAVTDGDKVEAELKFGFSVNTYAVGDLVAKIEAVSEGDLKALIEEYEATYTLSEELQANGAKRQSLIDAAKIELGMRAFLEEGGFKGFSNTFEDLYGMKQLPGIATQRLMADGYAYAGEGDWKTAALVRAMKVMGSGLEGGNAFMEDYTYHFDPNNSLVLGSHMLEVDPTLTTEKISCEVHPLGIGGKEDPVRLVFNGAGGNGLNASIVDMGNRFRLIVNDVEAVKPLKDLPNLPVARVMWKPMPDMKTGCAAWILAGGAHHTCFSQNLTSEHLNDFAVMAGIESVNIDKETTLRGIQNELRWSDAYYHFNDK Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1901 Echvi_1901 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrite reductase [NAD(P)H], large subunit MTKIVVIGNGMVGYKFCEKLRAQATEGDFEITVFGEEPWPAYDRVHLSAYFSGSTADDLMMAPRSWYDENNVDLHTNEMIVKIDRDAKKIISHTGHDYAYDKLILATGSAAFVPPIDGVDKKGVFVYRTLEDLDAIIDYSKKVKSAAVIGGGLLGLEAAKAVIDMGLDAHVIEFAPRLMPRQLDTAGSATLQAKLEALGIKIHLSKNTKKITGNGKITGMSFADNTNLNTEMLIISAGIKPRDELAKDAGLTTAPRGGIVVNEFLQTDDTDIYAIGEAASYQNMVYGLVAPGYEMATQVVNQLVNTEVKPFMGFDMSTKLKLIGVDVGSFGDPFGEIEPSKPIVYENKNSGIYKRINVSMDGKRLLGGILVGDASAYNILLQMTQNNMPLPPEPEDLILGARGGKEAAGAGVESLPEEAQVCSCENVTKGAICSLIENDGVTKVDEIKSCTKAGTGCGGCMPMVNDLLKHQLKSMGKTVKNVICEHFDYSRQELLDIVKVKGIKSYNELLDQFGQGDGCEVCKPAVASILASTWNELITKQDTIQDTNDRYLANIQKGGTYSVVPRIPGGEITPEKLIVLGDVAKRYNLYTKITGGQRIDLFGARVDQLPDIWEELIEAGFESGHAYGKSLRTIKSCVGSTWCRYGVQDSVSFAIEVEERYRGLRSPHKLKGAVSGCIRECAEAQSKDFGIIATEKGWNLYICGNGGSKPQHAQLLINDVDRETCLKYIDRFLMFYIRTAEPLTRTATWLNKLEGGMDYVRDVVVNDSLGIGEELEKEMAFMIDTYACEWKEVVNNPELRAKFKHFVNADEEDPNLKWQEMRGQKIPASWG Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1912 Echvi_1912 Nitrate reductase (EC 1.7.99.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.99.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Uncharacterized anaerobic dehydrogenase MSTAKPESYKSTCSYCGVGCGIIVNKDNKGRTTVEGDPDHPVNRGMLCSKGMNLHYVVEDKSDRLQYPQMRWGKSHPLERVDWDTALSRSAAVFKSIIKKHGPDAVAFYVSGQCLTEEYYLVNKLSKGFLKTNNIDTNSRLCMSSAVMGYIKTLGEDSVPISYEDIELADCFLVAGANPAWCHPILWRRVEKHKEENPDTKIIVVDPRVTQSCSLADLHLQLNPGTDEVLYLAIGRCLIENGDIDVDFIQHHADGFDAYKELVMETSLESAAATCGVPVEDIKLAASYIGDAKGFLSLWAMGLNQSAEGVNKNLALIDLNLITGHIGKPGSGPFSLTGQPNAMGGREVGGMATLLASHRNLMNPEHRQEVADFWGVDSLPDQPGKTATQIFEGLEEGSIKALWIICTNPLVSMPDARRVEAAMKKAKFVVVQDISAKAEAIPYADLVLPAAGWGEKEGTMTNSERRISYLNKFTDAPGEALPDAEILLKFAKKMNYSGFDFKNMAEVYAEYCQLTKGTNIDISGLDYDYLKSNGTVQWPFTDKSKGGTARLFTDKKFYTPNGRAQILANGPKNKTELPSDDYPLILTTGRIRDQWHTMTRTGKVSKLNKHIPTPFLEIHPEDAAERNLKDGETVLISGKRGEVRVHAQITDKIKKGVVFLPMHWGKILQNDFSRTNNLTGNGIDPVSKQPDFKFSTVQVAKYVKPRQKIVIVGAGAAAYRFINTYREFNQNDDIHVFSKEKHPFYNRVLLPDYVNRHKAWEDLLKFKNQGDMEKLNIQLYVENGIESIDRSNKTVTDEKGRVHHYDTLILATGSRAFVPPDMPMHLPGTFTMRSRYDADKLKEYLNYEGNVLIAGGGLLGLELAAALREINVGVTIVQLGSRLMERQLDPMASSLLRERIEEMGVKLYMNNQIAHLDSHEATKEVDVRLKSGQEIHCNAVVLAIGTRPNMELAKSAGLTCGRGIKVNDYLQTSDPSIFAMGEIAEHKGKLNGITAAAEMQADIAARFITGDLLSLYKGSIPMNILKFADLDLCSIGIPEVPANGEGYEEILLIDTAQTYYKKCIVHHDRLVGAILMGDKSEFAEFKGLIEEKTELSKKRQELLRGNANKEEMIGEMVCSCGNVGTGNISKAIQNGCHEFRQLCQQTGAGLGCGSCKPEVKSILETELPALVKA Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_2804 Echvi_2804 Fructokinase (EC 2.7.1.4) Specifically important for utilizing D-Fructose. Automated validation from mutant phenotype: the predicted function (2.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Sugar kinases, ribokinase family MNKKAVIFGEMLWDCFPDKQLPGGAPMNVALHLQHLGITTTFISKIGSDSLGADLLSFVQKNGLNGDFVQRDTAHETSRVVVDNSDKENIKYEIVKPVAWDFMEWNTAIQEKVDEADVFVFGSLAARSSQSQNTLFRLLETSTLKVLDINLRPPHYSTKVLERLLKNTDVLKINEDELEILIEMSALDKNEEKALSAIVDRYELQLVCMTKGSAGAIIYDGREFYRHPGYQVDVEDTVGSGDAFLSGFISQYLKGNHPNKILDFACALGALVATQKGGTPRYDTDQITAIQDNNS Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_2850 Echvi_2850 Alpha-amylase (EC 3.2.1.1) Specifically important for utilizing a-Cyclodextrin. Automated validation from mutant phenotype: the predicted function (3.2.1.1) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Glycosidases MRNLLRSFTYCTLVLLTASCMQDANEELEVKNYWPEAGITYEIFIQSFYDTDGDGIGDINGVTKKLDHVQELGANAIWFMPLMPSPSYHKYDVTDYKAIHPDYGTMDDFKQMLDEAHKRDIKVVIDMIINHTSDEHPWFQEAKKGRDNPYRDYYVWAQYDTIQDYLDKKVVTLDSDNIRQWHDPGQGDDYYYGFFTGDMPDLNFDNPKVREEIYEIGRYWLAEVGVDGFRLDAAKHIYPDDRAADSHEFWEEFRAEMEKVKPDVYLVGEVYDMKEVVAPYLTGLRALFNFDFHYTLLEAYKKEDGMLLAKKQHDILAFYNGITDDFIDATISSNHDQPRLLNELGKSKDKLKQAIAILMTMPGAPYIYYGEEIGMLGKKPDPNIREPFLWDVAEQDEGRTKWITPAFSTDNTVTPLAIQKEDADSYFNHYKRVIQLRNTHPALAIGSLELPAEKYPKAVMAYQRKTGEQELYVFHNLGKKSVEIPLPQGFDREVYHLKGAKVNGDKIKLPAFSSIVLGK Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS06130 RR42_RS06130 Gluconokinase (EC 2.7.1.12) Specifically important for utilizing D-Gluconic Acid sodium salt. Automated validation from mutant phenotype: the predicted function (GLUCONOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. gluconate kinase MIYILMGVSGSGKTTVGQLLAKTLQCGFHDADEFHSAANKAKMHNGIPLTDDDRWPWLAAMRAAIDAARAEGRTHVFTCSALRQTYRDRLTPADGGVTFVYMKGDAAIIGGRLAERSEHFFNPALLQSQFETLEEPREALVLDIRQTPEALVQCILAGVQAQKGVAIAR Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS11260 RR42_RS11260 Methylisocitrate lyase (EC 4.1.3.30) Specifically important for utilizing Sodium propionate. Automated validation from mutant phenotype: the predicted function (4.1.3.30) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 2-methylisocitrate lyase MTFSTSDLARSAGARFRQALADEHPLQVVGTINANHALLAKRAGYRAIYLSGGGVAAGSLGLPDLGISNLDDVLTDVRRITDVCDVPLLVDVDTGFGASAFNVARTTRSLIKFGAGAMHIEDQVGAKRCGHRPGKEIVSQGEMADRIKAAVDARTDENFVIMARTDALAVEGLDKAIERAVACVEAGADAIFPEAMTDLAMYRKFVDAVKVPVLANITEFGATPLFTTEELGGAGVSMVLYPLSAFRAMNKAAENVYAAIRRDGTQQNVVDTMQTRAELYESIGYHAYEQKLDALFAQGKAK Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS15385 RR42_RS15385 Kynureninase (EC 3.7.1.3) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (KYNURENINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. kynureninase MTAMTREQCLALDQEDPLRRLRDQFALPQGVIYLDGNSLGARPRSAAARAAEVVSEEWGTGLIRSWNTAGWFELPQRLGNMLAPLIGAGEDEVVVTDTTSSNLFKVLAAALRVQQTRDPKRKVIVSEASNFPTDLYIAQGLADLLQQGYSLRLVNAPEEIDAAVDADTAVLMLTHVNYKTGEMLDMASVTEMAHARGALTVWDLAHSAGAVPVALKASGADYAVGCTYKYLNGGPGSPAFLWVAPSLRDAFWQPLSGWWGHAAPFAMEPGYRPREGVARFLCGTQPIASLAMVECGLDIYAQTDMAVLRAKSLMLTDLFIALVETRCAAHPLELVTPRAHARRGSHVSFAHPDGFAVVQALIERGVIGDYREPRIARFGFTPLYTSFTEVWDAVEILRDVLDSGTYKAERHQTRGLVT Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS15390 RR42_RS15390 Tryptophan 2,3-dioxygenase (EC 1.13.11.11) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (RXN-8665) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. tryptophan 2,3-dioxygenase MSNHKGCPMSGAGATETSDASWHDAQMDFAKDMSYGDYLALDQILNAQHPLSPEHNEMLFIVQHQTSELWMKLALHELRAARECVRQDQLPPAFKMLTRVSRIMEQLVQAWNVLATMTPPEYSAMRPYLGMSSGFQSFQYREIEFILGNKNAAMLRPHAHQPQHLALLEEALRTPSLYDEAIRLMARRGFAIDAACIERDWTRPAGENASVEAAWLEVYRKPEAHWELYELGEKFVDLEDAFRQWRFRHVTTVERVIGFKRGTGGTEGVSYLRKMLDVVLFPELWKLRTDL Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS16895 RR42_RS16895 N-formylglutamate deformylase (EC 3.5.1.68) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (N-FORMYLGLUTAMATE-DEFORMYLASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-formylglutamate amidohydrolase MAFSTDTPAFTLHRGTRPMLVSMPHVGTHLPACVSDRLTAEARTVPDTDWHLERLYDFARELGASILVATHSRYVVDLNRPPDNANLYPGQDTTGLCPVDTFDKTPIYADASGLPADDEIAARRDAIWRPYHGALAEELARLRAEHGTVALWDAHSIRSVLPRFFEGKLTDFNLGTANGASCDAALANQLLDIAGALPGYTSVLNGRFKGGYITRQYGAPAQGVQAVQLELTQSAYMSETYPFAYDEARATRIQPTLKTMLETVLGYVEAR Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS16905 RR42_RS16905 Imidazolonepropionase (EC 3.5.2.7) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (IMIDAZOLONEPROPIONASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. imidazolonepropionase MSSSTESAKSADGVWHRCHLLPDGDPAKAIRDAALVVQQGRIVWLGMQAELPQAYAALPRHDAGSAWITPGLVDCHTHLVYGGQRADEFAMRLAGAGYEEIARAGGGIVSTVRATRAADEDTLFALAAARLAPLLAEGVTTLEIKSGYGLDLASERKQLRVARRLGDAFGVTVHTTFLGAHALPPEYAGRADDYITLVCETMMPVLADEGLIDAVDAFCESVGFSLAQTERVFQAAERHGLRVKLHAEQLSNLGGTALAARYRALSADHLEHLDEAGVVAMAGSGTVAVLLPGAYYFLRDTNLPPIDLLRRHGVPMAISTDHNPGTSPVTSLLLMMNMACTLFRLTVPEVLAGVTTHAARALGAADRHGLLAAGRAADFVLWNVDSPAELAYWFGRNPAAAVVRQGKVYPAATSVQGVRP Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS20080 RR42_RS20080 L-serine ammonia-lyase (EC 4.3.1.17) Specifically important for utilizing L-Serine. Automated validation from mutant phenotype: the predicted function (4.3.1.17) was linked to the condition via a SEED subsystem. This annotation was also checked manually. serine dehydratase MAVSVFDLFKVGIGPSSSHTVGPMRAALMFAQGLARDGLLPQVASVRVELYGSLGATGRGHGTDKGVILGLLGEAPDTIDPDTIDVRLAALRASRTLSLLGTHPVPFVEKEHIVFYRREAMAEHPNGMKFHAFNAGGERIREGRYLSVGGGFIITAGAANTHILEADQQLPHPFRSGRAMLEMAAASKKSIARLMMENECVWRSEAEVNAGLLQIWAVMQACVARGCRTDGELPGPFKVKRRAHDLFRNLTEHAERALADPLSVIDWVNLYAIAVNEENAAGGRVVTAPTNGAAGIIPAVLHYYDRFVPGANPQGVIDFLLTAGAIGMLYKLNASISGAEVGCQGEVGVACSMAAGALAAVMGGTPEQVENAAEIGMEHNLGLTCDPVGGLVQIPCIERNAMASVKAVNAARMALRGDGMHYVSLDSVIKTMRETGADMKTKYKETARGGLAVNIVEC Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS20125 RR42_RS20125 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) Specifically important for utilizing L-Proline. Automated validation from mutant phenotype: the predicted function (1.2.1.88, 1.5.5.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. transcriptional regulator MATTTLGVKLDDASRERLKRVAQSIDRTPHWLIKQAIFTYLEQVERGNIPHETSAAGTGSEGAADGADAFDGAASDGAIQPFLEFAQSVQPQSVLRAAITAAYRRPESECVPVLLEQARLPHQQAEAALAMARTLATRLRERKVGTGREGLVQGLIQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISGANWQSHLGQSPSVFVNAATWGLLFTGKLVATHTEAGLSKALTRIIGKGGEPLIRKGVDMAMRLMGEQFVTGETISEALANARKYEAEGFRYSYDMLGEAAMTEADAQRYLASYEQAINAIGQASRGRGIYEGPGISIKLSALHPRYSRAQHERVIGELYGRLKSLTLLARQYDIGINIDAEEADRLEISLDLLERLCFEPELAGWNGIGFVVQGYQKRCPFVIDYLIDLARRSRHRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYVACARKLLSVPDVIYPQFATHNAHTLAAIYQIAGHNYYPGQYEFQCLHGMGEPLYDQVVGPLADGKFNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADDTISLDELVADPVAVVEQMHADEGALGLPHPRIAQPRTLYGESRANSAGIDLSNEHRLASLSSALLAGTSEAVSAVPLLGTEAAAGEDVNQPAPVRNPSDQRDVVGHVTEASMAEVEAALQAAVNAAPIWQATPADVRAAALERAAELMEAQMQSLMGIIVREAGKTFSNAIAEVREAVDFLRYYAAQVRETFSSDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLREAGVPAGAVQLLPGRGETVGAALVGDARVKGVMFTGSTEVARLLQRSVAGRLDAAGRPVPLIAETGGQNAMIVDSSALAEQVVGDVVNSAFDSAGQRCSALRVLCLQEEVADRVLEMLKGAMDELTMGNPDRLSTDVGPVIDEEARGNIVRHIDAMRAKGRRVHQADPNGALSAACRNGTFVSPTLIELDSIEELQREVFGPVLHVVRYPRAGLDTLLAQINGTGYGLTMGIHTRIDETIEHIVERAEVGNLYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLHRLLSVCPLDAVARVVRASDTVGGADETGPVRRTLTETLATLKEWAQRESAALPGLVAACERFAAASAAGLSVTLPGPTGERNTYTLLPRAAVLCLAQQETDLAVQLAAVLAAGSQAVWVESPMARALFARLPKAVQSRVRLVADWSAGDTGFDAVLHHGDSDQLRAVCEQLATRPGPIISVQGLAHGEPNIAIERLLIERSLSVNTAAAGGNASLMTIG Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS21940 RR42_RS21940 4-hydroxybenzoate 3-monooxygenase (EC 1.14.13.2) Specifically important for utilizing 4-Hydroxybenzoic Acid. Automated validation from mutant phenotype: the predicted function (1.14.13.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 4-hydroxybenzoate 3-monooxygenase MRTQVAIIGAGPAGLLLGQLLAKAGIDAVIVEQRSPDYILGRIRAGILESVTADALERAGVAQRLQHDGLVHHGIELSYGGERHRIDFHALIGRSVTVYGQTEVTRDLMAARQAGNAVTIYDAQDVSVHDFDTATPMVRYRKGGQQYELRCDFIAGCDGFHGVTRRSVPEPSRRIFERVYPFGWLGVLADTPPVANELIYASHERGFALCSMRSLTRSRYYVQVSADERVEDWSDQRFWDELRSRLDTSAAEALVTGASIEKSIAPLRSFVCEPMRFGNLFLAGDAAHIVPPTGAKGLNLAASDVLYLADGLIARYLRDDASELDAYSQKCLRRVWKAERFSWWMTSLLHRFPDADDFALRIQQAELDYLAGSRAAQMSLAENYVGLPY Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS25890 RR42_RS25890 Branched-chain amino acid aminotransferase (EC 2.6.1.42) Specifically important for utilizing L-Isoleucine. Automated validation from mutant phenotype: the predicted function (BRANCHED-CHAINAMINOTRANSFERILEU-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. branched-chain amino acid aminotransferase MTQQTTFSLEPNPNALDAATRDALMRDPAFGRVFTDHMVTITWREGQGWQDAKVTARKPFSIDPACSVLHYGQEIFEGMKAYRGADGAVTLFRPLENARRFQASAKRMAMPALPESLFLEAIEQLVRIDQAWVPHGSGSLYLRPFMFANEVFLGIKPASEFIFCVIACPVGPYFKGGDKAVSVWVSENYTRAAPGGTGEAKCGGNYAGSLVAQNEATANGCDQVVFLDAAEHRWVEELGGMNIFFVMDDGTLVTPPLSGSILPGITRASVIELAREMGMVVEERRYSYPEWEADAKSGRLAEAFVCGTAATLVAIGEVRSARTRFAIGNGTAGNTVKVLRDRLVEIQRNQAAGPAGWVHHVAL Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS28295 RR42_RS28295 2-amino-3-ketobutyrate coenzyme A ligase (EC 2.3.1.29) Specifically important for utilizing L-Threonine. Automated validation from mutant phenotype: the predicted function (AKBLIG-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 2-amino-3-ketobutyrate CoA ligase MPTTDAFYAAIRQELESIEQAGLFKTERVIASPQGSLIRTTDGKEVINLCANNYLGLSSHPEVVEAAHRALGERGFGLSSVRFICGTQDLHKSLEARLASFLGTEDTILYGSAFDANGGLFETLLGSDDAVISDELNHASIIDGIRLCKAKRFRYKNNDLEDLREQLKAADAAGARFKLVFTDGVFSMDGTIARLDEIREICDEFGALLGIDECHATGFLGQRGRGSHEHRGIFGKVDIITGTLGKALGGASGGFTSGRKEVVALLRQRSRPYLFSNTVAPCIVGATLKVLDLLEADTTLRDKLERNARYFRGKLGTLGFDVKPGDHPIIPVMVYDAEKAQRLSRRLLELGVYVIGFFYPVVPRGQARIRVQISALHDSAELDQALEAFEIAGKELGIIQ Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS28545 RR42_RS28545 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) Specifically important for utilizing L-Valine. Automated validation from mutant phenotype: the predicted function (3.1.2.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. enoyl-CoA hydratase MRLNPNDAAQERPAAAPSADDEVRFDEINGIGLITLNRPRQLNALSYPMIGLLDAQLAAWAARDDIAAVVLRGAGPKAFCAGGDIRALYDSFHAGTALHRQFFVDEYQLDYRLHCYPKPVVALMDGIVMGGGMGLAQAAHLRVLTERSRVAMPETGIGLVPDVGASHFLSKLPLALALYVGLTGVTLGAADTLLCKLADIAVPAASLEHFEQTLAAINRTGDVLADLRAALQATPDAGEQAAPLQSVLPAVLRHFRADASVAGLLDSLAAESDPAYADWAARTLDILRGRSPLMMAVTRELLLRGRDLDLADCFRMELGVVSHAFSQGDFIEGVRALIVDKDNAPRWRVKDASEVSEAVVQSFFDSPWPREPHPLAMLGRSGQA Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS28860 RR42_RS28860 2-dehydro-3-deoxygluconokinase (EC 2.7.1.45) Specifically important for utilizing D-Gluconic Acid sodium salt. Automated validation from mutant phenotype: the predicted function (2.7.1.45) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 2-dehydro-3-deoxygluconokinase MSIDILAFGEALVEFNQQPDDPSRYLQGFGGDTSNFCIAAARQGARAGYISAVGEDTFGERLLALWTQERVDTRHVRIDAGAPTGVYFVTHDAHGHRFDYLRSGSAASHYSHENLPHHAIAEARYLHVSGISLAISTSACDAGLAAMEHARKAGCQVTLDTNLRLRLWTLARARGIMREAFALTDVCLPSWDDITVLTGLDDRDAIVDYLLGCGIGLVALKLGEEGAYVATPEARTLVPPYTVRPVDATGAGDCFGGSFVARLAAGDDPFDAARYANVAAALSTTGYGAVAPIPSIETVLARMAQSVSVIA Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS31275 RR42_RS31275 Homogentisate 1,2-dioxygenase (EC 1.13.11.5) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (1.13.11.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. homogentisate 1,2-dioxygenase MTQTQLNVVNVTGQAPDHGTPGYQSGFANEFATEALPGALPVGQNSPQRAPYGLYAEQISGTAFTAPRAHNRRSWCYRIRAAAMHEPFTRVEQSRIVSHFDAVPPSPNQMRWSPPAMPKEPTDFVDGIITMAGNGGPEAMSGCGIHLYLANRSMTDRFFYNADGEMLIVPQQGRLRLATEMGLLDVEPQEIVVIPRGVRFRVELPDGEARGYICENYGALFRLPDLGVIGSNGLANPRDFLTPHAWYEDREGDFELVAKFQGNLWRAAIGHSPLDVVAWHGNYAPYKYDLRRFNTIGSISFDHPDPSIFLVLQSPSDTPGVDSIDFVIFGPRWLAMQNTFRPPWFHRNIASEFMGLIEGVYDAKADGFSPGGASLHNCMSGHGPDAETFAKATAADTSQPHRIGDTMAFMFETPAVIRPTPYAAESAQLQDDYYRCWQGLKKHFNPNER Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS31785 RR42_RS31785 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate; Sodium nitrite. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrite reductase MKLIIIGHGMVGHKFLECLAEAGSQDLEVTVLCEEPRPAYDRVHLSEFFAGKSAEDLSLVEAGFFERSNMLLRLNARATGIDRAAKTVTVSTGETLSYDKLIMATGSYPFVPPLPGKDRKDCFVYRTIEDLEAMQECGARSRTGVVIGGGLLGLECAKALRDMGLQTHVVEFAPRLMAVQVDDGGGAMLRRKIEELGVTAHTRKNTVEIVDGEDGTHRMNFADGSHLDTDMIVFSAGIRPRDELARASGLAIGERGGIAVDNQCLSSDPDVYAIGECALWDGKIYGLVAPGYEMARVAAKHLLGHRAEFAGADMSTKLKLMGVDVASLGDPHGNAPGSRSFQFTDERKQVYKKLVVSECGKYLLGGVLVGDAEEYGTLLQMMLNKIELPESPEFLILPSSDGQAKPGLGADALPDSAQICSCNNVTKGDICAAVCSGTTNIGDMKRCTKAGSTCGGCVPLVTQVMKAEMKKQGLAVNNHLCEHFAYSRQELYHLVRVGGFKTFGELLAAHGKGLGCDVCKPTVASILASCWNEFVLKQEHASLQDSNDYFLGNIQKDGTYSVVPRMPGGEVTPDGLIAVGQVAKKYGLYTKITGGARVDMFGARVEELPMIWEELIAAGFESGHAYGKSLRTVKSCVGSTWCRYGVDDSVGLAIEIENRYKGLRAPHKIKFGVSGCTRECAEAQGKDVGIIATERGWNLYVCGNGGMKPRHAELLASDLDRATLLRYVDRFLMFYVRTADRLQRTSVWRDNMEGGLDYLKAVVLDDSLGIGAELEAQMQHVVDTYEDEWKAAVTNPETRKRFRHFVNSDLRDDNLVFMEERGQIRPATPEERNLRKSRLEQIPVIVKAA Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS31800 RR42_RS31800 Nitrate reductase (EC 1.7.99.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.99.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrate reductase MNLSDIPVILSTGSPTLLSADASVTVTDTTCPYCGVGCGVRATRHADGSVEVAGDTSHGSNQGRLCVKGSALAETVGLEGRLLHPQVRGADGALQPVSWDHALDKVAQGFKDIIAEHGPDAVALYVSGQLLTEDYYVANKLMKGFIGSANIDTNSRLCMSSAVAGHKRAFGEDLVPGNYEDLELADLVVLVGSNTAWCHPILFQRLLKAKEARPEMKLVVIDPRRTATCELADLHLPVKPGTDVWLFNGLLHYLAQHGAVDQSFVDAHTSGLDAALAAAGPDCADIAKVAKACKLDPEALRGFYALFAATPKVVTGFSQGVNQSSAGTDKVNSIINCHLATGRVGQPGMGPFSLTGQPNAMGGREVGGLANMLAAHMELADPLHREIVQSFWGSPAIADKPGLKAVELFEAIEQGRVKAVWVIATNPVVSLPDADQARRALAKCQLVVSSDIMLRTDTNDAAHVLLPALGWGEKDGTVTSSERRISRQRAFLPAPGEARADWRILCDVATRMGFDGFRFAGPHEIFDEHARLSTYRNAGSSDQPHAPRMFDLAGLAGMSQKQFDALSPVQWPVMATPPGRLANASGGTARLFADGRFAHPDGRARFIATAPRAPFHATDDEFPLVLNTGRVRDQWHTMTRTGKSPKLADHIAEPFVDMHPQDALLSGVSEGKLARVTTRWGAMVARVQHSGGIPRGSVFVPIHWNGQFSSDARVGALVNPVVDPVSGEPEFKHTPVRVEEFRVSWHGFVLSREDLQADELTYWTRVQGRQFQRYEFAGRENIADRAAWARQLLGIDDPNADWIEYEDRTAGIYHAGHVVDDRLQACLYVCTRPDLPSRAWLSTLFAKDRLEDADRIGLLLGQPMEKGADAGPTVCSCFGVGRNTICDAVRKHDLKTPAEVTACVKAGGNCGSCVPELKKLLAEIRVAEVA Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS33490 RR42_RS33490 Aromatic-amino-acid aminotransferase (EC 2.6.1.57) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (PHEAMINOTRANS-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. aromatic amino acid aminotransferase MFEHIDAYPGDPILSLNESFQLDPRTDKVNLSIGIYFDDEGRLPVMQAVREAEAALMADMGPRPYLPMAGFAAYRDAVQALVFGQPCQARAEGRIATVQTLGGSGALRVGADFLKRYFPDAQVWISDPSWENHRVIFERTGFTVNTYPYYDDATGGLKFDAMLDALRLIPKRSIVLLHACCHNPTGVDLNHDQWRQLITLLKQHELLPFVDMAYQGFGAGLDDDAFAVRELVAQGVPCLVANSFSKNFSLYGERCGGLSVVCDSAEETGRVLGQLTGAVRANYSNPPTHGARVVARVLTTPALRTIWERELAGKCERIAKMRAAIHKGLAAHVSGEALSRYLTQRGMFTYTGLTADQVDRLRTEHGVYLLRSGRMCVAGLNERNVTQVAQAIASVLAPAA Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS34260 RR42_RS34260 Alcohol dehydrogenase (EC 1.1.1.1) Specifically important for utilizing Ethanol. Automated validation from mutant phenotype: the predicted function (ALCOHOL-DEHYDROG-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. alcohol dehydrogenase MTAMMKAAVVREFGAPLTIDEVPVPQPGRGQIQVKIEASGVCHTDLHAAEGDWPVKPTLPFIPGHEGVGYVSAVGAGVSRVKEGDRVGVPWLYSACGYCEHCLQGWETLCEKQQNTGYSVNGGYGEYVVADPNYVGLLPDSVGFVEIAPILCAGVTVYKGLKVTDTRPGQWVVISGIGGLGHVAVQYARAMGLRVAAVDIDDKKLELARKLGAEVTVNARTTDPVAFLQKEIGGAHGALVTAVSPKAFGQAIGMVRRGGTIALNGLPPGDFPTPIFDVVLKGITIRGSIVGTRSDLQESLDFAAHGAVKATVSTAPLEKINEIFTRMRAGDIEGRVVMDFAA Dinoroseobacter shibae DFL-12 Dino 3607129 Dshi_0551 D-xylulose reductase (EC 1.1.1.9) Specifically important for utilizing Xylitol. Automated validation from mutant phenotype: the predicted function (1.1.1.9) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Alcohol dehydrogenase GroES domain protein (RefSeq) MARALVLEAARKLALRDIDLPDELGPEDVRIAIDTVGVCGSDVHYYTHGKIGPFVVKQPMVLGHEAAGIVTEIGAAVTHLALGDRVCMEPGIPNGSSKASKLGVYNVDPAVQFWATPPVHGCLTPSVVHPAAFTFKLPDHVSFAEGAMVEPFAIGMQAAAKARIKPGDVALVTGAGPIGVMVALAALAGGCAKVFVSDLVEDKLAIAAGYDNIHPILIPRDNPAEVLQEATEGWGADVVFECAGAAASIQAALEAAAPAGCVVWVGMPVDPVPVDIVLAQSRELRMETVFRYANMYDRAIALLASGKVDLKPLISATFPFEDSIAAFDRAVEARPTDVKIQIKMGAS Dinoroseobacter shibae DFL-12 Dino 3607303 Dshi_0718 Propionyl-CoA carboxylase carboxyl transferase subunit (EC 6.4.1.3) Specifically important for utilizing Sodium propionate. Automated validation from mutant phenotype: the predicted function (PROPIONYL-COA-CARBOXY-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. carboxyl transferase (RefSeq) MKDIQHELDQRRLDARMGGGEKRIASQHAKGKLTARERIELLLDEGSFEEFDMFITHRCTDFGMQEQKPAGDGVVTGWGTVNGRQVYVFSQDFTVLGGSVSATHAKKICKIMDMAIENGAPVIGINDSGGARIQEGVDSLAGYGDVFQRNIEASGVVPQISMIMGPCAGGAVYSPAMTDFIFMVKDSSYMFVTGPDVVKTVTNEVVTAEELGGASTHTRKSSVADAAFENDVEALAEVRRLIDFLPLNNREKAPVRPFFDDPARVEESLDTLIPDNPNQPYDMKELITKVADEGDFYEIQKDFAGNIITGFIRLEGQTVGVVANQPMVLAGVLDIDSARKAARFVRFCDCFEIPILTLVDVPGFLPGTGQEYNGVIKHGAKLLFAYGEATVPKVTVITRKAYGGAYVVMSSKHLRGDINYAWPTAEVAVMGAKGATEIIHRADLGDPEKIAARTAEYEDRFANPFVAAERGFIDEVIMPQSTRRRVARAFAALRNKRAVKPWKKHDNIPL Dinoroseobacter shibae DFL-12 Dino 3607308 Dshi_0723 Propionyl-CoA carboxylase biotin-containing subunit (EC 6.4.1.3) Specifically important for utilizing Sodium propionate. Automated validation from mutant phenotype: the predicted function (PROPIONYL-COA-CARBOXY-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Carbamoyl-phosphate synthase L chain ATP-binding (RefSeq) MFKKILIANRGEIACRVIKTARKMGIQTVAIYSDADRNALHVRMADEAVHIGPSPANQSYIVIDKVMDAIRQTGAEAVHPGYGFLSENKLFAEALEKEGVAFIGPPANAIEAMGDKITSKKIAQEANVSTVPGYMGLIADADEAVKISGEIGYPVMIKASAGGGGKGMRIAWNDAEAREGFQSSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLADTHGNCIYLGERECSIQRRNQKVVEEAPSPFLDEATRKAMGEQSCALAQAVGYASAGTVEFIVDGDRNFYFLEMNTRLQVEHPVTELITGVDLVEQMIRVAAGEKLPMTQDDVTLTGWAIENRLYAEDPYRNFLPSIGRLTRYRPPVEVAAGPLEANGKWHGDAPSGPTAVRNDTGVYEGGEISMYYDPMIAKLCTWGPDRPAAIEAMRNALDGFEVEGIGHNLPFVAAVMDHPVFIKGEMTTAFIKEQYPDGFEGVTLGAADLTRLAAAAAAMFRVAEIRRTRISGTLDNHERMVGTDWVVTAQDARFDVTIDADPGGSTVRFADGTAHRVTSRWTPGDSLATVEIDGAPMVLKVDKITSGFRMRFRGADVKVHVRTPRQAELNDLMPEKLPPDTSKMLLCPMPGLVVKIDVEVGDEVQEGQALCTVEAMKMENILRAEKTATVTKINAGAGDSLAVDDVIMEFE Dinoroseobacter shibae DFL-12 Dino 3607415 Dshi_0829 Phosphopentomutase (EC 5.4.2.7) Specifically important for utilizing Adenosine. Automated validation from mutant phenotype: the predicted function (PPENTOMUT-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. phosphopentomutase (RefSeq) MTRAFLIVMDSVGCGGAPDAADFGDEGANTLAHIAQACAAGRADAGRSGPLRMPVLDGLGLGAAIRLASGAETPGLAATPTGLWGAATEVSRGKDTPTGHWELAGVPVPWEWTTFPDTDPAFPPDLLAEMARAAGTEGTLCNTHASGTEVIERFGAEHLRTGWPICYTSVDSVLQIAAHEEAFGLDRLLDVCETLAPRLHAMKVGRVIARPFLGSEATGFARTQNRRDFAIAPPAPTLCDRVQAAGRRVHAIGKIKDIFSGRGIDTVAKGSDAALMEALIAAGQVAEEGSLTFANFVEFDSLYGHRRDVAGYARALEWFDAQLPRFLATLRPGDLAIFTADHGNDPTWHGTEHTRERVPVVGYGVGVHEVGIVGFRDVGATIGAHLGVEMFDMGKAMLP Dinoroseobacter shibae DFL-12 Dino 3607416 Dshi_0830 Adenosine deaminase (EC 3.5.4.4) Specifically important for utilizing Adenosine. Automated validation from mutant phenotype: the predicted function (ADENODEAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. adenosine deaminase (RefSeq) MKELPKLELHLHLEGAAPPAFIRGLAAEKSVNLSGIFDARGAYAYRDFVDFLRVYEAACTVLQTPQDFYRLTRAVLEASSAEGVIYTEAFLSPDFCGGRDLDAWRDYLAAMTEAAADAEAADGIVMRGIVTCIRHFGPEAARETARCAAETAGAFITGFGIAGDEMKGAPKDFAYAFDMAREAELQLTAHAGEWGGARSVRDAVRDLGVTRIGHGVQAIEDPALLEELAEAGITLEVCPGSNVALGVYPNWRAHPIERLRKAGVPVTVSTDDPPFFHTTMSGEYENLAQSFGWELPDFAAITYAALDAAFCDTATREALRTRLAPTFGEFT Dinoroseobacter shibae DFL-12 Dino 3607955 Dshi_1363 Dihydropyrimidine dehydrogenase (NADP(+)) (EC 1.3.1.2) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (1.3.1.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. dihydroorotate dehydrogenase family protein (RefSeq) MADLRSDFVGVKSPNPFWLASAPPTDKEYNVRRAFEAGWGGVVWKTLGFDPHVVNVNGPRYGAVWGADRRLLGLNNIELITDRPLEVNLREIKQVKRDYPDRAMVVSLMVPCEEDPWKKILPLVEETGADAVELNFGCPHGMSERGMGSAVGQVPEYIEMVARWCKQHTRMPVIVKLTPNITDIRYPARAAHAGGADAVSLINTISSITSVNLDSFSPEPSIDGKGSHGGYCGPAVKPIALNMVAEIARDAETAGMPISGIGGVTTWRDAAEFLALGAGNVQVCTAAMTYGFKVVQEMISGLSQYLDEKDMTLDDLIGRATPNVTDWQYLNLNYVTKARIDQDSCIKCGRCYAACEDTSHQAISMSADRVFEVIDAECVACNLCVNVCPVEDCITMVEMQPGEVDPRTGKVVEKDYANWTTHPNNPASQAAE Dinoroseobacter shibae DFL-12 Dino 3608263 Dshi_1667 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrite reductase (NAD(P)H), large subunit (RefSeq) MKQELVIIGAGMASGRVIEHLLKEDPDAFEITLFNAEPRGNYNRIMLSPVLSGDKSYADIITHTDDWYEQNGITCRFGEHVVRIDRETGTVVGQRGALPYDKLLIATGSAPFIIPVEGKDLPGVITYRDLDDTNAMIEAAASGGKAVVIGGGLLGLEAAAGLKERGMDVTVLHLMGHLMERQLDESAGFLLRRDLEKRGIKVKCRASTAAILGETRVEGVLLEDNEGLEADLVVMAVGIRPETRLATDAGLDVARGITVDAELRTSDPDIHAVGECVEFDGQLFGLVAPLYDQARVVADSLLGRSAAFTPKELSTKLKVTGCDLFSAGDFADGAGREDIVFRDPSRGVYKRLVLEENRLVGAVFYGDTRDSNWFFGLIQSGEDISEMRDTLIFGPAYQGGAALDPMAAVAALPLDAEICGCNGVSKGDIVAAIEGGATDLGTVRSLTKASSSCGTCTGLVEQVLGVTLGDDFVIPAAASICGCTDLSHEDVRRMIKSRELKSMAAVWQELGWKTSCGCHVCRPALNFYLLADWPLEYRDDPQSRFINERKHANIQKDGTYSVVPRMWGGMTTPDELRAIADAAEKYNVPTVHVTGGQRIDLLGVRGEDLPAIWADLNAAGMVSGHAYAKGLRTVKTCVGKDHCRFGTQDSTGLGIALEKRLWGSWTPHKVKLAVSGCPRNCAEATCKDIGVVCVDSGYQIGVAGAAGMDVKETERLADVATEQEALDLITAFFQLYRENAKYLDRPYKWVAKVGLDWVKDQVFDADTRQGLIERFELSQSIYQKDPWAEEARKSGEKYQPLADFKLEAAE Dinoroseobacter shibae DFL-12 Dino 3608265 Dshi_1669 Nitrate reductase (EC 1.7.99.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.99.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. molybdopterin oxidoreductase (RefSeq) MTDQSVCTTCPYCGVGCGVLASPDGTIAGDLAHPANLGRLCSKGSALGETLDLEGRLLAPQIGNRRAGWDEALDLVANRFRAAAETHGPDSVAFYVSGQLLTEDYYVANKLIKGFIGTANIDTNSRLCMASSVAGHKRAFGTDTVPGQYTDFETAELVVLVGSNLAWCHPVLFQRLQAAKAVRPELKVVVIDPRRTATSQLADLHLGLRPDGDAVLFNLLLTELVRRDLVDRRYVAEAVSGFDAAVAEAERAEAAQTGLDSFELAQFLDLWCRTEKVVTLYSQGVNQSACGTDKVNAILNCHLATGRIGRPGMGPFSMTGQPNAMGGREVGGLANMLTCHLDLENAAHRDAVQQMWSAPTMADKPGLKAVELFDACARGEIKALWIMSTNPVVSLPDADAVAAAIRAVPFTVMTDIMADTDTGRCVDVLLPATGWGEKSGTVTNSERCISRQRRFLPTPGEARADWNILADVGRRMGWPEAFDYRSEAEVFREFARLSTLGHTFGKDFDISGLADLTDAEYDALPPTVWPVPTEGPSGGRFFADGGFYHPDGKAKMLPIAAPASEAPNTARPVRLNTGRVRDQWHTMTRTGKAPRLGAHMAEPYLEIHPGDAAAAGLSDADLAKVSSAHGSAILRVMITDRSQQGSVFVPMHWTDIVSSTGRINAVVAPTTDPVSGQPASKGTAVALEQVAAHWYGFAVSTATMTPTRPYAAIARTRTGTRAEVADFKLPDNWEAEARKILSLPGGSASVIEDSARGTARVAIHEKGTLTGLFFAAATPVALSRSHVVALIGTAADPIQALAGVPAADRPDPGAMVCACFDVGANSLRRAIDGGATTLHALGVCTRAGTNCGSCRPELEAILTAATAMKLAAE Dinoroseobacter shibae DFL-12 Dino 3608604 Dshi_1997 Xylulose kinase (EC 2.7.1.17) Specifically important for utilizing Xylitol. Automated validation from mutant phenotype: the predicted function (XYLULOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. xylulokinase (RefSeq) MYLGLDLGTSGLKAVLIDENQALVAEATAPLEVARPHPGWSEQMPCDWLAATEAAMAALGARADLSGVRAIGLSGQMHGATLLDASHEVLRPCILWNDTRAAAEAAALDADPAFRSVTGNIVFPGFTAPKLAWVRAHEPDVFDRTALVLLPKDYLRLWLTGEAVAEMSDAAGTSWLDTGARDWSAPLLAATGLSRDHMPRLVEGSEVSGTLRDSLADAWGLPRGVPVAGGGGDNAASGIGMGVVRAGDGFVSLGTSGVLFAACDAYAPDPATAVHTFCHALPETWHQMGVILAATDALNWFARTCGTDAATLTGGLGPLQAPGRPVFLPYLGGERTPHNDAAIRGAFARIDHAADRDALARAVLEGVAFAFRDSFDALAATGTRLERLVAVGGGAKSDTWVRMIATLIGLPIDLPQAGDYGGAFGAARLGMMAATGQGAALATRPPIARSLDPVPALADAFGEAHATYRATYTALKGLDR Dinoroseobacter shibae DFL-12 Dino 3608667 Dshi_2060 Aconitate hydratase (EC 4.2.1.3) Specifically important for utilizing Trisodium citrate dihydrate. Automated validation from mutant phenotype: the predicted function (4.2.1.3) was linked to the condition via a SEED subsystem. This annotation was also checked manually. aconitate hydratase 2 (RefSeq) MSLYTAYLEEIAARKEQGLQPKPIDDAALTSEIIAQIKDPAHEHRADSLQFFIYNTLPGTTSAAGAKAQFLKEIILGESVVAEITPDFAFELLSHMRGGPSVEVLLDIALGDDASLAAQAAEVLKTQVFLYEADTDRLKAAHEAGNAVATGILQSYARAEFFTTLPEIEDEIEVVTYIAAEGDISTDLLSPGNQAHSRSDRELHGKCMISEAAQKEIEALKLQHPGKRVMLIAEKGTMGVGSSRMSGVNNVALWTGKQASPYVPFVNIAPVVAGTNGISPIFMTTVGVTGGIGIDLKNWVKKVDGDGNPILNNDGNPILEQKYSVDTGTVLKIDTKARKLMSADGGEELADVSSAFSPQAVEFMKAGGSYAVVFGKKLQTLAAETLGVEPTPVFAPAKEISHEGQGLTAVEKIFNANARGVTPGKVLHAGSDVRVQVNIVGSQDTTGLMTSQELEAMAATVLSPTVDGAYQSGCHTASVWDLKAQANTPRLMAFMHKFGLITARDPKGVYHSMTDVIHKVLNDITVSDWDIIIGGDSHTRMSKGVAFGADSGTVALALATGEATMPIPESVKVTFKGKMADHMDFRDVVHATQAQMLAQHGDNVFQGRVIEVHIGTLLADQAFTFTDWTAEMKAKASICISNDDTLIESLEIAKQRIQVMIDKGMDNDVQMLAGLIAKANARIAEIRSGEKPALKPDDTARYFAEVVVDLDQIVEPMIADPDVHNADVSKRYTHDTIRPISYYGAEKKIDLGFVGSCMVHKGDVKIVAQMLRNLEKANGEVKFKAPLVLAAPTYNIIDELKEEGDWDVLQKYAGFEFDDSAPKEKARTEYENILYLERPGCNLCMGNQEKAAKGDTVLATSTRLFQGRVVADSETKKGESLLGSTPVVVLSAILGRTPTVEEYKTAVEGINLTKFAPPLTPPIDAKSVHF Dinoroseobacter shibae DFL-12 Dino 3609048 Dshi_2437 L-rhamnose isomerase (EC 5.3.1.14) Specifically important for utilizing L-Rhamnose monohydrate. Automated validation from mutant phenotype: the predicted function (5.3.1.14) was linked to the condition via a SEED subsystem. This annotation was also checked manually. L-rhamnose isomerase (RefSeq) MGYENAKAAFAEWGVDTEAALARLKTIPISMHCWQGDDVVGFEQKTGSSGGGIQATGNHPGRARTPDELRADLEFAYAMIPGRHRLNLHAMYLDTEATPDRDEIEIAHFAPWVDWARAQGIGLDFNPTFFAHAKADDNLTLSHPDPGIRDFWIEHGKRSREIAAGMGAALGSACVNNIWVPDGYKDTPVDRMAARARLEASLDAMLAPPQDRARMLDAVESKLFGIGVEACTVGSHEFYMGYAIRKGTLLCLDMGHFHPTENIADKLSAVALSLDEILLHVSRPMRWDSDHVILLDDDILQMAQELVSADLLGRTRIGLDFFDATISRTAAWVIGTRNMQKALLRALLMPLDRLRAAEDALDFTTRLVVTEEVKDLPFGAVWAEFAAREDVPNGQKLIRELDRYQAQVSGRG Dinoroseobacter shibae DFL-12 Dino 3609574 Dshi_2958 Xanthine dehydrogenase (EC 1.17.1.4) Specifically important for utilizing Adenine hydrochloride hydrate. Automated validation from mutant phenotype: the predicted function (1.17.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Xanthine dehydrogenase small subunit (RefSeq) METTFLLNGETVRVADEAPTRTLLDWLRERRGLTGTKEGCNEGDCGACTVIVSDADGPRTLNACILFLPQLQGKAVRTVEGISGPDGSLHPVQAAMVAHHGSQCGFCTPGFIAAMACAHTRGETDHADQLAGNLCRCTGYAPILRAAEAAAEAPVPDWMAEPALPHIQEDTSFTAVREDTSLNAVREDTTAGAEAGVDALWAQPRSSDALAAWYAEHPDATLVAGATDVGLWVTKQLRELAPIAFLNRCDDLKTIETTDTHWRLGAMVTISALLETVRAEHPSFAEMLRRYGSVQVRNAATLGGNIANGSPIGDSPPPLIALGATLHLRKGDSRREMPLEDFFLAYGNQDRAPGEFVEAITIPRGHDGLRVYKLSKRMDQDISAVCGAFNITLAEGRVTGARIAFGGMAGTPHRAKAVETALISAPWSLETVTAAAEWMGDDYAPMSDMRASAAYRLRTAQNMLVRYFHETEGTRTDLREVAS Dinoroseobacter shibae DFL-12 Dino 3609575 Dshi_2959 Xanthine dehydrogenase (EC 1.17.1.4) Specifically important for utilizing Adenine hydrochloride hydrate. Automated validation from mutant phenotype: the predicted function (1.17.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Xanthine dehydrogenase molybdopterin binding subunit (RefSeq) MSVAKPLPHDAAALHVTGAARYVDDIPTPANALHLAFGLSEIAHGEITAIDLSEVRAAPGVVAVLTADDLPHHNDVSPSPLPEPMLATGQVHYVGQPIFLVAAESHLAARKAVRRAKIVYAEKPALLSIDDALAAGAIFEDAPRHYTKGDADAALAAAPKVIEGRIEIGGQEHFYLEGQAALALPQEGGDMVVHSSSQHPTEIQHKVAEALGVPMNAVRVEVRRMGGGFGGKESQGNALACASAVVAALTGRPAKMRYDRDDDMVITGKRHDFRIDYKVGIDEEGRILGLAFEQYCRCGWSLDLSLPVADRAMLHADNAYHLEHVSIRSHRLRTNTQSNTAFRGFGGPQGMVGIERVLDHVAFAVGRDPLEVRRLNYYAEAGGCLPPTPPEDISGPEKAEAPPVQTTPYHMEVEDFILHGLTDRLAETADYGVRRAEIRAWNSESPILKRGIALTPVKFGISFTLTHLNQAGALVHVYTDGSIHMNHGGTEMGQGLFQKVAQVAAARFGVDIGAVKITATDTGKVPNTSATAASSGSDLNGMAVQAACDTIRDRIAAFLAEEHQADPATVRFADGLVHVGGATYGFAEAVQKAYMARISLSATGFYKTPKIVWDRIKGTGRPFFYFAYGAAVTEVVVDTLTGENRILRTDILHDCGASLNPALDIGQIEGGYVQGAGWLTTEELVWDDRGRLRTHAPATYKIPATGDTPPVFNVALWEGENREETVYRSKAVGEPPLMLGISALMALSDAVAACGDGTVYPALDAPATPERLLWAIERVRA Dinoroseobacter shibae DFL-12 Dino 3610039 Dshi_3420 Glycerol kinase (EC 2.7.1.30) Specifically important for utilizing Glycerol. Automated validation from mutant phenotype: the predicted function (GLYCEROL-KIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glycerol kinase (RefSeq) MDRQRGQFLLNLRALKPRPGEGTVRHVLAIDQGTTSSRAIVFDADMNIVSIAQEEFAQHYPDSGWVEHDPEDLWDTVLRTCRNVLERTGLAATDLAGIGITNQRETTVVWDKSTGKPIHNAIVWQDRRTAPFCAELRKAGHDALITAQTGLLADPYFSGTKLKYILDTVEGARDRAKAGELLFGTVDSFLIWRLTNGAAHVTDATNAARTMLYDIHKGAWSAEICTLFDIPLGMLPQVHDCDAEFGTCTPEHLGGAVPILGVAGDQQAATIGQACFEPGMLKSTYGTGCFALLNTGEAPVTSTNRLLTTIAYQLDGKPTYALEGSIFVAGAVVQWLRDGLKLIANASETQPLAEAADPHDPVILVPAFTGLGAPYWNAECRGAVFGLSRGSGPEEFARAALESVGYQTRDLLEAMHKDWSDAREGQPTLRVDGGMTASDWTMQFLADIIDAPVDRPKITETTALGVAWLAGQKAGLYPDRAGFAANWALDQRFEPKMDATTRDTKYAAWKRAVAAVQQA Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_0348 N515DRAFT_0348 Arginase (EC 3.5.3.1) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (ARGINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. arginase MGNQAVSLIGAPTDIGAGHRGASMGPEALRVANLQARLKARGIDVVDRGNLQGPLNPWEPPREGYRHLSAVVDWNRAVYEAIYGELSLGRLPVMLGGDHCLAIGSITAVARHCREHHKKLRVLWLDAHADFNTAQITPSGNIHGMPVACLCGMGPEELTTLGGSKPATAPDVFRQIGIRSVDEGEKRLVREARVSIFDMRQIDESGMKRVMEEALEGVDADTHLHVSFDVDFLDPAIAPGVGTTVRGGPNYREAQLCMEMIADTGRLASLDIVELNPAFDKRNQTAKLAVDLVESLFGKSTLIR Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_1266 N515DRAFT_1266 Alanine dehydrogenase (EC 1.4.1.1) Specifically important for utilizing L-Alanine. Automated validation from mutant phenotype: the predicted function (ALANINE-DEHYDROGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. alanine dehydrogenase MRIGVPKEIKNHEYRVGLVPSSVQELVHHGHEVLIEAGAGLGAGLSDADYVAAGARIVEGPDAIFAQADMIVKVKEPLAVERKKLRKGQILFTYLHLAPDAEQTHDLIASGAVCIAYETVTAANGALPLLTPMSEVAGRLAPQVGAHSLEKAQGGRGVLLGGVPGVPAAEVVILGGGVSGTHAATIAVGMGAKVTVVDRSADALKRLATQFGTSISTVFSTRSAIEELVRRADLLIGTVLVPGAAAPKLVTHDMVRTMKPGSVIVDVAIDQGGCVETSKATTHSDPTYVVDGVVHYCVANMPGAVARTSTFALNSVTLPFTLALANKGWQKALADDAHLRNGLNVIDGKVVCEPVAQAHGLPYVKAETALGM Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_1919 N515DRAFT_1919 Fructokinase (EC 2.7.1.4) Specifically important for utilizing D-Fructose. Automated validation from mutant phenotype: the predicted function (2.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. fructokinase MPRNILCFGEALIDFHAEGRDAQGFPRSFIPFAGGAPANVSVAVARLGGPAAFAGMLGQDMFGDFLLDSLRRAGVDTAGVARTGEANTALAFVALDSHGERSFSFYRPPSADLLFRPEHFRAESFRGAAVFHVCSNSMTEPALAEATREGMRRAHTAGAWVSFDLNLRPALWPNQSASHDELWPALHLADVVKLSAEEFHWLAGDEGEEATLDRLWAGRARLLVVTDGSRTLRWFHPDASGEMPVYAVPTVDSTAAGDAFVGGLLHRLATVEKGADQLDHLVAELPRLHAMLRFAAACGALTVTRLGSFAAMPDEAEVLAFMDSHA Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_2015 N515DRAFT_2015 Branched-chain amino acid aminotransferase (EC 2.6.1.42) Specifically important for utilizing L-Isoleucine. Automated validation from mutant phenotype: the predicted function (BRANCHED-CHAINAMINOTRANSFERILEU-RXN, BRANCHED-CHAINAMINOTRANSFERLEU-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. branched-chain amino acid aminotransferase MAQQYPEWIWQNGQIKPWREATTHVMSHALHYGSSVFEGIRSYATPDGAAIFRLTDHLKRLYQSAKIYDMVLPYSQDQIAAACRDVIKQNGLGAAYLRPVAYRGLGGFGLSAETPIDVAVAAWPMGPYLGPEALESGIDACVSSWQRFAPNTIPAGAKAGGNYLSGQLIAREARRLGFGEGIALANTGLLSEGAGENLFLVFDGVLHTTPASASILTGITRHTLITLAREDGIEVIERDIPREYLYLCDELLMCGTAAEITPIRSVDGKKIGSGKAGRVTRRMQELFFGLFNGKTNDQWGWLEPV Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_2362 N515DRAFT_2362 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. assimilatory nitrite reductase (NAD(P)H) large subunit precursor MTTRLVVIGNGMVGHKLLEELAALGTPGLEITVLCEESRPAYDRVHLSEYFSGRSADELSLVTPGFFDQPGLHLRLATRAARIDRAFKRVTTADGEVIPYDKLVFATGSSPFVPPIPGNDRPGCLTYRTLDDLAALAGWGAQSKRGVVVGGGLLGLECAKAVRDMGLETHVVEFAPRLMAVQVDDGGGRILHRTIEELGLVVHTGKNTQAIVDGSGIDGANARHAMKFADGSTLETDLIVFSAGIRPRDELARQCDLGVGQRGGIMVDNFCRTRDRDVYAIGECAQWGGKVFGLVAPGYDMARVVAKHLHALLTREEARDLPEFAGADMSTKLKLMGVDVASLGDAHGATPGSRSYQFSDERRQVYKRLVVSEDGKRLLGGVLVGDATEYGTLLQMMLNGMDLPEAPESLILPASDGKSRPGLAVDALPAAAQVCSCNNVSKGQLCVAVAEGATSIGALKKATRAGTTCGGCVPLVTQIMKAEMARQGLAVNNHLCEHFAHSRQELYHLVRVERIRRFEDLLARHGQGLGCDICKPVAASILASCWNEFVLQQEHASLQDSNDYFLANIQKDGTYSVVPRMPGGEVTPDGLIAVGRIAKSYGLYTKLTGGQRVDLFGARLEQLPLIWEELIAAGFESGHAYGKSVRTVKSCVGSTWCRYGVQDSVGTAIDLENRYKGLRSPHKLKFAVSGCARECAEAQSKDVGVIATEQGWNLYVCGNGGMKPRHAELLAGDLDTATLIRYIDRFLMFYIRTADRLQRTSVWRDGLEGGMDYLRDVIVHDKLGLADELEAEMALVVDTYECEWKRAVTDPKVRARFRHFVNSEAGDDQVAFVPERGQIRPASAQEKRAFRGIPVVVETE Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_2363 N515DRAFT_2363 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrite reductase (NADH) small subunit MTNETSWISVCAVGDIVPDTGVCALVHGAQVAVFRVGGELYAIDNLDPCSGAAVLSRGLVGNLGERVVVASPIYKQHFDLRTGECVEAPEQAVRTWPVRRQGDHVQVGQADA Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_2364 N515DRAFT_2364 Nitrate reductase (EC 1.7.99.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.99.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. assimilatory nitrate reductase (NADH) alpha subunit apoprotein MSEAVRTTCPYCGVGCGVLASVDADGTTRVAGDPAHASNLGRLCVKGSALGDTVGPEGRLLHPVLRGQDGVAQRATWDEAIQRVADGFSRIVAEHGPDAVAFYVSGQLLTEDYYVVNKLAKGYLGTANIDTNSRLCMSSAVAGHKRAFGEDVVPGCYEDLEQAELVVLVGSNTAWCHPVLFQRVTAAREGRDGPRVVVIDPRFTATCEGADLHLPIRPGTDVRLFNGLLSFLFRHGVIDPDFIDAHTAGFDQALAAAEAESGDPAMVARQCGLQTADVVAFYRLFARHEKVVTLFSQGVNQSTSGTDKVNAIINCHLATARIGRPGMGPFSITGQPNAMGGREVGGLSNMLAAHLELGEPAHRDIVQAFWQSPHIAGTPGLKAVELFDAVGEGRIKALWIMATNPAVSLPDADKVRAALARCELVVCSDIVERTDTNAYAHVLLPALGWGEKDGTVTSSERRISRQRPFLPAPGEARADWRAVCEVAKRMGFERGFEFAHPHEIFVEHAQLTAFRNREPLADGVPAARRQLQLGPLAKLDRRAYDALAPVQWPVTEQGAGTPRLFADGRFSHADGRARFVTTASRAPAHAADREYPLVLNTGRIRDQWHTMTRTARSPRLNNHIGEPFVDMHPHDALRSGVREGSLARVVSRWGSMVARVRHGGGILAGTVFAPIHWSDQFASDARVGGVVNPAVDPVSGEPEFKHTPVRVEPFPVRWYGFALARRPLPASMLSYWTLIRGDRFLRYELAHRERPAEIEAWAKAWLGVTDDQADWLAFEDLDTGVYRAVHLREGRIESCLFLAAQPHLPSRQWLASLFARDRLDEADRLALLSGEAPGGGGDPGPVVCSCFGVGRNTILEVIRRNELDLPAQITAELRAGGNCGSCIPELRRLIAETRAASEA Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_3391 N515DRAFT_3391 Alpha-amylase (EC 3.2.1.1) Specifically important for utilizing a-Cyclodextrin. Automated validation from mutant phenotype: the predicted function (3.2.1.1) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Glycosidase MPPFRALSRLTVAFALALGATVAYAADSTPPVATSTAPKTQGSGVWYEIFVRAWYDTNGDGIGDLNGVTAKLDYLQSLGVSGIWLMPINPSPTYHGYDVTDYEGINPQYGSMADFEKLVSEAHKRGIEVIIDLVINHSSDQHPWFKSALDPHSQYRHWYTWAGKDTDLKAISAVDGPAWHANGKQHYLGDFTGAMPDLNYDEPAVRREMIAIGKFWLSKGADGFRLDAARHIYDDLKSDNGQPAVIRKNAQWWSEFRQGLRQVRPDVYLVGEVSARQPGELAPYLPALGSVFDFPLAEQLIASAKQEQAGKLPALLTESYAAFHAAAGDDYADAPFLSNHDQERVLSQLGGDLHHMRTAAAMLLTLPGRPYIYYGEEIGMLGRKPDENLREPMRWQRTPAAPGDSRWKTYSVKQGGDVSVQAERDQPDSLLNLYRTLIHWRVEVPALRDGALRVIATGKPALVAYERATADSRALVVHNLSGKPGSFKLDGDSAKAFSAIRLHTVPGATLANGQLTLPAYATVVLQ Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS00905 HSERO_RS00905 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) Specifically important for utilizing L-Proline. Automated validation from mutant phenotype: the predicted function (1.2.1.88, 1.5.5.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase MTHVASAAVAAPFGGFQAELLPTPSPLRAAITAAYRRDEREAVQWLLQQVQEEQPWKDATQQLARKLVQQVREKRTRSSGVDALMHEFSLSSEEGVALMCLAEALLRIPDRQTADRLIADKISKGDWRKHLGESPSLFVNAATWGLLITGKLVSTSSESGLTQAITRLIGKGGEPLIRKGVDLAMRMLGNQFVTGQTIEEALDNSRENEKRGYRYSYDMLGEAALTMHDADAYYQSYESAIHAIGRASNGRGIKDGPGISVKLSALHPRYSRAQHARVMSELLPRLKQLLLLAKQYDIGLNIDAEEADRLELSLDMMEVLVADPDLAGFDGLGFVVQGYQKRCPFVIDYLVDLARRNGRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVHTDLSYLTCAQKLLAATDVIYPQFATHNAHTLAAIYHWARQHQIDNYEFQCLHGMGETLYDQVVGPDNLGKACRVYAPVGSHQTLLAYLVRRLLENGANSSFVNQIVDEAVPLDRLVGDPIETVRAQGGLPHPAIAVPHRLYGEERKNSAGIDLSNEDRLQQLGQLFISMADRQWQAAPLLAADTAAQSAQAAQLVRNPADLREVVGQVSEATVADVDTALRAATDYAPQWQSTPATERAAMLERAADLLEEHIAELMALAVREAGKSLPNAIAEVREAVDFLRYYAIASRHDGNVLAWGPVVCISPWNFPLAIFIGEVSAALAAGNVVLAKPAEQTALIAHRAVQLLHEAGIPRAALQLLPGRGETVGAALTSDVRVKGVIFTGSTEVAQLINRTLAQRQHDDGDGSGEHGEVPLIAETGGQNALIVDSSALAEQVVQDVLSSAFDSAGQRCSALRILCLQEDIADRTLAMLKGAMAELRVGRPDRLSIDIGPVIDAEARQNLLDHIERMRASARAVHQLPLGEECQHGTFVAPTVIEIDDLAQLQREVFGPVLHVLRYRRDALPQLIDAINATGYGLTLGVHSRIDETIEFVAQRAHVGNIYVNRNIVGAVVGVQPFGGEGKSGTGPKAGGPLYLKRLQRNAQLHEELTRAQPADVPNALLDSLLDWARTHGHERLAANGQRYHRDSLLQRSLVLPGPTGERNTLGFAPRGLVLCAAGSVGTLLNQLAAAFATGNTALVDERSAAILPSGLPAPVRAAIRRASQLDAEPLQAALVDSHQAAHWRARLAAREGALVPLILCGEDTTIPLWRLLAERALCINTTAAGGNASLMTISV Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS03650 HSERO_RS03650 Mannose isomerase (EC 5.3.1.7) Specifically important for utilizing D-Mannose. Automated validation from mutant phenotype: the predicted function (5.3.1.7) was linked to the condition via a SEED subsystem. This annotation was also checked manually. N-acyl-D-glucosamine 2-epimerase MPQPDFESRRFLHAHVADTLAFYDRHAIDPLGGFFHYLKDNGRVYNAGHRHLVSATRLVFTQTMAYTHSGHTRYLRQARRAWDELARFRHASGPLQGLYAWTLQDERIEDATVMAYGQAFVLLACAHAHRIGLCGEDAVADAFERMETAFFEPAHQAYADEITPAGELIGYRGQNANMHMCEACLSAYEVTGQRRYLERALALIERFVFDLAQHTQGLVWEHYHQDWTPDLDYNKGKRSNIFKPWGFQTGHQTEWAKLLLIAHGHAPNAAFLPRAIELHQAAWTYGWDSIHGGLIYGFGLEREPYDRDKYFWVQAESFASAWRLWRATGEPAFRDQYRMLWAWSWQHMVDHEHGAWFRILAADGSKLEDTKSPAGKVDYHTMGACWDVLAVGGLGV Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS05205 HSERO_RS05205 L-arabonate dehydratase (EC 4.2.1.25) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (L-ARABINONATE-DEHYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. dihydroxy-acid dehydratase MSSDKKDKSRTLRSAGWFGTADKNGFMYRSWMKNQGIPDHEFQGKPVIGICNTWSELTPCNAHFRKIAEHVRRGIIEAGGFPVEFPVFSNGESNLRPTAMLTRNLASMDVEESIRGNPIDAVVLLTGCDKTTPALLMGAASCDVPAIVVTGGPMLNGKHQGRDIGSGTVVWQLSEQVKAGEITIHDFMAAEAGMSRSAGTCNTMGTASTMACMAESLGVSLPHNAAIPAVDARRYVLAHLSGMRIVDMVWEGLTLSKILTRKAFENAIRTNAAIGGSTNAVIHLKAIAGRIGVDLELEDWTRIGRGTPTIVDLQPSGRYLMEEFYYAGGLPAVLRRLGEADLLPHKDALTVNGQTMWDNVKDAPIYNDEVVRPLAKPLIEDGGICILRGNLAPRGAVLKPSAATPELMKHRGRAVVFEDFNHYKERINDPDLDVDASCVLVMKNVGPKGYPGMAEVGNMGLPPKVLATGVKDMVRISDARMSGTAYGTVILHVAPEAAAGGPLGIVQDGDFIELDAYAGKLQLDISEEEMKRRLEARAKVLAERKPEMVGGYQSLYVDRVLQADEGCDFDFLVGCRGAAVPKHSH Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS06870 HSERO_RS06870 L-2-keto-3-deoxyarabonate dehydratase (EC 4.2.1.43) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (4.2.1.43-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. cytochrome C biogenesis protein CcdA MSTPLYRGVFPVAPTIFDANGKLDLEGQKRAIDFMIDAGSNGLCILANFSEQFVLSDEERVQVQNTVLEHVAGRVPVIVTTTHYGSQICAERSRAAQDAGAAMVMVMPPYHGATFRVPEKQIYEFYKHVSDAIDIPIMIQDAPVAGTPLSAPFLARMAKEIEQVSYFKIETAGAASKLRDLIELGGDAVVGPWDGEEAITLIPDLDAGATGAMTGGGYPDGIRKIVDAYFAGDIEKAAELYMQWLPLINYENRQCGLSACKALMLEGGVIKSDMLRHPQPPLHPKVREGLLRVARRLDPLVLSWGR Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS11500 HSERO_RS11500 Ribokinase (EC 2.7.1.15) Specifically important for utilizing D-Ribose. Automated validation from mutant phenotype: the predicted function (RIBOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. ribokinase MIVIIGSVNMDLVLRVPRMPLPGETLAGDRFMTIPGGKGANQAVACARLAAPGTRVAMVACVGDDAFGGQMRQSITACGIDDRYIDEVAGEATGIASIMVDANAQNSIVIAAGANGRLDVERIERARALIEQASIVLLQLEVPMATVIHSIELAHALGKTVVLNPAPAQALPRALLQKIDYLILNEIEAAMLAEEQSEDIPMLARKLHDLGARNVVVTLGEKGVYGSFADGQQRHLPARKVQAVDTTAAGDTFIGGFIGAIAQGRDQFEAIAYAQAAAALSVTRVGAQTSIPTRDEVVL Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS12095 HSERO_RS12095 Myo-inositol 2-dehydrogenase (EC 1.1.1.18) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (MYO-INOSITOL-2-DEHYDROGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. myo-inositol 2-dehydrogenase MIDVAIFGAGRIGKIHAANIAAQAGVRLKYVCDVHAESAAELAQRHGAQVGRVEQVLDDSSVAAVVIASSTDTHADLILRAAAAGKAIFCEKPVDLDLQRAQACAEAVRAAGVTCMIGFQRRFDPTFESLSRRLEAGEIGDPEMLLVTSRDPGAPPLSYIASSGGIFKDMLIHDFDIFRWILADEAVSVFATGSCLTDPAIATAGDVDSTAVTLTTRSGRLCQINTSRRAAYGYDQRFEVLGSKGMLQAGNHRPTEVVAATASQVGSDLPEHFFLERYRAAYAREMAHFFQAMQSGAPVRTSIEDGVKALQLAEAAATSWRERRIVSLSA Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS12135 HSERO_RS12135 Myo-inosose-2 dehydratase (EC 4.2.1.44) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (MYO-INOSOSE-2-DEHYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. xylose isomerase VATPFNVKIGINPISWMNDDLPSLGGETPLEQALSEGAEIGYRGFELGNKFPRQPEALRAVLGKYQLECVSGWYSGQLATRSVEEEIVAVEAHLNLLAANGAQVMVYGEVADSIQGAPTPLYQRPRFGSEAAWQGYAQRLDQFARHLLQRGVRLAYHHHMGAYVETPEDLDKLMALTGEEVGLLFDSGHIAFAGGDPLAVLQRHLDRVCHVHCKDVRPAVVKLARNRDWSFLQAVINGAFTVPGDGAIDFAPLLQLLYRRGYSGWLVVEAEQDPAVAPSYRYAQMGYRHLSTLVAAIENGSLQEAA Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS15785 HSERO_RS15785 5-dehydro-4-deoxyglucarate dehydratase (EC 4.2.1.41) Specifically important for utilizing D-Galacturonic Acid monohydrate. Automated validation from mutant phenotype: the predicted function (4.2.1.41) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 5-dehydro-4-deoxyglucarate dehydratase MSQYTPQDLKQILSSGLLSFPLTDFDEQGDFRPKTYIERLEWLAPYGASALFAAGGTGEFFSLVPGEYSDIIRTAVDTCRGKVPIIAGAGGSTRAAIAYAQEAERLGAHGILLMPHYLTEASQDGIAAHVEAVCKSVKFGVIIYNRAVCKLNADTLQKLADRCPNLIGFKDGIGEIEPMVHIRRKLGDRFTYLGGLPTAEVYAAAYKALGVPVYSSAVFNFIPKTAVEFYQAIAKEDHDTVGKLIDEFFLPYLAIRNRKAGYAVSIVKAGARIAGHDAGPVRTPLTDCTPEEHEELAALMNKLGPQ Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS15800 HSERO_RS15800 Galactarate dehydratase (EC 4.2.1.42) Specifically important for utilizing D-Galacturonic Acid monohydrate. Automated validation from mutant phenotype: the predicted function (4.2.1.42) was linked to the condition via a SEED subsystem. This annotation was also checked manually. D-galactarate dehydratase MSTDTSASQASAPRYIMMNDTDNVAIVVNDGGLPAGTVFPDGLTLVDRVPQGHKIALRDLKQGEAIVRYDVAIGYAVRDIPKGGWIEESLVQMPPARELDNLPIATKKPAPQPPLEGYTFEGYRNADGSVGTRNLLAITTTVQCVAGVVEHAVKRIRAELLPKYPNVEDVVALEHTYGCGVAIDAPNAGIPIRTLRNISLNPNFGGQAMVVSLGCEKLQPNRLLPENMIPIHKQGEPYVVCLQDAEHVGFNSMIDSIMNMAEARLTELNKRRRETCPASDLVVGVQCGGSDAFSGVTANPAVGFATDLLVRAGASVMFSEVTEVRDGIDQLTSRAVNEEVAQAMIREMDWYDNYLKQGGVDRSANTTPGNKKGGLANIVEKAMGSIVKSGSSPISGVLSPGDKLQQKGLIYAATPASDFICGTLQLAAGMNLHIFTTGRGTPYGLAAVPVIKVATRNDLARRWHDLMDVNAGRIASGEASIEDVGWELFQLMLDVASGKKRTWAEQWKLHNALTLFNPAPVT Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS22200 HSERO_RS22200 Rhamnulokinase (EC 2.7.1.5) Specifically important for utilizing L-Rhamnose monohydrate. Automated validation from mutant phenotype: the predicted function (2.7.1.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. L-fuculose kinase IAVFDIGKTNIKLTLVDEHGQELAVRRRPNQPRQDGPYPHHDVAAIEAWLLENLAALARQWRIRAIVPVTHGATAALVDEAGLVLPVADYEHDFALPPAHRPYESLRPPFAQSASPLLGMGLNLGRQLYWQSQRYPDAFARARYLLMYPQYWSWRLSGVAAGELSSLGCHTDLWQPGQQCYSSLLAQCNWTPLMPPLRAAWERLGPLRPELAQRTGLPADCAVLCGVHDSNASLLRYLRGTGGGPRIVLSSGTWLIAAALDGCVSGLREEADMLANVNVLGAPVACMRFMGGREFAQIAGDDLPCSAEQLQALIDAQVFALPCFSECGGPFAGRRGSIVGQAPQQPGSRYALATLYCALMTAYCLDALDAPGEIVVEGSFTANPHFAALLAALVSRTVYRSSDASGTTLGGWLLDRWERAPETATLPALLPAEPLALRGLAAYREDWLRKLGELERVAA Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS22240 HSERO_RS22240 L-rhamnose isomerase (EC 5.3.1.14) Specifically important for utilizing L-Rhamnose monohydrate. Automated validation from mutant phenotype: the predicted function (5.3.1.14) was linked to the condition via a SEED subsystem. This annotation was also checked manually. sugar isomerase MSYRIDPQFIAEQNARAHQQLQSDYEALAGVLSRRGCDIEALTGQAQAFAVALPSWGVGTGGTRFARFPGQGEPRNVFDKIDDCGTIHQLTRVTPGVSLHFPWDRTTDARALREAATQHGLHFDAVNSNTFQDAAGQAHSYKFGSLTALDPEVRAQAVAHNIDCIELGHALGSKGLTVWIGDGANFPGQSNLRGALERYLESMRAIYAALPADWLVYIEHKLFEPAFYATTIADWGTSFACATELGPKAKCLVDLGHHAPNTNIEMIVARLAQFGKLGGFHFNDSKYGDDDLDSGSINPFQLFLVFNELRDAAQRDGQAFRPAYMLDQSHNVTDPIESLMTSAVEVQRAYLQAALVDTQALSHHQKNNDALMAAQTLKQAFRTDVSAILAMARYRSGGAIDPVALYRASAYRDHKREERPVVAGRSSSGIV Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1166 Ga0059261_1166 Beta-glucosidase (EC 3.2.1.21) Specifically important for utilizing D-Cellobiose. Automated validation from mutant phenotype: the predicted function (3.2.1.21) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Beta-glucosidase-related glycosidases MVPTGKPKLMFRLLSSAMLASLPVVMAATASARDDAAQAHPAMWPERRPTVPLDPAVELRVADLLAKMSLEQKVGQIIQADIASVTPADVHRYHLGSVLNGGNSDPGGRYNAPPRDWLAAADAFYAASMQPNGALPRIPVIWGSDAVHGHNNVVGATLFPHNIGLGAARNPDLIRRIGEATAIEMRVTGLDWTFAPTLAVVRDDRWGRTYEGFGETPEIATAYAAPLIEGLQGKIGDKDWLRGPHIIATAKHFLGDGGTRNGKDQGDTEIGEAGLRDLFSPPYLPALDAGVQSVMVSFSGWNGAKMHGNKSLLTGVVKQRWNFDGFLVGDWNGHGQVAGCTATNCPQSAIAGLDMYMAPDSWKALYEATLGQARDGTLPIDRLDDAVRRILRVKIRAGLFEAGKPSSRPYAGRYELLGSAEHRALAREAVRQSLVLLKNANGLLPLKPGGRILVAGDGADNLTKQTGGWTLSWQGTGTQRSDFPNAQSIWEGIEATVKAAGGTATLSVEGGYSAKPDAAIVVFGEEPYAEFQGDRPDVGYDDAKTLALLRTLKTAGVPTVAVFLSGRAMWVNPFLNASDAFVAAWLPGSEGGGVADVLFGKSDFSGKLGYSWPRSSDQTTVNIGDSNYDPLFPYGFGLKVADRGDLAALPETRATAAAAETGILFTAGKPGGGRRLLLGRPGELAANPGPELIDARPADRSAQEDSLRIRWTGAGQAVAAIVQDVPVDLSRQANGDLALELELKVNAAPSAEVSLLMRCGTDCAGGFPVRGILGEAAKTGKWTRVAVPLRCFEKAGVDMTRVETPLSIATAGSLDLTLSSARITSPSGPQLACK Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1644 Ga0059261_1644 Glucosamine-6-phosphate deaminase [isomerizing], alternative (EC 3.5.99.6) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (GLUCOSAMINE-6-P-DEAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Predicted phosphosugar isomerases MVPNAAGASLGTLMEREAAEAGAAVSRMLAANRDAIERVAARLRASPPAVVVTCARGSSDHAATYAKYLIETLTGVPTASAALSVASLYDAPVAPGNGLCLAISQSGKSPDLLATVEHQRKAGAFVVAMVNAEDSPLAALADIVIPLKAGPERSVAATKSYICSLAAIAALVAAWAQDEALETAVADLPAQLERAFALDWSAAVTALTGASGLFVLGRGYGYGIAQEAALKFKETCALHAESFSAAEVRHGPMAIVGEAFHVLAFASSDRAGESVRETVAEFRSRGAEVLLADPAARQAGLPAIAAHPAIEPILIVQSFYKMANALALARGCDPDSPPHLNKVTETL Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1645 Ga0059261_1645 N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (NAG6PDEACET-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-acetylglucosamine-6-phosphate deacetylase MRIRLENGRIVTPQGVLDGTDVTVADGTIIALTPASGSGVERKIDLGGGWLLPGFIDTQVNGGGGVLFNDQADVDAIAAIGAAHARFGTTAFLPTLISDTPDQIAAALDAVDAAIEQGVPGVVGIHVEGPFINEVKRGIHEARRIRRLDADTLALFTAPRRGRVMLTLAPELCDTDDVRTLVKHGVIVSAGHTNATYDEMMAAIGAGLTGFTHLFNAMSPLHHRNPGAVGAAFDSESWCGMIVDDAHLHPAVVRLAVRAKGIERLMLVTDAMPSVGTGDTEFMLQGKRIMVRNGVCLFEDGTLAGTHLDMASALRNTVEVTGLSVPDVAVMASTTPAHFLSLDRYGALAPGKRADWVWLDKDLQPRGTWIGGEPVADAEEFARAAQ Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_3899 Ga0059261_3899 Alanine dehydrogenase (EC 1.4.1.1) Specifically important for utilizing L-Alanine. Automated validation from mutant phenotype: the predicted function (ALANINE-DEHYDROGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. alanine dehydrogenase MRVGVPKEIKNHEYRVGLTPPLVAELTASGHDVIVETKAGSGIDFEDSDYVAAGARIVATAAEVFAQADMIVKVKEPQPQEVAMLEPRHTLFTYLHLAPDPEQAAGLIKSGATCIAYETVTANDRSLPLLKPMSEVAGRMSVQVGAHYLEKEQGGRGVLLGGVPGVAPAKVAILGGGVSGINAAQMATGLRADVTIYDINNSRLAELDMHFGSQIKTAYASKAAIAAAVANAHLVIGAVLVPGAAAPKLVTRDMLKTMKRGSVLVDIAIDQGGCFETSHATTHEDPVYEIDGVIHYCVANMPGAVARTSTFALNNATLPFVMKLANLGAEKAMAADPHLAAGLNVYKGAITHEAVAEALDLQFTAWKP Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_3961 Ga0059261_3961 Urocanate hydratase (EC 4.2.1.49) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (UROCANATE-HYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. urocanate hydratase (EC 4.2.1.49) MTSAMTNRTDNSRHIKAPTGTELSAKSWLTEAPLRMLMNNLDADVAEAPESLVVYGGIGRAARDWQSYDRIVDALRALDADQTLLVQSGKPVGVFRTHADAPRVLIANSNLVPHWATWEHFNELDRKGLAMYGQMTAGSWIYIGTQGIVQGTYETFVEAGRQHYGGDLSGKWVLTAGLGGMGGAQPLAATMAGASCLAVECQPSRIEMRLKTRYLDRAANSIDEALEIIRTSDKPVSVGLLGNAAEVLPELVRRGIRPDIVTDQTSAHDPVNGYLPAGWTLDEWFTKRETAPHEVEKAARASMATHVRAMLDFHEMGIPTLDYGNNIRQVAKDEGVENAFAFPGFVPAYIRPLFCRGIGPFRWAALSGNPEDIWKTDRKVKELLPGNHHLHNWLDMAKERIAFQGLPARICWVGLGDRHRLALAFNEMVASGELEAPIVIGRDHLDSGSVASPNRETEAMMDGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGYSQHSGMVIVADGTPEAAKRLERVLWNDPATGVMRHADAGYEIAKNCATEMGLDLPGIL Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_3962 Ga0059261_3962 N-formylglutamate deformylase (EC 3.5.1.68) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (3.5.1.68) was linked to the condition via a SEED subsystem. This annotation was also checked manually. N-formylglutamate amidohydrolase MIHVEQGSAPLIVSVPHAGTVIPADIQGLVSPELARYDADLYVDHLYAFARGLDATIVRTTVSRTVIDVNRDPSGQTLYPGQFTTGLCPIQTFDGTPLYEPGALPDAHEIERRRAEWFDPYHTALAIQIERLRAIHPAIVVYDAHSIRSVVPKLFDGELPNFNIGTNDGTSCAPALTQAVEAICDASPYSRVTNGRFKGGWITRHYARPAGGVHSIQMELAMRTYLVETPAHWPPPWHEETAQACQSVLRPILSAAIDFAKAPK Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_3963 Ga0059261_3963 Histidine ammonia-lyase (EC 4.3.1.3) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (HISTIDINE-AMMONIA-LYASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. histidine ammonia-lyase (EC 4.3.1.3) MITPGYTPLSTWNAIYRGEAAPLDPSCRDKIQASADAVEAILARHEPVYGINTGFGKLASVRIGDEDLETLQRNIVLSHAAGVGAPMPAPVVRLMIALKLASLAQGHSGVRPATIAMLQDMLDRGITPIIPSQGSVGASGDLAPLAHLAAAMIGTGEVLVDGVVRPARDVLAPLTLGPKEGLALLNGTQFSTAYALAALFETERLFRAALVTGALSTEAAKGSDTPFDPRIHQVRGHRGQIEVADALAGLMSGSAIRASHREGDERVQDPYCLRCQPQVMGACLDLIRQAAATLAIEANGVTDNPLIFPDTGEALSGGNFHAEPVAFAADMLAMALCEIGSLSERRIAMLVDPALSGLPAFLTPRPGLNSGFMIPQVTAAALVSENKQRAHPASVDSIPTSANQEDHVSMAGHGARRLMEMAANLANVLGIEYLAAAQGCDFHAPLTSSEPLEAARSLLRNQVPHLEDDRHFAPDMAAATALVAGGMLGPYLPGIER Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_3964 Ga0059261_3964 Imidazolonepropionase (EC 3.5.2.7) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (IMIDAZOLONEPROPIONASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. imidazolonepropionase (EC 3.5.2.7) MAIPADTLWRNARLATMTGDGLGIVEQGAIAATGGTISYIGPDSDAPDAAEIVDCQGRWITPGLVDCHTHLVHAGNRAREFEARLEGATYEEIARAGGGILSTVTATRAASEDELIASALPRLDQLIAEGVTTVEIKSGYGLTLDDELKMLRAARSLGEARNVHIRTTLLAAHAVPPEYKGDADGYVDLVCETIIPAAIGHADAVDAFCEGIGFSPEQTDRVLAAAVAHGLPVKLHAEQLSNLHGAALAAHHNALSADHLEHLDEAGIAAMAASGTVATLLPGAFYFTREEHRPPIAALRAAGVPIALATDCNPGTSPMASILLAANMGATFFRLTVTECLRGITVNGARALGLRTGTLEPGGPADLAIWNVTDLAELVYRIGANPLHSRIYAGT Klebsiella michiganensis M5al Koxy BWI76_RS00270 BWI76_RS00270 D-ribose pyranase (EC 5.4.99.62) Specifically important for utilizing D-Ribose. Automated validation from mutant phenotype: the predicted function (RXN0-5304) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. D-ribose pyranase MKKGTVLNADISSVISRLGHTDTLVVCDAGLPVPRSSTRIDMALTHGVPSFMQVLEVVTSEMQVEVAILAEEIKTLNPQLHATLLNHLEQLQQHQGNTIEIRYTSHEQFKKETADSQAVIRSGECSPYANVILCAGVTF Klebsiella michiganensis M5al Koxy BWI76_RS00290 BWI76_RS00290 Ribokinase (EC 2.7.1.15) Specifically important for utilizing D-Ribose. Automated validation from mutant phenotype: the predicted function (RIBOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. ribokinase MKTAGKLVVLGSINADHILNLDAFPTPGETVTGHHYQVAFGGKGANQAVAAGRSGANISFIACTGDDDIGERVRRQLESDNIDVAPVRAVAGESTGVALIFVNAEGENTIGIHAGANAALCVAQVDAEKERIASAQALLMQLESPLESVLAAAKIAHQNQTSVILNPAPARELPDELLTLVDIITPNETEAEKLTGVRVENDEDAAKAAKVLHDKGIGTVIITLGSRGVWASSEGNGRRVPGFKVQAVDTIAAGDTFNGALVTALLEGRELAEAIRFAHAAAAIAVTRKGAQPSVPWRKEIDEFLRQQG Klebsiella michiganensis M5al Koxy BWI76_RS00670 BWI76_RS00670 Rhamnulose-1-phosphate aldolase (EC 4.1.2.19) Specifically important for utilizing L-Rhamnose monohydrate. Automated validation from mutant phenotype: the predicted function (4.1.2.19) was linked to the condition via a SEED subsystem. This annotation was also checked manually. rhamnulose-1-phosphate aldolase MQTIIDAWFVQGMIKATSDAWLKGWDERNGGNLTLRLDEADIEPYAADFHAKPRYIALSQPMPTLANQPFIVTGSGKFFRNVQLDPAANLGVVKVDSDGAGYHILWGLTNDAVPTSELPAHFLSHSERIKLTNGKDRVIMHCHATNLIALTYVLENSSDLFTRKLWEGSTECLVVFPDGVGILPWMVPGTDEIGQATAEAMQKHSLVLWPFHGVFGSGPNLDETFGLIDTAEKSAEVLVKVYSMGGMKQTITREELIALGKRFNVHPLQSALDLYQ Klebsiella michiganensis M5al Koxy BWI76_RS00675 BWI76_RS00675 L-rhamnose isomerase (EC 5.3.1.14) Specifically important for utilizing L-Rhamnose monohydrate. Automated validation from mutant phenotype: the predicted function (5.3.1.14) was linked to the condition via a SEED subsystem. This annotation was also checked manually. L-rhamnose isomerase MTTQLEQAWEIAKQRYASVGVDVEEALRQLDRLPVSMHCWQGDDVVGFENPEGSLTGGIQATGNYPGKARNASELRADLEQAMSLIPGPKRLNLHALYLESDTPVSRNEIKPEHFKNWVEWAKTNKLGLDFNPSCFSHPLSADGFTLSHANDEIRQFWIDHCKASRRISAYFGEQLGTPSVMNIWIPDGMKDITVDRFAPRQRLLNALDEVISEKLDPAHHIDAVESKLFGIGAESYTVGSNEFYMGYATSRQTALCLDAGHFHPTEVISDKISAAMLYIPRLLLHVSRPVRWDSDHVVLLDDETQAIASEIIRHDLFDRVHIGLDFFDASINRIAAWVIGTRNMKKALLRALLEPTAQLRQLEVDGDYTARLALLEEQKCLPWHAIWEMYCQRHDTPAGSQWLDNVRAYENAVLSQRG Klebsiella michiganensis M5al Koxy BWI76_RS00680 BWI76_RS00680 Rhamnulokinase (EC 2.7.1.5) Specifically important for utilizing L-Rhamnose monohydrate. Automated validation from mutant phenotype: the predicted function (2.7.1.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. rhamnulokinase MSLRHCVAVDLGASSGRVMLASYQPGQQTLALREIHRFTNSLQKVDGFDCWDLDSLEGEIRRGLEKVCEQGILIDSIGIDTWGVDYVLLDKRGQRVGLPVSYRDSRTQGLMRHAEAQLGRAEIYRRSGIQFLPFNTLYQLRALVEQQPELVSQAAHALLIPDYFSFRLTGNMNWEYTNATTTQLVNINSDSWDEDLLNWSGAPREWFGTPTHPGNVIGHWICPQGNHIPVVAVASHDTASAVIASPLASKNAAYLSSGTWSLMGFESKIPCTSDAALRANITNEGGAEGRYRVLKNIMGLWLLQRVLREQNVSDLPALIARTAALPACRFVIDCNDDRFINPDDMSAEIQAACRESGQPVPDTDAELARCIFDSLALLYTRVLNELAALRGQPFSQLHIVGGGCQNELLNQLCADACGITVVAGPVEASTLGNIGIQLMTLDELNNVDEFRQVVRQNYALTTFTPNPENEIARFVAQFQPQQNKELCA Klebsiella michiganensis M5al Koxy BWI76_RS01295 BWI76_RS01295 Uridine phosphorylase (EC 2.4.2.3) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (URPHOS-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. uridine phosphorylase MSKSDVFHLGLTKNDLQGATLAIVPGDPERVEKIAALMDKPVKLASHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPMEFPAVADFECTTALVEAAKSIGATTHIGVTASSDTFYPGQERYDTFSGRVVSRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIVVEAARRLL Klebsiella michiganensis M5al Koxy BWI76_RS01665 BWI76_RS01665 Isocitrate lyase (EC 4.1.3.1) Specifically important for utilizing Potassium acetate. Automated validation from mutant phenotype: the predicted function (4.1.3.1) was linked to the condition via a SEED subsystem. This annotation was also checked manually. isocitrate lyase MKTRTQQIEELNKEWTKPRWEGITRPYSAEDVVKLRGSVNPECTLAQLGAAKMWRLLHGEAKKGYINSLGALTGGQALQQAKAGIEAIYLSGWQVAADANLASSMYPDQSLYPANSVPAVVDRINNTFRRADQIQWSAGIELNDPRYTDYFLPIVADAEAGFGGVLNAFELMKSMIEAGAAAVHFEDQLASVKKCGHMGGKVLVPTQEAIQKLVAARLAADVMGVPTLVIARTDADAADLITSDCDPYDRQFITGDRTSEGFFRTHAGIEQAISRGLAYAPYADLVWCETSTPDLELAKRFADAIHAKYPGKLLAYNCSPSFNWQKKLDDKTIASFQQQLADMGYKYQFITLAGIHSMWFNMFDLAHAYAQGEGMKHYVEKVQQPEFAAAKDGYTFVSHQQEVGTGYFDKVTTIIQGGTSSVTALTGSTEESQF Klebsiella michiganensis M5al Koxy BWI76_RS01720 BWI76_RS01720 L-sorbose 1-phosphate reductase (EC 1.1.1.-) Specifically important for utilizing L-Sorbose. Automated validation from mutant phenotype: the predicted function (R262-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-sorbose 1-phosphate reductase MQTTALRLYGKRDLRLETFELPAMQDDEILARVVTDSLCLSSWKEANQGEDHKKVPDDVATNPIIIGHEFCGEIIAVGKKWQHKFRAGQRYVIQANLQLPDRPDCPGYSFPWIGGEATHVVIPNEVMEQDCLLSWEGDTWFEGSLVEPLSCVIGAFNANYHLQEGSYNHVMGIRPQGRTLILGGTGPMGLLAIDYALHGPINPALLVVTDTNKPKLSYARQHYPSEPQTLIHYLDGRDASRETLMALSGGHGFDDIFVFVPNEQLITLASSLLAADGCLNFFAGPQDKQFSAPINFYDVHYAFTHYVGTSGGNTDDMRAAVALMQAKKVQAAKVVTHILGLNAAGETTLDLPAVGGGKKLVYTGKNIPLTPLGEIRDPQLAAIMERHHGIWSKEAEEYLLAHAEDIAHD Klebsiella michiganensis M5al Koxy BWI76_RS01745 BWI76_RS01745 Sorbitol-6-phosphate 2-dehydrogenase (EC 1.1.1.140) Specifically important for utilizing L-Sorbose. Automated validation from mutant phenotype: the predicted function (1.1.1.140) was linked to the condition via a SEED subsystem. This annotation was also checked manually. sorbitol-6-phosphate 2-dehydrogenase MNTWLNLKEKIITVTGGASGIGLAIVDELLAQGANVQMIDIHGGDKHQSSGNYNFWPTDISSASEVHKTVDHIIQRFGRIDGLVNNAGVNFPRLLVDEKAPSGRYELNEAAFEKMVNINQKGVFLMSQAVARQMVKQRSGVIVNVSSESGLEGSEGQSCYAATKAALNSFTRSWSKELGKHGIRVVGVAPGILEKTGLRTPEYEEALAWTRNITVEQLREGYSKNSIPLGRSGRLTEVADFVCYLLSERASYMTGVTTNIAGGKTRG Klebsiella michiganensis M5al Koxy BWI76_RS03070 BWI76_RS03070 Methylmalonate-semialdehyde dehydrogenase [inositol] (EC 1.2.1.27) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (RXN-2902) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. methylmalonate-semialdehyde dehydrogenase (CoA acylating) MTITGNFIGGKTVTSGSNKTMPVFDPATGKVVREVTLSTAQEVSDAIQVARDAFESWSRTTPLRRARVMFNFKMLLEQHAEELAGIIVSEHGKVFSDAMGELTRGMEVVEFACGIPHLIKGEFSSDVGTGVDSYSLMQPLGVVAGITPFNFPAMVPMWMFPLALACGNSFVLKPPALAPTAAVRLAELLKEAGLPDGVFNVVHCSNEDAEQLYRDPRIAAVSFVGSSGVAEHIYKTASAYGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVAVGDETADKLIARLKPLVESLKVGPGCMRGKEENEMGPVVSDTHQKKVLGYIDKGVSEGATLVVDGRKPQVPGFEEGYYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVADYHSALELVNSHEFGNGSAVFTSNGHTAREFVHDVQAGMVGVNVPVPVPMAFHSFGGWKRSVFGALNVHGPDGVRFYTRMKTATVRWPQGQQTVSEFSMPTLG Klebsiella michiganensis M5al Koxy BWI76_RS03095 BWI76_RS03095 Inositol 2-dehydrogenase (EC 1.1.1.18) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (1.1.1.18) was linked to the condition via a SEED subsystem. This annotation was also checked manually. NADH-dependent dehydrogenase MSLKLGVIGAGAIGKEHIRRCTQVLQGATVVAVSDINEENARAAVALPGVHAEVYADGHDVIKASDVDAILVTSWDPTHEEYTLAAIAAGKPVFCEKPLAMSAEGCRRIVDAEMKAGRRLVQVGFMRPYDEGYLALKKVIDDGDIGAPLMLRCAHRNQSVGENYTTDMAITNTLIHELDVLRWLLNDDYRSVQVRFPRSTSHTHARLKDPQIVSFETKKGTLIDVEVFVNCQYGYDIQCEVVGETGIARLPEPSAVQMRKAANLSTAILTDWKDRFIKAYDVELQAFINDVQAGQLHGPSAWDGYAASVAADACIKAQGTSDPVEVTLPECPAFYKR Klebsiella michiganensis M5al Koxy BWI76_RS03235 BWI76_RS03235 Neopullulanase (EC 3.2.1.135) Specifically important for utilizing a-Cyclodextrin. Automated validation from mutant phenotype: the predicted function (3.2.1.135) was linked to the condition via a SEED subsystem. This annotation was also checked manually. alpha-glycosidase MITISSLSHSAKSADSYAYNKETLHIRFRTVKGEVAKVSLWIGDPYQWEEGGLDGGNLGGSDAHGWSGGNEVHMEKEGQSESYDHWFAAFTPCKRRSRYGFILYGNNGEKLLFGERRCVDISKPPVAETELSNLSNFFCFPYINPGDVLSTPEWVKKTIWYQIFPERFCNGDPSISPENVQPWGTPPDSKNFMGGDLQGIINKLDYLQDLGVNGLYLCPIFTANASHKYDTVDYFNVDPHFGGNDRFKELVQKAHQRGMKVMLDAVFNHIGNQSPLWLDVVKNGDKSPYADWFWIKKFPVYPSGDKNEWDFRNFNYETFGNVIEMPKLNTENPACRDYLLQVARYWIEEFDIDGWRLDVANEVDHEFWRAFRRTVKSIKPDCYILGEIWHEGMPWLRGDQFDSLMNYPLMQATTDYFALQAYDKKTFIDIVTHAYLCYPRNVNEVMFNLLESHDTSRLLSLCGNDKRKARLAYLFMFSQVGSPCIYYGSEVGMNGSRAMGSEDNRKCMIWDEQKQDLEFKSFIKDLILWRKKHSEWNDPKIHWNNVDHPAVVAFSRGEVHFLLNNSDESLAINYQGRTLSLTPFGFYIIGLDHKDIIS Klebsiella michiganensis M5al Koxy BWI76_RS03535 BWI76_RS03535 Tryptophanase (EC 4.1.99.1) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (4.1.99.1) was linked to the condition via a SEED subsystem. This annotation was also checked manually. tryptophanase MKRIPEPFRIKMVENIRMTTFDDRVKALEEAGYNPFLLNSQDVYIDLLTDSGTGAMSDHQWAGLMMGDEAYAGSRNYQHLCEKVKEIIGYPYTIPTHQGRGAEQILFPSLIARRKSAHPVFISNFHFDTTAAHVELNGAKAINVVTPKAFDTTSWYDWKGNFDIVLLKATIAEHGAENVAAIITTVTCNSSGGQPVSLANMREVYQIARQNNIPVVIDSARFCENAWFIKQREEGYADKSVKEIILEMYQYGDMLTMSAKKDPMVNIGGLCCFRDDEDLFNEVRIRCVPMEGFVTYGGLAGRDMEALAIGLEEGTNEDYLAYRINQVEYLGERLREGGIPIQYPTGGHAVFVDAKLLLPHIPPEQFPAHALNNELYLEAGIRSVEIGSLLLGRDPQTGKQKASPMELLRLTIPRRVYTNDHMDYIADALIAVKARAATIKGLTFTYEPPVLRHFVARLKPVK Klebsiella michiganensis M5al Koxy BWI76_RS08725 BWI76_RS08725 Formiminoglutamase (EC 3.5.3.8) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (FORMIMINOGLUTAMASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. formimidoylglutamase MKLWQPTPAALWQGRDDSAEAANALRLFQTIVRAERFEPEMLAGDIALLGFACDEGVRRNKGRTGAERGPETLRRALANMASHDGHDRCVDMGTIHVADDALEAAQQALREAVTACQRAGKRTLVLGGGHETAFGHGAGVLDAFPGEEVGIINLDAHLDLRIADRASSGTPFRQLALACEAQRRAFHYACIGVSRAANTQALLDEAARRGVTIIEDLDVLNAFEARAIPELARNIARYDRLYLTIDLDVLPAREMPAVSAPAALGIPLATLLRIVEPLCRSGKLQAVDLVEFNPQYDIDSQGARAAARLAWQIAHWWQ Klebsiella michiganensis M5al Koxy BWI76_RS08735 BWI76_RS08735 Urocanate hydratase (EC 4.2.1.49) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (UROCANATE-HYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. urocanate hydratase MSQSKYRQQDVRAPRGTTLNAKSWLTEAPLRMLMNNLDPDVAENPHELVVYGGIGRAARNWECYDAIVKALKNLESDETLLVQSGKPVGVFKTHENSPRVLIANSNLVPHWATWEHFNELDAKGLAMYGQMTAGSWIYIGSQGIVQGTYETFVEAGRQHYQGSLKGRWVLTAGLGGMGGAQPLAATLAGACSLNIECQQSRIDFRLRTRYVDEQATSLDDALARIKKYTAEGRAISIALCGNAADIVPEMVKRGVRPDMVTDQTSAHDPLHGYLPKGWNWEEYQAKAESDPRGTILAAKRSMADHVQAMLAFHDMGVPTFDYGNNIRQMAQEMGVDNAFAFPGFVPAYIRPLFCRGIGPFRWVALSGDPQDIYKTDAKVKEIVKDDKHLHHWLDMARERISFQGLPARICWVGLEWRQKLGLAFNEMVRSGELSAPIVIGRDHLDSGSVASPNRETEAMRDGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGFSQHSGMVIVCDGTDEAAARIARVLHNDPATGVMRHADAGYDIAIECATEQGLNLPMVAATQGHAK Klebsiella michiganensis M5al Koxy BWI76_RS08740 BWI76_RS08740 Histidine ammonia-lyase (EC 4.3.1.3) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (HISTIDINE-AMMONIA-LYASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. histidine ammonia-lyase MNALTLIPGQLSLSQLRDVYSQPLKLALDESAFAAIDDSVACVNAILAEGRTAYGINTGFGLLAQTRISTEDLENLQRSLVLSHAAGVGEPLDDDLARLIMVLKINSLSRGFSGIRLSVIQALIGLVNAGVTPWIPAKGSVGASGDLAPLAHMSLTLLGEGKARVRGGEWLPATEALRQAGLEPITLAAKEGLALLNGTQASTAFALRGLFEAEDLFSSAVVCGALTTEAALGSRRPFDPRIHEARGQRGQIDAAALYRHLLTDDSAISQSHHNCTKVQDPYSLRCQPQVMGACLTQLRQAAEVLLVEANAVSDNPLVFASENDVISGGNFHAEPVAMAADNIALAIAEIGSLSERRIALMMDSHMSQLPPFLVKNGGVNSGFMIAQVTAAALASENKALSHPHSVDSLPTSANQEDHVSMAPAAGRRLWAMAENTRGVLAVEWLASVQGLDMREGLTSSPLLEEARHLLRERVTHYTEDRFFAPDIENAIALLAARHLTRLLPAVL Klebsiella michiganensis M5al Koxy BWI76_RS10705 BWI76_RS10705 Gamma-glutamyl-gamma-aminobutyrate hydrolase (EC 3.5.1.94) Specifically important for utilizing Putrescine Dihydrochloride. Automated validation from mutant phenotype: the predicted function (RXN0-3942) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. gamma-glutamyl-gamma-aminobutyrate hydrolase MENIMYKPVIGVVMCRNRLKGHQTQTLQEKYLNAIVNAGGVPIALPHALAEPELLSALLPKLDGIYLPGSPSNVQPHLYGENGDEPDADPGRDLLSMALIDAALERRIPIFAICRGLQELVVATGGTLYRRLFEQPELLEHREDPELPVEQQYAPSHEVQVQEGGLLSQLIPGCNTFWVNSLHGQGAKTTGPRLRVEARSPDGLAEAVSVNDHPFALGVQWHPEWNSSEYALSRMLFEGFITACQNYVAEKQRL Klebsiella michiganensis M5al Koxy BWI76_RS10710 BWI76_RS10710 Glutamate--putrescine ligase (EC 6.3.1.11) Specifically important for utilizing Putrescine Dihydrochloride. Automated validation from mutant phenotype: the predicted function (RXN0-3901) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. gamma-glutamylputrescine synthetase METNIVEVENFVQQSEERRVSAFTWEVKRYLERYPNTQYVDVLLTDLNGCFRGKRIPVSGLSKLEKGCYFPASVFAMDILGNVVEEAGLGQEMGEPDRTCVPVLGTLTPSAADPEYIGQVLLTMVDEDGAPFDVEPRNVLNRLWQQLRQRGLFPVVAVELEFYLLDRKRDAEGYLQPPCAPGTGDRNTQSQVYSVDNLNHFADVLNEIDEIAQLQLIPADGAVAEASPGQFEINLHHTDNVLDACDDALALKRLVRLMAEKHKMHATFMAKPYEEHAGSGMHIHISMQNNKGENVLADADGEDSAMLKRALAGMIDLMPASMALLAPNVNSYRRFQPGMYVPTQASWGHNNRTVALRIPCGDRHNHRVEYRVAGADANPYLVMAAIFAGILHGLDNPLPLQEEVEGNGLEQEGLPFPIRQSDALWEFMQNDHLRERLGERFCHVYHACKNDELLQFERLITETEIEWMLKNA Klebsiella michiganensis M5al Koxy BWI76_RS10795 BWI76_RS10795 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) Specifically important for utilizing L-Proline. Automated validation from mutant phenotype: the predicted function (1.2.1.88, 1.5.5.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. trifunctional transcriptional regulator/proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase MGTTTMGVKLDDATRERIKSAASRIDRTPHWLIKQAIFNYLEKLENDETLPELPALLSGAANESDEAGNPADEPYQPFLDFAEQILPQSVSRASITAAWRWAETDAVPMLLEQARLPQTLGEQAHKLAYQLAEKLRNQKTASGRAGMVQSLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSPHNETSLSRSLNRIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEDKGFRYSYDMLGEAALTADDAQAYMVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRAMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPFVIDYLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLIYPQFATHNAHTLAAIYQLAGQNYYPGQYEFQCLHGMGEPLYEQVTGKIADGKLNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADSTLPLDELVADPVAAVEKLAQQEGQVGLPHPKIPLPRDLYGKGRSNSAGLDLANEHRLASLSSSLLNSALHKWQALPMLEQPVAEGEMQPVINPAEPKDIVGYVREASDDEVQQALTSAVNNAPIWFATPPQERAAILERAAVLMEGQMPTLMGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRNDFDNETHRPLGPVVCISPWNFPLAIFSGQIAAALAAGNTVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTSDERVRGVMFTGSTEVATLLQRNIASRLDAQGRPTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDDIADHTLTMLRGAMAECRMGNPGRLTTDIGPVIDAEAKENIERHIQTLRAKGRKVFQAVRENGEDSREWASGTFVPPTLIELDSFDELKKEVFGPVLHVVRYNRNELEGLVEQINASGYGLTLGVHTRIDETIAQVTGSANVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSSRPQNAVGITLARQDPEYPLDAQLKTLLEKPLVALQQWAADRPELQALCQQFSKQAQAGTQRLLPGPTGERNTLTFMPRDRVLCVADNEQDALTQLAGVTAVGCEVLWPDAPLQRELAKKLPREVSERIHFAKAETLTTEPFDAVIYHGDSDQLRELCEQVAARDGAIVSVQGFARGESNLLLERLYIERSLSVNTAAAGGNASLMTIG Klebsiella michiganensis M5al Koxy BWI76_RS11670 BWI76_RS11670 Succinylornithine transaminase (EC 2.6.1.81) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (SUCCORNTRANSAM-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. aspartate aminotransferase family protein MSQSITRSNFDEWMMPVYAPAAFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPRLVKALTEQAGKFWHTGNGYTNEPVLRLAKQLIDATFADRVFFCNSGAEANEAALKLARKYAHDRFGSEKSGIVAFKNAFHGRTLFTVSAGGQPAYSQDFAPLPPQIQHAIYNDLDSAKALIDDNTCAVIVEPMQGEGGVVPADADFLRGLRELCDAHNALLIFDEVQTGVGRTGELYAYMHYGVTPDLLSTAKALGGGFPIGALLASERCASVMTVGTHGTTYGGNPLACAVAGEVFATINTREVLNGVKQRHQWFCERLNAINARYGLFKEIRGLGLLIGCVLKDEYAGKAKAISNQAAEEGLMILIAGANVVRFAPALIISEDEVNSGLDRFELACKRFLAGVSS Klebsiella michiganensis M5al Koxy BWI76_RS11685 BWI76_RS11685 Succinylarginine dihydrolase (EC 3.5.3.23) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (SUCCARGDIHYDRO-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. succinylarginine dihydrolase MKAWEVNFDGLPGLTHHYAGLSFGNEASTKHRYRVSNPQLAAKQGLKKMKALADAGYPQALIPPQERPNIPLLRQIGFDGSDEQVLEKAARQAPELLSAASSASSMWVANAATVSPSADSLDGRVHLTVANLNDKFHRASEAPTTEALLKAIFPDAQRFAVHGALPQVSLFGDEGAANHNRLGGDYGAPGVQLFIYGRQQGGEDNPQRYPARQTLEASQAVARLNQVNPRQVIFARQNPAVIDKGVFHNDVIAVSNQQVLFCHEQAFVDQPQLLQQLAQQVPGFTPLVVPASQVSVEDAVATYLFNSQLLSKREGGMRLILPLEAQEHPGVWRYLNRLVEGDNPIDELQVYDLRESMANGGGPACLRLRVVLTEDERQAVNPAVMMNDALFATLNDWVGRYYRDRLTQADLADPQLLREGREALDRLTQILRLGSVYPFQQ Klebsiella michiganensis M5al Koxy BWI76_RS17365 BWI76_RS17365 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrite reductase (NAD(P)H) MTRQLVIIGNGMAATRLAQALVERDARRFSITIIGDEPRQAYNRIQLSPVLGAEKTAGATRLLPAEWYSQHNVTVRAGETVTAVDMAARTLQTTAGELGWDELVFATGSLPFLPPLPGITLPHVFAFRTLADVEGILAIDGPAVVIGGGVLGVEAAAALRRHGDSVTLLHRGSWLMEQQTDAFVGEQLQMLLAERGIGCVMESRIAAIDEHQVLLEDGRAFAASRVVLATGVQPNKRLAERSGLACGRGILVDRRLATAQPGVSALGECCEIDGQTWGLVAPCLRQAEVLADRLCAIPGEDFRWQDSGTRLKVTDIELFSAGELRADEQDDVYTSWDPLDRHYRRLLLRDGKLRGVLLLGDCSSAAPLTALLGASAPAPAEWLFDPSSTMQPRAVGQTTMTKPVLVLVGHGMVGHHFLEQCVSRDLHQQYRIVVFCEERYAAYDRVHLTEYFAGRSAESLSLVEGDFFTQHGIELRLSESVASIDREARVVRDAFGHETHWDKLVLATGSYPFVPPVPGHNLEGCFVYRTLDDLDQIAARAATARRGVVIGGGLLGLEAANALKQLGLETHVVEFAPNLMAVQLDNGGAAMLREKISELGVGVHTSKATTEIVRNEQGLQLNFADGSSLATDMLVFSAGIRPQDALARSGGLSVGERGGICIDNQCRTSDPDVLAIGECALWENKIYGLVAPGYQMARAAAATLAGEAGSFSGADMSTKLKLLGVDVASFGDAQGRTPGCQSYQWTHGPQQVYKKIVVSADGKNLLGGVLVGDAGDYATLLQMMLNGMALPKHPESLILPALEGSAPKALGVAALPDGAQICSCHNVSKGDICQAVSGGAGDMAAIKSRTKAATGCGGCSALVKQVMEYQLAEQGVEVKKDICEHFPWSRQEIYHLVRVNHIRTFEQLIARYGQGHGCEVCKPLVASVLASCWNEYLLKPAHLPLQDTNDRYFANIQKDGTYSVVPRMAAGEVTPDGLIAIGQIAKRYQLYSKVTGGQRIDLFGARLEQLPAIWRELAEAGFETGHAYGKSLRTVKSCVGSTWCRYGVQDSTGLAVTLEHRYKGLRAPHKIKMAVSGCTRECAEAQGKDIGVIATEKGWNLYVCGNGGMKPRHADLFASDLDEATLIRSIDRLLMFYIRTADRLQRTSTWMDNLEGGVDYLREMILEDSLGIGEELEQEMARVVESYQCEWQTTLNDPQRLALFRSYVNSDEPDETVQRQTLRGQPQLAPFAAQGEPALPSRPWQAICDLDAIPQQAGIGARLGERQIALFRFGDQVYALDNLEPGSEANVLSRGLLGDAGGEPIVISPLYKQRIRLRDGRQCDGGEQAVRAWPVKVENGKVWVGNQQLLARAEAS Klebsiella michiganensis M5al Koxy BWI76_RS19515 BWI76_RS19515 D-lactate dehydrogenase (cytochrome c-553) (EC 1.1.2.5) Specifically important for utilizing Sodium D-Lactate. Automated validation from mutant phenotype: the predicted function (1.1.2.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. D-lactate dehydrogenase MSSATTNNNAFLAELTRLVGSSHLLTDPAKTQRYRKGFRSGQGDALAVVFPGTLLELWRVLNACVNADKIILMQAANTGLTEGSTPNGNDYDRDIVIISTLRLDKLHLLDKGEQVLAYPGTTLYSLEKALKPLGREPHSVIGSSCIGASVVGGICNNSGGSLVQRGPAYTEMSLYAQIDENGKLSLVNHLGIDLGTTPEQILSRLDDERVKDEDVRHDGRHAHDHDYVTRVRDVNADTPARYNADPDRLFESSGCAGKLAVFAVRLDTFPAAKRQQVFYIGTNRPEVLTEIRRHILAEFNHLPVAGEYMHRDIYDIAEQYGKDTFLMIDKLGTDKMPFFFTMKGRTDAMLEKVSLFKPHFTDRFMQKLGHVFPAHLPERMKTWRDKYEHHLLLKMAGDGIEEAQAWLGEYFKNAEGDFFVCTAEEGSKAFLHRFAAAGAAIRYQAVHADEVEDILALDIALRRNDTDWFEHLPADIDSQLVHKLYYGHFMCHVFHQDYIVKKGVDAHELKEKMLVLLKERGAQYPAEHNVGHLYEAPESLKRFYRENDPTNSMNPGIGKTSKQKYWGEAPDKTTSAADPQ Klebsiella michiganensis M5al Koxy BWI76_RS19610 BWI76_RS19610 Cytidine deaminase (EC 3.5.4.5) Specifically important for utilizing Cytidine. Automated validation from mutant phenotype: the predicted function (CYTIDEAM2-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. cytidine deaminase MHPRFQAALPQLAADLQAAIAPMLTDRHFPALLNADQVAALQSATGLDEDALAFALLPLAAACARADLSHFNVGAIARGISGTWYFGGNMEFLGATMQQTVHAEQSAISHAWLRGEKSLRAITVNYTPCGHCRQFMNELNSGLALRIHLPGREAHSLQHYLPDAFGPKDLDIKTLLMDEQDHGFPLSGDALAQAAIQAANRCHTPYSNSPSGVALELKDGTLFTGSYAENAAFNPTLPPLQGALNLLSLNGYDYPDIQRAILAEKADAALIQWDATAATLKALGCHNIDRVLLG Klebsiella michiganensis M5al Koxy BWI76_RS22230 BWI76_RS22230 Sorbitol-6-phosphate 2-dehydrogenase (EC 1.1.1.140) Specifically important for utilizing D-Sorbitol. Automated validation from mutant phenotype: the predicted function (1.1.1.140) was linked to the condition via a SEED subsystem. This annotation was also checked manually. sorbitol 6-phosphate dehydrogenase MNQVAVVIGGGQTLGEFLCRGLAAEGYRVAVVDIQSDKATRVAQSINAEYGEGTAWGFGADATSEASVVALARGVDDIFSRVDLLVYSAGIAKAAFISDFALGDFDRSLQVNLVGYFLCAREFSRLMIRDGIKGRIIQINSKSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEYGITVHSLMLGNLLKSPMFQSLLPQYATKLGIPEEQVEQYYIDKVPLKRGCDYQDVLNVLMFYASPQASYCTGQSINVTGGQVMF Klebsiella michiganensis M5al Koxy BWI76_RS22915 BWI76_RS22915 L-fuculose phosphate aldolase (EC 4.1.2.17) Specifically important for utilizing L-Fucose. Automated validation from mutant phenotype: the predicted function (FUCPALDOL-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. fuculose phosphate aldolase MERNRLARQIIDTCLEMTRLGLNQGTAGNVSVRYQGGMLITPTGIPYEKLTEAHIVYIDAEGQHEQGKLPSSEWRFHLAAYQTRPDAHAVVHNHAVHCTAVSILNRPIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVAVALKNRKATLLQHHGLIACEENLEKALWLAHEVEVLAQLYLSTLAIIDPVPVLDDEAIAVVLEKFKTYGLRIEE Klebsiella michiganensis M5al Koxy BWI76_RS22930 BWI76_RS22930 L-fuculokinase (EC 2.7.1.51) Specifically important for utilizing L-Fucose. Automated validation from mutant phenotype: the predicted function (FUCULOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-fuculokinase MKKDVILVLDCGATNVRAIAVDRRGNIIARAATTNASDIAVENSAWHQWSLEAILQRFAECCRQISDPLSSCTVRGITVTTFGVDGALVDEQGKLLYPVISWKCPRTAAVMDNISRFMPAQQLQQISGVGAFAFNTLYKLIWLKENHPQLLEKARAWLFISSLLNQRLTGEFTTDITMAGTSQMLDIHQRDFSTQILQATGLPRRLFPRLVEAGQQIGTLQSDAAKMLGLAVGIPVISAGHDTQFALFGAGAEQDEPVLSSGTWEILMVRSAQVNTPLLSHYAGSTCELDSQPGRYNPGMQWLASGVLEWVRQLLWTPETPWQTLIDEARALPDGAQKVKMQCDLLSSPNAGWQGITLNTTRGHFYLAALEGLAEQLANNLQTLQKIGHFNASELLLVGGGSRNALWNQIKANRLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQVSYQYRYFYPQTEPELIEGV Klebsiella michiganensis M5al Koxy BWI76_RS23870 BWI76_RS23870 Glycine dehydrogenase (aminomethyl-transferring) (EC 1.4.4.2) Specifically important for utilizing Glycine. Automated validation from mutant phenotype: the predicted function (1.4.4.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. glycine dehydrogenase (aminomethyl-transferring) MTQTLGQLENRDAFIERHIGPDALQQQEMLKTVGADSLNALIGQIVPQDIQLATPPQVGEATTEFAALAELKAIAGRNKRFKSYIGMGYTAVQLPPVIQRNMLENPGWYTAYTPYQPEVSQGRLESLLNFQQVTLDLTGLDIASASLLDEATAAAEAMAMAKRVSKLKNANRFFVAADVHPQTLDVVRTRAETFGFDVIVDDAEKALDHQDVFGVLLQQVGTTGEVHDYSKLIADLKARKVIVSVAADFMALVLLTAPGKQGADIVFGSAQRFGVPMGYGGPHAAFFAAKDEFKRSMPGRIIGVSKDAAGNTALRMAMQTREQHIRREKANSNICTSQVLLANIASLYAVFHGPAGLKRIASRIHRLTDILADGLQKKGLKLRHAHYFDTLCVEVADKAAVLARAEALRINLRSDIHHAVGITLDEATTREDVLNLFRAILGDDHGLDIDTLDKDVALDSRSIPASMLRDDAILTHPVFNRYHSETEMMRYMHALERKDLALNQAMIPLGSCTMKLNAAAEMIPITWPEFAELHPFCPVDQAEGYHQMIAQLSDWLVKLTGYDAVCMQPNSGAQGEYAGLLAIRHYHESRNEGHRDICLIPSSAHGTNPASAQMAGMQVVVVACDKNGNIDLADLRAKAEQHAANLSCIMVTYPSTHGVYEETIREVCEVVHQFGGQVYLDGANMNAQVGITSPGFIGADVSHLNLHKTFCIPHGGGGPGMGPIGVKSHLAQFVPGHSVVQIEGMLTRQGAVSAAPFGSASILPISWMYIRMMGAEGLKQASQMAILNANYIATRLKDAFPVLYTGRDGRVAHECILDIRPLKEETGISELDIAKRLIDFGFHAPTMSFPVAGTLMVEPTESESKVELDRFIDAMLAIRGEIDRVKAGEWPLEDNPLVNAPHTQGELVSAWNHPYARELAVFPAGLNNKYWPTVKRLDDVYGDRNLFCSCVPMSEYQ Klebsiella michiganensis M5al Koxy BWI76_RS23880 BWI76_RS23880 Aminomethyltransferase (EC 2.1.2.10) Specifically important for utilizing Glycine. Automated validation from mutant phenotype: the predicted function (2.1.2.10) was linked to the condition via a SEED subsystem. This annotation was also checked manually. glycine cleavage system protein T MAQQTPLFEQHTLCGARMVDFHGWMMPLHYGSQIDEHHAVRGDAGMFDVSHMTIVDFHGSRIREFLRYLLANDVAKLTVPGKALYSGMLTASGGVIDDLIVYFLSEDYFRLVVNSATREKDLAWIAQQSESYGLEITVRDDLSLIAVQGPRAKEKAATLFTDAQRQAVEGMKPFFGVQAGDLFIATTGYTGEAGYEIALPNEQAVDFWRGLLDAGVKPCGLGARDTLRLEAGMNLYGQEMDEGVSPLAANMGWTIAWEPTDRDFIGREALEMQREKGTEQLVGLVMTEKGVLRGGLPVRFSDADGNQKEGIITSGTFSPTLGYSIALARVPEGIGETAVVQIRNREMPVKVTKPVFVRNGKAVV Klebsiella michiganensis M5al Koxy BWI76_RS24235 BWI76_RS24235 Branched-chain-amino-acid transaminase (EC 2.6.1.42) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (2.6.1.42) was linked to the condition via a SEED subsystem. This annotation was also checked manually. aminotransferase MHDRRLAARAGELKPSAVRELLKHSKLPGVISLGGGIPAPELFDTEGLNLAVQQVMNGRFNDAFQYGLTEGYPPLRQAVSELCQARGVACPASHVYITSGSQQSLDIVARTLLDPGDAIVVERPTYLAALQVFQLAQANILSVDTDDDGMLVEQLADLLETTRVKAVYLVPTFGNPGGKTLSEARRRRLVELAKKHDFVIIEDDPYGEISFTDEVRRPLYQYAVELGCEDQVVYTSTFSKILAPGMRIGWIVMPDWLAQQTVIVKQAADLHTNMLSQVITAEYLSMNRLESQIALIREDYRKKCVALADALESQLGEHLEFSRPKGGMFLWARFRYPFDTMEWMKKTLENGVVYVPGEAFYNDNPDTRTLRLSYSTVSADGLMTAVERLAKSL Klebsiella michiganensis M5al Koxy BWI76_RS26160 BWI76_RS26160 4-alpha-glucanotransferase (EC 2.4.1.25) Specifically important for utilizing a-Cyclodextrin. Automated validation from mutant phenotype: the predicted function (2.4.1.25) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 4-alpha-glucanotransferase METKRLDNAALAAGISPSYINAHGKPQSIAAATKQRLLDAMHRTTVTPKVAVNPLPAVQVFTHGKKMSLPVAGQGEFHWILTTEEGKQYQGQARGGETLPLPARLPEGYHTLTLTQDGDRWHCRAIVAPARCYEPQALKDGQKLWGTCVQLYTLRSEKNWGIGDFGDLRAMLPEIARRGGSFIGLNPIHALYPANPESASPYSPSSRRWLNVIYIDVNAVEDFRHSKEAQKWWHSPATQQTLQAARQTDDVDYTAVTTLKLTALRMAWKGFSARNDEAMAEFRQFVTREGDSLYWQAAFDALHAWQVKQDPMRWGWPAWPKAYQDTDSPEVKAFCAEHADEVNFYLWLQWLAYTQFAECWHTSQNDSMPIGLYRDLAVGVAEGGAETWCDRELYCLKASVGAPPDILGPLGQNWGLPPMDPHIMVARAYEPFVELLRANMQNCGALRIDHVMSVLRLWWIPYGETADHGAYVQYPVDDLLSILALESKRHRCMVIGEDLGTVPVEIVGKLRKSGVYSYKVLYFENDHEKTFRAPKAYPEQSMAVATTHDLPTLRGYWESGDLTLGKSLGLYPDEVVLRGLYQDRELAKQGLLDALHRYGCLPKRTGHKASLMAMTPTLNRGMQRYIADSNSALLGLQPEDWLVMAEPVNIPGTSTEYPNWRRKLSTTLEAMFADEQVNKLIKDLDKRRKAASKKKPA Klebsiella michiganensis M5al Koxy BWI76_RS26165 BWI76_RS26165 Glycogen phosphorylase (EC 2.4.1.1) Specifically important for utilizing a-Cyclodextrin; D-Maltose monohydrate. Automated validation from mutant phenotype: the predicted function (2.4.1.1) was linked to the condition via a SEED subsystem. This annotation was also checked manually. maltodextrin phosphorylase MSQTSFNKAQFQAALTRQWQHFGLQSASEMTQRQWWRAVSGALSELLSAQPVAKATEGERHVNYISMEFLIGRLTGNNLLNLGWYQQVSDELQAHDVNLTDLLEEEIDPGLGNGGLGRLAACFLDSMATVGQSATGYGLNYQYGLFRQSFADGQQMEAPDDWGRNSYPWFRHNEALDVQVGLGGKVTKGGEWVPAFVITGEAWDLPVLGYRNNVAQPLRLWQAKHAHPFNLTKFNDGDFLRAEQQGIDAEKLTKVLYPNDNHQAGKKLRLMQQYFQCACSVADILRRHHLAGRKLAELADYEVIQLNDTHPTIAIPELLRVLIDEHQLSWDEAWAITSKTFAYTNHTLMPEALECWDEKLVKALLPRHMQIIKEINDRFKTLVDKTWPGDKQVWAKLAVVHDKQVRMANMCVVSGFAVNGVAALHSDLVVKDLFPEYHQLWPNKFHNVTNGITPRRWIKQCNPALAALLDKTLKKEWANDLDQLINLEKYADDAKFRQTYRDIKLANKVRLAEFVKRRTGIEINPQAIFDIQIKRLHEYKRQHLNLLNILAQYKEIRENPQADRVPRVFLFGAKAAPGYYLAKNIIWAINKVAAAINNDPLVGDKLKVVFLPDYCVSAAEMLIPAADVSEQISTAGKEASGTGNMKLALNGALTVGTLDGANVEIAEQVGEENIFIFGHTVEEVKALKAKGYDPLKWRKKDKLLDAVLKELESGKYSDGDKHAFDQMLHSLLKGGDPYLVLADFEAYVAAQKQVDELYRDQEAWTRATILNTARCGMFSSDRSIRDYQQRIWQAKR Klebsiella michiganensis M5al Koxy BWI76_RS27020 BWI76_RS27020 Xylulose kinase (EC 2.7.1.17) Specifically important for utilizing D-Xylose. Automated validation from mutant phenotype: the predicted function (XYLULOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. xylulokinase MYIGIDLGTSGVKAILLNEQGEVVASHTEKLNVSRPHPLWSEQDPEHWWLATDSAMKALGAQHSLRAVKALGIAGQMHGATLLDKQQRVLRPAILWNDGRCGEECALLEEKVSRSRQITGNLMMPGFTAPKLLWVQRHEPEIFRQVDKVLLPKDYLRLRMTGEFASDMSDAAGTMWMDVARRDWSDEMLAACGLSRDNMPALFEGCEVTGSLRPAVAQAWNMPEVLVVAGGGDNAAGAVGVGMADAGQAMLSLGTSGVYFAVSDGFLSKPESAVHSFCHALPGRWHLMSVMLSAASCLDWAATLTGLGTVPALIAAAEAANDDADPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPAELARAVLEGVGYALADGMDVVHACGVKPESVTLIGGGARSAYWRQMLADISGQQLDFRTGGDVGPALGAARLAQLALHRNVAFSDLLPQLPLEQAHLPDAERFARYAPRRETFRQIYQQLLPLMS Klebsiella michiganensis M5al Koxy BWI76_RS27025 BWI76_RS27025 Xylose isomerase (EC 5.3.1.5) Specifically important for utilizing D-Xylose. Automated validation from mutant phenotype: the predicted function (XYLISOM-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. xylose isomerase MQTYFDQLDRVRYEGPKSANPLAFRHYNPDELVLGKRMEDHLRFAACYWHTFCWNGADMFGVGSFNRPWQQPGEAMEMAKRKADVAFEFFHKLNVPYYCFHDVDVSPEGASLKEYANNFAQMVDVLAEKQQQSGVKLLWGTANCFTNPRYGAGAATNPDPEVFSWAATQVVTAMDATHKLGGENYVLWGGREGYETLLNTDLRQEREQIGRFMQLVVEHKHKIGFQGTLLIEPKPQEPTKHQYDYDASTVYGFLKQFGLEKEIKLNIEANHATLAGHTFHHEIATAIALGLFGSVDANRGDPQLGWDTDQFPNSVEENALVMYEILKAGGFTTGGLNFDAKVRRQSTDKYDLFYGHIGAMDTMALALKVAARMIEGGELDKRVAKRYAGWNGELGQQILKGQMNLADIAQYATQHNLAPQHQSGHQELLENVVNRYLFDR Klebsiella michiganensis M5al Koxy BWI76_RS27255 BWI76_RS27255 2-amino-3-ketobutyrate coenzyme A ligase (EC 2.3.1.29) Specifically important for utilizing L-Threonine. Automated validation from mutant phenotype: the predicted function (AKBLIG-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glycine C-acetyltransferase MRGDFYKQLTNDLDTARAEGLFKEERIITSAQQADITVGGSQVINFCANNYLGLANHPELIAAAKSGMDSHGFGMASVRFICGTQDSHKALEKKLADFLGMEDAILYSSCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRFRYANNDMVELEARLKEARDAGARHVLIATDGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGKALGGASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEAGSELRDRLWSNARLFREKMTAAGFILAGADHAIIPVMLGEATVAQEFARELQKEGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQIERAVEAFTRIGKQLGVIA Shewanella oneidensis MR-1 MR1 199292 SO0095 hutI Imidazolonepropionase (EC 3.5.2.7) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (IMIDAZOLONEPROPIONASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. imidazolonepropionase (NCBI ptt file) MSWDQVWIDVNVATMDPSISAPYGAITHAAIAVKDGKIAWLGPRSELPAFDVLSIPVYRGKGGWITPGLIDAHTHLVFAGNRANEFELRLKGATYEEIARAGGGIISTVNACREADEAALFELGRQRLNALAKEGVTTVEIKSGYGLDTETELKILRVARELGKHHHVDVKTTFLGAHAVPPEYKGNSDGYVDLIINKMLPAVIKENLADAVDVFCENIAFNLEQTERVLSAAKAAGLQVKLHAEQLSNMGGSELAARLGAKSVDHIEYLDEAGVKALSESGTCAVLLPGAFYFLRETQKPPIDLLRQYGVPMVLASDFNPGSFPICSTLLMLNMGCTLFRLTPEEALAGLTLNAAKALGIEDKVGSLVVGKQADFCLWNIATPAQLAYSYGVNPCKDVVKNGKLVHQ Shewanella oneidensis MR-1 MR1 199539 SO0344 prpC 2-methylcitrate synthase (EC 2.3.3.5) Specifically important for utilizing Sodium propionate. Automated validation from mutant phenotype: the predicted function (2.3.3.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. methylcitrate synthase (NCBI ptt file) MSDAKKLTGAGLRGQSAGETALSTVGVSGSGLTYRGYDVKDLAENATFEEVAYLILYGELPTTAQLAAYKTKLKGMRGLPQALKEVLERIPADAHPMDVMRTGCSMLGNLEAEHSFSEQSQIADRLLAAFPSIICYWYRFSHDGVRIDTETDDDQIGAHFLHLLHGKAPSALHTKVMDVSLILYAEHEFNASTFTARVCASTLSDMHSCVTGAIGSLRGPLHGGANEAAMELIQDMKDEADARDVLMGKLERKEKIMGFGHAIYRDSDPRNAIIKEWSEKLAADYGDDRLYRVSVACEALMWEQKKLFCNADFFHASAYHFMGIPTKLFTPIFVCSRVTGWTAHVMEQRSNNRIIRPSADYVGVSPRKVIPIANR Shewanella oneidensis MR-1 MR1 199807 SO0619 astD Succinylglutamic semialdehyde dehydrogenase (EC 1.2.1.71) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (SUCCGLUALDDEHYD-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. succinylglutamic semialdehyde dehydrogenase (NCBI ptt file) MTHFIKGQWHTGKGHDVASSNPANGEIIWRGQTATAEQVNAAVDAAREAQFDWFILGFDARLKIVEAYRSQLEANKAELAETIAQETGKPQWETATEVAAMIGKIGLSASAYNKRTGTETNDTPAGRAVLRHKPHGVVAVFGPYNFPGHLPNGHIVPALLAGNSVVFKPSELTPKVAELMVTLWEKSGLPAGVLNLVQGEVDTGKALASHPQLDGLFFTGSSRTGHLLHQQYAGHPGKILALEMGGNNPLIIKGVADIKAAVHDILQSAYISSGQRCTCARRLYVEQGEQGDALVAKLVEAVKQIKVGPWNAQPQPFMGSMISEAAAKGMVAAQANLLSLGGVPLVELMHLQAGTGLVSPGLIDVTAVSELPDEEYFGPLLQLVRYSDFDQAIKLANQTRYGLSAGILADSREDYEYFLARIRAGIVNWNKQITGASGAAPFGGVGASGNHRASAFYAADYCAYPVASVEADAVSLPATLSPGLTLS Shewanella oneidensis MR-1 MR1 200397 SO1219 deoB Phosphopentomutase (EC 5.4.2.7) Specifically important for utilizing Adenosine. Automated validation from mutant phenotype: the predicted function (PPENTOMUT-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. phosphopentomutase (NCBI ptt file) MKRTVIMMLDSFGVGAAGDAAKFGDVGSDTFGHIAKACAEGKADTGRKGPLALPNLARLGLAHAAMESTGAFAPGFADNVDLIGAYGHAQELSSGKDTPSGHWEMAGVPVLFEWGYFSEHQNSFPKELTDKILARAGLDGFLGNCHASGTTILEELGEEHMRSGKPIFYTSADSVFQIACHEGTFGLENLYRLCEIAREELEPYNIGRVIARPFDGTGPSDFARTGNRKDYSLEPPAKTVLDKLKAAGGEVVSVGKIADIYAYCGITKKVKANGLEALFDATLAEVKSAGENTIVFTNFVDFDSHYGHRRDVAGYAKGLEYFDARLPEMLALLDEDDLLILTADHGCDPTWQGTDHTREYVPVLAYGAGLKAGSLGRRNSFADIGQSIASYFKLEPMEYGESFI Shewanella oneidensis MR-1 MR1 200445 SO1267 Gamma-glutamyl-gamma-aminobutyrate hydrolase (EC 3.5.1.94) Specifically important for utilizing Putrescine Dihydrochloride. Automated validation from mutant phenotype: the predicted function (RXN0-3942) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. hypothetical Glutamine amidotransferase (NCBI ptt file) MSVLLPLIGVIACNQRLGSHPFNIVGEKYLLGVVNGAKGWPLVIPSLGADQPIEAILARLDGILFTGSPSNVEPHLYAGVPSEAGTHHDPKRDATTLPLIRAAIAAGVPVLGICRGFQEMNVAFGGSLHQKLHEVGHFIEHREDKEASLEVQYGPSHSITVEPGGVIYEAWGRNSAEVNSVHTQGVERLGIGLRPEACAPDGLVEAFSVIDATEFALGVQWHPEWKVSDNPFYLSIFNAFGDACRRRATTRVK Shewanella oneidensis MR-1 MR1 200446 SO1268 Glutamate--putrescine ligase (EC 6.3.1.11) Specifically important for utilizing Putrescine Dihydrochloride. Automated validation from mutant phenotype: the predicted function (RXN0-3901) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glutamine synthetase (NCBI ptt file) MNKLIAFLKERKITEVECVICDMTGIARGKIAPVDKFLDEKGMRLPESVLLQTVTGDFVDDDIYYSLLDDADIDFVCVPDENAVFMLPWTIEATAQVIHDCYDRMGNPIELSPRNVLKKVLSLYDEKGWEPVIAPEMEFYLTSRSDDHDLPLKPPIGRSGRPEAGRQSFSIDAANEYDPLFEDMYDWCEIQGLDIDTLIHEDGPAQMEINFSHGNPLSLADQVFVFKRTLREAALKHNVCATFMAKPVTDEPGSAMHIHQSVINKETGKNIFTNEDGTQSALFLSYIAGLQKYIPEFLPLMAPNANSFRRFLPGTSAPVNLEWGIENRTCGLRIPESSPQNRRIENRIPGADANCYLAFAAGLLCGYIGMVEGLKPSTPVQGKANESRSNNPHCLPLTLEEALVAMEESDACKEYLGESFTTGFVAVKQAELENFRRVVSSWEREFLLLSV Shewanella oneidensis MR-1 MR1 200654 SO1483 aceB Malate synthase (EC 2.3.3.9) Specifically important for utilizing Tween 20. Automated validation from mutant phenotype: the predicted function (MALSYN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. malate synthase A (NCBI ptt file) MTEHTLSEQQVNLTLNKATANGTLALVGNTIPGQEVIFTEGAMALLESLCREFGAEVPTLLAKRKDRQARIDKGALPDFLPETRAIRDGAWKIRGIPNDLLDRRVEITGPVERKMVINALNANAKVFMADFEDSLAPSWQKVVEGQINLRDAVRGEIEYTAPETGKHYKLGPNPAVLICRVRGLHLKEKHVEFNQQSIPGGLFDFAMYFYHNYRQLLAKGSGPYFYIPKLESHIEARWWAKVFAFVEERFCLQAGTIKCTCLIETLPAVFEMDEILYELRSNIVALNCGRWDYIFSYIKTLKRHGDRVLPDRQAVTMDTPFLSAYSRLLIKTCHKRGALAMGGMAAFIPAKDPAQNEAVLQRVRKDKELEARNGHDGTWVAHPGLADTAMGIFNEYIGQDHQNQLHITRDVDAPILAAELLKTCDGERTEQGMRLNIRIALQYLEAWISGNGCVPIYGLMEDAATAEISRASIWQWIQHGKSLSNGKLVTKQLFKDMLVEELANVKKEVGSDRFTHGKFTQAAVLLEDITTSDELVDFLTLPGYEMLTA Shewanella oneidensis MR-1 MR1 200655 SO1484 aceA Isocitrate lyase (EC 4.1.3.1) Specifically important for utilizing Tween 20. Automated validation from mutant phenotype: the predicted function (ISOCIT-CLEAV-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. isocitrate lyase (NCBI ptt file) MTKATQTSRQAQIDAIKKDWAENPRWKNVRRPYTAEEVVALRGSIVPENTIAKRGAAKLWDLVNGGSKKGYVNSLGALTGGQAVQQAKAGIEAIYLSGWQVAADANLAGTMYPDQSLYPANSVPAVVSRINNSFRRADQIQWSNGVNPEDENFVDYFLPIIADAEAGFGGVLNAFELMKSMIDAGAAGVHFEDQLASVKKCGHMGGKVLVPTQEAVQKLVAARLAADVSGVETLVIARTDANAADLLTSDCDPYDRDFVTGERTNEGFYRVNAGLDQAISRGLAYAPYADLIWCETAKPDLEEARRFAEAIHAQYPDQLLAYNCSPSFNWKKNLDDATIARFQQALSDMGYKYQFITLAGIHNMWYNMFDLAYDYARGEGMKHYVEKVQEVEFAAAKKGYTFVAHQQEVGTGYFDQVTTVIQGGHSSVTALTGSTEEEQF Shewanella oneidensis MR-1 MR1 200831 SO1666 phhA Phenylalanine 4-monooxygenase (EC 1.14.16.1) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (1.14.16.1) was linked to the condition via a SEED subsystem. This annotation was also checked manually. phenylalanine-4-hydroxylase (NCBI ptt file) MTIDTVHTAPYVARSADDSGYIHYPQEEHDIWRQLYARQAVNLPGRACKEYLQGLDALAMPKDRIPQLAEIDKVLMATTGWKTADVPALISFGRFFELLANKEFPVATFIRRKEEFDYLQEPDIFHEIFGHCPLLTNPSFAHFSHMYGQLGLNASKEDRVFLARLYWFTVEFGLLKPQEGELCIYGGGILSSPGETLYAMESQVPERKPFDLLDVLRTPYRIDIMQPIYYVIEHIDVLDEIAKMDIMAYVAKARQLGLFAPKYPPKAKKAS Shewanella oneidensis MR-1 MR1 200836 SO1671 Maleylacetoacetate isomerase (EC 5.2.1.2) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (5.2.1.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. glutathione S-transferase family protein (NCBI ptt file) MILYGYWRSSAAYRVRIALNLKGVSAEQLSVHLVRDGGEQHKADYIALNPQELVPTLVVDDEQDGDALTQSLAIIEYLDELYPKTPLLPASALERAHVRAMALTIACEIHPLNNLRVLQYLTQKLTVNEEAKSAWYHHWVATGFTALETQLVRHSGRYCFGDKVTIADLCLVPQVYNAQRFNVDLTPYPNIMRVWAECNQLPAFADAAPERQADAV Shewanella oneidensis MR-1 MR1 200842 SO1677 atoB 3-ketoacyl-CoA thiolase [isoleucine degradation] (EC 2.3.1.16) Specifically important for utilizing L-Isoleucine. Automated validation from mutant phenotype: the predicted function (METHYLACETOACETYLCOATHIOL-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. acetyl-CoA acetyltransferase (NCBI ptt file) MSTELLNQEIVIVAAKRTPMGSFQGSLSGITSLSLAATAIKALLADTQVAPDKVDEVLMGCVLPAGLGQAPARQATLGAGLPLSVGATTVNKVCGSGMKTVMLAHDLIKAGSAKVVIAGGMESMSQAPYLLDKARAGIRMGHGKVLDHMFLDGLEDAYTGGAMGTFAQKTADEFGITREQMDAFALSSLEKANAAINSGAFKTEIVPVTVSDRRGDVTIDTDEQPGNARPEKIPTLRPAFAKDGTITAANSSSISDGAAALMLTTRANAEQLGLTVLATIKGHTTHAQEPALFTTAPVGAMAKLLSNVGWSKDEVDLFEINEAFAMVTMLAVSELGLDMTKVNVNGGACALGHPIGCSGARLLVTLIHALKARGLKRGVASLCIGGGEATAMAIEV Shewanella oneidensis MR-1 MR1 200974 SO1812 mdeA Methionine gamma-lyase (EC 4.4.1.11) Specifically important for utilizing L-Methionine. Automated validation from mutant phenotype: the predicted function (4.4.1.11) was linked to the condition via a SEED subsystem. This annotation was also checked manually. methionine gamma-lyase (NCBI ptt file) MQDKSSKMWKAATQAIHAGHEREAFGSLVTPLYQTATFVFDSAQQGGERFAGNEPGYIYTRLGNPTVAELERKMAILERAEAAAATASGMGAVSAALLANLQIGDHLVASNAVYGCTFALMTNQFARFGIEVTLVDFSDVELIERAIKPNTKVIFCETPVNPHLQVFDLSAIAAIAKRHSLTSIVDNTFMTPLLQQPIALGIDVVVHSATKYLNGHGDVIAGIVCGSEAQLHRVKYEILKDIGAVMSPHDAWLILRGLKTLDVRLQRHCESAQRVAEFLEQHPAVTRVYYPGLKSHSGHRFIGQQMRRAGGVIAFELAADFTQAMAFVGNLKLFSIAVSLGDAESLIQHPASMTHSPYSPEARAAAGIGDNLLRISVGLEDCDDIIADLSQALAALV Shewanella oneidensis MR-1 MR1 201123 SO1962 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (RXN-10815) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 4-hydroxyphenylpyruvate dioxygenase (NCBI ptt file) MASELNPLGLLGIEFTEFASSDTDFMHKVFIDFGFSLLKKAKNKDILYYKQNDINFLLNKQREGFSAKFAKSHGPAICSMGWRVEDASFAHRVAVERGAKAADDSAKDLPYPAIYGIGDSLIYFIDTFGANNNIYATDFEDLSEPVITQEKGFIEVDHLTNNVYKGTMEHWANFYKNIFGFTEVRYFDISGVQTALVSYALRSPDGSFCIPINEGKGNDKNQIDEYLKEYNGPGVQHLAFRSRDIVKSLDAMEGSSIQCLDIIPEYYDTIFDKVPQVTENRDRIKHHQILVDGDESGYLLQIFTKNLFGPIFIEIIQRKNNLGFGEGNFTALFQSIERDQMRRGVL Shewanella oneidensis MR-1 MR1 201124 SO1963 Homogentisate 1,2-dioxygenase (EC 1.13.11.5) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (1.13.11.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. conserved hypothetical protein (NCBI ptt file) MPFYVKQGQVPHKRHIAFEKENGELYREELFSTHGFSNIYSNKYHHNMPTKALEVAPYRLGHGAHWEDSLVQNYKLDSRSADREGNFFSARNKIFYNNDVAIYTAKVTQDTAEFYRNAYADEVVFVHEGEGTLYSEYGTLEIKKWDYLVIPRGTTHQLKFNNYSNVRLFVIEAFSMVEVPKHCRNEYGQLLESAPYCERDLRTPILQAAVVERGAFPLVCKFGDKYQLTTLEWHPFDLVGWDGCVYPWAFNITEYAPKVGKIHLPPSDHLVFTAHNFVVCNFVPRPYDFHERAIPAPYYHNNIDSDEVLYYVDGDFMSRTGIEAGYITLHQKGVAHGPQPGRTEASIGKKETYEYAVMVDTFAPLKLTEHVQHCMSKDYNRSWLEN Shewanella oneidensis MR-1 MR1 201844 SO2706 astB Succinylarginine dihydrolase (EC 3.5.3.23) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (SUCCARGDIHYDRO-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. succinylarginine dihydrolase (NCBI ptt file) MKHFEANFDGLVGPTHNYAGLSFGNVASLNNAALVSNPKAAAKQGLQKAKALADLGMIQGMLAPQERPDLNTLRRIGFSGSDAQVLQQAAKTAPALLNACCSASSMWTANAATVSPSADTRDGKLHFTPANLVDKLHRSIEPITTGRILTATFNDPHYFYHHNHLPEHNSFGDEGAANHTRLCQEYGHAGVELFVYGQEATNPHAPKPLKFPARQTLEASMAIARLHQLEEDNCVFIQQNPAVIDQGVFHNDVIAVGNQNVLFYHEQAFLNTQAKLDEIKRKLDTELYFIEVPTAKVSINDAVKSYLFNTQIITLPSGEMAIIAPTDCQENPAVYAYLNELLSLNTPIKQVLYFDVKQSMQNGGGPACLRLRVAMNEREVAAVNQHTLLTDALFTRLNTWVEKHYRDRLSTEDLADPQLVIESRTALDELTQIMKLGSVYPFQR Shewanella oneidensis MR-1 MR1 201923 SO2791 cdd Cytidine deaminase (EC 3.5.4.5) Specifically important for utilizing Cytidine. Automated validation from mutant phenotype: the predicted function (CYTIDEAM2-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. cytidine deaminase (NCBI ptt file) MQDRFIRSITQLPTPLADALIPLLHQGFAGHIDAQHLAELVKSSNMTESEVLLALLPIAAALAKPPISEFYVGAIAKGKSGDIYMGANLELPGEALFHSVHAEQSAISHAWLSGESQIVDMIVNASPCGHCRQFMNELVDGGQIKIHLPSQDSHLLSYYLPYAFGPKDLNVQSPLLVKQETEFALDSSDPMVIEALDHAGLSYAPYTQSYAAVVLETADGATYCGRYAENAAFNPSMLPMQMALSNLTRHNRDFAEIRRAVLVESSQGKISLVGAAMDALHAVAAIELEHIVVDPI Shewanella oneidensis MR-1 MR1 202473 SO3365 glsA Glutaminase (EC 3.5.1.2) Specifically important for utilizing L-Glutamine. Automated validation from mutant phenotype: the predicted function (GLUTAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glutaminase A (NCBI ptt file) MPETALLEEVVDRVRPLLGQGKVANYIPALANIDPGKLGIAVTTIDGETIGAGDYLEPFSIQSISKVFSLTLALTLYEETEIWSRVGKEPSGHSFNSLVQVELERGKPRNPFINAGALVIADLLQSRLGAPKHRMLELVRALSQNDKVCFDKQVADSEYQHSARNAAIAYLMKSFGNFQGDVDTVLRTYFHYCALKMNCADLSKAMLYLANRGKTLDGTELISQVQTRQLNALLATSGLYDGAGEFAYRVGMPGKSGVGGGIIAVIPGELSVCVWSPELDTQGNSLAGTAMLEQLSQRLGRSIF Shewanella oneidensis MR-1 MR1 202606 SO3505 nagA N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (NAG6PDEACET-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-acetylglucosamine-6-phosphate deacetylase (NCBI ptt file) MKFTLIAEQLFDGESFHQDVPVTIEDGLIASFDTALGAKEVRYTGTLVPGFIDVQVNGGGGALFNTSPTVACIETIGKAHARFGTTGFLPTLITDNVQVMAKAADAVALAVAQKSAGVLGVHFEGPHLSVPKKGVHPQGFIREITEAELAIFCRQDLGIRVVTLAPENVSPEVIRLLVESGVKVCLGHSNADYDTVVAALKAGATGFTHLYNAMSPLGSREPGVVGAAIESETAWCGLIVDGHHVHPAAARIALRAKPRGKMMLVTDAMPPVGMDDETSFELFGTQVLRVGDRLNAVTGELAGCVLDMASAVHNTVNMLGLPLGEALRMAALYPAEFLGIADSVGRLAVGQRADLVLLDNQYQVLANYIAGNAVYVRP Shewanella oneidensis MR-1 MR1 202607 SO3506 Glucosamine-6-phosphate deaminase [isomerizing], alternative (EC 3.5.99.6) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (GLUCOSAMINE-6-P-DEAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. SIS domain protein (NCBI ptt file) MTNTIMEQEARTAPQKIAGQLAANADLMQQLGEKLRAFDPRFVMIVGRGSSDHAGVFAKYLFEIEVGVPTFAAAPSVASVYGKTLKLEGGLVIVISQSGRSPDILAQARMAKNAGAFCVALVNDETAPIKDIVDVVVPLRAGEEKAVAATKSYLATLSAILQLASAWTQSESLAAAVSSLPQALQTAVVAEPQLTPESVENVKNLVVLGRGLGYAVSKEIALKLKEVCSIHAEAFSSAEFLHGPVTLVEKKLTIVDVCIGDESYASHIEQIENVSQRGADLVHLNQTSTDIHPRVAPLALLQRFYIDVAAVAIARGIDPDQPAGLKKVTQTL Shewanella oneidensis MR-1 MR1 203216 SO4133 udp Uridine phosphorylase (EC 2.4.2.3) Specifically important for utilizing Cytidine. Automated validation from mutant phenotype: the predicted function (URPHOS-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. uridine phosphorylase (NCBI ptt file) MADVFHLGLTKAMLDGATLAIVPGDPERVKRIAELMDNATFLASHREYTSYLAYADGKPVVICSTGIGGPSTSIAVEELAQLGVNTFLRVGTTGAIQPHVNVGDVIVTQASVRLDGASLHFAPMEFPAVANFECTTAMVAACRDAGVEPHIGVTASSDTFYPGQERYDTVTGRVTRRFAGSMKEWQDMGVLNYEMESATLFTMCATQGWRAACVAGVIVNRTQQEIPDEATMKKTEVSAVSIVVAAAKKLLA Shewanella oneidensis MR-1 MR1 203800 SO4731 add Adenosine deaminase (EC 3.5.4.4) Specifically important for utilizing Adenosine. Automated validation from mutant phenotype: the predicted function (ADENODEAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. adenosine deaminase (NCBI ptt file) MINTSIPLVDLHRHLDGNVRVNTIWELGHQHGIALPADSLETLAPFVQIQGKETSLVAFLKKLDWMVAVLADLDAVKRIAYENVADAALSGLDYAELRFSPYYMAMNHKLPIEGVVEAVIDGVKAGLKDYQVNINLIGIMSRSFGQPACTQELEGLLAHKQHLVAMDLAGDELGFPGELFNEHFKRVRDAGLAITAHAGEAAGSQSMWQAIQELGATRIGHGVNAIHDPKLMEYLAKHRIGIESCPTSNLHTSTVSSYAEHPFRTFMDAGVLIGLNTDDPGVSAIDIKHEYRIAKFELGLSDAELAQVQRNGVEMAFLSESERKALYAAKA Marinobacter adhaerens HP15 Marino GFF1550 HP15_1512 Enoyl-CoA hydratase (EC 4.2.1.17) Specifically important for utilizing Tween 20. Automated validation from mutant phenotype: the predicted function (ENOYL-COA-HYDRAT-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. multifunctional fatty acid oxidation complex subunit alpha MIYEGKAITVKEIEGGIAQLNFDLQGESVNKFNRLTIEELRAATDALKAQKNLKGLVVTSSKDSFIVGADITEFTELFAGSEEDLVANNLKANEVFNAVEDLPFPTVTAINGMALGGGFEMCLATDYRVMDKKAKVGLPEVKLGIFPGFGGTVRLSRLVGVDNAVEWISGGTENRADVALKVGAVDAVLDSDKLVDAAVAIINQCNEGKLDHEARREEKKGKIKLNAMESMMAFEISKAFVAGKAGKNYPAPVEAIKVMQKHAGMTRDKAIEVEAKGFAKMAKTNVAACLVGLFLNDQELKKKAKAWEKEANDVNLAAVLGAGIMGGGVAFQSALKGTPIIMKDINQDGIALGLKEAKKLLSKRVEKGKMKPDQMADVLNSITPTLNYGDFKNVDLVVEAVVENPKVKDAVLRETEDAVREDTILTSNTSTISIDLLAKNLKRPENFCGMHFFNPVHMMPLVEVIRGEKTSDRAIATTVAYAKAMGKTPIVVNDCPGFLVNRVLFPYFGGFIGLVRDGADFQHVDKVMEKFGWPMGPAYLLDVVGMDTGKHAGEVMADGFPDRMKHEGTTAIDVMFDNNRYGQKNDKGFYKYELDRKGKQKKVVDEETYKLLEPVVQGKNEFSEEDIIARMMIPLCLETVRCLEDGIVEDPADADMGLIFGIGFPPFRGGALRYIDDMGVDKFVELADKFADLGPLYHPTEKLREMAKTGKKFFG Marinobacter adhaerens HP15 Marino GFF1551 HP15_1513 Acetyl-CoA C-acyltransferase (EC 2.3.1.16) Specifically important for utilizing Tween 20. Automated validation from mutant phenotype: the predicted function (KETOACYLCOATHIOL-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. acetyl-CoA acetyltransferase MGRAKNGCFRNVRAETLSANLIEALFERNPKLDPKEVEDVIWGCVNQTKEQGFNVARQISLLTRIPHESAAQTVNRLCGSAMSAIHTAAQAIMTGNGDVFFVGGVEHMGHVPMTEGFDHNPAASKYSAKASNMMGLTAEMLAKMHGITREQQDEFGARSHRLAHEATLEGRFKNEIVPIEGHDENGFKVLIEEDETIRPETTAESLSQLKPAFDPKNGTVTAGTSSQLTDGAAAMVLMSAERAEALGLKPIAKIRSMAVAGCDPAIMGYGPVPATKKALKRAGLKVEDIDFWELNEAFAGQSLPVLKDLKLLGVMEEKVNLNGGAIALGHPLGCSGARISTTLLNVMQAKGGKLGVSTMCIGLGQGIATVWERL Marinobacter adhaerens HP15 Marino GFF1672 HP15_1631 Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase (EC 2.3.1.168) Specifically important for utilizing L-Isoleucine. Automated validation from mutant phenotype: the predicted function (2.3.1.168) was linked to the condition via a SEED subsystem. This annotation was also checked manually. dihydrolipoamide acetyltransferase MTDKAMVEITAPKAGRVTKLYHQQQAMAKVHAPLFAFIPRDREEPEEARTKPEPAAQLSTATASPVAAASRQRIPASPAVRRLVREHELNLSDIQGSGKDGRVLKADVLAYIEEGPKQAQNQAPADDAQTATTRSARRAPAADQEARVEPIRGIKAAMAKSMVKSATTIPHFIYSEDIDVTDLLKLREQLKPEAEARGSRLTLMPFFMKAMALAVQEFPVLNSQLNDDVTEIHYLPQCNIGMAVDGKAGLTVPNIKGVESLSLLGIADEVARLTEAARSGRVSQEDLKGGTITISNIGALGGTYTAPIINAPEVAIVALGRTQKLPRFDANGQVVERAIMTVSWAGDHRIIDGGTIARFCNRWKGYLESPQTMLLHMG Marinobacter adhaerens HP15 Marino GFF2744 HP15_2688 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) Specifically important for utilizing L-Proline. Automated validation from mutant phenotype: the predicted function (1.2.1.88, 1.5.5.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase MRPQQSQTPELVDSRQAIRDYYLADEHKVIHEMIAGAQLSQAERDAISARAAELVRSVRKNAKSTIMEKFLAEYGLTTKEGVALMCLAEALLRVPDNTTIHELIEDKITSGAWGTHVGKASSGLINTATVALLMTSNLLKDSERNTVGETLRKLLKRFGEPVIRTVAGQAMKEMGRQFVLGRDIDEAQDEAKEYMAKGYTYSYDMLGEAARTDDDAKRYYDSYSNAIDSIAKASKGDVRKNPGISVKLSALLARYEYGNKERVMNELLPRARELVKKAAAANMGFNIDAEEQDRLDLSLDVIEELVADPELAGWDGFGVVVQAYGKRSSFVLDWLYGLAEKYDRKFMVRLVKGAYWDAEIKRAQVMGLNGFPVFTRKACSDVSFLSCATKLLNMTNRIYPQFATHNAHSVSAILEMAKTKGVDNYEFQRLHGMGESLHNEVLKVSGVPCRIYAPVGPHKDLLAYLVRRLLENGANSSFVNQIVDKRITPEEIAKDPIVSVEEMGNNISSKAIVHPFKLFGDQRRNSKGWDITDPVTVNEIEKGRGAYKDYRWKGGPLIAGEVAGTEIQVVRNPADPDDLVGHVTQASDADVDTAITSAAAAFESWSAKSAEERAACVRKVGDLYEENYAELFALTTREAGKSLLDAVAEIREAVDFSQYYANEAIRYKDSGDARGVMCCISPWNFPLAIFTGQILANLAAGNTVVAKPAEQTSLLAIRAVELMHQAGIPKDAIQLVPGTGATVGAALTSDSRVSGVCFTGSTATAQRINKVMTENMAPDAPLVAETGGLNAMIVDSTALPEQVVRDVLASSFQSAGQRCSALRMLYVQRDIADGLLEMLYGAMEELGIGDPWLLSTDVGPVIDENARKKIVDHCEKFERNGKLLKKMKVPEKGLFVSPAVLSVSGIEELEEEIFGPVLHVATFEAKNIDKVVDDINAKGYGLTFGIHSRVDRRVERITSRIKVGNTYVNRNQIGAIVGSQPFGGEGLSGTGPKAGGPQYVRRFLKGETVEREADSNARKVDAKQLQKLIGQLDKLKASRPEARMDAIRPIFGNVPEPLDAHVEALPGPTGETNRLSNHARGVVLCLGPDKETALEQAGTALSQGNKVVVIAPGTQDVVDQANKAGLPIVGAQGLLEPEALATIDGFEAVVSCGDQPLLKAYREALAKRDGALLPLITEHTLDQRFVIERHLCVDTTAAGGNASLIAASE Marinobacter adhaerens HP15 Marino GFF3097 HP15_3040 Arginine N-succinyltransferase (EC 2.3.1.109) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (2.3.1.109) was linked to the condition via a SEED subsystem. This annotation was also checked manually. arginine N-succinyltransferase subunit beta MLVIRPLQENDLDDLYAMAQSAGKGLTTLPADRELLQKKINHARETFNQRIAPEAGLYLFALEDTERKKTVGISGIQARVGLDEVFYNYRLSVTVNASKELGVHVRTPTLHLSNDMTDTSEICSLLLSDEYKGGGSGLLLSRCRFMYLDEFRKHFSEKIFAEMRGVSDANGRSPLWDALGTKFFDMEFSEADMLSGLGNKSFIAELMPKYPIYLSMLPDSARAVIGRVHDNTAPALRMLQSEGFNFNGLVDIFDGGPVVEAFVHNVRTVREGMNRHAMVTRKPVNLDVPSEERVMVSNRSFRDFRVTTVPIDCIGPDTVSLPPEVAEALQIESGDPVRLAPLKDSGLLTKHSYRSSVPGGASKWQS Marinobacter adhaerens HP15 Marino GFF3098 HP15_3041 Arginine N-succinyltransferase (EC 2.3.1.109) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (2.3.1.109) was linked to the condition via a SEED subsystem. This annotation was also checked manually. arginine N-succinyltransferase, alpha chain MWLVRPAEPDDLDQILAIAGTQCARLSSTLPKQGDALAYKIEQSLASFAGRISAEDDPPRFLFVLEDTETGDIAGTAGIDAHAGNGQPFYSYRRDALIHASHELGVSRRVEVLYPSHSLTDVSLLCSFSIRPELQGTDAFELLSRARILFIADHREWFTQRMAVEIQGVQLEDGSVPFWDSLGRHFFDMDFETADQYSGQLSKTFIAELMPPNPIYVTLLSEAAQKAMGQPHQITVPNFELLQREGFQPGNYLDIFDAGPVLEARTDSLKTLVTSHPKELHGTNEDTGETCLIAAGEGEQFRCTLTPVAESLDDKLKVPVSTWNTLNRTAGDRVRIAPL Marinobacter adhaerens HP15 Marino GFF3202 HP15_3144 Aldehyde dehydrogenase (EC 1.2.1.3) Specifically important for utilizing Ethanol. Automated validation from mutant phenotype: the predicted function (RXN66-3) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. NAD-dependent aldehyde dehydrogenase MGIGVYIEWVNAKGRVALRQTQQEVEIMIYAQPGKDGSVVSFKSRYENYIGGEWVAPVKGQYFENITPVTGNVICEIPRSSAEDIDLALDAAHKAAPAWGKTSPTERSNILLKIADRIEANLEKLAVAETWDNGKAVRETLNADIPLAADHFRYFAGCLRAQEGHMGEIDHNTVAYHFHEPLGVVGQIIPWNFPILMAAWKLGPCLAAGNCTVLKPAEQTPASILVLMEIIGDLLPPGVLNIVNGYGIEAGQALATSKRIAKIAFTGSTPVGSHILKCAAENIIPSTVELGGKSPNIYFSDVMKAEPEFIDKCVEGLVLAFFNQGEVCTCPSRALVQEDMFEEFMQKVVQRTKSIKRGNPLDTDVQVGAQASKEQFDKIMSYLAIGKEEGAVVLTGGDREHLDEEFNNGFYIQPTLFKGDNKMRVFQEEIFGPVVGVTTFKTEEEALAIANDTEFGLGAGVWTRDTNLAYRMGRNIQAGRVWMNCYHAYPAHAAFGGYKKSGVGRETHKMALEHYQQTKCMLTSYDTNPLGFF Marinobacter adhaerens HP15 Marino GFF3491 HP15_3433 Aconitate hydratase (EC 4.2.1.3) Specifically important for utilizing Potassium acetate. Automated validation from mutant phenotype: the predicted function (4.2.1.3) was linked to the condition via a SEED subsystem. This annotation was also checked manually. aconitate hydratase 1 MSNESLSKDSLNTLSSLDAGGKTFHYYSLPKAADTLGDLNRLPFSLKVLMENLLRNEDGTTVDRSHIDAMVQWMKDRHSDTEIQFRPARVLMQDFTGVPGVVDLAAMREAVQAAGKDPAMINPLSPVDLVIDHSVMVDKFGDASSFKDNVAIEMERNQERYEFLRWGQQAFDNFRVVPPGTGICHQVNLEYLGKTVWQKDQDGKTIAYPDTLVGTDSHTTMINGLGILGWGVGGIEAEAAMLGQPVSMLIPEVVGFKITGKLREGITATDLVLTVTEMLRKKGVVGKFVEFYGDGLKDMPVADRATIANMAPEYGATCGFFPVDEQTIKYMRLTGREEEQLELVEAYAKAQGLWREPGHEPVYTDNLELDMGEVEASLAGPKRPQDRVALKNMKSSFELLMETAEGPAENREANLESEGGQTAVGVDDSYKHHASQPLEMNGEKSRLDPGAVVIAAITSCTNTSNPSVMMAAGLIAQKAVQKGLSTKPWVKTSLAPGSKVVTDYLKVGGFQDDLDKLGFNLVGYGCTTCIGNSGPLPDAVEKAISDGDLTVASVLSGNRNFEGRVHPLVKTNWLASPPLVVAYALAGNVRLDLSQDPLGNDKDGNPVYLKDLWPSQQEIAEAVEKVKTDMFRKEYAEVFDGDATWKSIKVPESKVYEWSDKSTYIQHPPFFEGLKEEPDAIDDIKDANILALLGDSVTTDHISPAGSFKPDTPAGKYLQEHGVEPKDFNSYGSRRGNHEVMMRGTFANVRIRNEMLDGVEGGYTKFVPTGEQMAIYDAAMKYQEKGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVVAESYERIHRSNLIGMGVMPLQFPEGTDRKSLKLTGEETISIEGLSGEIKPGQTLKMTVKYKDGSTETCELKSRIDTANEAVYFKHGGILHYVVREMLRTA Desulfovibrio vulgaris Miyazaki F Miya 8499231 DvMF_0011 L-serine ammonia-lyase (EC 4.3.1.17) Specifically important for utilizing L-Serine. Automated validation from mutant phenotype: the predicted function (4.3.1.17) was linked to the condition via a SEED subsystem. This annotation was also checked manually. serine dehydratase alpha chain (RefSeq) MQPLVATIETSLFDMFEAGPGPSSSHTIGPMKAGHDFRTLCAALPPEVLACAADIRVRLFGSLSATGVGHGTTGAVLAGLLGHRPATCPPGLLESLPALPEGERTLRLGPAALVLAEGTVRRDAVQHAYPFSNTLVMELLDAHGAVLCEREYYSVGGGFIQWKGWQPEERGRPAHPYRSMAQLRARLVETGLTIHELILENEMAVTGMGRAAILDRLAAIIELMEASVRRGIEDGGPLPGTLGVHRKARVLLMRAQRLPNEVDVFLGRLNAYAFAAAEENAAGGVIVTAPTCGAAGVMPALLYAMRHDLAIGDRAVREGVLASAAVGFLAKHNAGIAGAEVGCQGEVGVASAMAAAMLAHARGNPVHVVENAAEIALEHHLGLTCDPVGGYVQIPCIERNAVGAVKAYNACLLATCEDPRHHRVTLDSVIAAMAEIGRDMNAKFKETSSGGLAVSVVEC Dechlorosoma suillum PS PS Dsui_0516 Dsui_0516 Propionyl-CoA carboxylase biotin-containing subunit (EC 6.4.1.3) Specifically important for utilizing Sodium propionate. Automated validation from mutant phenotype: the predicted function (PROPIONYL-COA-CARBOXY-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. acetyl-CoA carboxylase, biotin carboxylase subunit MFKKILIANRGEIACRVIKTARKMGIKTVAVYSEADKDALFVEMADEAVCIGPAASKESYLVADKIIAACKQTGAEAVHPGYGFLSENAEFSRRLEEEGIKFIGPKHYSIAKMGDKIESKKLAIEAKVNTIPGYNDAIDGPDAAVEIAKKIGYPVMIKASAGGGGKGLRVAYNDAEAHEGFSSCVNEARNSFGDDRVFIEKYVLEPRHIEIQVLGDSHGNYVYLNERDCSIQRRHQKVIEEAPSPFVDPEMRKAMGEQAVALARAVNYESAGTVEFVVSGATKEFYFLEMNTRLQVEHPVTELITGLDLVEQMIRVAYGEKLPLTQADVQINGWAMECRINAEDPFRGFLPSTGRLVKFQPPAEVDGQVRVDTGVYDGGEISMYYDSMIAKLIVHGASREQAIARMRDALNGFVIRGISSNIPFQAALMQHARFQSGIFDTGFIAKEYPKGFDASMVPHDDPALLIGVAAFVHRRYIDRAAQVSGQLPGHERKVGDEWVVIRNGERHPVVAKPIEGGYLVTYNGEKYELLSDWRQGQSLFNGTCNGEEFTLQVERHRMTYQLFHWGTRADMMVMSARAAELLALMPEKAAPDLSKFLLSPMPGLLREVSVAVGQEVKAGEKLAVIEAMKMENILKAEQDCKVKKISVTAGSSLSVDEIIIEFE Dechlorosoma suillum PS PS Dsui_0517 Dsui_0517 Propionyl-CoA carboxylase carboxyl transferase subunit (EC 6.4.1.3) Specifically important for utilizing Sodium propionate. Automated validation from mutant phenotype: the predicted function (PROPIONYL-COA-CARBOXY-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. acetyl-CoA carboxylase, carboxyltransferase component (subunits alpha and beta) MHDIIHELEKKREAARLGGGQKRIDSQHKKGKLTARERLELLLDPDSFEEWDMFKEHRCTDFGMAETKNPGDGVVTGYGTINGRLVFVFSQDFTVFGGSLSETHAEKICKVMDHAMKVGAPVIGLNDSGGARIQEGVASLGGYADVFQRNVMASGVIPQISMIMGPCAGGAVYSPAMTDFIFMVKDSSYMFVTGPEVVKTVTHEEVTAEELGGAVTHTTKSGVADLAFENDVEALNYLRRLVNFLPANNREKPPVQKTNDPAERLDFSLDTLVPDNANKPYDMKELIIKMVDDCDFFEIQPDYAKNIITGFARMDGHPVGIVANQPLVLAGCLDIKSSIKAARFVRFCDAFNIPVVTLVDVPGFMPGTSQEYGGIIKHGAKLLYAYAECTVPKVTLITRKAYGGAYDVMSSKHLRGDVNLAWPSAEIAVMGPKGAVEIIFREEKNDPAKLAEREAEYKAKFANPFVAGARGFIDDVIMPNETRKRICRSLAMLRDKKLDNPWRKHGNIPL Dechlorosoma suillum PS PS Dsui_0519 Dsui_0519 Methylmalonyl-CoA mutase (EC 5.4.99.2) Specifically important for utilizing Sodium propionate. Automated validation from mutant phenotype: the predicted function (METHYLMALONYL-COA-MUT-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. methylmalonyl-CoA mutase MSADASKPQLPNSDNLDAWAKAAAKSAPGGDVNALNWITPEGLTVKPLYTKKDVEDLPYADTLPGFAPYLRGPQATMYAVRPWTIRQYAGFSTAEESNAFYRKALAAGGQGVSVAFDLATHRGYDSDNPRVLGDVGKAGVAIDSVEDMKILFDGIPLDKISVSMTMNGAVLPILAGYIVAAEEQGVSQEQLSGTIQNDILKEFMVRNTYIYPPKPSMKIISDIFGYTAQHMPKFNSISISGYHIQEAGANQAIELAFTLADGMEYVRTGIASGLDVDAFAGRLSFFWAVGMNFYLEIAKMRAGRMLWHRIMSQFNPKSAKSLMLRTHSQTSGWSLTEQDPYNNVVRTTIEAMAAVFGGTQSLHTNALDEAIALPTEFSARIARNTQLIIQEETHICNVVDPWAGSYMMEKLTQDMADKAWSIIQEIEAMGGMTKAVESGWAKMQVETCAADKQARIDSGKDVIVGVNKYKLAKEDQIDILDIDNHAVREAQIARLKKIRASRDSAAVQAALDALTQCAESGEGNLLDLSVKAIRLRATVGEVSDALEKVFGRFRANNQTISGVYGGVVEGQESWESIKADIAKFAEEEGRRPRIMIAKLGQDGHDRGAKVVATAFADLGFDIDMGPLFQTPEEAARQAVENDVHAIGVSSLAAGHKTLLPALVNSLKEQGADDIIVFAGGVIPAQDYDTLYAAGAKAIFGPGTRIEDSAKRVLEEIRKSRG Shewanella loihica PV-4 PV4 5208303 Shew_0815 Glucosamine-6-phosphate deaminase (EC 3.5.99.6) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (GLUCOSAMINE-6-P-DEAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glucosamine-6-phosphate isomerase (RefSeq) MQIVILKDSAEVAEYGANLIINQLKRKPDSVLGLATGSTPVSLYQRLVAANQAGAVSFEGVTSFNLDEYLGLEGSHPQSYRYFMDSQLFDAIDINKANTHVPPGDAEDPIAACEAYEAQIQAAGGIDIQLLGIGRNGHIGFNEPSSGLMSRTRVKTLTQATIEDNARFFAEGEYQPHLSITMGIGTILDAKKVLLLATGESKADAIRAAVEGALSAACPASALQLHRDAVLVIDEAAASKLADKEFYRHIEAENQLLQARLAALKAGE Shewanella loihica PV-4 PV4 5208606 Shew_1117 N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (NAG6PDEACET-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-acetylglucosamine-6-phosphate deacetylase (RefSeq) MKQTLIAERVFDGEHFHHNQAITIEDGRIVSFDRASDVEPILLAGTLVPGFIDVQVNGGGGALFNDAPSVEKIKTIGQAHARFGTTGFLPTLITDEIEVMRAAADAVAEALALNTPGVLGIHFEGPHLSVPKKGVHPANYIRRISDEELAVFARNDLGTKVVTLAPENVAPEVIHALVECGVRVCLGHSNADYDTVIKALEAGATGFTHLFNAMSPMDSRAPGMVGAALESQDAWCGLIVDGHHVHPASAKVAIAAKPRGKVMLVTDAMPPVGMDDNASFELFGTQVVRRGDRLNAVTGELAGCVLDMIGAVNNSVSMLGVAHEEALRMAARYPAEFIGHRQRGVFTIGARADMVLLGSDNQVARTYIDGQLVYQA Shewanella loihica PV-4 PV4 5208774 Shew_1276 Isocitrate lyase (EC 4.1.3.1) Specifically important for utilizing Potassium acetate. Automated validation from mutant phenotype: the predicted function (4.1.3.1) was linked to the condition via a SEED subsystem. This annotation was also checked manually. isocitrate lyase (RefSeq) MLTPEMEKIMTKATTQISRQQQIDAIKQDWAENPRWAGVRRPYSAEDVVALRGSIVPENTLATRGAEKLWQLVNGGAKKGYVNSLGALTGGQAVQQAKAGIEAIYLSGWQVAADANLAGTMYPDQSLYPANSVPAVVQRINNSFRRADQIQWSNEIDPQDERYTDYFLPIVADAEAGFGGVLNAYELMKNMIDAGAAGVHFEDQLASVKKCGHMGGKVLVPTQEAVQKLVSARLAADVSGVPTLVIARTDANAADLLTSDCDPYDRDFITGERTSEGFYRVNAGIDQAISRGLAYAPYADLIWCETAKPDLEEARRFAEAIHAQYPDQLLAYNCSPSFNWKKNLDDATIARFQQELSDMGYKYQFITLAGIHNMWYNMFDLAYDYARGEGMKHYVEKVQEVEFAAAKKGYTFVAHQQEVGTGYFDKVTNVIQGGESSVTALTGSTEEEQF Shewanella loihica PV-4 PV4 5210846 Shew_3272 Aldose 1-epimerase (EC 5.1.3.3) Specifically important for utilizing D-Maltose monohydrate. Automated validation from mutant phenotype: the predicted function (5.1.3.3) was linked to the condition via a SEED subsystem. This annotation was also checked manually. aldose 1-epimerase (RefSeq) MVRFRPLDAWNDPRGGQIERIIIDNGTLAIEVLSLGGIIRSLWAPDNKGERGNIVLGCDSAQDYLTQDAHLGAIAGRYANRIAGARLSRDGQAFSLDNNHQDNCLHGGREGFNRKQWHIGQLSDGVRLSLFSPDGDMGFPGNANVQLDYRLVGNNLYVEILASTDKPCPISLTQHSYFNLEGSSERSSLGHIIQSDSQHYLTTDEQGIPTDVTQVAGTPLDLSQGQSLASLKTALEAEPTRGIDHCYLTPNHDGKALSRFGTVSAPASGRRMTLYTNQPGVQIYGSNFLEGTLGKQGQKLASYQAVCVEPQQLPDAPNQAHLAGTPWLMPGEVYHHMSRYQFDLIK Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS08615 CA265_RS08615 L-arabinose isomerase (EC 5.3.1.4) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (ARABISOM-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-arabinose isomerase MIDLKKLQVWFITGTQHLYGEETLKQVAAHAQEVADSLNQNGSISVSVVYKPIVKTTEEIFETLQQANIDENCIGVITWMHTFSPAKMWIRGLNVLQKPLLHLHTQFNRDIPWNTIDMDFMNLNQSAHGDREFGFMVSRMRKDRKVVVGHWQDEEVAKQIDTWCRAAAGWHDWQGAKFARFGDNMRYVAVTDGDKVEAEMKFGFAVNTYGIGDLVAVINGIGEDAIQSLLEEYEATYEMADDLKAGGARHSSVYEAAKIELGLRKFLVDGGFKGFSDTFEDLHGMIQLPGIAAQRLMADGYGFAGEGDWKTAALVRACKVMGAGLAGGNAFMEDYTYHFDPANSMVLGSHMLEVDASLASGKASLEVHPLGIGGKADPARLVFNVAGGDALNAALIDMGNRFRLLVNEVKAVEAEHDLPNLPVARVLWKPLPDMKTGCAAWIYAGGAHHTAYSQNLTTEHLLDFANIAGLEYVNIGADTKINQFRNELHWNEVFYK Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS08620 CA265_RS08620 L-ribulose-5-phosphate 4-epimerase (EC 5.1.3.4) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (RIBULPEPIM-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-ribulose-5-phosphate 4-epimerase MSNYQDIKEQAYQANMQLPKLGLVLFTFGNVSAADRSKGVFAIKPSGVPYEDLSPEKMVIVDFNGNTVEGTLRPSSDTKTHAVLYQHWAEIGGIVHTHSTYGTAWAQAQRAIPIFGTTHADHLTVDIPCAPPMADEMIKGNYEYETGFQIMNHFESLGLSYQEVEMILVGNHAPFTWGKTAEKAVYNSAVLETVAQMALLTEQINPQAPKLKDSLIEKHYERKHGDGAYYGQK Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS08625 CA265_RS08625 Ribulokinase (EC 2.7.1.16) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (RXN0-5116) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. ribulokinase MSTANYVIGVDYGTDSVRSVLVDTANGKEIASSVFLYPRWQKGLYCKPAVNQFRQHPLDYIEGLTHTIKDCLAKAGGAEIAHLVKGISVDTTGSSPVAVDATGTPLALTKDFEENPNAMFVLWKDHTSVKEAAEINEHATKFDTNYLKYVGGIYSSEWFWSKLLHILRVDLTIKKGAASWVEHCDWIPFLLCGGNDISTMKRSRCAAGHKALWAEEFNGLPPEDFFSSLDPLLAGFRAKLFTDTYTSDVSAGTLSEEWANKLGLNTDVVVGVGAFDAHMGAVGGQIEPYYLSKVMGTSTCDILVAPNQDLHGKLINGICGQVNGSVIPGMAGLEAGQSAFGDVYAWFKNLISWPLNHLLTESEVIDEATATALKAELEGKIIANLSKQADALPNEDYAELAIDWLNGRRTPDANQELKGAITGLGLGTDAPRFFRALAAATCFGAKAIVDRFKEQGVPVKGIIGIGGVAKKSAYIMQMMADVLEMPIRIHRFEHTCALGAAMFAAVAAGIYPDIETAMAAMGTGFEKEYKPNIKKQKLYRQHYQQYLGLGRYLEKYNKKDVKPYLS Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS09125 CA265_RS09125 Methylglutaconyl-CoA hydratase (EC 4.2.1.18) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (4.2.1.18) was linked to the condition via a SEED subsystem. This annotation was also checked manually. methylglutaconyl-CoA hydratase MENLVLYQVAERIATITINRPEKKNALNPQLIAELTAAFIKASEDDLVKVVILNANGDAFSAGADLAYLQQLQYNTFEENVADSNHLKKLFTTIYYLPKVVIAQVEGHAIAGGCGLATICDIVFATPESNFGYTEVKIGFVPAIVSCFLKEKVSESIAKEILLTGKIFSAEEALKYNLINFVTNSSDIHQIVREFALSLCSGSSGNSLMITKQLITQTTNPLLEKCLETAVQINARVRESEDFKKGISSFLNKEKINW Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS09995 CA265_RS09995 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrite reductase (NAD(P)H) MKEPQIIVIGNGMVGYKFCEKLRSKTSSFNLIVFGEEPRRAYDRVHLSEYFNGKTADDLSLSTENWYQEQNITLFLNNPITKIDRELQKVYTANGLDYSYDILVFATGSGAFVPNIPGIEKEGVFVYRTIEDLDLISNYAKKAKTASVIGGGLLGLEAAKALIDLGIEKTSIIEFAPRLMPRQIDAAGSDMLKSKLADLGLQIHLSKNTTSIEGDGRITALKFSDDTALDVDMLVISAGIKPRDELAKACGIEVGPRGGIVVDEKMQTSDPAVFAIGECALYDGMIYGLIAPGYEMAEVLAANLCEGDKTFTGFDMSTKLKLIGIDVASFGDNFITEPDCRTIIFENKHKGVYKRINVSNDGQYLLGGILIGDATAYNLLLQTSNNRIVLPENPEELILGARGGSEAAGGAGITGLPDSALICSCEGVSKGDICTAVADGTCENIDDLKKCTKAGTGCGGCLPMVKDLMTYTLKSQGKYIKNVICEHFNYSRQELFDLIHIHELKSYDEVLDALGKNDGCEVCKPLVSSLLASLWNEMILKKGNDVAQDSNDRFLANIQKGGSYSVVPRVPGGEITPDKLIVIGEVAKKYNLYTKITGGQRIDLFGAHLNDLPIIWEELIAAGFESGHAYGKGLRTVKSCVGSTWCRFGLHDSVSFAIRIEERYRGIRAPHKFKSAVSGCIRECAEAQSKDFGIIATEKGWNLYVCGNGGSKPQHALLLATDLDSETCIQYIDRFLMFYIRTADPLTRTATWLNKMEGGIDYLRNVIINDSLGMAAQWESEIENLIATYKCEWKEAVENPAIRKRFSHFVNAPEEKDPTIEFVEMRGQKRTAEWKTF Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS10015 CA265_RS10015 Nitrate reductase (EC 1.7.99.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.99.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. NAD(P)H-nitrite reductase MSPNKTTTCCYCGVGCGIVINKDIHERITVEGDKNHPVNKGMLCSKGMNLHYTANDKSDRLLYPEMRYNKNMPLQRVSWDTALERTAAVFKALIKKHGPDSVAFYASGQCLTEEYYVVNKLIKGFIGSNNIDTNSRLCMSSAVVGYKMSLGEDTVPISYDDIEIADCIFVAGANPAWCHPILWRRVEAAKEKNPDLKIIVSDPRKTQTCSLANVHLQLNPGTDITLHHAIGRCLIEDGKIDADFIINSTNGYEKYHTTVFETSVAEAAAICGIKESDIRLAASYIGNAKGFISMWTMGLNQSVVGTHKNLSLINLNLITGHIGKPGSGPFSLTGQPNAMGGREVGGLSNLLPAHRVLANESHRNEVEKFWQIPLGTIQAKPGLTATEMFDELNTGKLKAVWILCTNPLISLPDVRVAEEGLKKAKFVVVQDISNKVETLKYADVVLPAAAWVEKEGTMTNAGRYISYLSKVTEAPGEALADSEIICRFAKKMGYHGFDFQNASEIYDEHAALTEGTNIDISGLNYQILKEKRAVQWPYPKEEKAFGTARLFTDHQFYTPDKKANILSFDDQNQSEALTPEHPLILTTGRIRDQWHTRSKTGKVNKLNQHISESFLEINPIDAEIRNIKDSDIIEISSLRGNVRVKAKFSEDIKPGVVFMPMHWGKILKSDLNRVNNLTNNLVDPQSKEPDFKFSAVEVKLYKKARQKIIVIGAGAGACGFVKSYRALNTEDDIEIFSKENFPFYNRVLLPDYIIGTLPWHNLIKMSDSEETDYRIKLHRGLGIDKINKEDKTVTDSNGEIHPYDVLLLATGSRAFVLKDIPKLNGIFTMRSRNDADSFKKHVDTTNGKVVIVGGGLLGIELATSLAETGSKVTIIQRISRLMGRQLDALGSQLLHEELISKGIEIFYNDEVDRIIGEKSITGMRLKSGLLIDCESLVIAIGTVPNTELIKEAGIECKRGVVVDEYLRTNEKDIYAIGEIAEFKGQMYGITAAAEQQAEIVARFLCGDIAKFYQGSLLMNILKMHSLELCSLGLAEIPNNDPTYEEIVFIDKAKRYYKKCIVHNDKLVGAILIGDKSEFLEFRNLIENKMELSEKRLQLLRSGKTTEPIIGKTVCSCNNVGEGNLINKIKDGCKDHLQLCQLTGAGMGCGSCRPEVKAILDSFVNVLKTEPKPVLADT Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS11300 CA265_RS11300 N-acetylglucosamine kinase (EC 2.7.1.59) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (2.7.1.59) was linked to the condition via a SEED subsystem. This annotation was also checked manually. sugar kinase MEQSYAIGIDVGGSSLKCGVVNQNGEILYSIIVSLKNAKTQGAIIALIVEAIHTCAKKFKNPILGVGIGFPGIIYNNKIIAGADNLPGFKQLALGEILQEVTRYNIVMDNDANLMGLGEMTYGAAKDCSDVVFLTVGTGIGGAVMIDNKLYGGFRNRGTELGHIVVQHNGLACACGGRGCLEAYASVTALLNHYQSIHPNPPEEIDGKYMVEKYLAREEYAVEAMESHFDYLATGIISFVNVFSPQKIVIGGGISESGAFYVREIERRIKTLAVPIAPGNELVVAARLGNKAGLLGCAANVFQKFKAFDYVVK Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS11605 CA265_RS11605 Proline dehydrogenase (EC 1.5.5.2) Specifically important for utilizing L-Proline. Automated validation from mutant phenotype: the predicted function (1.5.5.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. proline dehydrogenase MDLSPNKQPNFDNTEVAFRQKTNGELKKAYWLFKMIGSNFLTKVGPAITNFFLNIGLPIQGAIKATIFQQFCGGETIAECDKAIEQLHKGGVGTILDYSVEGEEEEQVFDETCAEIIRTIMRADGDVKIPITVFKITGIGRFALLQKLDAKETLNASEKAEYEKVKQRCEKICQTAFDKGVPIMIDAEETWIQDTIDELALDMMRKFNRERIIVYNTYQMYRHDKLADMKADHLIAKADGFILGVKMVRGAYMEKERKRAAEMGYPSPIQPDKAASDRDYNESLRYCVDHIEEIAIVAGTHNEDSSRLLTYLLEEKNITHNHPHVYFAQLLGMSDNLSFNLADSNYNVAKYVPYGPIKAVMPYLFRRAQENTSVAGQTGRELGLIERELKRRKL Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS13115 CA265_RS13115 Hydroxymethylglutaryl-CoA lyase (EC 4.1.3.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (HYDROXYMETHYLGLUTARYL-COA-LYASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. hydroxymethylglutaryl-CoA lyase MSQNNFKLVECPRDAMQGLHDFVPTKLKAEYLNLLLQVGFDTLDFGSFVSPKAIPQMADTAEVLAQLDLSNTSTKLLAIVANLRGVEDAVKHQAVNYLGFPFSISETFQQRNTNSSIAQSLNTVEEMLSLCAKNNKKAVVYLSMGFGNPYGDKWNYEIVEKWADVLVSRGVEILSLADTVGISTPEKIENILPKLISRFSNTEIGIHLHSTPAERFEKIEAAYHSGVKRIDSALKGFGGCPMAADDLTGNIATEDVITFLNMKGEKLNLNMDKWNEAMVLSGKIFG Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS14455 CA265_RS14455 L-lysine 6-transaminase (EC 2.6.1.36) Specifically important for utilizing L-Lysine. Automated validation from mutant phenotype: the predicted function (L-LYSINE-AMINOTRANSFERASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-lysine 6-transaminase MYQLTVPADRVNESLSKHILADGFDLTYDMEKSHGAYIYDAKHNRTLLDFFTCFASVPLGYNHPKMINDEAFKKNLFLAALANPSNSDVYTQQYAQFVETFSKVGIPDYLPHAFFIAGGGLAVENAIKVAMDWKVQKNFAKGYTEEKGFKVLHFERAFHGRTGYTLSLTNTLPDKTKWFAKFDWPRVAVPEVKFPLSGNNLSHAIQTEETSLAQIKKAIADNKDDICAIIVEPIQSEGGDNHLREEFLIQIKALADENDAFLIYDEVQTGVGLTGKFWCHQHFSEKARPDILAFGKKMQVCGILVGHKVDQVETNVFKVPSRINSTWGGNLVDMVRSTQILQIVEEDQLCENATKVGLYLKDQLENLSHRFDQMTNVRGRGLLCSFDFPTKEMRNTFIAKGLENNVMFLGCGEKTIRFRPALCIEQKHIDEGLTVMDKILPLL Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS16075 CA265_RS16075 Cytidine deaminase (EC 3.5.4.5) Specifically important for utilizing Cytidine. Automated validation from mutant phenotype: the predicted function (CYTIDEAM2-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. cytidine deaminase MNSINLNISFEQYESIAELTLADRTLCALAEQALNTSYSPYSKFRVGTAIRLASGETVLGSNQENLAYPSGLCAERVALFTIGATYPNAVIESMAITAQTDNFEILKPVTSCGGCLQVMAEFERKQNAPIEVIFYCLNGEILKVPSVKSLLPFAFVEDRLER Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS19860 CA265_RS19860 2-dehydro-3-deoxy-phosphogluconate aldolase (EC 4.1.2.14) Specifically important for utilizing D-Galacturonic Acid monohydrate. Automated validation from mutant phenotype: the predicted function (KDPGALDOL-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase MSNKHKILDAILEQGMLPLFYQDSESGSVEILRTLYKAGVRVFEYTNRGKSALPNFKKLKEIRDAEMPDLYLGIGTIKTPADANAFIEAGTDFIVAPIVNPAVAEIANKIGMLWIPGCMTPTEISVAQEHKAMLIKIFPANILGPEFISSIKDLFAGQLFMPTGGVEINADNLKTWFKSGVCAVGMGSKLISKDVMSKGLYEELFDNTKLALDLIQQSK Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS19865 CA265_RS19865 2-dehydro-3-deoxygluconate kinase (EC 2.7.1.45) Specifically important for utilizing D-Galacturonic Acid monohydrate. Automated validation from mutant phenotype: the predicted function (DEOXYGLUCONOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. carbohydrate kinase MSTQIFASSKKGEKVLSFGEILLRICPDMDGQWLKENKLPFYVGGAELNVATALALWNVPSTYLSAVPDNSVTREIVDYLDARNIDTTPMVYHGERLGLYYLPKGKDLKNAGVIYDRANSAYADLKVGQINWDEVFEGVSWFHFSAICPAINQSIADVCLEALKVASAKNITISLDLNYRAKLWKYGKDPIDVLPQLAQYCTLIMGNVWAANKMLGTALHEDLIPTEGYAKETLLQQATDTSKEILSLFPACKAVANTFRFDHGKGIRYYTAIYTADELTVSEEYVSEEILDKVGSGDCFMAGLIYGFYNQLSAKETLNFATAAAYDKLYIPSDATTSTVADIEKRIIRND Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS19870 CA265_RS19870 Glucuronate isomerase (EC 5.3.1.12) Specifically important for utilizing D-Galacturonic Acid monohydrate. Automated validation from mutant phenotype: the predicted function (5.3.1.12) was linked to the condition via a SEED subsystem. This annotation was also checked manually. glucuronate isomerase MKPFLDENFLLQSKTAEKLYHNFAKSLPIIDYHNHLIPEQIANNTQFANISQVWLAGDHYKWRAMRANGVDEKYITGVGSDYEKFEKWAETVPYTLRNPLYHWTHLELQRYFGITDLLSGKTAQKIFDECSAKLQTPEYSVRGLLAKMNVEAVCTTDDPLDSLNFHQQLAREGANLKMLPAFRPDKAMNSDDIEGLNEYIDKLESVADKTISNFQDYIDALKSRHDYFAANGCSVSDHGLEQIYAEDYTEAEIASIFDKIRSKQHISYEENLKFKSAMLVYFAEWDHEKGWVQQYHLGALRNNNARMLRQLGPDTGWDSIGDFSQARMLSKFLNRLDNQDKLAKTIIYNLNPADNELIATMIGNFNDGSVAGKVQFGSAWWFLDQKDGMIKQLNALSNMGLVSRLVGMLTDSRSFLSFPRHEYFRRIVCNLFGEDIENGELPNDLEWVGKIVQDISYFNAKNYFKF Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS19875 CA265_RS19875 Altronate dehydratase (EC 4.2.1.7) Specifically important for utilizing D-Galacturonic Acid monohydrate. Automated validation from mutant phenotype: the predicted function (ALTRODEHYDRAT-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. altronate hydrolase MVTRILKIHPNDNVLVALQNLAKGETVIYDGHEYILQDDIQAKHKFFMQDMNAGDHIIMYGVLVGKAQHFILKGGLMDTENTKHASDPYEFRPYHYEWHAPDVSKFEGRTFNGYIRSDGRVGTANYWLFIPTVFCENRNLDVIREALHNELGYAVTDKYKSYAHQLVEAYKNGEILAEADPSSIGLANPSANRVFKNVDGIKFLNHQGGCGGTRQDAAVLSKLLAAYADHPNVAGVTVLSLGCQNLQVKDFMDDLKHRSPNFDKPLFVFEQQQSQSEEQLVKEAIRKTFIGLTEINKIERQPAPLSKLVLGVKCGGSDGFSGISANPAVGYTSDLLVALGGTVLLAEFPELCGAEQQLIDRTKDETAARKFIQLMTAYNQSAENVGSGFFMNPSPGNIKDGLITDAIKSTGAAKKGGTSPVEDVLDYTEPATKPGLNLVCTPGNDVEATTGKAASGATLILFTTGLGTPTGNPVCPTIKVSTNNALTKRMGDIIDINCGPVIEGEKTIEQMGEDILEYCIKAASGEVIPKAVLLNQDDFIPWKRGVSL Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS19880 CA265_RS19880 Altronate oxidoreductase (EC 1.1.1.58) Specifically important for utilizing D-Galacturonic Acid monohydrate. Automated validation from mutant phenotype: the predicted function (ALTRO-OXIDOREDUCT-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. altronate oxidoreductase MILNKENLKNINGDKVIKPSAEILALPEKVIQFGTGVLLRGLPDYFIDKANQKGIFNGRVLVVKSTSKGGADAFSKQDNLYTLCVKGIEDGAHVEENSINASISRVLSASQDWAEILKAAHQPEMQVVISNTTEVGIVKSEDKITDNPPQSYPGKLLAFLHERYTAFNGSAESGMVIVPTELISDNADKLKEILLDLAIQNKLGWDFENWLKTANHFCKTLVDRIVPGKLPESAQKAIESELGYEDELMIMAEPFRLWAIESSSEKVKEILSFAKADKGVFIVPSIDKFKELKLRLLNGTHTISCGLAILAGFNTVKEAMANEDFSANVLKLMKDEIAPVVVNEDITYDEAIAFAKSVVDRFSNPSLEHQWQAITLNFTSKMQMRNMPLIRRYYALKNEVPQLTALGVAAYILFMNVNQDGDTYTASANGKTYPVQDEFAEILYEYWKNPETVVDNTLGDRRLWDKNLNNYPGFNAAVKSYVDLLQNKGAKETLSNLHSERTI Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS21455 CA265_RS21455 Formiminoglutamase (EC 3.5.3.8) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (FORMIMINOGLUTAMASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. arginase MDNLKIYSQGDIDHLIITRDGETKLGERVNVYSGDSSSTAGISVEGLKASSAKFVLLGIPEDIGVRANLGLAGAASMWKPGLVAFLNTQSNRFLSGEEVLVLGHFEIDEPEDSSLKGLRNKVAQIDDLVYPVIEKIVATGKIPVVIGGGHNNAYPMIKGTSLAHKRPITVLNVDAHADLRELEGRHSGNGFSYALKENYLNNYLMYGLHQNYNNEAILNQIDTNPKLKAVFFDDILTGADFTNLVNEIGSVAGLEIDLDCVQNVLSSAETPSGFAVNDIRKLILTSAKKFSYLHLSEGATRMLDGRVSKLTSKLVAYLVSDFIKAH Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS21925 CA265_RS21925 Glucosamine-6-phosphate deaminase (EC 3.5.99.6) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (GLUCOSAMINE-6-P-DEAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glucosamine-6-phosphate deaminase MARLNLLEETRFEKLPVSVFENPKIASINVAHRIAELIKSKQANNTPAVLGLATGVTPIAVYAELVRLHKEEGLSFKNVITFNLDEYYPMAPTAAQSYVTFMNENLFNHIDIDKKNVHIPDGTLALEDIPAFCLEYEKKIGDLGGLDIQILGIGRTGHIGFNEPGSAPNSGTRLVTLDDLTRRDAARDFGGKTFVPTKAITMGIGTIFKAREIILMAWSRKKASIIKKAVEGEISGDVPATFLQLSDHVEFILDAPAASELTRFYTPWLVKDCVWTDALIRKAVIWLANTLKKPILKLTEDDYNNNGMAQLATEKGPVYNINIHIFNKLQHTITGWPGGKPNADDSQRPERAEPAKKRVIIFSPHPDDDVISMGGTFLRLVDQGHDVHVAYQTSGNTAVWDDDALRFVEFNVDFTEKMGMDNTHLKDLYNKMRAFIEQKKPNQIDTPEIQTVKGLIRKGEAIAGARYCGLEDDHIHFQALPFYESGKVQKNPVTDADIELTIELLQKVKPQQVYAAGDFEDPHGTHIVCFNIILEALKRLRKTEAWAQDCWLWMYRGAWHEFETHEIEMAVPISPQELERKKYAIFKHQSQKDRAVFPGDDSREFWQRAEDRNRDTAKAYDELGLAEYEAMEAFVRWKFED Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS22270 CA265_RS22270 Histidine ammonia-lyase (EC 4.3.1.3) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (HISTIDINE-AMMONIA-LYASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. histidine ammonia-lyase MSEQQIFNYGTDHLTAKLALAISNGQIKGVLSQSTRDKVLESSQVVERIAVSGKAVYGINTGFGPLCTSMISAIDTRKLQENILKSHAVGVGEPIDSEISKLMLVLKLQALAQGYSGIKIETLDRMIWFLEIGATPVVPKQGSVGASGDLAPLSHLFLPLIGLGKLHYKGEIIATAQLLQEYQMSPLQLGPKEGLALINGTQFIAAHAVKVVQRLENVLDSADIIAAMMIEGLQGSEKPFHAQLHQLRPYPANIAVAEQVRKLLQGSEIMKSHADCAKVQDPYSLRCIPQVHGASRTAWLHLKEALEIELNSVTDNPVIFNDDLTISGGNFHGQPLALPLDYACLAASEIGNISDRRIYLSLEGNTPGVPKLLMKETGLNSGFMIVQYTSAALASENKGLCFPASADSIPTSLGQEDHVSMGSISGRKALQVIENVEKILGIELFCAAQAVDYHHPLKPGKILAAVHDFVRTEIDHFEEDQIMYDRMENAIQMVQQGKIVAVAAEAESTLT Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS25090 CA265_RS25090 L-asparaginase (EC 3.5.1.1) Specifically important for utilizing L-Asparagine. Automated validation from mutant phenotype: the predicted function (ASPARAGHYD-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-asparaginase 1 MTKILIIYTGGTIGMVNDPTNGMLIPFDFQQIKENVPELSRLDYDLDVHSFNPVLDSSNMDPEIWKTLAELVYHKYDAYDGFVILHGSDTMAFTASALSFMLENLAKPVVLTGSQLPIGEIRTDAKENLITALEIAATKEDGKALFPEVCIYFDAQLFRGNRSIKYNSEKFEAFRSPNYPILAEAGVHLQFHRNYILKATEGELKLHTNFNSNIGVLKLYPGITPQAVQAITDSKVDAIILETFGSGNTTTAQWFLDSLRQAILNGKIIIDISQCKKGSVQLGRYETSRELLKMGILSGYDLTFEATVTKLMFVMGLGLSIEESRKLMEESLRGELTKD Phaeobacter inhibens BS107 Phaeo GFF1011 PGA1_c10280 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (RXN0-2301) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. isovaleryl-CoA dehydrogenase MFNASMTFDLGEDVNALRDMVHRWAQERVRPMAQEIDQKNEFPAELWQEMGELGLLGITVPEEFGGAGMSYLAHTVAVEEIARASASVSLSYGAHSNLCVNQIKLNGNAEQKAKYLPRLVSGEHVGALAMSEAGAGSDVVSMSLRAEKRNDHYRLNGNKYWITNGPDADTLVVYAKTDPDAGSKGMTAFLIEKEFKGFSTSQHFDKLGMRGSNTAELVFEDVEVPFENVLGEEGKGVRVLMSGLDYERVVLAGIGTGIMAACMDEMMPYMKERKQFGQPIGNFQLMQGKIADMYTAMNTARAYVYEVAKACDKGTVTRQDAAACCLYASEVAMTQAHQAVQAFGGAGYLSDNPVGRIFRDAKLMEIGAGTSEIRRMLIGRELMSQM Phaeobacter inhibens BS107 Phaeo GFF1160 PGA1_c11750 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) Specifically important for utilizing L-Proline. Automated validation from mutant phenotype: the predicted function (1.2.1.88, 1.5.5.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. bifunctional protein PutA MTAPQSKTTPEMPSAPTPEYSDALRYRIDAGTYVDQAQMRDQLFALANLDATDRSTISANAAALVRDIRGHSSPGLMEVFLAEYGLSTDEGVALMCLAEALLRVPDADTIDALIEDKIAPSEWGKHLGKSTSSLVNASTWALMLTGKVLDEKRSPVSALRGAMKRLGEPVIRTAVSRAMKEMGRQFVLGETIEGAMKRAAGMEAKGYTYSYDMLGEAARTEADAARYHLAYSRAISAIAAACNSADIRQNPGISVKLSALHPRYELAQETSVKEQLVPRLQALALLAKAAGMGLNVDAEEADRLSLSLEVIEEVISDPALAGWDGFGVVVQAYGPRTGAALDALYDMANRYDRRLMVRLVKGAYWDTEVKRAQVEGVDGFPVFTHKSLTDVSYIANARKLLSITDRIYPQFATHNAHTVSAILHMAKDTDKGAYEFQRLHGMGETLHNMVLEQNQTHCRIYAPVGAHRDLLAYLVRRLLENGANSSFVNQIVDENVPPELVAADPFAQVEDLTANLRKGPDLFQPERPNSIGFDLGHAPTLAAIDAARAPWKSHSWAAEPLLAKAPETATTTDEPVRNPADLTTVGRVQTAGQAEIETALSAATPWNASAETRAEVLNRAADLYEANYGELFALLTREAGKTLPDCVAELREAVDFLRYYAARISAEPPVGVFTCISPWNFPLAIFSGQIAAALAVGNAVLAKPAEQTPLIAHRAISLLHEAGVPRSALQLLPGAGAVGGALTSDARVGGVAFTGSTATALKIRAAMAEHLRPGAPLIAETGGLNAMIVDSTALPEQAVQSIIESAFQSAGQRCSALRCLYLQEDIADNVLKMLKGAMDALHLGDPWNLSTDSGPVIDETARAGILAHIDAARAEGRVLKEMTAPQGGTFVAPTLIEITGIQALEQEIFGPVLHVVRFKSQDLDQIIRDINATGYGLTFGLHTRIDDRVQYICDRIHAGNLYVNRNQIGAIVGSQPFGGEGLSGTGPKAGGPFYMMRFCAPDRQKSVDSWPSDAPAMTMLPAPTGQPMQEITTSLPGPTGESNRLSQLARPPLLCLGPGPQAVVAQARAVHALGGTAIEATGPLDMRQLLTMEGTSGVIWWGDETTAREIESWLARRNGPILPLIPGLPDKARVQAERHVCVDTTAAGGNAALLGGMG Phaeobacter inhibens BS107 Phaeo GFF1175 PGA1_c11900 Propionate--CoA ligase (EC 6.2.1.17) Specifically important for utilizing Sodium propionate. Automated validation from mutant phenotype: the predicted function (6.2.1.17) was linked to the condition via a SEED subsystem. This annotation was also checked manually. propionate-CoA ligase PrpE MSYSEVYEGWKANPEQFWMEAAEAISWDSAPTKALTDKGDGLYEWFADARVNTCYNAVDRHVEQGRGEQTAIIYDSPITHTKREISYVELRNRVATLAGALRAKGVEKGDRVIIYMPMIPEALEAMLACARLGAVHSVVFGGFAANELAVRIDDATPKAIIAASCGLEPGRTVHYKPLLDGAIDLATHKPDFCVIFQREQEVAELIEGRDVNWHGFQYGVEPAECVPVEGNHPAYILYTSGTTGQPKGVIRHTAGQLVALNWTMKNIYNVDPGDVFWAASDVGWVVGHSYICYGPLIHGNTTIVFEGKPIGTPDAGTFWRVISEHKVKSFFTAPTAFRAVKREDPKGEFVKKYDLSCLKQVYLAGERADPDTITWAQEQLKVPVIDHWWQTETGWSIAANPLGIEELPTKLGSPAVPMPGYTVDILDEGGHPVAPGELGAIAVKLPLPPGTLPTLWNAEDRFKKSYLTTFPGYYETGDAGMKDEDGYLYIMARTDDVINVAGHRLSTGAMEEVLAGHPDVAECAVIGVSDSLKGQAPVGFLCLNAGCDTPHEDVVAQVVKLVREKIGPVAAFKLACVVDRLPKTRSGKILRGTMVNIADGTDWKMPATIDDPAILDEITTALQGLGYAK Phaeobacter inhibens BS107 Phaeo GFF1176 PGA1_c11910 Malate dehydrogenase (decarboxylating) (EC 1.1.1.39) Specifically important for utilizing L-Malic acid disodium salt monohydrate. Automated validation from mutant phenotype: the predicted function (1.1.1.39-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. NAD-dependent malic enzyme MTKNPKSDTQTLRDAALHYHAYPNPGKLEIRATKPMANGRDLARAYSPGVAEACLEIKSDPADAAKYTSRGNLVAVVTNGTAVLGLGNIGALASKPVMEGKAVLFKKFASIDCFDIEVNESDPEKLADIVCSLEPTFGAINLEDIKAPDCFIVEKICRERMNIPVFHDDQHGTAIVVGAAAKNALHVAGKRFEDIKIVSTGGGAAGIACLNMLVKLGVRRENIWLCDLHGLVYEGRTEDMNPHKSAFAQKTDLRTLDDVIGGADLFLGLSGPNVLKPEMVAKMTDRPIIFALANPNPEILPDVAREVSPDAIIATGRSDFPNQVNNVLCFPFIFRGALDVGATEINDEMQIACVEGIAEMARMTTSAEAAAAYQGEQLTFGADYLIPKPFDPRLVGVVSSAVAKAAMESGVAQRPIDDLAAYRAKLNQTVFKSALLMKPVFEAAKAAARRIVFTEGEDERVLRTAQGILEETTETPILIGRPEVIETRCERLGLRIRPGTDFQIVNPENDPRYYDYWTSYHRVMQREGVTPDLAKAIMRTNTTAIGAIMVHRGEADSMICGTFGEYRWHMNYVNQVLGGGTYEPHGALSLVILEDGPLFIGDTHVRIEPTPEQIAQTVIGAARHVRRFGLEPKIALCSQSQFGNTRCDSGARLRAAIGILDETPRDFIYEGEMNIDTALDPELRARIFPNSRLEGEANVLIFAHADAASGVRNILKMRAGGLEVGPILMGMGNRAHIVSPSITARGLLNMAAIAGTPVTHYS Phaeobacter inhibens BS107 Phaeo GFF1178 PGA1_c11930 Cytidine deaminase (EC 3.5.4.5) Specifically important for utilizing Cytidine. Automated validation from mutant phenotype: the predicted function (CYTIDEAM2-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. cytidine deaminase Cdd MSLKDAATAVRENAHAPYSNFKVGAAIRAASGTVYVGCNVENVAYPEGTCAEAGAIAAMVAAGETRLEAAYVIADCPAPIPPCGGCRQKLAEFGAADAQVTLATTDGLERATTIGDLLPGAFGADHMERS Phaeobacter inhibens BS107 Phaeo GFF1266 PGA1_c12820 Dihydropyrimidine dehydrogenase (NADP(+)) (EC 1.3.1.2) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (1.3.1.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. dihydroorotate dehydrogenase-like protein MADLTADFLGIKSPNPFWLASAPPTDKEYNVRRAFEAGWGGVVWKTLGSEGPPVVNVNGPRYGAIWGADRRLLGLNNIELITDRPLEVNLEEITRVKKDYPDRAIIVSLMVPCEEQAWKDILPRVEATGADGIELNFGCPHGMAERGMGSAVGQVPEYIQMVTEWCKKYYSKPVIVKLTPNITDIRQPARAAKAGGADAVSLINTINSIVSVNLDAMAPEPTIGDKGTHGGYCGPAVKPIALNMVAEIARCPQTHGLPISAIGGVTTWRDAAEFMTMGAGNVQVCTAAMTYGFNVVKEMISGLNQWMDDKGYDQLDDFVGKAVPNVTDWQYLDLNYIAKAKINQDDCIKCGRCFAACEDTSHQAIAMSEDRVFTVKDDECVACNLCVNVCPVEGCITMEELPVGQIDERTGKVVSDDYANWTTHPNNPSATAAE Phaeobacter inhibens BS107 Phaeo GFF1268 PGA1_c12840 Beta-ureidopropionase (EC 3.5.1.6) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (3.5.1.6) was linked to the condition via a SEED subsystem. This annotation was also checked manually. N-carbamoyl-L-amino acid hydrolase AmaB MTSLGQNLKINGDRLWDSLMEMAKIGPGVAGGNNRQTLTDADAEGRALFQSWCEAAGCTMGLDTMGNMFARREGTDPDALPVYMGSHLDTQPTGGKYDGVLGVLGGLEVVRTLNDLGIKTKHPIVVTNWTNEEGTRFAPAMLASGVFAGKHTQDWAYAREDADGKTFGDELKRIGWVGEEQVGARKMHAMFELHIEQGPILEVENKDIGVVTHGQGLWWLQCTVTGKDAHTGSTPMNMRVNAGLGMARMTEAAHQIAMAHQPHAVGAVGHCDVYPNSRNVIPGKVVFTVDFRSPDLEKLTSMRAQYEVKAKEIADELGLGLEIEPVGHFDPVTFDEGCVNAVRSAAERLGYSHMDIVSGAGHDACWINDLAPTAMIMCPCVGGLSHNEAEDISKDWAAAGTDVMLHAVLETAEIVA Phaeobacter inhibens BS107 Phaeo GFF1269 PGA1_c12850 Dihydropyrimidinase (EC 3.5.2.2) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (3.5.2.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. D-hydantoinase/dihydropyrimidinase Dht MAKVIRNGTVVTADLTYKADVLIENGVITEIGPNLKGDEELDASGCYVMPGGIDPHTHLEMPFMGTYSSDDFESGTRAGLAGGTTMVVDFALPNPGESLLDALKRWDNKSTRANCDYSFHMAVTWWGEQVFDDMKTVIETRGINTFKHFMAYKGALMVNDDELYASFQRLSELGGIAMVHAENGDVVAELSAKLLAEGNNGPEAHAYSRPPQVEGEATNRAIMIADMAGVPLYVVHTSCEDSHEAIRRARMQGKRVWGEPLIQHLTLDESEYFNSDWDHAARRVMSPPFRNKQHQDSLWAGLQSGSLSVVATDHCAFSTEQKRYGVGDFTKIPNGTGGLEDRMPMLWTHGVETGRLTPNEFVAVTSTNIAKILNCYPKKGAVLVGADADLVVWDPAKTKTISAASQQSAIDYNVFEGKEIKGLPRYTLTRGHVAVHDGEIRCQEGHGKFLEREANTTVNKALSTWKDLTAPRPVARSGIPATGV Phaeobacter inhibens BS107 Phaeo GFF1383 PGA1_c14000 Xylose isomerase (EC 5.3.1.5) Specifically important for utilizing D-Xylose. Automated validation from mutant phenotype: the predicted function (XYLISOM-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. xylose isomerase XylA MAGYFDDIAAITYNPESDRLAYRHYNPDEMIMGKRMEDHLRFAVCYWHNFVWEGNDPFGGQTFQRPWFPADTMDLARMKADAAFDMFRILGVPYYCFHDHDIRPEGASLAESHKRLNQIGDLLEQKMADGGPKLLWGTANMFSNRRYMSGASTNPDPDVFAYCASTVRACMDLTHRLNGENYVLWGGREGYETLLNTDLSRELEQMGRFLSMVVDYKHKIGFMGAILIEPKPQEPTKHQYDYDVATVYGFLKRFGLEEEVKVNIEQGHAILAGHSFEHEIAMANALGIFGSIDMNRNDYQSGWDTDQFPNNVPEVALAYYEILRGGGLKTGGTNFDAKLRRQSLDAEDLIAAHVGAMDVCARGLRAAAAMLESDSLEAKRRDRYAGWTTAEAQAYLAEGATLEAIADQAEARALNPQPVSGRQEQLEALVNRFV Phaeobacter inhibens BS107 Phaeo GFF1384 PGA1_c14010 Xylulose kinase (EC 2.7.1.17) Specifically important for utilizing D-Xylose. Automated validation from mutant phenotype: the predicted function (XYLULOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. xylulose kinase XylB MYLGIDLGTSGLRALMTDAAGKPVASAEAQYDVQTPHPGWSEQDPGDWITALDQAMAQLQGSPGYSDICGIAVAGHMHGAVLLDGSDQVLRPCILWNDTRSAAEAAELDAAEKVRDLSGNIVFPGFTAPKLLWVQRHEPEIFANTAKVLLPAAYLNLHLTGRHVADMSDSAGTSWLDVGARDWSEWLLEAGHMRRDQMPDLVEGSAAAGTLRPELAVRWGLTGPVTIAGGAGDNAAAACGTGVMAPGQGFVSLGTSGVVLTARDGFRPDPATAVHTFCHAIPDRWYQMGVMLSATDCMNWLGRITGQSPADLTAGLGEELQPPGPVTFMPYLSGERTPHNSASLRGGFQGLSIATTAEDLARAVMEGVCYGLRDCLEALRKTGAEIDSCLVIGGGSKSAYWVKLLATILDLPLQLPKDGEFGAALGAARLARLAVTGDDPADVLTAPESAMTVAPDPLLRDGYEAGYAAFRRRGAELT Phaeobacter inhibens BS107 Phaeo GFF1711 PGA1_c17350 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) Specifically important for utilizing L-Valine. Automated validation from mutant phenotype: the predicted function (3.1.2.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. putative 3-hydroxyisobutyryl-CoA hydrolase MSDIDIRITGRAGRITLTRSKALNALSYDMCMAVDAALKAWADDDAVDLVVMDAEGEKAFCAGGDIAELYQTGTSGDYDYGRRFWRDEYRMNARIFEYPKPVLSFLQGFVMGGGVGLGCHGTHRIVGDSTKIAMPEVGIGLIPDVGGTLMLALAPGRLGEYLGLTGARMTAADAIYAGFADHYVPETRWPNLISELEQTGRADLLAESAETAPAGTLAPMYDDIGRNFGGETLTDILTALDHDDSSFADATLKTLRRNAPLSMAATVELLHRLRLGNMGIRKALELEYRFTHRAMEKGDFLEGIRAQIIDKDRQPKWQYADRDVPATAVSQMLMPLATQTLQFEEENT Phaeobacter inhibens BS107 Phaeo GFF2746 PGA1_c27890 Glucosamine-6-phosphate deaminase [isomerizing], alternative (EC 3.5.99.6) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (GLUCOSAMINE-6-P-DEAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. putative hexosephosphate binding protein MTDITKMRREIDEIPTAVDRLLSHGRVEIEAVADAARALDPNVMVTVARGSSDHVCTYLKYASEIMLGVPVASVGPSVASIYKAPLRLKGALSLAVSQSGKSPDIVSMAGSARKDGALSVALTNDAASPLAAAADHTLDIHAGPELSVAATKTFVTSAVAGLWLLAQWDRNQAVLAALHALPEQLDRACRIDWPEVRDAIGARSSLFTLGRGQALAVSNEAALKFKETCQLHAESYSSAEVLHGPVSIVEEGFPVLGFAAADAAEGALAGIADQIAAKGAQVFATTDKVTAARRVDHVRTDHALTDPISLIVSFYAMVEAFAASRGIDPDAPRHLKKVTETV Phaeobacter inhibens BS107 Phaeo GFF3000 PGA1_c30490 Malyl-CoA lyase (EC 4.1.3.24) Specifically important for utilizing Potassium acetate. Automated validation from mutant phenotype: the predicted function (4.1.3.24) was linked to the condition via a SEED subsystem. This annotation was also checked manually. putative citrate lyase subunit beta MSFRIQPAAPARPNRCQLFGPGSNTKLFPKMAASAADVINLDLEDSVAPLDKDVARANVIEALNTVDWGNKYISVRINGLDTPYWYRDVVDLLEQAGDRLDQIMIPKVGCAEDVYAVDALVTAIERAKGRAKPISFEVIIESAAGIAHVEAIAAASPRLQAMSLGAADFAASMGMQTTGIGGTQEDYYMLRAGEKHWSDPWHWAQAAIVAACRTHGILPVDGPFGDFSDDDGYIAQAKRSATLGMVGKWAIHPKQIALANQVFTPSDEAVGEAREILAAMEQAKANGEGATVYKGRLVDIASIKQAEVIVAQSELIAQNG Phaeobacter inhibens BS107 Phaeo GFF3379 PGA1_c34320 L-threonine 3-dehydrogenase (EC 1.1.1.103) Specifically important for utilizing L-Threonine. Automated validation from mutant phenotype: the predicted function (1.1.1.103) was linked to the condition via a SEED subsystem. This annotation was also checked manually. L-threonine 3-dehydrogenase Tdh MKALEKSHPREGLWMVQAPVPEIGPDEVLIKIRTTGICGTDIHIWNWDEWASHTVPVPMITGHEFAGEIVEIGRNVTDLAVGQRCSGEGHLIQTDSRQSRAGKFHLDPGTRGIGVNEQGAFAQYLKLPAFNVVPLPEDIPDEIGAILDPLGNAVHTALSFDLLGEDVLITGAGPIGVMAAAVARHAGARHVVITDINPDRLALAEHVVPAVRAVNVAEEDLQDVVRELGLKQGFDVGLEMSGSQAALDQMVEALVMGGKIALLGIPPGKSPVDWSRIVFKAITIKGVYGREMFETWYKMIAMLQNGLDVSRVITHRFDVEDFAEGFAAMKSGRSGKVVLRWP Phaeobacter inhibens BS107 Phaeo GFF3380 PGA1_c34330 2-amino-3-ketobutyrate coenzyme A ligase (EC 2.3.1.29) Specifically important for utilizing L-Threonine. Automated validation from mutant phenotype: the predicted function (AKBLIG-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 2-amino-3-ketobutyrate coenzyme A ligase Kbl MSTDFLTDISKTLEEIKADGLYKRERMITSPQGGEIRVGDAAVINLCANNYLGLADHPDLIAAARGVMDDKGFGMASVRFICGTQDIHRELEQRLAKFLGKDDAILFAACFDANGGLFEPLLGPEDAIISDSLNHASIIDGIRLCKAKRYRYLNSDMNDLEAWLKQAREDGARHIMIATDGVFSMDGYLAKLPEIRALADKYDAIVMVDDCHATGFMGATGAGTPEHFGVDVDIVTGTLGKALGGAIGGYIAGPQPVIDLLRQRARPYLFSNSLPPSIVAAGLEAIRLVEEGNGLRAQLFENAKYWRAGLEKLGFDLLPGEHPIIPVMLGEAQLAQDMASRLFDEGVYVSGFFFPVVPRGQARIRTQMNAALTRDELDRALAAFGKVGKELGILS Phaeobacter inhibens BS107 Phaeo GFF3577 PGA1_c36320 Urocanate hydratase (EC 4.2.1.49) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (UROCANATE-HYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. urocanate hydratase HutU MSDPRKNTRDIFPPTGPEITAKSWMTEAPMRMMMNNLHPDVAENPHELVVYGGIGRAARTWQDFDLIVETLKNLEEDQTLMVQSGKPVGVFQTHKDAPRVLIANSNLVPHWANWDHFNELDKKGLMMYGQMTAGSWIYIGTQGIVQGTYETFAEAGRQHFGGSLKGKWILTGGLGGMGGAQPLAAVFAGASCLAVECNPDSIDFRLRTKYLDEKAETLDEALQMIERWTAAGEAKSVGLLGNAAEIFPELVKRAETGGIRPDIVTDQTSAHDPVNGYLPLGWTMGEWKERRESDKKAVEKAARASMKVQVKAMCDFHAMGVPTVDYGNNIRQMALEEGLENAFDFPGFVPAYIRPLFCRGIGPFRWAALSGDPEDIRKTDAKMKELFPENAGLHRWLDMAQERIAFQGLPARICWIGLGDRHKAGLAFNEMVRTGELSAPVVIGRDHLDSGSVASPNRETESMLDGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGFSQHSGVVICCDGSEDADRRVGRVLWNDPATGVMRHADAGYDIAKDCAQEHGLNLPGIL Phaeobacter inhibens BS107 Phaeo GFF3578 PGA1_c36330 N-formylglutamate deformylase (EC 3.5.1.68) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (3.5.1.68) was linked to the condition via a SEED subsystem. This annotation was also checked manually. N-formylglutamate deformylase HutG MIEVTQGASPLVLGLPHTGTDVPPEVWACLNETGRALADTDWHIHDLYAGLAEGITTVRTPVHRYVIDVNRDPGGISLYPGQNTTTLVPLTDFDGLPIWQEGKEPNEAEITRRRDAYHAPYHAALMAELERVKAIHGFAILYDCHSIRGDIPFLFEGRLPDFNTGTNMGTTCDPEIEALTVAHCEAAEGYTSTLNGRFKGGWTTRHYGRPADGLHAIQMELAQATYCQESPPWTYLPERAEQLRAPLTNILTDLKNWRPSA Phaeobacter inhibens BS107 Phaeo GFF3579 PGA1_c36340 Histidine ammonia-lyase (EC 4.3.1.3) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (HISTIDINE-AMMONIA-LYASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. histidine ammonia-lyase HutH MIEMIPGTVTLSTLEDIYRNLTPAKLASSAREPVEAAAQMVAEAAAGQEAVYGINTGFGKLASTKIAPEDTATLQRNLILSHCCGVGEALPEDKTRLMMTLKLLSMGRGASGVRWLVIDQIEKMLAHGVIPVIPSQGSVGASGDLAPLAHMAAAMIGAGEATYDGTRMSSAEALKKAGLEPIVLGPKEGLGLINGTQFSTACALAGLFDAWRMAEASMTIASLSTDAIMGSTAPLIADIHTLRGHAGQINVAQQMREIMDGSEIRESHREGDTRVQDPYCIRCQPQVVGAALDVLRMAAKTLEIEANAVTDNPLVLVNEGRIVSGGNFHAEYVGFAADQIALAVAEIGAIAQRRVALMVDPTLSHDLPPFLTPDPGLNSGFMIAEVTTAALMSENKHLANPCVTDSTPTSANQEDHVSMAAHGALRLARMNANLSVILGVEMLCAAQGVEARAPLQTSARLQDVLGMLRADIPALAEDRYLAPDIEDASAMVRAGRVAEAAGVKVTA Phaeobacter inhibens BS107 Phaeo GFF3580 PGA1_c36350 Imidazolonepropionase (EC 3.5.2.7) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (IMIDAZOLONEPROPIONASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. imidazolonepropionase HutI MGDTDSYLICDATLATMTGSDPAYGLVPDGLIVVQNGWIRWCGSEAQLPKDYSDWPRVSMGGRLVTPGLIDCHTHIVFGGNRAMEFEMRLNGASYEDVARAGGGIVSTVSATRTASLEDLVQGALPRLDALIAEGATVVEVKSGYGLDRETELNMLRAARRLAVLRSVTVNTTFLGAHATPGEYKGRDDAYIDEVCIPALRAAHAEGLVDAVDGFCENIAFAPAQIERVFKAARELGLPVKLHAEQLSHQGGTALSAQYGALSVDHVEYATEDDAKMMAAAGSVAVILPGAFYTIREIQAPPIEHFRSHGVPMALATDCNPGSSPLTSLLLTMNMGCTLFRMTPEEALAGVTRNAASALGLTDRGQISAGMRADLAVWDVETPGELAYRIGFNPLYTRIYEGNQ Phaeobacter inhibens BS107 Phaeo GFF3581 PGA1_c36360 Formiminoglutamic iminohydrolase (EC 3.5.3.13) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (FORMIMINOGLUTAMATE-DEIMINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. putative formiminoglutamate deiminase MQTIFAQHARMPQGWVTDLRLTIEAGKIATLEPGAAVQPQDHRVGALVPALANLHSHSFQRAMAGMTETRVSGRDSFWSWRKLMYQFVDHLTPEQYEAIAALVFMEMLEAGYASVGEFHYVHHQPGGQPYEVLGELSHRVFAAADLTGIGLTHLPVLYTYGGAGQAPLGGGQQRFGNDVTRYANLLSDCRTTARELLPMDARVGIAPHSLRATAPDELAEVLTLRAESPVHIHIAEQPQEVADIGGWLGERPVQWLLNNCAVDKDWCLIHATHMTEQETHDLARSGAVAGLCPITEANLGDGPFNGVLFQNNGGRFGVGSDSNIRISLSEELRLLEYSQRLRDLARNVMVPEEGSVGAALYLGAACGGAQALGRDAGRLEVGALADLMAFDTTDVTLCALRPDQFLDGLCFAADDSVVRDVWSAGRHVVSGGRHANREQIIARYNSAVAALLSAL Phaeobacter inhibens BS107 Phaeo GFF709 PGA1_c07240 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (2.7.1.92) was linked to the condition via a SEED subsystem. This annotation was also checked manually. putative 5-dehydro-2-deoxygluconokinase MGQPSKARSDLAGRNFLVIGRVGMDLCPTPAGTATADAQDMMVAMGGSSANIAAGLVKMGCRSALVTSVSDDAVGWYCLNQLDHYGVDRTHVKRITGEYRTSLAVYESRVEDHQSVIYRNNAADFQMTIADVEAVDYSQYSALITAGTVFAAEPSRSATFRAFDLARAAGLPIIFDVDYRPYSWPSPEVAADVLSRAGAMSDIIVGNDEEFGFMAGGIDKGRAKARALAETSASVVVYKMGPKGAVTFADGQEIRTGIYPVDALKPTGAGDSFMAGFLASLSEGRPMKDAILRGSACASVVVAKPGCAPAMPDLAALEAFLATHPGATEL Phaeobacter inhibens BS107 Phaeo GFF712 PGA1_c07270 Myo-inosose-2 dehydratase (EC 4.2.1.44) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (MYO-INOSOSE-2-DEHYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. putative iolE/mocC family protein MTIRIGNAPCSWGVEFAQDPRNPDWRSVLKDCAEAGYKGIELGPVGYMPEDPAILRDALAEYDLELIGGVVFRAFHDPDQWDDVLDGAHRTCKALQAHGAQHLVLIDSISPRRAPTAGRASEAEQMNHAEWSAFRDRLATVAQIGTEEYGLTVGIHAHAAGFMDFEPELERLLNEVDDKILKICFDTGHHSYAGFDPVAFMKRHMDRISYMHFKDIDPKVKADVIAKRTNFYDACGQGIFCNLGEGDVDFPAVRQLLVDTGFSGWCTVEQDCDPTLDPDPVGDARANREYLESIGFN Phaeobacter inhibens BS107 Phaeo GFF770 PGA1_c07840 Beta-glucosidase (EC 3.2.1.21) Specifically important for utilizing D-Cellobiose. Automated validation from mutant phenotype: the predicted function (3.2.1.21) was linked to the condition via a SEED subsystem. This annotation was also checked manually. beta-glucosidase A MFRNSRADFPKDFLFGTATSAYQIEGHGFGGAGPTHWDSFAATPGNVVRAEHGQRACDHYHRYAEDLDLAAAAGFDCYRFSTSWARVMPEGRGAPNPEGLDFYDRLTDAILERGLKPCVTLYHWELPQALADLGGWRNAEIANWFGDYAEVIMGRIGDRMYSAAPINEPWCVGWLSHFLGHHAPGLRDIRATARAMHHVMLAHGTAIQAMRALGMSNLGGVFNLEWATPVDDSEAAQQAAARYDAIYNGFFLGGAFHGRYPDLALEGLEPHLPKGWQDDFATITAPVDWCGLNYYTRKQIAPDAGPWPQYAEVDGPLPKTQMGWEIYPQGLYDFLTRTARDYTGDLPLIVTENGMANADVVTKGKVEDAARITFVDDHLDAVRRAIADGVPVQGYFLWSLLDNYEWALGYEKRFGLVHVDFETLKRTPKASYHALRSALTGASK Phaeobacter inhibens BS107 Phaeo GFF939 PGA1_c09550 Glutaminase (EC 3.5.1.2) Specifically important for utilizing L-Glutamine. Automated validation from mutant phenotype: the predicted function (GLUTAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glutaminase A MAAKLQRVLDEISQQMRASTDWGEVASYIPELGEVRPDQFAISVATADGGLFSAGDFQTRFSAQSITKVFTLAIALGRAGDQLWHRVGREPSGTAFNSIVQLEHEQGRPRNPFVNAGAIVTTDEVLAGREPREALAEFLGFVRAAAEDDDIHINADVARSETAHGHRNAAHAHFLASFGNLKNPPEKVLGTYFHHCATEMTTQQLAKAGRFLIGTGSYPRMVSLDRVRRLNALMLTCGHYDGSGEFAYRVGLPAKSGVGGGILGVVPGQASIAVWSPGLNRNGNSKLGTEAMEQLAREMDWSVF Pseudomonas putida KT2440 Putida PP_1171 PP_1171 Uronate dehydrogenase (EC 1.1.1.203) Specifically important for utilizing D-Glucuronic Acid. Automated validation from mutant phenotype: the predicted function (1.1.1.203) was linked to the condition via a SEED subsystem. This annotation was also checked manually. uronate dehydrogenase MTTTPFNRLLLTGAAGGLGKVLRERLKGYAEVLRLSDISPMAPAAGPHEEVITCDLADKAAVHTLVEGVDAIIHFGGVSTEHAFEEILGPNICGVFHVYEAARKHGVKRIIFASSNHTIGFYRQDERIDAHAPRRPDSYYGLSKCYGEDVASFYFDRYGIETVSIRIGSSFPQPQNLRMLCTWLSYDDLVQLIERGLFTPGVGHTIVYGASDNRTVWWDNRHAAHLGYVPKDSSETFRAAVEAQPAPAADDPSMVYQGGAFAVAGPFN Pseudomonas putida KT2440 Putida PP_3599 PP_3599 5-dehydro-4-deoxyglucarate dehydratase (EC 4.2.1.41) Specifically important for utilizing D-Glucuronic Acid. Automated validation from mutant phenotype: the predicted function (4.2.1.41) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 5-dehydro-4-deoxyglucarate dehydratase MNPQELKSILSHGLLSFPVTDFNAQGDFNPAGYIKRLEWLAPYGASALFAAGGTGEFFSLAASEYSQVIKTAVDTCATSVPILAGVGGSTRQAIEYAQEAERLGAKGLLLLPHYLTEASQDGVAAHVEAVCKSVNIGVVVYNRNVCRLNADLLEKLAERCPNLIGYKDGLGDIELMVSIRRRLGERFSYLGGLPTAEVYAAAYKALGVPVYSSAVFNFVPKTAMDFYNAIARDDHATVAKLIDDFFLPYLDIRNRKAGYAVSIVKAGARIAGYDAGPVRTPLTDLTAEEYEMLAALMDKMGPQ Shewanella amazonensis SB2B SB2B 6935813 Sama_0031 fadA Acetyl-CoA C-acyltransferase (EC 2.3.1.16) Specifically important for utilizing Tween 20. Automated validation from mutant phenotype: the predicted function (KETOACYLCOATHIOL-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 3-ketoacyl-CoA thiolase (RefSeq) MKQAVIVDCIRTPMGRSKGGVFRNVRAETLSAELMKALLLRNPGVDPNTIEDVIWGCVQQTLEQGFNIARNASLLAGVPKTAGAVTVNRLCGSSMEALHQASRAIMTGMGDTFIIGGVEHMGHVPMNHGVDFHPGLAANVAKASGMMGLTAEMLGKLHGISREMQDQFAVRSHQRAHAASIEGRFANEIYAIEGHDANGALIKVDYDEVIRPETTLESLAGLRPVFDPANGTVTAGTSSALSDGAAAMLVMEEEKARALGLTIRARVRSMAVAGCDAAIMGYGPVPATQKALARAGLSIQDMDVIELNEAFAAQSLPCVKDLGLMDVVEDKVNLNGGAIALGHPLGCSGARISTTLINLMEHKDATLGLATMCIGLGQGIATVFERV Shewanella amazonensis SB2B SB2B 6935814 Sama_0032 fadB Enoyl-CoA hydratase (EC 4.2.1.17); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) Specifically important for utilizing Tween 20. Automated validation from mutant phenotype: the predicted function (ENOYL-COA-HYDRAT-RXN, OHACYL-COA-DEHYDROG-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. multifunctional fatty acid oxidation complex subunit alpha (RefSeq) MIYQSPTIQVELTADKIARLCFNAPGSVNKFDRETLASLNAALDVLKDSDAKAAVLTSGKDTFIVGADITEFLALFAEEDAKLMEWIAQANVVFNKLEDLPFPTVSAIKGFALGGGCEAILATDFRVADTSAKIGLPETKLGLIPGFGGTVRLPRLIGADNALEWITTGKDQRPEDALKVGAIDAVVAPENLEAAAIQMLNDALAGKLDWQARRARKQAPLTLPKLEAMMSFTTAKGMVYAVAGKHYPAPMAAVSVVEQAAGMSRAEALVVEHNAFIKLAKTDVATALIGIFLNDQLVKGKAKKASKLAKDIKHAAVLGAGIMGGGIAYQSASKGTPIVMKDINQAALDLGVNEAAKLLSAQVARGRSTPDKMAKVLNNITPALDYAPLKDVNVVVEAVVENPKVKAMVLADVENVVADDAIIASNTSTISIDLLAKSLKNPARFCGMHFFNPVHKMPLVEVIRGKDTSEETVASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFNGLLADGGDFAAIDKVMEKQFGWPMGPAYLLDVVGLDTGHHAQAVMADGFPDRMGKSDKDAIDVMYEAGRLGQKNGKGFYQYSIDKRGKPKKDVDPASYTMLAEAFGAQKAFEADEIIARTMIPMIIETVRCLEEGIVASPAEADMGLVYGLGFPPFRGGVFRYLDTMGVANFVALADKYAHLGGLYQVTDAMRELASNNGSYYPKA Shewanella amazonensis SB2B SB2B 6935950 Sama_0165 Phosphoenolpyruvate carboxykinase [ATP] (EC 4.1.1.49) Specifically important for utilizing Tween 20. Automated validation from mutant phenotype: the predicted function (PEPCARBOXYKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. phosphoenolpyruvate carboxykinase (RefSeq) MAEGINRVHRNPSTAELVELALRRGEGELTANGALVAKTGARTGRSPNDRFIVKEAGSEADIEWGNVNKPFAPEAFNALWDRVAAYLADKEVFVSDLEVGADPEHYLPVTVTTEYAWHQLFARNLFIIPEHFNQAGKPTWQIMNAPGFVCEPERDGTASEATVIINFAERKVLLAGLKYAGEMKKSMFSVQNFLLPAKGVLPMHCSANVGKDGDTTLFFGLSGTGKTTLSADPKRFLIGDDEHGWAPGSVFNIEGGCYAKCIDLSQKNEPVIWDAIRFGTVLENVVLDDKRVPDYKNASLTENTRAAYPLEHIAQRQEENRGGEPRAVVFLTCDVSGVLPPVSKLTKEQAAYHFLSGYTAKVGSTEMGSTAAIQSTFSTCFGAPFFPRPAGVYAELLMKRIEEFGSQVYLVNTGWTGGPYGVGKRFDIPTTRAIVDAIVSGELASVETVHLEKLNLEVPVAVPGVETALLNPVNTWADKAKYQEYAQKLAEEFQANFAKYQVPDSIKNAGPKA Shewanella amazonensis SB2B SB2B 6936223 Sama_0412 Uridine phosphorylase (EC 2.4.2.3) Specifically important for utilizing Cytidine and Uridine. Automated validation from mutant phenotype: the predicted function (URPHOS-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. uridine phosphorylase (RefSeq) MADVFHLGLTKNMLDGATLAIVPGDPERVKRIAELMDKPTFLASHREFTSYLAYLDGKPVVVCSTGIGGPSTSIAVEELAQLGINTFLRVGTTGAIQPHVNVGDLIVTQASVRLDGASLHFAPMEFPAVANFECTTAMVAACRDAGVEPHVGVTASSDTFYPGQERYDTVSGRVTRRFEGSMKEWQEMGVLNYEMESATLFTMCASQGWRAACVAGVIVNRTQQEIPDEATMKNTEVSAVSVVVAAARKLLA Shewanella amazonensis SB2B SB2B 6936346 Sama_0535 Aldose 1-epimerase (EC 5.1.3.3) Specifically important for utilizing D-Maltose monohydrate. Automated validation from mutant phenotype: the predicted function (5.1.3.3) was linked to the condition via a SEED subsystem. This annotation was also checked manually. aldose 1-epimerase (RefSeq) MVRHSVLDAWKDPRGGEIERVRLDNGQLAIEVLSLGGIIRSLWAPDSRGERANLVLGCDSLEDYLAQNAHLGAIAGRYANRIALGKLHYDGEDFQLDINQATNCLHGGHEGFNRKQWALGLLPDGVRLSLSSPDGDMGFPGNCSVQLDYRLAGNNLYVEIMAMTDRPCPVNLTQHSYFNLDGRADCLDHTVTMHARAFLRCNEAGIPTGRATTAGTPLALQDVRLGDRVQHPDLASTRGFDHCFIIDKTQDELALAAELHSPHSGRLLKLYTNQPGVQLYGANFLDGERGRQGKIYRPYQGVCLEPQLFPDAPNQPDLGKAWLMPGEIYHHISRYQFEVKD Shewanella amazonensis SB2B SB2B 6936758 Sama_0945 Glucosamine-6-phosphate deaminase [isomerizing], alternative (EC 3.5.99.6) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (GLUCOSAMINE-6-P-DEAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glutamine--fructose-6-phosphate transaminase (isomerizing) (RefSeq) MTNTIMEQEARTAPAKIAAQLAANAQITAELGAKLRELNPRFVMIVGRGSSDHAGVFGKYLFEIETGVPTFAAAPSVASVYGKSLKLEGALVIVISQSGRSPDILAQARMAKNAGAFCVALVNDESAPIKDIVDVVLPLRAGEEKAVAATKSYLCTLSALIQLAAAWTQSESLAKAVDTMPTALEAAVNAEPQLTAEGIGAVRNLVVLGRGLGYAVSKEIALKLKEVCSIHAEAFSSAEFLHGPVTLVEKKLTIVDVCVGDESYASHIEQIENVSSRGADLVHLNQTSTDIHPRVAPLALLQRFYIDVAAVAVARGIDPDAPAGLKKVTQTL Shewanella amazonensis SB2B SB2B 6936759 Sama_0946 N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (NAG6PDEACET-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-acetylglucosamine-6-phosphate deacetylase (RefSeq) MKTTLIAERLFDGEQFHHNVPLTVEDGQVLALDTVAGCAEVRLQGTLVPGFIDVQVNGGGGVLFNDTPTVAAIEAIGAAHARFGTTGYLPTLITDKVETMARAADAAAEAIAKGSTGVLGVHFEGPHLSVPKKGVHPESHIRRIGDRELEIFARQDLGLKVVTLAPENVSPEVICALVDVGVKVCLGHSNADYATTVAALEAGATGFTHLYNAMSALTSREPGVVGAAIDSDEAWCGLIVDGHHVHSAAARIAIKAKPRGKVMLVTDAMPPVGMDDNASFELFGIQVVRQGDKLNALTGELAGCVLDMAGAVQNTVDMLGLPQAEAIRMASLYPAAFLGIDNRVGTLSVGKQADMVLLDDNGRCRGTWIGGRQVFGL Shewanella amazonensis SB2B SB2B 6937151 Sama_1321 Succinylarginine dihydrolase (EC 3.5.3.23) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (SUCCARGDIHYDRO-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. succinylarginine dihydrolase (RefSeq) MKHFEANFDGLVGPTHNYAGLSFGNVASQSNAAQVSNPKDAAKQGLKKAKALADMGMVQGMLAPQERPDIHTLRRVGFTGSDADVLSQAAKASPVLLQACASASSMWTANAATVSPSADSDDGKLHFTPANLVDKLHRSIEPVTTGNILKAIFTDERYFAHHQHLPEHPHFGDEGAANHTRLCHDYGQAGVEVFVYGRSVADLSRPAPVKYPARQTLEASQAVARLHQLSDDRTVYMQQNPDVIDQGVFHNDVIAVGNQNVLFYHEQAFLETQAKLAEIDKKMHGNMYFIEVPTAKVSVQDAVKSYLFNTQIITLSDGNMAIIAPTDCQENPAVHAYLNELVTLNTPIKAVHYFDVKQSMQNGGGPACLRLRVAMNETELAAVNPQVMMNDALFARLNQWVDKHYRDRLSTQDLADPQLLMESRTALDELTQIMKLGSVYQFQR Shewanella amazonensis SB2B SB2B 6937192 Sama_1362 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (RXN0-2301) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. isovaleryl-CoA dehydrogenase (RefSeq) MSHLYSTLNFGLGEDVDMLRDAVYEFAKGEIAPLAEKVDRDNAFPNELWAKFGDMGLLGVTVAEEYGGVNMGYLAHVVAMEEISRASASIGLSYGAHSNLCVNQIYRNGNEAQRAKYLPKLISGEHIGALAMSEPNAGSDVVSMKLHARKEGDRYILNGNKMWITNGPDAHTYVIYAKTDLDKGPHGITAFIVERGFKGFSQAQKLDKLGMRGSNTCELVFEDCEVPEENILGGLNNGVKVLMSGLDYERVVLSGGPLGIMTACMDIVVPYVHERVQFGKSIGEFQLVQGKLADMYTGMNAAKSYVYNVARACDRGETTRKDAAGVILYAAELATKMALDAIQLLGGNGYVNEYATGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETK Shewanella amazonensis SB2B SB2B 6937234 Sama_1404 Beta-glucosidase (EC 3.2.1.21) Specifically important for utilizing D-Cellobiose. Automated validation from mutant phenotype: the predicted function (3.2.1.21) was linked to the condition via a SEED subsystem. This annotation was also checked manually. beta-glucosidase (RefSeq) MKFALSKTTLALACVLGGVMSGKVSAAESSSLTERDVNRWPEAVYHTPIQADVEAKVHKLLAAMTLEQKVAQIIQPEIRDFGVEDMRRYGFGSFLNGGGSFPGNNNRAKAADWVALADQMYHAAMDDSIDGIAIPPMWGTDAVHGHGNVFGATLFPHNIGLGATQNPQLIKAIAAATAKEVRATGIDWVFAPTVALVDNLRWGRTYEGYARDPELIERYAEAFVDGMQGEGKSWLGDDYTLATAKHFIGDGGTDNGDDRGDTRVDENTLIARHGQGYVGALGHGVQTVMASFNSWNGEKLHGSKYLLTDVLKERMGFDGVVVGDWLGHGFVPGCSYEHCAEAVNAGVDILMAPGDSWKALYANTIADVKSGVLPLSRLDDAVKRVLRVKLRAGLFDNKAPSANPYAGKQEWIGHPEHRAIARQAVAESLVLLKNNRPANGARPVLPIAANARVLVVGEGADSIPQQSGGWSMTWQGTEVTNADFPGATSIFAGIKAALNAAGGDALLSSDGTIPVGFKPDVVIAVYGEQPYAEGNGDLDNLEYQRGDKRSLAMLSALKATGLPLVSVVLSGRPLWMNPEINVSDAFVAAWLPGSEGAGVADVLIGDKNAQPRADFKGRMPFPWPATPSADGFVSDTGSAGQDQPKPLFSLWQGFDYRSDATLAALSEDNGSSEADNRLAIFDKAIKAPWHLAVGDDKGLHRVGPGLWQQGPWAVRSVNRIVQEDARRFEFGAAGTLSFRDDFTLDLRRFAPDSSLLSFDIALTALPGKLQLSMVCEGGCRQAVELSGQLKADGQWQRVEVPLSCFGVTADELARTFSPMTMSLPQGGTLTLANVSLEGMVQRDASAKAVECGLPPVSDK Shewanella amazonensis SB2B SB2B 6937475 Sama_1631 Histidine ammonia-lyase (EC 4.3.1.3) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (HISTIDINE-AMMONIA-LYASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. histidine ammonia-lyase (RefSeq) MRFRYGVDHLTLETVNGIANGSIQAELCQQAIDKINASRHNVDVMAASDKAIYGINTGFGPLCDTQISPAETHLLQKNLLITHAVGVGEPIAKSISKLMLITKVHALSQGFSGIRLDVVERMLAFIALDLIPVVPEQGSVGASGDLAPLSHLFLPLLGEGEFWQGDKIVPAREALKAHGLEPLELHAKEGLALINGTQFILSHAITALTKMGYLLDLADLAGAMSIEGMQGSQSPFRAELHEIRPFAGNIEVAARMRSFFKDSENMASHEDCDRVQDPYSLRCIPQVHGASRNAYNHLKELAEIEMNSVTDNPIVISAEEAISGGGFHGQPLAMVLDYTSIAAAELGNISDRRCYLLLEGLHGLPRLLTTSGGLNSGMMIPQYVTAALVTENKSLCFPPSADSVPTSMGQEDHVSMGSISGRKLNQILGNLEKIFAIELMYAAQAIDFRRPNRCSDIIEQNHALIREKVAKLEEDRLLKPDIDAIIALVKAQAFTVK Shewanella amazonensis SB2B SB2B 6937476 Sama_1632 Urocanate hydratase (EC 4.2.1.49) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (UROCANATE-HYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. urocanate hydratase (RefSeq) METNMTFAEQIKQGIPAELPSPKPYPADANRAPKRKDILTAAEKQLAVRNALRYFPAEWHQELAAEFAKELNDFGRIYMYRFKPEYAMKARAISEYPAKCEQAAAIMLMVDNNLDPAVAQHPEELITYGGNGAVFQNWAQYRLTMKYLSEMEADQTLHLYSGHPMGLFPSSVDAPRVVVTNGMMIPNYSKPDDWERFNALGVTQYGQMTAGSFMYIGPQGIVHGTTITVMNGFRKVLEKGDSPKGKIFLTAGLGGMSGAQPKAGNIAGCITVCAEVNPKAATKRHAQGWVDELIDNMDALVARVKQAQANEEVVSIAFIGNVVNVWEAFDEHDIFVHLGSDQTSLHNPWSGGYYPVDISYDESNRLIREEPELFKTKVQATLKRHADAINRHTAKGTYFFDYGNAFLLEASRAGGDVMAENGIDFKYPSYVQDILGPMCFDYGFGPFRWVCTSGNSADLDRTDAIAAEVLARIMAEAPAEIQQQMQDNITWIKDAKQNKLVVGSQARILYADAEGRMEIAKAFNDAISRGEIGPVVLGRDHHDVSGTDSPFRETSNIYDGSRFTADMAIHNVIGDSFRGATWVSIHNGGGVGWGEVINGGFGMLLDGTEAAERRLKSMLLFDVNNGIARRSWARNEEANFAIKREMARTPKLKVTLANSVDDDIINGLEF Shewanella amazonensis SB2B SB2B 6937833 Sama_1974 Cytidine deaminase (EC 3.5.4.5) Specifically important for utilizing Cytidine. Automated validation from mutant phenotype: the predicted function (CYTIDEAM2-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. cytidine deaminase (RefSeq) MQDRFVRRINELPKALADELLPMLGEQFCGHLDAQQVKQLCAVSAMDSHELGLALLPIAAALAKPPVSNFYVGAIAVGSGGDFYMGANLELQGEALFHSVHAEQSAISHAWLSGETQISDIIVNASPCGHCRQFMNELVQGQAIRIHLPGQDTAPLSHYLPYAFGPADLNVTAPLLSKQQTELVLESDDPLLIEALDHAGLSYAPYSQCHAAVVLETEDGASFCGRYAENAAFNPSMLPMQMALSALVRHNRSFSDIKRAVLLESSQGKISLVGATMDALHAVAVVELEHLVVDPV Shewanella amazonensis SB2B SB2B 6938260 Sama_2380 Isocitrate lyase (EC 4.1.3.1) Specifically important for utilizing Tween 20. Automated validation from mutant phenotype: the predicted function (ISOCIT-CLEAV-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. isocitrate lyase (RefSeq) MSKYISRQEQIDALKKDWAENPRWKGVRRPYTAEEVVSLRGSFVPENTVAQRGAAKLWDLVNGGAKKGYVNSLGALTGGQAVQQAKAGIEAIYLSGWQVAADANLAGTMYPDQSLYPANSVPAVVGRINNSFRRADQIQWSNGVGPEDDKFVDYFLPIVADAEAGFGGVLNAYELMKSMIDAGAAGVHFEDQLASVKKCGHMGGKVLVPTQEAVQKLVAARLAADVSGVETLVIARTDANAADLLTSDCDPYDSDFITGERTSEGFYRVRAGLDQAIARGLAYAPYADLIWCETAKPDLEEARRFAEAIHAKYPDQLLAYNCSPSFNWKKNLDDATIAKFQQALSDMGYKYQFITLAGIHNMWFNMFDLAYDYARGEGMKHYVEKVQEAEFAAASKGYTFVAHQQEVGTGYFDKMTNIIQGGASSVTALTGSTEEEQFH Shewanella amazonensis SB2B SB2B 6938368 Sama_2487 Glutaminase (EC 3.5.1.2) Specifically important for utilizing L-Glutamine. Automated validation from mutant phenotype: the predicted function (GLUTAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glutaminase (RefSeq) MLEQALLDDLVAKVRPLLGQGKVADYIPALARVSPYKLGIAVTTIDGTTLGAGDWQEAFSIQSISKVFSLTGAMMLYEEREIWSRVGKEPSGHSFNSLVQVELERGIPRNPFINAGALVIADLLQSRLGAPKQRMLEIVRMLSQNHKVCYDKVVADSEYQHSARNAAIAFLMKSFGNFHNDVDKVLRSYFHYCSLSMSCADLSRAMVYLANQGVSLDGNEVVSPTQTRRLNALLATSGLYDGAGEFAYRVGMPGKSGVGGGIIAVIPGDMSVCVWSPALDASGNSLAGTRLLELLAQELGRSIF Shewanella amazonensis SB2B SB2B 6938573 Sama_2676 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) Specifically important for utilizing L-Proline. Automated validation from mutant phenotype: the predicted function (1.2.1.88, 1.5.5.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase (RefSeq) MFKASEVLAGRYDNANLDELFSLISQNYIVDEEAYLKELIALVPSSDEEIARITSRAHDLVAKVRQYEKKGLMVGIDAFLQQYSLETQEGIILMCLAEALLRIPDAETADALIADKLSGAKWDEHMSKSDSVLVNASTWGLMLTGKIVQLDKNLDGTPSNLLSRLVNRLGEPVIRQAMYAAMKIMGKQFVLGRTIEEGLKNAAEKRKLGYTHSYDMLGEAALTMKDADKYYRDYANAIQALGTAKFDESEAPRPTISIKLSALHPRYEVANEDRVMTELYATLIKLIEQARSLNVGIQIDAEEVDRLELSLKLFKKLYQSDAAKGWGLLGIVVQAYSKRALPVLMWLTRLAKEQGDEIPLRLVKGAYWDSELKWAQQAGEAGYPLFTRKAATDVSYLACARYLLSEATRGVIYPQFASHNAQTVAAITAMVGDRKFEFQRLHGMGQELYDTVLAEAAVPTVRIYAPIGAHKDLLPYLVRRLLENGANTSFVHKLVDPKTPIESLVTHPLKTLQGYKTLANNKIVKPADIFGAERKNSKGLNMNIISESEPFFAALEKFKDTQWSAGPLVNGETLSGEVRDVVSPYNTTLKVGQVAFANEATIEQAIAGADKAFASWCRTPVETRANALQKLADLLEENREELIALCTREAGKSIQDGIDEVREAVDFCRYYAVQAKKMMSKPELLPGPTGELNELFLQGRGVFVCISPWNFPLAIFLGQVAAALATGNTVIAKPAEQTCLIGFRAVQLAHEAGIPKDVLQFLPGTGAVVGAKLTSDERIGGVCFTGSTTTAKVINRALAGRDGAIIPLIAETGGQNAMVVDSTSQPEQVVNDVVSSAFTSAGQRCSALRVLYLQEDIAERVLDVLKGAMDELTLGNPGSVKTDVGPVIDAAAKANLNAHIDHIKQVGRLIHQLSLPEGTENGHFVAPTAVEIDSIKVLTKENFGPILHVVRYKAAGLQKVIDDINSTGFGLTLGIHSRNEGHALEVADKVNVGNVYINRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLTRFVTEKTRTNNITAIGGNATLLSLGDAD Shewanella amazonensis SB2B SB2B 6938906 Sama_3009 astD Succinylglutamic semialdehyde dehydrogenase (EC 1.2.1.71) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (SUCCGLUALDDEHYD-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. succinylglutamic semialdehyde dehydrogenase (RefSeq) MTQFINGQWLAGEGKEMQSKNPANGEVIWQGKAAVPAQVQAAVMAARDAQFEWFMLGFEGRQAIVEAYRNELEANKAELAEVIAQETGKPRWETATEAAAMIGKIGLSVSAYHKRTGTEVNEGAAGRAVLRHKPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPKVAELMLKLWEKAGLPAGVINLVQGEVETGKALASHPQLDGLFFTGSSRTGHLLHQQYAGHPGKILALEMGGNNPLIVKGVSDTRAAIHDIIQSAFISSGQRCTCARRLYVEKGAEGDKLLAGLVEAVKAIKVGPWNADPQPFMGSMISETAAKGMLDAQRNLLNLGAKSLVEMTHLQAGTGLVSPGLIDVTEVIELPDEEYFGPLLQVVRYTSFDEAIRLANDTRYGLSAGILADDKADYEYFLARIRAGIVNWNKQITGASGAAPFGGVGASGNHRASAFYAADYCAYPVASMEADSVTLPASLSPGLTL Shewanella amazonensis SB2B SB2B 6938907 Sama_3010 Arginine N-succinyltransferase (EC 2.3.1.109) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (ARGININE-N-SUCCINYLTRANSFERASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. arginine N-succinyltransferase (RefSeq) MLIIRPIRASDFDALYRIAVESGHGFTSLPVNEDLLRRKIARSEASFQKVVETPYDEGYLMVLEDTQTQEVVGTCALEAAVGMEDAFYHYRLGTEVYHSQQINVRNEVETLTLCHDYTGAAELCTLFLRGAYRKDNNGRMLSRSRFLFLAQHANRFGETVIAEMRGVSDENGNSPFYGWLQKHFLGIDFVEADYLSGLGRKAFMAEMMPRNPVYVCLLPEEAQKVIGEVHTNTRPALSLLRAEGFRCRGYVDIFDGGPTVECNLQDIRGVRESRLLTVRIGEMPASDDSFILSNTQLVDYRATSVELMVSSDSDEVILSPELAAGLLVSDGEQVRVLAI Shewanella amazonensis SB2B SB2B 6938941 Sama_3039 Phosphoglycerate dehydrogenase (EC 1.1.1.95) Specifically important for utilizing Glycine. Automated validation from mutant phenotype: the predicted function (1.1.1.95) was linked to the condition via a SEED subsystem. This annotation was also checked manually. D-isomer specific 2-hydroxyacid dehydrogenase family protein (RefSeq) MRHKLLLLTRENERYRSLLASCHLPELELLDDNPANIRLADIWLAEPGLAAPLVNHASGLRWMQSTFAGVDLLVKPRQRRDYLLTNVRGIFGPLMSEYLFGYLLARQREHDLYKSQQQQKLWLPGSYKTLQGSELLLLGTGSIAKHLAQTAKHFGMKVAGINRSAKATEGFDEVATLEALPTLMARADAIASILPSTEATRGILNENILARMKPDAVLFNLGRGDVLDLDALERQLRQHPQQQAVLDVFNQEPLPEDHPIWGLGNVIVTPHIAAPSFPEQVAEIFSSNYHKFLLGETLSHRVNFERGY Shewanella amazonensis SB2B SB2B 6939103 Sama_3201 Formiminoglutamase (EC 3.5.3.8) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (FORMIMINOGLUTAMASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. arginase/agmatinase/formiminoglutamase (RefSeq) MQHLIIFSAKDMTPILGKRPGETRLGNHFLLPEGPTLVAILESAKAQGARFVLLGVGEDAGPRANLGRGGATNAFEAMLKYLVNLQSNRFYRGDDCLLLGQLDFGDLLPGEDADVDALRAAVAAMDERVIEVASAIMEAGLEPIVIGGGHNNAFGLLMSVKNAFGRPAAAVNLDPHSDFRLREGRHSGNGFSYAAASGALDFYHVLGLHELKNSEANLEQLAAFGGSWHTLQQIWVRGELSLDDALKHIGKTLRATGLPVALELDLDAIANMPSSAMTAAGVPLLDAARYISHIARHCDCAYLHLAEAAPSCHDSGEDAGLRETGQSLTELVYAYIRGRHLALGA Sinorhizobium meliloti 1021 Smeli SM_b20850 SM_b20850 L-lactate dehydrogenase (cytochrome) (EC 1.1.2.3) Specifically important for utilizing L-Rhamnose monohydrate. Automated validation from mutant phenotype: the predicted function (1.1.2.3) was linked to the condition via a SEED subsystem. This annotation was also checked manually. L-lactate dehydrogenase MTQILEIRDLKALARRRVPKLFFDYADSGAWTEGTYRANEEDFAGIKLRQRVLVDMSDRSLETTMIGQKVSMPVALAPTGLTGMQHADGEMLAAQAAEAFGVPFTLSTMSICSIEDVASVTTKPFWFQLYVMREREFVLDLIDRAKAAKCSALVMTLDLQILGQRHKDLRNGLSAPPRLTPKHLWMMATRPGWCMKMLGTNRRTFRNIVGHAKSVADLSSLQAWTNEQFDPQLSWKDVEWIKERWGGPLILKGILDPEDAKMAAKTGADAIIVSNHGGRQLDGAHSSISMLPRIVEAVGDQIEVHLDGGIRSGQDVLKAIALGAKGTYIGRPFLYGLGALGKEGVTLALDIIRKEMDTTMALCGKRRITEVGRDIIAE Sinorhizobium meliloti 1021 Smeli SM_b20899 SM_b20899 Inositol 2-dehydrogenase (EC 1.1.1.18) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (MYO-INOSITOL-2-DEHYDROGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. myo-inositol dehydrogenase MTVRFGLLGAGRIGKVHAKAVSGNADARLVAVADAFPAAAEAIAGAYGCEVRTIDAIEAAADIDAVVICTPTDTHADLIERFARAGKAIFCEKPIDLDAERVRACLKVVSDTKAKLMVGFNRRFDPHFMAVRKAIDDGRIGEVEMVTITSRDPSAPPVDYIKRSGGIFRDMTIHDFDMARFLLGEEPVSVTATAAVLIDKAIGDAGDYDSVSVILQTASGKQAIISNSRRATYGYDQRIEVHGSKGAVAAENQRPVSIEIATGDGYTRPPLHDFFMTRYTEAYANEIESFIAAIEKGAEIAPSGNDGLAALALADAAVRSVAEKRQISIA Sinorhizobium meliloti 1021 Smeli SM_b20984 SM_b20984 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrite reductase [NAD(P)H], large subunit protein MTETAREKLVIVGNGMAPGRMLEELFEKAPGRYAVTIFNAEPRVNYDRIMLSPVLSGEKEYEEIIIHGDGWYIKHGITLYKGHKIIAIDRDAKTVTSDHGVTESYDKLVIATGSVPFIIPVPGKELRGVITYRDLDDVQAMLLAAQSREKAVVIGGGLLGLEAAAGLQARGMDVTVLHVMPTLMERQLDPAAGYLLQKAVEERGIKVVTKANTKRILGEEKVEGIELDDGRIIPATLVVMAVGIRPNAGLAKEAGLAVNRGIVVDAGMQTSDGDIMALGECAEVGGMVYGLVAPLYEMARVAASHLAGDRRAAFAHSDTPTKLKVTGINLYSVGDFADADGREEIVLRDATAGIYKRLVLKDNRIIGTVLYGDTADGAWFNDLLKRGTDISEMRDTLIFGQAYQGGSPLDPTAAVAALPDDAEICGCNGVCKGKIVGAITSKGLTSLDDVRAHTKASASCGSCAGLVEQIMSLTLGDTYNPASVQPMCNCTDLGHDDVRRLIKAKKLKSIPAVMQELEWKTSCGCAKCRPALNYYLVCDWPDEYADDYQSRFINERVHANIQKDGTYSVVPRMWGGVTNSKELRAIADVVDKFNVPLVKVTGGQRIDLLGIEKEDLPAVWADLGQAGFVSGQAYAKGLRTVKTCVGSDWCRFGTQDSTGLGIRIEKFMWGSWTPAKLKMAVSGCPRNCAEATCKDVGVICVDSGFEIHFAGAAGLDIKGTEVLGLVRTEDEALEHIVALTQMYREQARYLERIYKWAKRVGLDEIRRQIMDDVEKRKAYFDRFVFSQKFAQVDPWSERVSGKDKHEFRPMATVGFNQAAE Sinorhizobium meliloti 1021 Smeli SM_b20986 SM_b20986 Nitrate reductase (EC 1.7.99.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.99.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrate reductase, large subunit protein MAQEVKTTCPYCGVGCGVIARVGDDGAVSVKGDPEHPANFGRLCSKGSALAETLDLDGRLLHPEIGGRRAGWSEALDLVAERFSRSIAEHGPDSVAFYVSGQLLTEDYYIANKLMKGFIGSANIDTNSRLCMSSSVAGHRRAFGSDTVPGAYEDLELAELVVLTGSNLAWCHPVLYQRLSAAKANRPEMKIVVIDPRRTMTADIADMHLAIAPDGDVALFNGLLAHLAASGAVDRNYISNYTSGFDEAVAAASRLDLPALSTATGLTVAQLRAFFRLFETTEKVVTCYSQGVNQSAAGTDKVNAIINCHLATGRIGRPGMGPFSLTGQPNAMGGREVGGLANMLAAHMDIEKSLHRDQVRRFWGAPSVASKPGLKAVDMFRAVADGRIKALWIMATNPVVSMPDADAVEAAIKACPFVVVSDIVRDTDTARHAHVLLPSLGWGEKDGTVTNSERRISRQRPFLAAPGEARPDWWQLAEVGRRMGFAAAFTHGSPAVIFAEHAALSGFENEGRRDFDISAHAEIDGPAYDGLRPFQWPQPQGSAPQKKRFFAEGAFYHPDGRARLVAVEVPRPRSANDAFPFTLNTGRVRDHWHTMTRTGKSARLSGHLAEPFVEIHPRDAQGAGISDADLVTLESPHGAAIVRALVTDRQAEGNLFVPMHWNDQFASKARIDALVAPVTDPVSGQPASKNMPVRASRFAAAAYGFAVSARKPRELDAAYWALARAEGGWRVELAFAETNADWLDWCRKTFAIAAGIEPIGYTDRTSGELRLAFFEGDRLLATLFLSPRPVAVARSWAVSQLGASHHNLAKRFAVTAGRPGADTPDPGATVCSCFSVGVNQITAAVRDGCHSVEAVGERLSAGTNCGSCRAEIRGIINGCLTLAAE Sinorhizobium meliloti 1021 Smeli SM_b21009 SM_b21009 Glycerol kinase (EC 2.7.1.30) Specifically important for utilizing Glycerol. Automated validation from mutant phenotype: the predicted function (GLYCEROL-KIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glycerol kinase MGGYILAIDQGTTSTRAIVFDGNQKIAGVGQKEFKQHFPKSGWVEHDPEEIWQTVVSTVKEAIEKSGITANDIAAIGITNQRETVVVWDRETGKPIHNAIVWQDRRTAAFCDKLKKKGLEKTFVKKTGLLLDPYFSGTKLNWLLSNVKGAQVRAAKGELCFGTIDTFLIWRLTGGECFCTDATNASRTLLYNIAENAWDDELTEVLRVPKEMLPEVKDCAADFGVTDPSLFGAAIPILGVAGDQQAATIGQACFKPGMLKSTYGTGCFALLNTGKDMVRSKNRLLTTIAYRLDGETTYALEGSIFVAGAAVQWLRDGLKVIKAAPDTGSLAESADPSQEVYLVPAFTGLGAPHWDPDARGAIFGMTRNTGPAEFARAALEAVCYQTRDLLEAMHKDWRRNGNDTVLRVDGGMVASDWTMQRLSDLLDAPVDRPVILETTALGVAWLAGSRAGVWPNQEAFAKSWARDRRFEPHMDEATRKVKLKGWRSAVKRTLIAA Sinorhizobium meliloti 1021 Smeli SM_b21121 SM_b21121 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (RXN0-2301) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. isovaleryl-CoA dehydrogenase MFEAGLNFALGEEIDALRASVRRFASERIAPLADDADRSNAFPMSLWREMGELGLLGITADEAHGGAGLGYLAHCVAMEEISRASASVGLSYGAHSNLCVNQINRNGKPAQKSRYLPKLISGEHVGALAMSEPGAGSDVVSMKLKADKRGDRYVLNGSKMWITNGPDADVLVVYAKTDPAAGPRGITAFLVEKAFPGFSAGQKLDKLGMRGSNTSELIFTDCEVPEENVLGGVGEGVKVLMSGLDYERVVLSAGPLGIMAACLDVVVPYLHERKQFGQPIGEFQLMQGKLADMYVTMNAARAYVYAVAAACDRGETARKDAAGCILYAAEKATAMALEAIQALGGNGYTNDYPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFAETK Sinorhizobium meliloti 1021 Smeli SM_b21125 SM_b21125 Hydroxymethylglutaryl-CoA lyase (EC 4.1.3.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (HYDROXYMETHYLGLUTARYL-COA-LYASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. hydroxymethylglutaryl-CoA lyase MTSPAKERVTIVEVAPRDGLQNESRLVATEDKIRLVDLLADCGYERIEVTSFVSPRWVPQLADAPAVMAGIVRRPGTRYAALTPNMRGFEAALAAGADEVAIFASASESFSERNINCSIAESIERFRPVAEASRHRGVPLRGYVSCVVECPYEGAIVPAETARVARLLADLGCYEISLGDTIGRGTPEAVDAMLAAALREIDAPKLAGHFHDTSGRALENIAVALERGIRVFDASAGGLGGCPYAPGAAGNVDTLAVNAFLEAQSFATGLDSEKLDRAAAFARSLRSTA Sinorhizobium meliloti 1021 Smeli SM_b21163 SM_b21163 Urocanate hydratase (EC 4.2.1.49) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (UROCANATE-HYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. urocanate hydratase MNNPRHNIREVRSPRGTEISAKSWLTEAPLRMLMNNLDPDVAENPHELVVYGGIGRAARTWADFDRIVASLKDLNEDETLLVQSGKPVGVFRTHKDAPRVLIANSNLVPHWATWDHFNELDKKGLAMYGQMTAGSWIYIGTQGIVQGTYETFVEAGRQHYGGSLKGKWILTGGLGGMGGAQPLAAVMAGACCLAVECNPDSIDFRLRTRYLDEKAETLEEAMEMIERWTKAGEPKSVGLLGNAAEILPEMVRRGIRPDMVTDQTSAHDPINGYLPKGWTMAEWKAKRESDPKAVEKAARASMRDHVEAMLAFWDSGVPTLDYGNNIRQVAKDEGLERAFDFPGFVPAYIRPLFCRGIGPFRWAALSGDPEDIYRTDRKVKELLPDNKHLHNWLDMARERIAFQGLPARICWVGLGDRHRLGLAFNEMVRSGELKAPIVIGRDHLDSGSVASPNRETEAMKDGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGFSQHSGMVICCDGTDDAARRIERVLWNDPATGVMRHADAGYDIAVDCAREKGLRLPGILGE Sinorhizobium meliloti 1021 Smeli SM_b21165 SM_b21165 Histidine ammonia-lyase (EC 4.3.1.3) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (HISTIDINE-AMMONIA-LYASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. histidine ammonia-lyase MTVILRPGSVPLSDLETIYWTGAPARLDAAFDAGIAKAAARIAEIVAGNAPVYGINTGFGKLASIKIDSSDVATLQRNLILSHCCGVGQPLTEDIVRLIMALKLISLGRGASGVRLELVRLIEAMLDKGVIPLIPEKGSVGASGDLAPLAHMAAVMMGHGEAFFAGERMKGDAALKAAGLSPVTLAAKEGLALINGTQVSTALALAGLFRAHRAGQAALITGALSTDAAMGSSAPFHPDIHTLRGHKGQIDTAAALRQLLTGSPIRQSHIEGDERVQDPYCIRCQPQVDGACLDLLRSVAATLTIEANAVTDNPLVLSDNSVVSGGNFHAEPVAFAADQIALAVCEIGAISQRRIALLVDPALSYGLPAFLAKKPGLNSGLMIAEVTSAALMSENKQLSHPASVDSTPTSANQEDHVSMACHGARRLLQMTENLFSIIGIEALAAVQGIEFRAPLTTSPELQKAAAAVRGVSSSIEEDRYMADDLKAAGDLVASGRLAAAVSAGILPKLEN Sinorhizobium meliloti 1021 Smeli SM_b21166 SM_b21166 Imidazolonepropionase (EC 3.5.2.7) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (IMIDAZOLONEPROPIONASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. imidazolonepropionase MPGGVAGARSQRPPPMPILFPCFWPAAPIALSHGSYFSLVIAGIMYIHYWRRRAAPMDGNENPNPARTSLWRNARLATLREELGPLGIIEDGVIAVRGERIVYAGPEAGLPSELARADQVFDCEGRWVTPALIDCHTHIVHGGNRAREFQLRLEGATYEEIARAGGGIASTVEATNALSVEALVEAALPRLDTLLAEGVSTVEVKSGYGLNVEAELKMLRAARRLESLRPVRIVTSYLAAHATPPEFRGRNGDYIAEVVLPGLTAAHAEGLADAVDGFCEGIAFSPAEIASVFGRAKSLGLPVKLHAEQLSDLGGAKLAASYGALSADHLEYLDAAGAAAMAKAGTVAVLLPGAFYTLREKQLPPVEALREAGTRIAIATDCNPGTSPLTSLLLTLNMSATLFRLTLEECLAGVTREAARALGILGETGTIEAGKSADLAIWNIDQPAELIYRIGFNPLRERIFKGERILR Sinorhizobium meliloti 1021 Smeli SM_b21655 SM_b21655 Beta-galactosidase (EC 3.2.1.23) Specifically important for utilizing Beta-Lactose. Automated validation from mutant phenotype: the predicted function (BETAGALACTOSID-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. beta-galactosidase MMRSVTSFNDSWVFSEGFDAADAGTLRAGQPISLPHNAVELPFNYFDERCYQRAFTYQRVLAWRPDFSGREVSLVFDAAMADAVVYLNGEEIVAHRDGYTPFEARLTDRLLEGDNLITVKIDGSENPEIPPFGGRIDYLTYAGIYRDVWLKVTDPVSIANIKIETRDVLSDTKAVSLRCDLSNPQGLSFSGTISALLKNAAGEVLAEVAGETTGQSLAFEMDGLKGLSLWDIDDPVLYVIEVELRTGQGSDCFAAHFGFRTAEFTTEGFRLNGRPLKIRGLNRHQSFPYVGYAMGRTAQERDADIMKHRLHCNLVRTSHYPQSKWFLDHCDRIGLLVFEEIPGWQHIGGEEWKQEAIRNVRRMIERDWNHPSIVIWGVRINESQDSHDFYAETNRLARELDPTRQTGGVRYITDSEFLEDVYTMNDFILGNEELPGANRPRTALRPQQECTGLPRKVPYLITEFGGHMYPTKIYDQEQRQAEHVRRHLEVLNAAYGDPGISGAIGWCMFDYNTHKDFGSGDRICYHGVMDMFREPKFAAYVYASQCDPSEEIVMKPVTFWARGERNIGGVLPLIVLTNCDEIELKYGSLTKRVGPDRENFPHLPHPPVVIDHRHFTKDELGVWGMKWESAEFTGFIAGKPVADLRMAADPVPTTLQVEADSKTLRAEGRDSVRLILRALDQAGNVQPFLNDAVDIEIHGPARLVGPARIVLQGGSAGFWLESTGAAGAIVVSVASSRLGAAKLDLVALADGAASA Sinorhizobium meliloti 1021 Smeli SMc00433 SMc00433 Myo-inosose-2 dehydratase (EC 4.2.1.44) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (MYO-INOSOSE-2-DEHYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. myo-inositol catabolism protein MIRYGTNPIAWSNDDDHSIGAHLTLEDCLSDCRKIGFDGIEKGHKMPSDPEALKQKLSSYDLVFVSGWHSTNLLTHDVEAEKKAIQPHLDLLKHNGCKVAIVCETSNAIHGDDSKSLVKDKPVLPADKWEKFGTDLEAIAEYCAGQGVDLVYHHHMGTIVQTGEEIDLLMRNTGPATKLLLDTGHAWFGGSDPAEVARKYMGRVRHIHCKNVRPAVRKVVEGEGLSFLEGVRRGVFTVPGDEEGGVDFLPVLKTAAEHGYDGWLVIEAEQDSAVRNPFEYQSLGLKSLKTFAREAGLDRA Sinorhizobium meliloti 1021 Smeli SMc00486 SMc00486 Glutaminase (EC 3.5.1.2) Specifically important for utilizing L-Glutamine. Automated validation from mutant phenotype: the predicted function (GLUTAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glutaminase MREPKPQEDLQAIIDDIYRELTPRLGEGKVADYIPQLARVDARHFGMAIVTTGGEVYRVGDAEMPFSIQSISKVFTLTLALGKHGENIWNRVGREPSGSAFNSIVQLEHEGGKPRNPFINAGAIRISDLILAGHTPKELIGEIVRFVRYLADDENIVIDHEVARSETATGYRNIALANFMRSFGRLDHPVEHVLGVYFHHCALAMTCSQLAKAGLFLAAGGTNPLTGHSVVSRQRARRINALMLTCGHYDGSGDFAYRVGLPGKSGVGGGIMAVAPGKASIAVWSPGLNDYGNSLLGSLALEMLAARTGWSVFGP Sinorhizobium meliloti 1021 Smeli SMc00673 SMc00673 Formiminoglutamic iminohydrolase (EC 3.5.3.13) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (FORMIMINOGLUTAMATE-DEIMINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-formimino-L-glutamate deiminase MTASSAHRLFAEQALLPTGWSENVAISVDAAGRILAVEAGQSKAPGDEHLSGPIVPAMANLHSHAFQRAMAGLAEVAGTGDDSFWTWREEMYRTVGLVDPDDLEAIAAKLYVEMLKGGFGRVVEFHYLHHQLDGTPYADPAEMSLRILRAAQTTGIGLTHLPVFYAHANFGGAAPSAGQRPFLHDPDRFLALLERLSPACNATGARLGYAIHSLRAATPEEMREILQSSPLTGPIHIHVAEQPREVEDCLAWSGRRPVEWLLDNMPVDERWCAIHATHMTPDETRRLAHSGAVAGLCPATEANLGDGIFPAVDFVAAGGRFGVGTDSHVATSVAEELRLLEYGQRLRDRRRNRLAAPGASVGRSIFDAALAGGAQAAGQAAGMEEPGIRVGAMADLVVLDGSNPYIAAASGNQILDRWLFALGGDTVRDVMIAGEWKIRNGRHDREEDIDRAFARVLNKLK Sinorhizobium meliloti 1021 Smeli SMc00774 SMc00774 Acetoacetate--CoA ligase (EC 6.2.1.16) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (6.2.1.16) was linked to the condition via a SEED subsystem. This annotation was also checked manually. acetoacetyl-CoA synthetase MQAERPLWVPDREIVERSPMAEFIDWCGERFGRSFADYDAFHDWSVSERGAFWTAVWEHCKVIGESGEKALVDGDRMLDARFFPEARLNFAENLLRKTGSGDALIFRGEDKVSYRLTWDELRALVSRLQQALRAQGIGAGDRVAAMMPNMPETIALMLATASVGAIWSSCSPDFGEQGVLDRFGQIAPKLFIVCDGYWYNGKRQDVDSKVRAVAKSLGAPTVIVPYAGDSAALAPTVEGGVTLADFIAGFQAGPLVFERLPFGHPLYILFSSGTTGVPKCIVHSAGGTLLQHLKEHRFHCGLRDGERLFYFTTCGWMMWNWLASGLAVGATLCLYDGSPFCPDGNVLFDYAAAERFAVFGTSAKYIDAVRKGGFTPARTHDLSSLRLMTSTGSPLSPEGFSFVYEGIKPDVQLASISGGTDIVSCFVLGNPLKPVWRGEIQGPGLGLAVDVWNDEGKPVRGEKGELVCTRAFPSMPVMFWNDPDGAKYRAAYFDRFDNVWCHGDFAEWTPHGGIVIHGRSDATLNPGGVRIGTAEIYNQVEQMDEVAEALCIGQDWEDDVRVVLFVRLARGVELTEALTREIKNRIRSGASPRHVPAKIIAVADIPRTKSGKIVELAVRDVVHGRPVKNKEALANPEALDLFAGLEELKS Sinorhizobium meliloti 1021 Smeli SMc01103 SMc01103 Ribokinase (EC 2.7.1.15) Specifically important for utilizing D-Ribose. Automated validation from mutant phenotype: the predicted function (RIBOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. ribokinase MITVFGSINMDLIATTARLPKPGETVAGTDFSTAAGGKGANQALAARRAGASVRMAGAVGSDAFAEGALALLKEAGTDLDLTKTVGEPTGTAHIIVGGDGENVIVVVASANARVSGDDAANVVAQMSAGDTLMLQLEIPSASVEKALSEAKRRGIRSIINIAPLTPDAARLGRMADIVIANETEFELLAGKAGIAGAEREEAMNGLHAETRQTVIVTLGAEGVVAIHEGELHRAKGLTIEPVDTVGAGDTFCGYLAAGLDAGLAFSEALRRAAIAGSLACLKPGAQPSIPLAAEVAARL Sinorhizobium meliloti 1021 Smeli SMc01815 SMc01815 Dihydropyrimidine dehydrogenase (NADP(+)) (EC 1.3.1.2) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (1.3.1.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. dihydropyrimidine dehydrogenase MADLRNNFVGIKSPNPFWLASAPPTDKAYNVERAFKAGWGGVVWKTLGEEGPPVVNVNGPRYGAIWGADRRLLGFNNIELITDRDLYVNLREMKQVKMNWPDRALIASIMVPCEENAWKAILPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPEYIEMVVRWCKQYTRMPVITKLTPNITDIRKPARAAKAGGTDAVSLINTINSITGVNLDTFSPEPSIDGRGSHGGYCGPAVKPIALNMVAEIARDPETYGLPISGIGGVTTWRDAAEFMALGAGNVQVCTAAMTYGFKIVQEMITGLSDWMDAKGHRTLDDISGRAVPNVTDWQYLNLNYIAKAKIDQDACIKCGRCHIACEDTSHQAITQFVNGVRHFEVIEEECVGCNLCVNVCPVENCITMEPLAAGTLDRRTGKPVDPNYANWTTHPNNPMARQAAE Sinorhizobium meliloti 1021 Smeli SMc01820 SMc01820 Beta-ureidopropionase (EC 3.5.1.6) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (3.5.1.6) was linked to the condition via a SEED subsystem. This annotation was also checked manually. allantoate amidohydrolase MAAPGENRRVNADRLWDSLMEMAKIGPGVAGGNNRQTLTDADGEGRRLFQSWCEEAGLSMGVDKMGTMFLTRPGTDPDALPVHIGSHLDTQPTGGKFDGVLGVLSGLEAVRTMNDLGIKTKHPIVVTNWTNEEGARFAPAMLASGVFAGVHTLEYAYARKDPEGKSFGDELKRIGWLGDEEVGARKMHAYFEYHIEQGPILEAENKQIGVVTHCQGLWWLEFTLTGREAHTGSTPMDMRVNAGLAMARILEMVQTVAMENQPGAVGGVGQMFFSPNSRNVLPGKVVFTVDIRSPDQAKLDGMRARIEAEAPKICERLGVGCSIEAVGHFDPVTFDPKLVETVRGAAEKLGYSHMNLVSGAGHDACWAAKVAPTTMIMCPCVGGLSHNEAEDISREWAAAGADVLFHAVLETAEIVE Sinorhizobium meliloti 1021 Smeli SMc01821 SMc01821 Dihydropyrimidinase (EC 3.5.2.2) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (3.5.2.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. phenylhydantoinase MSTVIKGGTIVTADLTYKADVKVEGGRIVEIGPNLSGAETLDATGCYVMPGGIDPHTHLEMPFMGTYSSDDFESGTRAALAGGTTMVVDFALPSPGQSLLEALTMWDNKSTRANCDYSFHMAITWWGEQVFNEMETIVKDKGINTFKHFMAYKGALMVDDDEMFSSFQRCAALGALPLVHAENGDVVAQLQAKLLAEGNSGPEAHAYSRPAEVEGEAANRAIMIADMAGCPVYVVHTSCEQAHEAIRRARAKGMRVFGEPLIQHLTLDETEYFDKDWDHAARRVMSPPFRNKLHQDSLWAGLASGSLQVVATDHCAFTTEQKRFGVGDFTRIPNGTGGLEDRMPMLWTYGVATGRITMNEFVAVTSTNIAKILNIYPKKGAILVGADADLVVWDPKRSKTISAKTQQSAIDYNVFEGKTVTGLPRFTLTRGVVSIEEGTVKTQEGHGEFVRRDPFPAVSTALSTWKEVTAPRAVQRSGIPASGV Sinorhizobium meliloti 1021 Smeli SMc03163 SMc03163 Xylose isomerase (EC 5.3.1.5) Specifically important for utilizing D-Xylose. Automated validation from mutant phenotype: the predicted function (XYLISOM-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. xylose isomerase MSTGFFGDIAKIKYEGPESTNPLAFRHYNPDDVVLGKRMEDHLRFAVAYWHTFVWPGGDPFGGQTFERPWFKDSMEAAKLKADVAFEFFQLLGVPYYCFHDADVRPEGRNFAENTSNLNAIVDYFAGKQGETGVKLLWGTANLFSNRRFMAGAATNPDPDVFAFAAATVKTCIDATQRLDGENYVLWGGREGYETLLNTDLKRELDQLGRFLNLVVEYKHRIGFKGTILIEPKPQEPTKHQYDYDVATVYGFLKRYGLENEVKVNIEQGHAILAGHSFEHELALANALGIFGSIDMNRNDYQSGWDTDQFPNNVPEMALAYYHVLAGGGFKTGGTNFDAKLRRQSIDPEDLLIGHIGGMDCCARGLKAAAKMIEDKALSAPLEARYAGWNVPEAKKMLDGGFSLEEIEAWVLKSDVNPQPKSGRQELLENVVNRYV Sinorhizobium meliloti 1021 Smeli SMc03164 SMc03164 Xylulose kinase (EC 2.7.1.17) Specifically important for utilizing D-Arabinose and D-Xylose. Automated validation from mutant phenotype: the predicted function (XYLULOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. xylulose kinase MYLGLDLGTSGVKAMLMDGEQRIIGSASGALDVDRPHPGWSEQDPADWIRAAEEAIARLRETHAQALAAVRGIGLSGQMHGATLLDEGDAVLRPCILWNDTRSFREAAALDGDPQFRALTGNIVFPGFTAPKLAWVRENEPEIFARVRWVLLPKDYLRLWLTGEHMSEMSDSAGTSWLDTGKRKWSASLLAATHLEERQMPDLVEGTDAAGTLRPELAARWGMGPGVVVAGGAGDNAASACGMGTVGEGQAFVSLGTSGVLFAANASYLPNPESAVHAFCHALPNTWHQMGVILSATDALNWHSGVTGRSAAELTSELGESLKAPGSVTFLPYLSGERTPHNDATIRGVFAGLGHESSRAVLTQAVLEGVSFAIRDSLEALRAAGTKLKRVTAIGGGSRSRYWLSSIATALNLPVDLPADGDFGAAFGAARLGLIAATGADPAAVCTAPETAETIAPEASLVPAYEDAYQRYRRLYPAIKEAAL Sinorhizobium meliloti 1021 Smeli SMc03203 SMc03203 Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase (EC 2.3.1.168) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (2.3.1.168) was linked to the condition via a SEED subsystem. This annotation was also checked manually. branched-chain alpha-keto acid dehydrogenase E2 subunit MGEFIIKMPDVGEGVAEAELVEWHVKPGDPVREDMVLAAVMTDKATVEIPSPVTGKVLWLGAEVGDTVAVKAPLVRIETAGEAGEAAPDSIPEALAEQVLDEPVAVSSRLEAKAPPQPEKPAPKPAPAPREAPDLSAKPLASPAVRLRARESGIDLRQVAGTGPAGRITHEDLDLFISRGAEPLPAQTGLVRKTAVEEVRMIGLRRRIAEKMSLSTSRIPHITYVEEVDMTALEDLRATMNRDRKPEQAKLTILPFLMRALVKTVAEQPGVNATFDDHAGVIHRHAAVHIGIATQTPAGLTVPVVRHAEARGIWDCAAELNRLADAARTGTATRDELTGSTITISSLGAIGGIASTPVINHPEVAIVGVNKIAVRPVWDGAQFVPRKIMNLSSSFDHRVIDGWDAAVFVQRLKTLLETPALIFVEG Sinorhizobium meliloti 1021 Smeli SMc03204 SMc03204 Dihydrolipoyl dehydrogenase (EC 1.8.1.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (1.8.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. dihydrolipoamide dehydrogenase MKEISCKLLVLGAGPGGYVAAIRAGQLGVNTVIVEKAKAGGTCLNVGCIPSKALIHAADEYHRLRAAASGKGPLGLSLSAPAIDLRRTIAWKDGIVGRLNGGVTGLLKKAGVKAVIGEGRFVDGKTVDVETETGLQRIRAEAIVIATGSAPVELPDLPFGGSVISSTQALALTDVPQTLAVIGGGYIGLELGTAFAKLGSKVTVLEALDRILPQYDADLSKPVMKRLGELGVEVFTRTAAKRLSADRRGLLAEENGRAFEVPAEKVLVTVGRRPVTDGWGLEEIDLDHSGRFIRIDDQCRTSMRGVYAIGDVTGEPMLAHRAMAQGEMVAEIVAGHKRSWDKRCIPAVCFTDPEIVGAGLSPEEARAAGIDVKIGQFPFQANGRAMTTLSEDGFVRVIARADNHLVLGIQAVGHGVSELSATFALAIEMGARLEDIAGTIHAHPTQSEAFQEAALKTLGHALHI Sinorhizobium meliloti 1021 Smeli SMc03879 SMc03879 Acetyl-CoA acetyltransferase (EC 2.3.1.9) Specifically important for utilizing L-Lysine. Automated validation from mutant phenotype: the predicted function (ACETYL-COA-ACETYLTRANSFER-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. acetyl-CoA acetyltransferase MSNPSIVIASAARTAVGSFNGAFGNTLAHELGAAAIKAVLERAGVEAGEVDEVILGQVLPAGEGQNPARQAAMKAGLPQEKTAWGMNQLCGSGLRAVALGMQQIATGDAKVIVAGGMESMSMAPHCAHLRGGVKMGDYKMIDTMIKDGLTDAFYGYHMGITAENVARKWQLTREEQDEFALASQNKAEAAQKAGRFADEIVPFVVKTRKGDVNVDQDEYIRHGATLDSIAKLRPAFDKEGTVTAGNASGLNDGAAAALLMTEAEAARRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVADIELVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGVSKGLATLCIGGGMGVAMCVERL Pseudomonas simiae WCS417 WCS417 GFF1099 PS417_05575 Glycerol kinase (EC 2.7.1.30) Specifically important for utilizing Glycerol. Automated validation from mutant phenotype: the predicted function (GLYCEROL-KIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glycerol kinase MTDIQNKNYIIALDQGTTSSRAIIFDRDANVVCTAQREFAQHYPQAGWVEHDPMEIFATQSAVMVEALAQAGLHHDQVAAIGITNQRETTVVWDKVTGRPIYNAIVWQCRRSTEICQQLKRDGHEQYISDTTGLVTDPYFSGTKLKWILDNVEGSRERARNGELLFGTVDSWLIWKFTGGKTHVTDYTNASRTMLFNIHTLEWDAKMLEILDIPREMLPEVKSSSEIYGRTKSGIAIGGIAGDQQAALFGQMCVEAGQAKNTYGTGCFLLMNTGDKAVKSKHGMLTTIACGPRGEVAYALEGAVFNGGSTVQWLRDELKIINDAHDTEYFAGKVKDSNGVYLVPAFTGLGAPYWDPYARGALFGLTRGVRVDHIIRAALESIAYQTRDVLDAMQQDSGERLKALRVDGGAVANNFLMQFQADILGTQVERPQMRETTALGAAYLAGLACGFWGSLEELRGKAVIEREFEPQLDEAAKEKLYAGWQKAVSRTRDWEPHEGAE Pseudomonas simiae WCS417 WCS417 GFF2146 PS417_10945 Xylose isomerase (EC 5.3.1.5) Specifically important for utilizing D-Xylose. Automated validation from mutant phenotype: the predicted function (XYLISOM-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. xylose isomerase MPYFPGVEKVRFEGPSSDAPLAFRHYDANKLILGKPMREHLRMAACYWHTFVWPGADMFGVGTFKRPWQRSGDPMELAIGKADAAFEFFSKLGIDYYSFHDTDVAPEGSSLKEYRHHFAQMVDHLERHQEHTGIKLLWGTANCFSNPRFAAGAASNPDPEVFAYAAAQVFSAMNATLRLKGSNYVLWGGREGYETLLNTDLKREREQLGRFMRMVVEHKHKIGFKGDLLIEPKPQEPTKHQYDYDSATVFGFLHEYGLEHEIKVNIEANHATLAGHSFHHEIATAVSLGIFGSIDANRGDPQNGWDTDQFPNSVEEMTLATYEILKAGGFKNGGYNFDSKVRRQSLDDVDLFHGHVAAMDVLALALERAAAMVENDRLQQFKDQRYAGWQQPLGQAVLAGEFSLESLAEHAFAHELDPQAVSGRQEMLEGVVNRFIYR Pseudomonas simiae WCS417 WCS417 GFF2325 PS417_11855 Myo-inosose-2 dehydratase (EC 4.2.1.44) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (MYO-INOSOSE-2-DEHYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. xylose isomerase MPAIRIGINPISWSNDDLPALGGETPLSTALSEGKDIGYEGFELNGKFPKDAKGVGDVLRPYDLALVSGWYSSRLARRSVAEEIEAIAGHVELLKHNGATVLVYGEVADSIQGSRIRLIERPRFHSEQAWQDYADKLTELARFTLSQGVRLAYHHHMGAYVESPEDIDQLMRRTGPEVGLLFDSGHCYMGGGEPIEVLRKHIDRVCHVHFKDVRKAVVQLARNQMWSFPDCIVNGTFTVPGDGDIDFAELLDVLLAAQYEGWLVVEAEQDPAVAPSYIYAKKGYDTLRALLNERT Pseudomonas simiae WCS417 WCS417 GFF2329 PS417_11875 Inositol 2-dehydrogenase (EC 1.1.1.18) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (1.1.1.18) was linked to the condition via a SEED subsystem. This annotation was also checked manually. inositol 2-dehydrogenase MSLKLGVIGTGAIGRDHIRRCSQTLLNSQVVAVTDINLEQAAKVVADLNISAEVYADGHALIHSPEVEAVLVTSWGPSHEEFVLAAIAAGKPVFCEKPLAVTAEGCRKIVDAEVAFGKRLVQVGFMRPYDDGYRALKAVIDSGQIGEPLMLHCAHRNPTVGENYKTDMAITDTLIHELDVLRWLLNDDYVSVQVVFPRKSSKALAHLRDPQIVLLETAKGTRIDVEVFVNCQYGYDIQCEVVGETGIAKLPEPSQVQLRSGAKLSNAILMDWKDRFIGAYDVELQAFIDSVRAGQVGGPSAWDGFAAAVAADACIEAQNSEQIVKVSLPDRPHFYG Pseudomonas simiae WCS417 WCS417 GFF2880 PS417_14725 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrite reductase MSQLNTQRNLATWKRVCSESDLVSNSGVVVWLDGAQVALFYLPGAQDQTLYAIDNHDPESGANVIGRGLIGSIKGDLVVAAPIYKQHYRLEDGQCLEAPDQRLRVWPVRLNGGGVELALD Pseudomonas simiae WCS417 WCS417 GFF2881 PS417_14730 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrite reductase MNNLKTLIVVGNGMVGHHCVAQLIERGALDHYRLHVFSEEPMRAYDRVHLSEYFSGRDAESLALSDASLYQTPGVTLHLGVPVLEIDRARCEVITADGCVAYDKLVLATGSYPFVPPIDGAEGDSRLVYRTLEDLDAIRKAAANARRGVVVGGGLLGLEAANALKSLGLEAHVVEFAPRLMPVQLDDFGGLALKAQIERLGVGVHLSRATQSISAGEHYRYRMNFANDEFLETDLIVFSAGIRAQDALARQAGLDIGPRGGVVINDECLSCDPNIYAIGECASWNGSLFGLVAPGYQMARGVAALLCKQTAEPFVGADMSTKLKLLGVDVGSIGDAHAHTPGARSYQFIDEASASYRRLVVDASGKQVIGAVLVGDNSYYDTLLQYMQNGIALPSEPASLILPSAAGAPTLGPGALPESATVCSCHNVTKGAICSAIDSGCSDLGLLKSQTKACTGCGGCAGLLKQVFEHELIARGVSVDKSLCEHFAYTRQELYALVRVEGIITFDELLAKHGRGHTGCDVCKPAVGSILASCWNQPIMDASLVPLQDTNDTFMANMQKNGTYSVVPRIPGGEITADKLIVIGEVAKKYDLYTKITGGQRIDLFGAQLHELPDIWSELIAAGFETGHAYGKSTRTVKSCVGSTWCRYGVQDSVKMALQIEDRYKGLRSPHKLKFAVSGCTRECAEAQSKDVGVIATEKGWNLYIAGNGGMRPRHAELFATDLDDATLIQYIDRFLMFYIRTADKLQRTSVWRESLEGGLDFLKDVILHDSLGLGAELEAQMQQVVDRYECEWANALADPEKLKRFRTFVNDKRPDPDIHFVQERGQRRPIMAAELNLIPVTEEIA Pseudomonas simiae WCS417 WCS417 GFF2882 PS417_14735 Nitrate reductase (EC 1.7.99.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.99.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. reductase MANQSIRSVCPYCGVGCGIVMQVENNKVVKVIGDTAHPTNFGRLCTKGTTCGQAIADSGRMENAYVRQAREHDPVRIGIDKAISETARRLRHILDTHGPQALAFYVSGQMSLEAQYLINKLAKGFVRTHHIESNSRLCMASAGSGYKLSLGADGPPGSYEDFDRADLFFVIGANMADCHPILFLRMMDRVKAGAKLIVVDPRRNATADKANLFLPIKPGTDLALLNGLLHLLVKNGHTDPAFIAAFTDGWEAMPAFLEDYSPEHVAVITGLAEADIRQAADWIGQAAEWMSCWTMGLNQSTHGTWNTNALCNLHLATGAICRPGSGPFSLTGQPNAMGGREMGYMGPGLPGQRSVLVEADRAFIEDLWQIPPDSLPRQAGAGTVGMFEQMAAGQIKACWIICTNPVASVPNRQTVIKGLQTAELVITQDAFLDTETNRYADILLPGALWAEAEGVMINSERNLTLMQKAVDAPGETLPDWQIIARVASEMGFAEAFTYASASEVFEEIKRAWNPKTGYDIRGASYPRLREKPLQWPCASDTAADRNPIRYVDKGPVTFATDNGKAQFLARPHMPPAELPDEAFPFVLNTGRVQHQWHTLTKTGKVATLNKLNPGPFVELHAEDAARLGIKDKDRVEIRSRRGHAVLPAVITDRVRPGNCFAPFHWNDVFGDNLAINAVTNDAVDPISLQPEFKCCAVALARVELIGLQSLDRPSPVAEDTAMSRLDAFAEIAGIRHLSAPPLSDSERTYLAGFLSGLQANAARQAVGIPTMPTNAPLADASRLWLNGLLGALFSPTESLATPSPAVTLLWASQTGNAEALAERFAKRLRDAGISVELSAMSDFPASKLASTHTLALISSTFGDGDPPDNGEGFWHSLSTAETRLESLRFAVLALGDPNYDQFCNHGKQLDQRLLELGATRLLERVDCDTEFEALADAWLVRFQQTLTPAKPVALATPAGKTKLYGSRLLLNRQLNPLSAHKETRQFALDLADSGLTYEAGDALGVRPRNCPELVNELLDLTRLKASTCVNIDTFGDVPLQQALTQHFEIARPSSDTLAFIAERSANPGLKHLLNPEHKAELNDWLWGRQLADVLQEYPIECSADELLGTLKRLQPRLYSIASSAKAHPHEVHLTVAAVRYGKRKGVSSTFLADRVGDGEVPLFVQPSKHFRTPTDGDVPMIMIGPGTGIAPFRAFLQERRALGHQGRNWLFFGEQHAASDFYYQDELQGMQRDGLLSHLSLAFSRDQAQKVYVQDRIREQGAELWRWLQDGAKLYICGDASHMAKDVDQALRHVAQTHGGLGVEGAVDYWRQLSEQKRYLRDVY Pseudomonas simiae WCS417 WCS417 GFF3325 PS417_17015 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (RXN0-2301) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. isovaleryl-CoA dehydrogenase MSYPSLNFALGETIDMLRDQVQSFVSKEIAPRAAQIDRDNLFPADLWQKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNHSQKLKYLPKLISGEHVGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDASTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEENILGTLNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR Pseudomonas simiae WCS417 WCS417 GFF335 PS417_01705 Formiminoglutamic iminohydrolase (EC 3.5.3.13) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (FORMIMINOGLUTAMATE-DEIMINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-formimino-L-glutamate deiminase MSAFFAERALLPNGWANDVRLEVSADGLLIKVEANARAEGAERLRGPVLAGMPNLHSHAFQRAMAGLAEVAGNPNDSFWTWRDLMYRMVGKINPDQLQVIARQLYIEMLKAGYTSVAEFHYVHHDISGQPYADRTELSRQISQAAARSGIGLTLVPVLYTHSGFGGQAPNEGQRRFINSTEHYLDLQAQLKPILAAQPAQQLGLCFHSLRAVTPEQINAVLAASDKACPVHIHIAEQQKEVDDCLAWSGKRPLQWLYDNVEVDERWCLVHATHADADEVARMAKSRAIAGLCLTTEANLGDGIFPAVDFLAQGGRMGIGSDSHVSLSVVEELRWLEYGQRLRDQRRNRLYRGDQPMVGRTLFDAALDGGAQALGQPIGRLEVGKRADWIVLDGNDPYLATATEDGILNRWLFAGGDRQVRDVLVNGKWVVRDGHHAGEEDSNRAFTQVLKDLLD Pseudomonas simiae WCS417 WCS417 GFF338 PS417_01720 Urocanate hydratase (EC 4.2.1.49) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (UROCANATE-HYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. urocanate hydratase MTKPTKYRDVEIRAAHGNKLTAKSWLTEAPLRMLMNNLDPQVAENPKELVVYGGIGRAARNWECYDQIVESLTHLNDDETLLVQSGKPVGVFKTHSNAPRVLIANSNLVPHWASWEHFNELDAKGLAMYGQMTAGSWIYIGSQGIVQGTYETFVEAGRQHYNSDLTGRWVLTAGLGGMGGAQPLAATLAGACSLNIECQQVSIDFRLNSRYVDEQATDLDDALARIAKYTKEGKAISVALLGNAAEILPELVKRGVRPDMVTDQTSAHDPLNGYLPAGWTWDEYRARAKTEPAAVIKAAKQSMAVHVKAMLEFQKQGIPTFDYGNNIRQMAQEEGVENAFDFPGFVPAYIRPLFCRGIGPFRWAALSGDPQDIYKTDAKVKELIPDDAHLHNWLDMARERISFQGLPARICWVGLGQRAKLGLAFNEMVRSGELSAPVVIGRDHLDSGSVASPNRETEAMQDGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGFSQHSGMVIVCDGTDEAAERIARVLHNDPATGVMRHADAGYQIAIDCAKEQGLNLPMIK Pseudomonas simiae WCS417 WCS417 GFF3386 PS417_17330 Dihydropyrimidine dehydrogenase (NADP(+)) (EC 1.3.1.2) Specifically important for utilizing Cytidine. Automated validation from mutant phenotype: the predicted function (1.3.1.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. dihydropyrimidine dehydrogenase MADLSIVFAGIKAPNPFWLASAPPTDKAYNVVRAFEAGWGGVVWKTLGEDPAAVNVSSRYSAHYGPNREVMGINNIELITDRSLEINLREITQVKKDWPDRALIVSLMVPCVEESWKTILPLVEATGCDGIELNFGCPHGMPERGMGAAVGQVPEYVEQVTRWCKTYCSLPVIVKLTPNITDIRVAARAAYRGGADAVSLINTINSITSVDLERMVALPVVGTQSTHGGYCGSAVKPIALNMVAEIARDPQTQGLPICGIGGIGNWRDAAEFVALGCGAVQVCTAAMLHGFRIVEEMKDGLSRWMDSQGYNSLQDFSGRAVGNTTDWKYLDINYQVIAKIDQEACIGCGRCHIACEDTSHQAIASLKQADGTHKYEVIDDECVGCNLCQITCPVADCIEMVPMDTGKPFLNWTQDPRNPYREAV Pseudomonas simiae WCS417 WCS417 GFF3432 PS417_17560 Dihydrolipoyl dehydrogenase (EC 1.8.1.4) Specifically important for utilizing L-Leucine; L-Isoleucine. Automated validation from mutant phenotype: the predicted function (1.8.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. dihydrolipoamide dehydrogenase MTQTLNTTLLIIGGGPGGYVAAIRAGQLGIPTILVEGQALGGTCLNIGCIPSKALIHVAEQFQQTIHHSQGSHLGIEVDVPTLDIRKSVEWKDGIVDRLTTGVAALLKKHKVQVIHGWAKVVDGKTVEVGDQRIQCEHLLLATGSKSVNLPMLPIGGPIISSTEALAPTRVPKRLIVVGGGYIGLELGIAYRKLGAEVSVVEAQDRILPAYDAELTQPVNESLKHLGVKLYLKHSVTGFTDGSLQVRDPNGDTVSLATDQVLVAVGRKPNTQGWNLEALNLEMNGAAIKIDSRCQTSMRNVYAIGDLSGEPMLAHRAMAQGEMVAELISGKHREFNPAAIPAVCFTDPELVVVGKTPDEAKAAGLDCIVSSFPFAANGRAMTLESKTGFVRVVARRDNHLIVGWQAVGVGVSELSTAFGLSLEMGSRLEDVAGTIHAHPTLGEAVQEAALRALGHALHL Pseudomonas simiae WCS417 WCS417 GFF3737 PS417_19130 L-lactate dehydrogenase (cytochrome) (EC 1.1.2.3) Specifically important for utilizing Sodium L-Lactate. Automated validation from mutant phenotype: the predicted function (1.1.2.3) was linked to the condition via a SEED subsystem. This annotation was also checked manually. lactate dehydrogenase MIISSASDYRAAAKRKLPRFLFDYIDGGAYAEHTLRANSSDLAEISLRQRILRNVDNLSLKTTLFGQELDMPVILSPVGLTGMYARRGEVQAAKAAANKGIPFCLSTVSVCPIEEVASQSAQAIWFQLYVLKDRGFMRNALERAQAAGVTTLVFTVDMPTPGARYRDAHSGMSGPFAAQRRMLQAVTKPQWAFDVGLMGRPHDLGNISKYLGKPTHLEDYIGWLANNFDASISWKDLEWIREFWKGPMIIKGILDPQDAKDAVSFGADGIVVSNHGGRQLDGVLSTAKALPPIADAVGDDLTVLVDSGIRSGLDVVRMLALGAKACLLGRATAYALAADGQHGVENLLDIFAKEMRVAMTLTGVTSIAQIDRSTLV Pseudomonas simiae WCS417 WCS417 GFF4076 PS417_20885 Xanthine dehydrogenase (EC 1.17.1.4) Specifically important for utilizing Inosine. Automated validation from mutant phenotype: the predicted function (1.17.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. FAD-binding molybdopterin dehydrogenase MIQFLLNQELRSEHALDPNLTVLNYLREHLGKSGTKEGCASGDCGACTVVVGELHTDDTGAEQIRYRSLNSCLTFVSSLHGKQLISVEDLKHQGQLHSVQKAMVECHGSQCGFCTPGFVMSLFALQKNSDAPDNQKAHEALAGNLCRCTGYRPILAAAEQACCNKPQDQFDSRQAETIARLKAIAPTQTGELNSGDKRCLVPLTVADLADLYDAYPQARLLAGGTDLALEVTQFHRTLPVMIYVGNIEEMKRIDDFDDRLEIGAAAALSDCYTALHHAYPDFGELLHRFASLQIRNQGTLGGNIGNASPIGDSPPLLIALGAQIVLCKGETRRTLALEDYFIDYRVTARQDSEFIEKIIVPKGHALFRAYKVSKRLDDDISAVCAAFNLKIDNGVIGEARVAFGGMAATPKRAKNCEAALVGATWNCATVEKACAALAEDFTPLSDFRASKEYRLLSAQNLLRKYFIELQTPHIETRVTAYV Pseudomonas simiae WCS417 WCS417 GFF4077 PS417_20890 Xanthine dehydrogenase (EC 1.17.1.4) Specifically important for utilizing Inosine. Automated validation from mutant phenotype: the predicted function (1.17.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. xanthine dehydrogenase MSNHHAVVKTQAELAELFAQDLTSGVGRSVKHDSAAKHVCGEAQYIDDRLEFPNQLHLYARMSDRAHARIISIDTAPCYAFEGVRIVITHEDVPGLKDIGPLMPGDPLLAIDTVQFVGQVVLAVAARDLETARKAAMAAVIEYEDLEPVLDVVEAFRKKHFVLDSHTHQRGDSAGALATAKNRIQGTLHIGGQEHFYLETQISSVMPTEDGGMIVYCSTQNPTEVQKLVAEVLDVSMNKIVVDMRRMGGGFGGKETQAASPACLCAVVARLTGQPTKMRLPRVEDMLMTGKRHPFYIEYDVGFDDTGRLHGINLELAGNCGCSPDLSNSIVDRAMFHSDNSYYLGDATVNGHRCKTNTASNTAYRGFGGPQGMVAIEEVMDAIARHLGLDPLAVRKINYYGKNERNVTHYYQTVEHNMLEEMTAELEASSQYAERREAIRLYNAHSPILKKGLALTPVKFGISFTASFLNQAGALIHIYTDGSIHLNHGGTEMGQGLNTKVAQVVAEVFQVEIDRVQITATNTDKVPNTSPTAASSGADLNGKAAQNAAETIKQRLVEFAARKYDVSEADVAFHNGHVRVRDQILTFEALIQQAYFAQVSLSSTGFYKTPKIYYDRSQSRGRPFYYFAFGAACCEVIVDTLTGEYKMLRTDILHDVGASLNPAIDIGQVEGGFIQGMGWLTMEELVWNDKGKLVTNGPASYKIPAVADMPLDLRVKLVENRKNPEDTVFHSKAVGEPPFMLGIASWCAIKDAVASLGDYRHQPKIDAPATPERVLWGCEQMRQLNAARAVEIETEMASL Pseudomonas simiae WCS417 WCS417 GFF4308 PS417_22065 Long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) Specifically important for utilizing Sodium octanoate. Automated validation from mutant phenotype: the predicted function (ACYLCOASYN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. long-chain fatty acid--CoA ligase MNEDFWKDKYPAGIAAEINPDEYPNIQAVLKQSCQRFANKPAFSNLGKTITYGELYELSGAFAAYLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAIRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVVPKTAVKHVIVTEVADLLPPLKRLLINSVIKYVKKMVPAYHLPNAIKFNDVLAKGHGQPVSDASPTSSDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGSNLNEGCEILITPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELSKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKVTLSGGMALQLAAAERWKAVTGCGICEGYGMTETSPVATVNPIQHIQIGTIGIPVPSTVCKVIADDGTELALGETGELCVKGPQVMKGYWQRQDATDEMLDSEGWLKTGDIAIIQPDGYMRIVDRKKDMILVSGFNVYPNELEDVLAGLPGVLQCAAIGVPDEKSGEHIKLFIVVKPGATLTKEQVMEHMRANVTAYKVPKAVEFRDALPTTNVGKILRRELRDEELKKLGLKK Pseudomonas simiae WCS417 WCS417 GFF4367 PS417_22360 Glycine dehydrogenase (aminomethyl-transferring) (EC 1.4.4.2) Specifically important for utilizing Glycine. Automated validation from mutant phenotype: the predicted function (1.4.4.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. glycine dehydrogenase MTVQLTTANEFIARHIGPRQEDEQQMLASLGFDSLEALSASVIPESIKGTSVLGLEDGLSEAEALAKIKAIAGKNQLFKTYIGQGYYNCHTPSPILRNLLENPAWYTAYTPYQPEISQGRLEALLNFQTLISDLTGLPIANASLLDEATAAAEAMTFCKRLSKNKGSNAFFASIHSHPQTLDVLRTRAEPLGIDVVVGDERELTDVSPFFGALLQYPASNGDVFDYRELTERFHAAHGLVAVAADLLALTLLTPPGEFGADVAIGSAQRFGVPLGFGGPHAAYFSTKDAFKRDMPGRLVGVSVDRFGKPALRLAMQTREQHIRREKATSNICTAQVLLANIASMYAVYHGPKGLTQIARRVHQLTAILAKGLTALGQNVEQAHFFDTLTLNTGANTAAVHDKARAQRINLRVVDAERVGVSVDETTTQADIETLWAIFADGKALPDFAAQVESTLPAALLRQSPVLSHPVFNRYHSETELMRYLRKLADKDLALDRTMIPLGSCTMKLNAASEMIPVTWAEFGALHPFAPAEQSAGYLELTSDLEAMLCAATGYDAISLQPNAGSQGEYAGLLAIRAYHQSRGDERRDICLIPSSAHGTNPATANMAGMRVVVTACDARGNVDIEDLRAKAIEHRDHLAALMITYPSTHGVFEEGIREICGIIHDNGGQVYIDGANMNAMVGLCAPGKFGGDVSHLNLHKTFCIPHGGGGPGVGPIGVKSHLTPFLPGHAAMERKEGAVCAAPFGSASILPITWMYISMMGGAGLKRASQLAILNANYISRRLEEHYPVLYTGSNGLVAHECILDLRPLKDSSGISVDDVAKRLIDFGFHAPTMSFPVAGTLMIEPTESESKEELDRFCNAMIAIREEIRAVENGTLDKDDNPLKNAPHTAAELVSEWTHPYTREQAVYPVPSLIEGKYWPPVGRVDNVFGDRNLVCACPSIESYA Pseudomonas simiae WCS417 WCS417 GFF4369 PS417_22370 Aminomethyltransferase (EC 2.1.2.10) Specifically important for utilizing Glycine. Automated validation from mutant phenotype: the predicted function (2.1.2.10) was linked to the condition via a SEED subsystem. This annotation was also checked manually. glycine cleavage system protein T MSTETLLKTPLHALHIELGARMVPFAGYDMPVQYPLGVMKEHLHTRDQAGLFDVSHMGQIRLTGANAAKALETLVPVDILDLPVGMQRYAMFTNDQGGILDDLMVANLGNEELFLVVNAACKDQDLAHLRQHIGDQCTIEPLFEERALLALQGPAAVKVLARLAPEVTKMTFMQFATLRLLGVDCYVSRSGYTGEDGFEISVPAANAESLARSLLAETEVQAIGLGARDSLRLEAGLCLYGHDMNTDTTPIEASLLWAISKARRADGARAGGFPGADTIFTQQQAGVSRKRVGLLPQERTPVREGAQIVDADGTVIGSVCSGGFGSTLGGPLAMGYLDSAFIALDTEVSALVRGKKVPLRVSKMPFVPQRYYRG Pseudomonas simiae WCS417 WCS417 GFF4431 PS417_22685 Glucokinase (EC 2.7.1.2) Specifically important for utilizing D-Trehalose dihydrate. Automated validation from mutant phenotype: the predicted function (GLUCOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glucokinase MKLALVGDIGGTNARFALWRDQELHSIRVHATADHSSPEDAIKVYLKEEGLEIGDIGAVCLSVAGPVSGDEFKFTNNHWRLSKTAFCKTLQVDELLLVNDFSAMALGMTRLKPDEFRVVCEGTPEPLRPAVVIGPGTGLGVGTLLDLGAGRFAALPGEGGHVDLPLSSPRETQLWQHIYTEIGHVSAETALSGGGLPRLYRAICAVDGHTPVLETPEAITAAGLAGDPVAMEVLDQFSIWLGRVAGNNVLTTGGRGGVYIVGGVIPRFADFFINSGFAKSFADKGCMSDYFKGIPVWLVTAPYSGLTGAGVALEQAFA Pseudomonas simiae WCS417 WCS417 GFF4491 PS417_22985 N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (NAG6PDEACET-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-acetylglucosamine-6-phosphate deacetylase MSEDNILTPDGWIRGRLVHEHGKVIAIEGTPCDPAENDLPYLLPGFIDLHVHGGGGADIMEGGAAFETITRTHVRFGTTSLLATTMTAPVEEISRVLGQLGTFCERRPAGSARVLGVHLEGPYINPGKLGAQPNFAHTALMAEVEAYLRLAPIRVITIAPEIAGHDGLIRALSERGVRMQIGHTLGSYEEGVAALAAGATSFTHLYNAMSPLHHREPGIVGAALAHAKFAELIPDLLHVHPGAMRVALRSIPCLYCVTDSTAAAGMPDGEYKLGSHTVTKCLGGVRLADGTLAGSTLTMDQALRNLVKIGLPISEASQRLSQFPADYLGLEERGRLQPGSFADCVRLDRSLTLTDVMVEGETIDFKNA Pseudomonas simiae WCS417 WCS417 GFF4502 PS417_23045 Alpha,alpha-phosphotrehalase (EC 3.2.1.93) Specifically important for utilizing D-Trehalose dihydrate. Automated validation from mutant phenotype: the predicted function (3.2.1.93) was linked to the condition via a SEED subsystem. This annotation was also checked manually. trehalose-6-phosphate hydrolase MQDWQHSVIYQIYPKSFHSHAGNATGDLLGIVDKLDYLKWLGVDCLWITPFLRSPQRDNGYDISDYYAIDPSYGTMADCDLLISEAAKRGIKLMLDIVVNHTSIEHEWFQQARSSLDNPYRDFYIWRDQPNNWESKFGGSAWEYEAQTGQYFLHLFDHTQADLNWDNPKVRAEVFKLMRFWRDKGVGGFRLDVINLISKPADFPEDNTDGRRFYTDGPNVHEYLQEMHREVFEGHDLINVGEMSSTSLEHCIRYSRPESKELSMTFNFHHLKVDYPNLQKWVKADFDFLQLKQIFTDWQLGMQAGGGWNALFWCNHDQPRVVSRFGNDGEHRVVSAKMLATALHFLQGTPYVYQGEELGMTNPGFDRIEQYRDVESLNIFRLKRDAGEPEASSMAAIMQKSRDNGRTPMQWNAGENAGFSTGEPWIGIPANAAQINVESQLDDPDSVLHHYRALIALRRHEPLIQEGVYRPLLQDHLRVWAYLREGHGERLLVLNNFYGTPCEIQLPDNVINPAREQRVLISNYPDCPQRTATVTLRPYESFVLHLTD Pseudomonas simiae WCS417 WCS417 GFF4622 PS417_23650 Kynureninase (EC 3.7.1.3) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (KYNURENINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. kynureninase MTTRSHCQALDAQDPLAPLRSQFALPEGVIYLDGNSLGARPVAALARAQAVIAEEWGNGLIRSWNNAGWADLSLRLGNRLAPLIGARDNEVAITDTTSINLFKVLSAALTVQRQRQPGRKVIVSEASNFPTDLYIAEGLAELLQQGYSLRLVNSPDELPQAIDQDVAVVMLTHVNYKTGYMYDMQALTALSHECGALSIWDLAHSAGAVPIDLHQAGADYAIGCTYKYLNGGPGSQAFVWVNPALVDVVRQPLSGWFGHTRQFAMESTYAPSAGIARYLCGTQPITSLAMVECGLEIFAQTDMASLRSKSLALTDLFIALVEARCAAHDLKLITPREHAKRGSHVSFEHPEGYAVIQALIARGVIGDYREPRIMRFGFTPLYTRFTEVWEAVEILGDILDNHTWNQPQFKVRNSVT Pseudomonas simiae WCS417 WCS417 GFF4624 PS417_23660 Catechol 1,2-dioxygenase (EC 1.13.11.1) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (CATECHOL-12-DIOXYGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. catechol 1,2-dioxygenase MSIRLSQTAHAQQFLEEASGNLNDGGNPRTKALVYRILRDTVNIIEDLEVTPEEFWKAVNYLNELGKHQEAGLLAAGLGLEHYLDLLMDAADEKAGKSGGTPRTIEGPLYVAGAPLSKYEARLDDGKDDAVPLFMRGQVRDTEGKPLAGAIVDVWQANTAGTYSWFDPTQSEFNLRRRIETDAQGNYRFRSIVPSGYGCPPSGPTQQLLDQLGRHGQRPAHIHFFISAPGHRHLTTQINLSDDPYLHDDFAYATRDELIAQIRFSDDPQLAREFGVEGRFAQIDFDFELQVADAPVEQKRMQRVRALED Pseudomonas simiae WCS417 WCS417 GFF4625 PS417_23665 Muconolactone isomerase (EC 5.3.3.4) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (MUCONOLACTONE-DELTA-ISOMERASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. muconolactone delta-isomerase MLFHVKMTVNLPLDMNPERAAGLKAEEKALAQRLQQEGKWRHLWRIAGHYANYSVFDVDSVQELHDLLMQLPLYPYMAIEVNALCRHPSSIHEDDR Pseudomonas simiae WCS417 WCS417 GFF4626 PS417_23670 Muconate cycloisomerase (EC 5.5.1.1) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (MUCONATE-CYCLOISOMERASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. muconate cycloisomerase MPICAIESIDTIIVDLPTLRPHKLAMHTMQNQTLVIIRLRCADGIEGIGEATTIGGLSYGNESPDSIKVNIDRHFAPLLIGQDASNINAAMLRLERSIRGNTFAKSGIESALLDALGKRLNLPVSELLGGRVRDALPVAWTLASGNTEKDIAEAEKMLDLRRHRLFKLKIGAGEVSHDLAHVIAIKKALGDRASVRVDVNQAWDEAVALRACKVLGDNGIDLIEQPISRNNRGGMARLNLSSPAPIMADESIECVEDAFNLAREGAASVFALKIAKNGGPRAVLRTAAIAEAAGIGLYGGTMLEGGIGTLASAHAFLTLNKLAWDTELFGPLLLTEDILTEPPVYRDFQLHVSTAPGLGLAIDEERLAFFRRDKH Pseudomonas simiae WCS417 WCS417 GFF4630 PS417_23690 Anthranilate 1,2-dioxygenase (deaminating, decarboxylating) (EC 1.14.12.1) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (1.14.12.1-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. benzene 1,2-dioxygenase MNAQLQYQIEQFFYRKSELCDAQDWDAYVQLFDPQSEFHLPQWDSEHVYTRDPKREMSLIYYANRSGLEDRVFRLRTGKAASATPMPRTLHLINNVRIAEQADGTLEVRLNWHTLFYRLATSEQFYGHATYRLKPDGDSWLITRKHALLLNDTINSVLDFYHL Pseudomonas simiae WCS417 WCS417 GFF4633 PS417_23705 Tryptophan 2,3-dioxygenase (EC 1.13.11.11) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (RXN-8665) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. tryptophan 2,3-dioxygenase MSQCPFSADYQPPEEWHNAELNFSESMSYGDYLDLGKVLSAQHPLSPDHNEMLFIIQHQTSELWMKLMLHELKAAREHVRLGELPPAFKMLARVSRIFDQLVHAWAVLATMTPSEYKSIRPFLGQSSGFQSFQYREIEFILGNKSAALLRPHAHRPELLNELKVAIATPSLYDEAINLMIQAGLAIDPKRAERDPTAATVHDESVEAAWREVYRDPSRYWDLYQLAEKFIDLEDSFRQWRFRHVTTVERIIGFQPGTGGTEGVGYLRKMLDTVLFPELWRVRSTL Pseudomonas simiae WCS417 WCS417 GFF4634 PS417_23710 Kynurenine formamidase, bacterial (EC 3.5.1.9) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (ARYLFORMAMIDASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. kynurenine formamidase MNPIKTWWDISPPLSTATPTWPGDTPFQEERVWQFGPECPVNVGRITLSPHTGAHVDAPLHYSADGAPIGEVSLDVYMGPCRVLHCLDSGALVQPHQLEGRVDKLPERVLLRTYPQAPLTEWDSNFTAVAPQTIELLASLGVRLIGIDTPSLDPQQSKTMDSHNAVARHGMAILEGIVLDDVPEGDYELIALPLRFANLDASPVRAILRPLKEPTR Pseudomonas simiae WCS417 WCS417 GFF547 PS417_02785 Urease (EC 3.5.1.5) Specifically important for utilizing Urea. Automated validation from mutant phenotype: the predicted function (3.5.1.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. urease subunit alpha MKISRQAYADMYGPTVGDKVRLADTELFVEVEKDFTVYGEEVKFGGGKVIRDGQGQSQLLAHEVVDTLITNALIIDHWGIVKADVGLKNGRIHAIGKAGNPDIQPGVTMSIGASTEVIAGEGMILTAGGIDSHVHFICPQQIEEALTSGVTTMIGGGTGPATGTNATTCTSGPWHLARMLQASDSFPMNIGFTGKGNASLPEPLIEQVKAGAIGLKLHEDWGTTPASIDNCLSVADQYDVQVAIHSDTLNESGFVETTLAALKGRTIHTYHTEGAGGGHAPDIIKACGFPNVLPSSTNPTRPFTRNTIDEHLDMLMVCHHLDPSIAEDVAFAESRIRRETIAAEDILHDLGAFSMISSDSQAMGRVGEVITRTWQTADKMKKQRGALPGDGPGNDNFRAKRYIAKYTINPAITHGVSHIVGSIEVGKWADLVLWRPAFFGIKPTLILKGGAIASSLMGDANASIPTPQPVHYRPMFASFGGSLHATSLTFISQAAQDAGLPEALGLKKQIAVVKGCRDVQKTDLIHNDYLPDIEVDPQTYQVKADGVLLWCEPADVLPMAQRYFLF Pseudomonas simiae WCS417 WCS417 GFF826 PS417_04195 5-dehydro-4-deoxyglucarate dehydratase (EC 4.2.1.41) Specifically important for utilizing D-Galacturonic Acid monohydrate. Automated validation from mutant phenotype: the predicted function (4.2.1.41) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 5-dehydro-4-deoxyglucarate dehydratase MNPQELKSILSHGLLSFPVTDFNAQGDFHQAGYIKRLEWLAPYGATALFAAGGTGEFFSLAASEYSQVVKTAVDTCATSVPILAGVGGSTRQAIEYAQEAERLGAKGLLLLPHYLTEASQDGVAAHVEAVCKSVKIGVVVYNRNVCRLTAPLLERLAERCPNLIGYKDGLGDIELMVSIRRRLGDRFSYLGGLPTAEVYAAAYKALGVPVYSSAVFNFIPKTAMDFYHAIAKDDHATVSKIIDDFFLPYLDIRNRKAGYAVSIVKAGAKIVGYDAGPVRTPLTDLLPEEYEALAALIDKQGAQ Pseudomonas simiae WCS417 WCS417 GFF829 PS417_04210 Galactarate dehydratase (EC 4.2.1.42) Specifically important for utilizing D-Galacturonic Acid monohydrate. Automated validation from mutant phenotype: the predicted function (4.2.1.42) was linked to the condition via a SEED subsystem. This annotation was also checked manually. galactarate dehydrogenase MQLIEHADSPRSIRLHERDNVVIVVNDQGVPAGTEFPDGLVTVDFIPQSHKVTLEDIPEGGQIIRYGQTIGYALAPIPRGSWVQEDQLRMPTAPPLDSLPLSTEVPEAQAPLEGFTFEGYRNADGTVGTRNILGITTTVQCVTGVLDHAVKRIKDELLPKYPHVDDVVALTHSYGCGVAITATDAYIPIRTVRNLARNPNLGGEALVISLGCEKLQAGQVMHDNDSSVDLSEPWLYRLQDSSHGFTEMIEQIMALAETRLKKLDQRRRETVPASELILGMQCGGSDAFSGITANPALGYASDLLLRAGATVMFSEVTEVRDAIYLLTSRAENTQVAQELVREMDWYDRYLAKGEADRSANTTPGNKKGGLSNIVEKSLGSIVKSGSSAINGVLGPGERFKGKGLIFCATPASDFVCGTLQLAAGMNLHVFTTGRGTPYGLAMAPVVKVSTRTELAQRWPDLIDIDAGRIATGRATIEELGWELFHFYLDVASGRKQTWAEHHKLHNDITLFNPAPIT Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_1015 Aromatic-amino-acid aminotransferase (EC 2.6.1.57) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (PHEAMINOTRANS-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Aromatic-amino-acid aminotransferase (EC 2.6.1.57) MQFADRLNNVETSAIRELFKLLGKPGIISFAGGFPDSAMFDVEGIRAASNAALAEEPGAALQYGATEGYNPLREQLAAFMTSKGAKDVAADNLIVTTGSQQALDLLGKTLISPGDKVIVEGPTFLATIQCFRLYGAELISAPIDGNGVKTDELEKLIAEHKPKFVYLIPTFGNPSGAMLSLERRKAVLEMAVKHNTLIVEDDPYGDLYFGDAPPPSLLNLSATVPGSRELLVHCGSLSKVLSPGLRVGWMIAPAELLGKATMCKQFSDAHTSTFAQATAAQYLKAGRMPGTLANVRKVYAERAQAMGDALRKELGDAIEFVQPQGGLFVWARLTGAGGKVADGNVLAKRAIEKGVAFVPGTPFFCANPDHATFRLSFATADVDKIREGVARLGQAV Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_1140 2-methylisocitrate dehydratase (EC 4.2.1.99) Specifically important for utilizing Sodium propionate. Automated validation from mutant phenotype: the predicted function (4.2.1.99) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Aconitate hydratase (EC 4.2.1.3) @ 2-methylisocitrate dehydratase (EC 4.2.1.99) MATSRKSSPQPARHAFANTLKSFRTASGKDGQFYSLPALAKQFPEIKRLPVSIRIVLESVLRNCDGRKVTPEHVEQLARWAPNAERKDEIPFVVSRVVLQDFTGVPLLADLAAMRSVAAKLGKNPKKIEPLVPVDLVVDHSIMIDHYGKKNSLDLNMKLEFQRNRERYEFMKWGMQAFDTFGVVPPGFGIVHQVNLEYLARGVHKRKDGVFYPDTLVGTDSHTTMINGIGVVGWGVGGIEAEAAMLGQPVYFLTPDVVGFEMTGRLREGVTATDLVLTVTELLRKHKVVGKFVEFFGEGTRTLALPDRATIGNMAPEYGATMGFFPVDEKTIDYFQGTGRTKAEIEAFEAYFKAQGLFGVPLAGEVDYSQVVTLDLGSVTPSLAGPKRPQDRIELGQVSRQFADLFSQPAAHNGFNRPAELLHTRFHIHRAAEVVADVTPDGKPTPAGAPRSVVEMEANKPALATAHAEARSATLPARGADPTVGNGDVLIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLKVQPHIKTSLAPGSRIVTEYLSETGLLPYLEKLGFSIAGYGCTTCIGNAGDLTPELNEAITQNDLVCAAVLSGNRNFEARIHPNLKANFLASPPLVVAYAIAGTVLKDLMTEPVGQGKGGKDIYLGDIWPSSDEVHALLKFAMKGKAFRDNYAKVATDPGKLWEKIQGVSGTAYTWPASTYIAEPPFFAQFALEKGANKASGTRGEGQKDAQLPSVMGARIMALFGDSITTDHISPAGSIKESSPAGQWLLQHGVQKADFNSYGARRGNHDVMVRGTFANVRIKNLMIPPTADGSREEGGVTVFQNEGALQGEKMFIFDAAMQYMAQGTPTVVFAGEEYGTGSSRDWAAKGTQLLGIKAVVARSFERIHRSNLVGMGVLPLQFKAGDSWETLGLTGNEVIDVLPDPALTPQSDARLVIRRADGTVREVVVTLRIDTPIEVDYYRAGGILPFVLRQLLEG Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_1623 L-lactate dehydrogenase (cytochrome) (EC 1.1.2.3) Specifically important for utilizing Sodium D,L-Lactate; Sodium L-Lactate. Automated validation from mutant phenotype: the predicted function (1.1.2.3) was linked to the condition via a SEED subsystem. This annotation was also checked manually. L-lactate dehydrogenase (EC 1.1.2.3) VPDLSKITCIEDLRAIAQRRVPRMFYDYADSGSYTEGTYRANESDFQRIKLRQRVAVNMEGRSTRTTMVGQDVAMPVAIAPTGLTGMQHADGEILGAKAAKAFGIPFTLSTMSICSIEDIAEHTGRHPFWFQVYVMRDRDFIERLIDRAKAANCSALQLTLDLQILGQRHKDIKNGLSAPPKPTIANLINLATKPRWCLGMLGTKRRSFGNIVGHAKGVGDLSSLSSWTAEQFDPQLNWGDVEWIKKRWGGKLILKGIMDAEDARLAVNSGADALIVSNHGGRQLDGAPSSIAALPGIADAVAQMGGGIEVWMDGGIRSGQDVLKARALGAQGTLIGRSFLYGLGAYGEAGVTRALQIIQKELDITMAFCGHTNINTVDRSILLPGTYPV Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_1847 Phenylalanine 4-monooxygenase (EC 1.14.16.1) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (1.14.16.1) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Phenylalanine-4-hydroxylase (EC 1.14.16.1) VRKVMAAKEKKMGQAPVVYGQSTRPPRGDYSRANADYTCPQDYAAYTDADHDTYRRLYERQRALLPGLASQAFIDALPSLGASDQIPRFEEVNERLYKATGWELVGVPGLIPEVPFFTLLANRQFPVTDWIRKPEEFEYIVEPDIFHDLFGHVPLLFNPVFADYVQRYGQGGLKAQGLGSCEMLSRLYWYTIEFGLIREAGELRAYGAGILSSSGELAYSVQSPEPQRIPLALERTMRTRYKIDTYQQTYFVIDSFEQLFEMTAADFAPIYERLRGLPEFAADEREAVAA Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_1849 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (1.13.11.27) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) MTFINECRRHPMNAALPQETAAQLQAWDNPMGLMGFEFVEFTSPQPGVLEAVFEKLGFTLVAKHRSKDVVLYRQNGINFILNREPHSQAAYFGAEHGPSACGLAFRVKDAHKAYNRALELGAQPIEIPTGPMELRLPAIKGIGGAPLYLIDRFEDGKSIYDIDFEFIEGVDRRPAGHGLNLIDHLTHNVYRGRMGFWANFYEKLFGFREIRYFDIQGEYTGLTSKAMTAPDGKIRIPLNEESKQGGGQIEEFLMQFNGEGIQHIALICDNLLDVVDKLGMAGVQLATAPNEVYYEMLDTRLPGHGQPVPELQSRGILLDGTTADGTPRLLLQIFSTPMLGPVFFEFIQREGDYRDGFGEGNFKALFESLERDQIRRGVLNA Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2306 Maleylacetoacetate isomerase (EC 5.2.1.2) Specifically important for utilizing L-tyrosine disodium salt. Automated validation from mutant phenotype: the predicted function (MALEYLACETOACETATE-ISOMERASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Maleylacetoacetate isomerase (EC 5.2.1.2) @ Glutathione S-transferase, zeta (EC 2.5.1.18) MQLYNYFRSSASFRVRIALQIKGLAYDYLPVHLVKGEHKAPEYASRIGDALVPTLVTDGGTALSQSMAIIEYLDETHPTPALLPATPLARARVRALAQMVACEIHPINNLRVLKYLVRDLKVDEDAKNAWYRHWVRSGLEAFERQFALLAQERAAQGLAPSVLCWGDTPTLADCCLVPQIFNGQRFNVNLDGLPLTMGAFEACMALPAFQQAQPSACPDFEA Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2548 N-formylglutamate deformylase (EC 3.5.1.68) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (N-FORMYLGLUTAMATE-DEFORMYLASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-formylglutamate deformylase (EC 3.5.1.68) MTTTPPPFTFHQGTAPLLVSMPHAGTYVPPVLAARFTDEARQVPDTDWHMERLYAFAKDMGASILVATHSRYVVDLNRPPDGASLYPGQSVTGLCPVDTFDDTPIYAQGDVPDDAEVAARRDAVWAPYHAQLRAELSRIRAQHGVAVLWDAHSIRSVLPRFFEGKLPDLNLGTADGASCDPALAQALLAIAQSAPGYTGVLNGRFKGGHITRHYGQPAQNIHAVQLEMTQCSYMQEALPFDYLPEVAAEVQPHLERLLEAALAFAAARRK Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2549 Formiminoglutamic iminohydrolase (EC 3.5.3.13) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (FORMIMINOGLUTAMATE-DEIMINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Formiminoglutamic iminohydrolase (EC 3.5.3.13) MSEPLQRQLFAADALLPTGWARDVLVAWDGAGRITAVTPNAQPNGAAVAPGPLLPGMPNLHSHAFQRAFAGLTEYRGESQDSFWSWRNLMYRFAARITPESLEAIATWLYVEMLEAGYTSVCEFHYVHHDQDGRPYADDATLSLALLRAAKSAGIGITLLPVLYQTSGFGAKPPRADQARFIRSTDNMLSLLERLAPATRALGGILGLAPHSLRAVPPDSLAAAVQGLTALNPQAPIHIHIAEQTQEVEDCIAWSGQRPVQWLLEHAPVDERWCLVHATHMTPQEYADAARTGAVAGICPTTEANLGDGIFDMPLWLQHGGRWGVGSDSHACVNAAEELLMLEYGQRLSLRQRNVLASRSQAEVATAMTLQAVQGGAQASGRSVSGLAVGQQADLVALDARHVALAGLPAPSMLSSHVFGSHRTSAIDSLWVAGVLRVAQGRHALHDAAAQAFVAARSTTIAAD Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2550 Imidazolonepropionase (EC 3.5.2.7) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (IMIDAZOLONEPROPIONASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Imidazolonepropionase (EC 3.5.2.7) VGRQMQHMDNHGHPSGSAASQNADGVWHNLQPAPGLWVADVAVPEGQPACVVVQQGQMAWVGPEAQLPAAYKALSRHDARGALATPGLVDCHTHLVYGGQRANEFAMRLAGATYEEVAQAGGGIVSSVKATRAASEDELFAQAAPRLQALLDEGVCAIEIKSGYGLALEHERKQLRVARRLGEVFGVTVRTTFLGAHALPSEYAGRSGDYTDLVCNEMLPALAAEGLVDAVDVFCERIAFTLAETEQVFQAAQKLGIPVKLHAEQLSDMGGSALAARYGALSCDHIEHLSADGIAAMKAAGTVAVLLPGAYYTLRDTHLPPIAQLREAGVPMAVSTDHNPGTSPALSLLLMANMACTLFRLTVPEALAGITTHAARALGLQDSHGLIASGRPANFVLWPVGEAAELAYWFGQKPACTIVRQGCIHGVMP Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2557 Urocanate hydratase (EC 4.2.1.49) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (UROCANATE-HYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Urocanate hydratase (EC 4.2.1.49) MNANDAIIAAASNTDPRHDASRVIRAPRGSQLTCKSWLTEAAYRMIQNNLDAEVAERPQDLVVYGGIGRAARNWECYDQILASLKDLNDDETLLIQSGKPVGVFKTHANAPRVLLANSNLVPKWANWEHFSELDQKGLFMYGQMTAGSWIYIGTQGIVQGTYETFAEAGRKHYGGSLEGKWILTAGLGGMGGAQPLAATFAGAVSLNIECQQSSIDFRLRTRYVDKQARDIDHAFELIQQHTAAKEAVSIALLGNAAEILPELVRRAKAGGLKPDLVTDQTSAHDLVNGYLPAGWTVAQWRAAQQDVTQHEVLKKAAAKSCAVHVQAMLDFQHMGIPVVDYGNNIRQVAFDEGVKNAFDFPGFVPAYIRPLFCEGKGPFRWVALSGDPEDIRKTDAKIKELFPENKHVHRWLDMAGERIAFQGLPARICWLGLGERHIAGLAFNEMVKNGELKAPIVIGRDHLDTGSVASPNRETEGMKDGTDAVSDWPLLNALLNTSGGATWVSLHHGGGVGMGYSQHSGMVIVADGTDAAAQRLANVLVNDCGSGVMRHADAGYELAVETAKKQGLKLPMVK Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2558 Histidine ammonia-lyase (EC 4.3.1.3) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (HISTIDINE-AMMONIA-LYASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Histidine ammonia-lyase (EC 4.3.1.3) MTHNASSLTLHPGRVTLAELRRIHAGPVQLVLDASARAGLQKSLATVQRIVDEDQVVYGINTGFGKLASTKIAHERLAELQRNLVLSHSVGTGDPLPDDVVRLILATKAVSLARGHSGVRPELVDALLALANANVLPVIPAKGSVGASGDLAPLAHMACVLIGEGQAKVDGKVVPGAEAMRSIGLQPFVLGPKEGLALLNGTQVSTALALAGLFGAESVFSAALVAGCLSLEAIKGSVKPFDARIHEARGQAGQIAVAAAVRALLDGSAIDPSHPHCGRVQDPYSIRCVPQVMGACLDNLHHAARVLTIEANAASDNPLVFDNGDVISGGNFHAEPVAFVADIIALAVAEIGAISERRLSLLLDPGLSGLPAFLIRDSGVNSGFMIAQVTAAALAAENQCLANPSSVTSLPTSANQEDHVSMATYGARRLGDMVRNAAVMVGIEAMAAAQGMEFDRSLKSSPLIEAQFAAIRERVAYLEQDRYLAPDIEAMRAWAQQSTWPAALTQCLPSFA Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2831 Isocitrate lyase (EC 4.1.3.1) Specifically important for utilizing Tween 20. Automated validation from mutant phenotype: the predicted function (ISOCIT-CLEAV-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Isocitrate lyase (EC 4.1.3.1) MPQSLNEQLSREQQIAALEKDWATNPRWKGVKRGYSAADVVRLRGSLPIEHTLAKRGAEKLWDKINGGAKKGYVNAFGAISAGQAMQQAKAGLEAVYLSGWQVAADGNTSETMYPDQSLYAYDSVPTMVRRINNTFKRADEIQWGRGINPGDKEFIDYFLPIVADAEAGFGGVLNAFELMKNMIQSGAAGVHFEDQLAAVKKCGHMGGKVLVPTQEACEKLISARFAADVMGVSTIVLARTDAEAANLITSDHDANDKPFLTGERTQEGFYRVKNGLEQAISRGVAYAPYADLVWCETGVPDIGFAREFAQAVHAACPGKLLSYNCSPSFNWKKNLNDKQIASFQEDLSALGYKYQFITLAGIHINWFNTFQFAHAYANGEGMKHYVNMVQEPEFAARDKGYTFVSHQQEVGAGYFDDVTTVIQGGSSSVKALTGSTEEEQFH Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2850 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) Specifically important for utilizing L-Proline. Automated validation from mutant phenotype: the predicted function (1.2.1.88, 1.5.5.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Transcriptional repressor of PutA and PutP / Proline dehydrogenase (EC 1.5.99.8) (Proline oxidase) / Delta-1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12) MTLPTAPFADFAPRTPLANPLRAAITAAITAATRHPEPEALAPLLAQARLPADQAAAAEQLALRIAKALRERKASAGRAGIVQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISHGQWDAHLGKSPSLFVNAATWGLLITGKLVATHSEGSLGNSLSRLIGKGGEPLIRKGVDMAMRMMGEQFVTGETIDEALRNARTMEAEGFRYSYDMLGEAALTSEDAKRYYSSYEQAIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQFGRVMDELYPLVLRLTALAKQYDIGLNIDAEETDRLELSLDLLERLCHEPTLAGWNGIGFVIQAYQKRCPFVIDCVVDLARRTQRRLMVRLVKGAYWDSEIKRAQVDGLKDYPVYTRKVHTDISYIACAKKLLAAPEAVYPQFATHNAETVATIYQLAGSNYYAGQYEFQCLHGMGEPLYEQVVGAITAGKLGREIGKGGLGRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADETIALDELVKSPVQVVDQQAATEGTAGLPHPRIPLPAALYGAHRSNSRGLDLSNENTLTELAATLQATASHAWTAAPLLAADVPAGTTQPVRNPADHNDVVGQVQEATTADVDQALVHAQAAATSWAATPPAERAAALLRTADLLEERIQPLMGLLMREAGKSASNAVAEVREAVDFLRYYAAQVQSTFDNATHIPLGPVACISPWNFPLAIFMGQVAAALAAGNPVLAKPAEQTPLIAAEAVRLLWQAGVPRAAVQLLPGQGETVGARLIGDARVMGVMFTGSTEVARILQRTVAGRLDAAGRPIPLIAETGGQNAMIVDSSALVEQVVGDAVSSAFDSAGQRCSALRVLCVQEEAADRVVEMLQGAMGELRVGNPGELRVDVGPVIDAEAQAGIAQHIEKFKAQGHRVFQHPNHVSAISAPGTFVPPTLIELNHIGELQREVFGPVLHLVRYARSDLDQLLDQINATGYGLTQGVHTRIDETIARVVNRAHAGNVYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLLRLLSQRPADALARTFAEADRTSPHDTERRERHLAPLATLQQWAHNQGNLALAGHCQRFAQETQSGTSRTLPGPTGERNVYTLAPRARVLCLAHSVDDLLVQTAAVLASGGTALWPHAHAGLRAKLPTHVQAQVMLQDNTLSDGSVALDAVLHHGDAPSLQAVCTTLARRPGPIVGVTALQPGAADIPLERLLIERALSVNTAAAGGNASLMTIG Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2954 Dihydropyrimidine dehydrogenase (NADP(+)) (EC 1.3.1.2) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (1.3.1.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Dihydropyrimidine dehydrogenase [NADP+] (EC 1.3.1.2) MADIRSNFLGIQSPNPFWLASAPPTDKEINVTRAFEAGWGGVVWKTLGEDPAVVNVNGPRYSTLMSQDRRVIGLNNIELITDRPLQTNLEEIKRVKRNWPDRAMIVSLMVPCEEQSWKAILPLVEDTGADGIELNFGCPHGMSERGMGAAVGQVPEYIQMVTAWCKHYSKLPVIVKLTPNITDVRQPARAAKAGGADAVSLINTINSIMGVDLDRMVMSPSTDGWGSHGGYCGPAVKPIALNMVAEIARDAQTAGLPISGIGGITTWRDAAEYIALGCGTVQVCTAAMVYGFKIVQDMCDGLSNFMDEHGYATLDDFKGQAVPTVKDWKNLNLNHIEKAVINQDACIQCGRCHVVCEDTSHQAITFTKEGGVRKFEINEAECVGCNLCVSICPVPECITMRALEPGEVDVRTGKKVTGEYANWTTHPNNPQRVSAAA Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2956 Dihydropyrimidinase (EC 3.5.2.2) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (3.5.2.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Dihydropyrimidinase (EC 3.5.2.2) MTQALVIRGGTVVNADREQRADVLCVDGRIVAVGDGAAAQAPAGAQVLDASGQYVLPGGIDPHTHMQLPFMGTVTMDDFFTGTAAALAGGTTSIIDFVIPDPQEPILDAYRKWRGWAEKSAADYSFHVAITWWSEQVRADMGTLVQQEGVNSFKHFMAYKNAIMCDDETLVNSFKRALELGAMPTVHAENGELVYLLQQEVAKMGITGPEGHPLSRPPMVEAEAANRAIAIADVLGVPIYVVHVSCMESADAIARARARGQRVYGEVLAGHLLVDDSVYRDPDFAKAAAYVMSPPFRPKGHQEALWRGLQSGQLHTTATDHCTFCAAQKAMGKENFAKIPNGTGGVEERMAALWDGGVNTGRLTPSEFVAITSANAAKLFNIYPRKGFIGEGADADLVLWDPQGTKTFSAKTQFSKGDFNIFEGRTVRGIPTHTVSQGRVVFSNGDLRAEQGKGRYIKRPAFGANFQAVQKRAQDLAPAAVARS Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2991 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (RXN0-2301) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) MSIPANLPGLNFQLGEDIDALRDAVRDFAQAEIAPRAADIDKSDQFPMDLWRKMGDLGVLGITVPEQYGGAAMGYLAHMVAMEEISRASASVGLSYGAHSNLCVNQINRNGNEAQKAKYLSKLISGEHVGALAMSEPGAGSDVISMKLKAEDKGGYYLLNGSKMWITNGPDADTLVVYAKTEPELGARGVTAFLIEKGMKGFSIAQKLDKLGMRGSHTGELVFQDVEVPAENVLGGLNQGAKVLMSGLDYERAVLTGGPLGIMQSVMDNVIPYIHDRKQFGQSIGEFQLIQGKVADMYTVLQAGRSFAYTVAKNLDMLGTDHVRQVRKDCASVILWCAEKATWMAGEGVQIYGGNGYINEYPLGRLWRDAKLYEIGAGTSEIRRMLIGRELFAETC Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2994 3-ketoacyl-CoA thiolase (EC 2.3.1.16) Specifically important for utilizing L-Isoleucine. Automated validation from mutant phenotype: the predicted function (METHYLACETOACETYLCOATHIOL-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 3-ketoacyl-CoA thiolase (EC 2.3.1.16) MSTTIQDPIVIVGAARTPMGSLQGDFSSLAAHDLGGAAIKAAIERAGVSPDAVGEVLFGNCLMAGQGQAPARQAAFKGGLPKGAGAVTLSKMCGSGMKAAMMAHDMLLAGSHDVMVAGGMESMTNAPYLLQKGRGGYRLGHDRIFDHMMLDGLEDAYEAGRSMGTFGEDCAAKYSFTREQQDAFATASVQRAKAATESGAFAAEIVPVTVKTRAGETVVSVDEGPGKVKLEKIATLKPAFKKDGTITAASSSSINDGAAALVMMRESTAKKLGAKPLARIVSHATHAQEPEWFATAPLGATQKALAKAGWQVGDVQLWEINEAFAVVPMALMKELDLPHDKVNVNGGACALGHPIGASGARIMVTLIHALKARGLTKGLATLCIGGGEATAVALELV Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2996 2-methyl-branched-chain-enoyl-CoA reductase (EC 1.3.8.5) Specifically important for utilizing L-Isoleucine. Automated validation from mutant phenotype: the predicted function (2-METHYLACYL-COA-DEHYDROGENASE-RXN) was linked to the condition via a SEED subsystem. A more specific reaction was selected manually. Butyryl-CoA dehydrogenase (EC 1.3.99.2) MLLTQDQEMIRDAVRDFAQTELWPHAARWDKEHHFPKDAHQGLAALGAYGICVPEEFGGANLDYLTLALVLEEIAAGDGGTSTAISVTNCPVNAILMRYGNAQQKRDWLTPLARGEMLGAFCLTEPHVGSDASALRTTAVKQGDEYVINGVKQFITSGKNGQVAIVIAVTDKGAGKKGMSAFLVPTNNPGYVVARLEDKLGQHSSDTAQINFDNCRIPAENLIGAEGEGYKIALGALEGGRIGIAAQSVGMARSAFDAALAYSKERESFGTAIFNHQAVGFRLADCATQIEAARQLIWHAAALRDAGKPCLKEAAMAKLFASEMAERVCSAAIQTLGGYGVVNDFPVERIYRDVRVCQIYEGTSDVQKIIIQRALA Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_3009 Acetoacetate--CoA ligase (EC 6.2.1.16) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (6.2.1.16) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Acetoacetyl-CoA synthetase (EC 6.2.1.16) / Long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) VTSSAAATNSAPLVDSHARGATDVPLIEQTIGAFFADMVARQPEREALVSVHQGRRYTYAQLQTEAHRLASALLGMGLTPGDRVGIWSHNNAEWVLMQLATAQVGLVLVNINPAYRTAEVEYALNKVGCKLLVSMARFKTSDYLGMLRELAPEWQGQQPGHLQAAKLPQLKTVVWIDDEAGQGADEPGLLRFTELIARGNAADPRLAQVAAGLQATDPINIQFTSGTTGFPKGATLTHRNILNNGFFIGECMKLTPADRLCIPVPLYHCFGMVLGNLACFTHGATIVYPNDGFDPLTVLQTVQDERCTGLHGVPTMFIAELDHPRFAEFNLSTLRTGIMAGSPCPTEVMKRVVEQMNLREITIAYGMTETSPVSCQSSTDTPLSKRVSTVGQVQPHLEVKIVDPDTGAVVPIGQRGEFCTKGYSVMHGYWGDEAKTREAIDEGGWMHTGDLATMDAEGYVNIVGRIKDMVIRGGENIYPREIEEFLYRHPQVQDVQVVGVPDQKYGEELCAWIIAKPGTQPTEDDIRAFCKGQIAHYKVPRYIRFVTSFPMTVTGKIQKFKIRDEMKDQLGLEEQKTA Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_3034 Fructokinase (EC 2.7.1.4) Specifically important for utilizing D-Fructose. Automated validation from mutant phenotype: the predicted function (2.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Fructokinase (EC 2.7.1.4) MVFPIQTADSIPANTAPPLRVATAGEALFDLIEEPDGRLQPCAGGAVYNLTRALGLQGVGTLYLNPLSGDLLGRQLARGLHDAGVALAAPTPVRAPSALALAALDAEGKASYSFYRDGVADRQVTAAALTAACSALPELQVVATGCLALVAQDAALYLPWLAAQRAAGRMVVVDANLRLSAVDDADAYRANVMAALQHAHLIKVSDDDLEALAIPGANALERAHFLQQQTQAQWLALTLGPNGAWLLQRDGLAVHAREEAPITVVDTVGAGDCFLAGLITAWLAGPERGEDALALRAGGLTAPVTEARLRAVLHHALASASHCVERAGCTPPRYEEVRERLSLRRAATTR Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_4848 D-alanine dehydrogenase (EC 1.4.99.-) Specifically important for utilizing D-Alanine. Automated validation from mutant phenotype: the predicted function (DALADEHYDROG-RXN) was linked to the condition via a SEED subsystem. A more specific reaction was selected manually. D-amino acid dehydrogenase small subunit (EC 1.4.99.1) MKTIVLGAGIIGISTAWHLLERGHEVIVIDRQPDAALETSFANAAQISVSYCEPWANREAPLKALKWMFDKEAPLLFRPQMDWQQWRWGLQFLAQCNDTAFERNVQQIVALGAYSHAALKDLVGTTGIEYNRLERGIAHFYTDQKSFDAAGHAVELMRKHGVQRRLVSRDELLQIEPAFRAYGDKITGGTYTSTDESGDARVFTQELARRCIARGAQFLYGHDVLRLNKIGNAIDSVAVMARQPGGGGKKDFILKADAVVVACGSYSAPLLRSVGVDLPIYPGKGYSATFPLLRPEGAPMVSTIDDGKKIAMSRLGNHLRVAGTIELNGWDLTLDSSLARARCHMLSRRIEAILPGVCDTRTPEEGGDPQYWTGLRPATPTNIPFIGRTRVGKLWVNAGHGTLGWTHGAGSGKALAELISGQVPAMNFGFCGMEQGNRTLTAKVA Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_612 2-ketoglutaric semialdehyde dehydrogenase (EC 1.2.1.26) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (25-DIOXOVALERATE-DEHYDROGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 2-ketoglutaric semialdehyde dehydrogenase (EC 1.2.1.26) MKLGDLQLSPRHLINGRWEIGTTTGISTNPSDTREVVAEYARADRNQTELAVRAAADALPTWSQSTPQRRADVLDMIGSELLARKDELGALLAREEGKTLPEGVAEVARSGQIFKFFAGEALRIQGELLASVRQGVQVDVTREPVGVVGIIAPWNFPFAIPAWKIAPALAYGNTVVFKPAELVPACGWALAEIISRSGLPAGAFNLIMGSGREVGQTLVDHPLVNALSFTGSVATGDRILRAASQRRAKVQLEMGGKNPLIVLADADLDQAVDCALQGSYFSTGQRCTASSRLIVEAEVHDAFVARLRNRLASLKVGHALERGTEMGPVVDDNQLAQNLGYIDIAKSEGAEHVWGGERLERPTPGHYMSPALFLARPEHRVAREEIFGPVACVLRADDYDHALALANDTPFGLCAGICTTSLKRAMHFKRHAAVGMTMVNLPTAGVDFHVPFGGRKESSYGAREQGRYAAEFYTTVKTGYMLA Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_701 Arginase (EC 3.5.3.1) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (ARGINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Arginase (EC 3.5.3.1) VDTRTVHKGHGGLISPRTVHWHPKPRECPGATARAAAWPLPLSTPAQKALTMPPNTLRSAQPTSLIGAPTDIGAGARGASMGPEALRVAGLQAALELHGLQVFDRGNLGGPSNPWLPPVNGYRHLPEVAQWNRLVYDAVYAELQLGHLPILLGGDHSLGLGSISAVARHCAESGKKLRVLWLDAHADFNTSELTPSGNVHGMPVACLCGFGPAELTQLAAMPGGGPALRPEQIRQIGIRSVDAGEKRFVHEQGLEVFDMRAIDEVGMRQVMERALAGMDAHTHLHVSFDVDFLDPDIAPGVGTTVPGGPTYREAQLCMEMIADSGRLASLDIVELNPALDVRNKTAVLAVDLVESLFGKSTLMRTRPV Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_929 L-serine ammonia-lyase (EC 4.3.1.17) Specifically important for utilizing L-Serine. Automated validation from mutant phenotype: the predicted function (4.3.1.17) was linked to the condition via a SEED subsystem. This annotation was also checked manually. L-serine dehydratase (EC 4.3.1.17) MSVSVFDLFKIGIGPSSSHTVGPMIAARQFACHVQGTLGLDAVHHVTVELFGSLSATGVGHGTDKAVLLGLAGHEPDHIDPDQILPAIADIRTRQTLALLGEHPVPFVEKEHLLFRRKSLPLHPNGMAFHAFDAQGNEIATREYYSVGGGFVIDAAGERVLNSAATAGPDAVGHAQGLPHPFRTGAELLAQCQATGLTPAQLMAANEQHWRSASEVRRQLMAIWKTMAGAVQRGCASTGTLPGPMHVRRRAAELHHKLSSAPEAALRDPLSMLDWVNLYAMAVNEENAAGGRVVTAPTNGAAGVIPAVLHYYVNFLPGANEDGIATFLLTAGAIGIIYKENASLSGAEVGCQGEVGVACSMAAGALAAVMGGSPEQIENAAEIGMEHNLGMTCDPVGGLVQIPCIERNAMGAIKAINAARMALRGDGQHVVSLDKVIKTMMQTGADMKVKYKETSRGGLAVNVVEC Azospirillum brasilense Sp245 azobra AZOBR_RS06555 AZOBR_RS06555 Branched-chain-amino-acid transaminase (EC 2.6.1.42) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (2.6.1.42) was linked to the condition via a SEED subsystem. This annotation was also checked manually. GntR family transcriptional regulator VTVDWGNVFAGRVAGMGASEIRELLKLLERPEIISFAGGIPDPDFFPTAAIARAYEKIFQSNSGAGGALQYTISEGFTPLREWICAYLGRRGIQAGLDEVLVTSGSQQALEFVGKLLIGPGEKILVTRPTYLGALQAFSPYEPQYLSVPGDAEGPDLAAVEAALEQKPKFFYLVPDFQNPNGTTISLARREALLDLCAKHGVPIVEDAAYTELRYEGEPIPSMVALDAARNGGKITNVLFCGSFSKTMVPALRVGWINGPAEVINRLVLMKQAGDLHTSTINQIVLHDVVSQNFDSHIRRLRAGYKERRDAMLTALSEFAPAGVTWTKPEGGMFVWIELPEGTDGVDLLARAIKDANVAFVPGSAFHADRSGKNTLRLSFSNNNPERIREGIRRLCGLLQTVAA Azospirillum brasilense Sp245 azobra AZOBR_RS08020 AZOBR_RS08020 D-alanine dehydrogenase (EC 1.4.99.-) Specifically important for utilizing D-Alanine. Automated validation from mutant phenotype: the predicted function (DALADEHYDROG-RXN) was linked to the condition via a SEED subsystem. A more specific reaction was selected manually. D-amino acid dehydrogenase small subunit MRVIVLGSGVIGVSTAYFLAKAGHEVTVVDRQPGPALETSYANAGEVSPGYSAPWAAPGLMAKAVKWMLMKHSPLVIRPKMDPAMWSWCLKLLANANERSYEINKGRMVRLAEYSRDCLRVLRDETGIRYDERAKGTLQVFRTQKQVDAAATDMAVLDRFKVPYSLLDVEGCAAVEPALRLVKEKIVGGLLLPGDETGDCFRFTNALAAMATELGVEFRYNTGIRKLESDGRRVTGVVTDAGTLTADSYVVAMGSYSPTLVKPFGLDLPVYPVKGYSLTLPIVDAAGAPESTVMDETHKIAVTRLGDRIRVGGTAELTGFDLTLRPGRRGPLDHVVSDLFPTGGDLSKAEFWTGLRPNTPDGTPIVGPTPVRNLFLNTGHGTLGWTMAAGSGRVVADVVGGRQTEIDMDGLTVARYGRSAAAASRPTVGGVARPAA Azospirillum brasilense Sp245 azobra AZOBR_RS18565 AZOBR_RS18565 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrite reductase MSTHTNPPTPRERLVVVGNGMAGIRTLEELLAKAPDRYDITVFGAEPHPNYNRIMLSPVLAGEKTFEQIVLNGRDWYEANGIRLLTGDRVEVIDRANCTVTAISGLTVPYDKLLIATGSTPVIIPVPGSTLTGVVGFRDLADVDTMLEAAARGGRAVVIGGGLLGLEAANGLKVKGMDVTVLHLMDTLMERQLDRSAGALLRHELERRGITVLTGADTAEIVGSEKVSAVRLKNGQELPADLVVMAVGIRPNTTLGKAAGLACGRGIQVDDAMTTSDPAILSVGECVEHRGQTYGLVAPLFEMAKVAAARLAGSAEAAYTGSVTSTKLKVTGVDVFSAGDFTGGKDCEDIVFRDAARGVYKRVVVKENRILGAVLYGDTKDGGWYFQMLKDGTEVAPVRDTLIFGQSFGGEGAANPKAAVAALPDSAEICGCNGVCKGTIVTAITEKGLSSLDEVRAHTKASASCGSCTGQVEQLLALTLGDGYAGEAKAKPMCKCTDRTHDEVRRAITALDLKTIPDVMQRLEWRTPDGCHHCRPALNYYLLCEWPGEYKDDSRSRYINERVHANIQKDGTYSVVPRMWGGLTSAKELRAIADVVDKFAIPTVKVTGGQRIDLFGVKKEDLPAVWADLNAAGMVSGHAYAKGLRTVKTCVGSEWCRFGTQDSTGLGVKLERMTWGTWTPHKVKLAVSGCPRNCAEATIKDLGVVCVDSGYELHVGGNGGMHVRACDLLVKVETEAEVLEYTGAYMQLYREEARYLERTAPWVERVGLDHIRRRLVDDAEGRAALNARFLFSQSFSQDDPWAERANGSVDRHEFAPLAQVG Azospirillum brasilense Sp245 azobra AZOBR_RS23695 AZOBR_RS23695 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) Specifically important for utilizing L-Proline. Automated validation from mutant phenotype: the predicted function (1.2.1.88, 1.5.5.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. transcriptional regulator IDTRTAPPSAAPGEAAPFADFAPPIRPATELRAAITAAYRRPEPECLPFLFEQASLPPGVITAAAATARKLITALRAKPRGRGVEGLIHEYSLSSQEGMALMCLAEALLRIPDHATRDALIRDKIAGGDWQAHLGKGGSMFVNAATWGLLITGKLTSAGGEQALSSALTRLIARGGEPLIRRGVDFAMRMMGEQFVTGQTIQEALTNARTMEAEGFRYSYDMLGEAALTAEDAARYYADYVNAIHAIGTASAGRGVYEGPGISIKLSAIHPRYSRAQADRVMDELLPRVKALALLAKGYDIGLNIDAEEADRLELSLDLMESLCFDPDLAGWNGIGFVVQAYGKRCPYVIDFLIDLARRSGHRLMIRLVKGAYWDSEIKRAQLDGLPDFPVYTRKVYTDVSYVACARKLLAAPEAVFPQFATHNAQTLATIYEMAGSDFQVGKYEFQCLHGMGEPLYKEVVGPLKRPCRIYAPVGTHETLLAYLVRRLLENGANSSFVNRIADPAVPVDELVADPVAVARAIAPTGAPHALIALPRNLYAPERANSAGIDLSDETELARLSAALSASAEMTWTAAPLLADGERAGQAQPVRNPADRRDVVGSVTEASEALVAEAFGHAVAAASAWAATPPEERAASLFRAADTMQERMPTLLGLIVREAGKSLPNAIAEVREAIDFLRYYGAQVRDRFDNATHRPLGPVVCISPWNFPLAIFSGQIAAALAAGNPVLAKPAEETPLIAAEAVRILHAAGIPAGALQLLPGAGEVGAALVGHEAVRGVMFTGSTEVARLIQRQLAGRLLPDGAPIPLIAETGGQNAMIVDSSALAEQVVGDVIASAFDSAGQRCSALRILCLQEDVADRTLAMLKGAMRELRIGNPDRLAVDVGPVISEEARATIAAHIEAMRAKGRNVEFLPLPAETADGTFIAPTVIEIGGIHELEREVFGPVLHVVRFHRDDLDALVDSINATGYGLTFGLHTRIDATIERVTGRIGAGNVYVNRNTIGAVVGVQPFGGHGLSGTGPKAGGPLYLSRLLSRRPKGWLEFRGPDAARAAGLAYGEWLRAKGFTAEASRCAGYVARSAIGGGAELNGPVGERNLYELHGRGRVLLLPQTRTGLLLQLGAVLATGNSAAVDAPPDLAELLRGLPPALAARVRTTADWRDVGPLAAVLVEGDRERVTAINRRVADLPGPILLVQAATAEALAAGRGEGYDLDLLLNERSVSVNTAAAGGNASLVAMS Pseudomonas stutzeri RCH2 psRCH2 GFF1051 Psest_1084 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (1.3.8.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Acyl-CoA dehydrogenases MNYSSLNFALGETIDMLREQVQAFVAAEIAPRAEAIDQENLFPADMWRKFGEMGLLGVTVSEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNPEQKARYLPKLISGEHVGALAMSEPNAGSDVVSMKLRAEKRGDRYVLNGSKTWITNGPDANTYVIYAKTDLDKGAHGITAFIVERDWKGFSRGNKFDKLGMRGSNTCELFFDDVEVPQENVLGAENGGVKVLMSGLDYERVVLAGGPTGIMQSCLDVVVPYIHDRKQFGQSIGEFQFIQGKVADMYTQLNASRAYLYAVAQACDRGETTRKDAAGVILYTAENATQMALQAIQILGGNGYINEFPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFNESR Pseudomonas stutzeri RCH2 psRCH2 GFF1148 Psest_1181 Glyoxylate carboligase (EC 4.1.1.47) Specifically important for utilizing Glycolic Acid. Automated validation from mutant phenotype: the predicted function (GLYOCARBOLIG-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glyoxylate carboligase MARMRAIDAAVAVLRKEGIDTAFGIPGAAINPLYSALRADGSIRHILARHVEGASHMAEGYTRTKAGNIGVCIGTSGPAGTDMITGLYSAWADSIPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVLIDLPFDVQMAEIEFDIETYEPLAVYKPAATRKQIEKAIDMLCAAERPLIVAGGGIYNAGAEALLVEFAETVGVPVIPTLMGWGSIPDDHPLMAGMCGLQTSHRYGNANMLASDFVLGIGNRWANRHTGSVEVYTKDRTFVHVDIEPTQIGRVFSPDFGITSDAGAALALFVEVAKERKAAGQLPDRTPWAADCQERKRTMLRKTHFDSVPMKPQRVYQCMNNAFGKDACYVSTIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVVAADPTRKVVALSGDYDFQFMIEELAVGAQFKLPYIHILVNNAYLGLIRQSQRGFEMDYCVQLGFENINADQSGMEGYGVDHVAVVEGLGCKAIRVFRQEDLRPAIEQAQAWMAEYRVPVVIEVILERVTNIAMGTEIDAINEFEPLAERREDAPTAVGLLD Pseudomonas stutzeri RCH2 psRCH2 GFF1302 Psest_1335 Long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) Specifically important for utilizing Tween 20. Automated validation from mutant phenotype: the predicted function (ACYLCOASYN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Acyl-CoA synthetases (AMP-forming)/AMP-acid ligases II MTDNFWKDKYPVGVSSEINPDEYQNIQAVLKQSCERFADKPAFSNLGKTLTYGELYKLSGDFAAYLQQNTDLQPGDRIAVQLPNLIQYPIVVFGAMRAGLIVVNTNPLYTAREMEHQFNDAGAKALVCLANMAHLAEEVLPKTGIKHVVITEVADMLPPLKRMLVNAVVKHVKKMVPAYSLPKAVKLNDALALGRGKPVREALPKSDDVAVLQYTGGTTGVAKGAMLTHRNIVANMLQCKALMGSNLNDGSEVLIAPLPLYHIYAFTFHCMAMMLSGNHNILISNPRDLPAMIKDLGKYRFSGFVGLNTLFVALCNSEDFRKLDFSALKVTLSGGMALQLATAERWKQVTGCPICEGYGLTETSPVASVNPIEHIQLGSIGIPVPSTQFKVINDDGQDLAQGEIGELCIKGPQVMKGYWQRPEATDEVIDAQGWFKTGDIGVIQEDGYIRIVDRKKDMILVSGFNVYPNELEDVLASLPGVLQSAAIGVPDEKSGEAIKLFVVVKPGESLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEELRKLGHKK Pseudomonas stutzeri RCH2 psRCH2 GFF1888 Psest_1928 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrite reductase [NAD(P)H], large subunit MKKLKLVMIGNGMAGVRTLEELLKLTNELYDITVFGAEPHPNYNRILLSPVLAGEQQFEEIVLNDLNWYAENDIHLKLNCKVVKIDRVKRRVIADDGSEAEYDRLLIATGSNPFILPIPGKDLQGVIGYRDIADTQVMMETAKTHKHAVVIGGGLLGLEAANGLKLRGMDVTVVHIGDWLMERQLDKTAGTLLQSALESRGLKFLLPKHTAELLDNGEGRVCAVKFKDGEVVPADLVVMAAGIRPNSELAEQAGIPCNRGILVNDTLQTYDPRIYAVGECANHRGTAYGLVAPLFEQAKVCANHLAMLGFSRYLGSVTSTKLKVTGIDLFSAGDFIGGDGTETITLSDPIGGVYKKLVIKDDVLVGACLYGDTADGGWYFRQVREGQNVGQIRDHLMFGEGAIGDAGHQGQSKAMSMPDDMEVCGCNGVCKGTIVKAIQEHGLFSVDEVKKHTKAASSCGSCAGLVEQILINTVGGAADVKPKSEKAICGCSDLNHGQVRKAIREHHLTSIPAAMAFMEWRTPNGCATCRPALNYYLISTWPGEAKDDPQSRFINERAHANIQKDGTYSVIPRMWGGVTNAAELRRIADVADKYQVPMVKVTGGQRIDLLGIRKEDLPGVWKDLDMPSGHAYGKSIRTVKTCVGSEFCRFGTQNSTQMGIDLEHALFNMWSPHKVKLAVSGCPRNCAESGIKDVGIIGVDSGWELYIGGNGGIKTEAGEFFVKVKTAEEVMEYSLAFLQLYREEAFYLERTVHYMQRVGMDHIKKAVLNDAERRKALHQRLLFSLSFEQDPWQEQLSKPQLKKEFDRIAVKQLENA Pseudomonas stutzeri RCH2 psRCH2 GFF1903 Psest_1944 NAD-specific glutamate dehydrogenase (EC 1.4.1.2), large form Specifically important for utilizing L-Glutamic acid monopotassium salt monohydrate. Automated validation from mutant phenotype: the predicted function (GLUTAMATE-DEHYDROGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. NAD-specific glutamate dehydrogenase MAFFSAASKADFQQQLQTALAQHVDSKILPQLNLFAEQFFGIVALPELTERRMSDLVGSTLASWRLLERFEPSTPEVQVFNPDFEKHGWQSTHSVVEVLHPDMPFLVDSVRMELTRRGYSIHTLQTSVLQVRRAADGSLLELLPKDERAADSHAESLIFVEIDRCASPSALRELEQSLLGVLADVRQVVGDFAAMKGKAVELQGRLEQVNLSIDGDELDEIRDFMRWLADDHFTFLGYEEFSVQEQADGGRIFYDESSLLGLSRTMRTGLSEEEQSLTAQSMSYLREPLLLSFAKAAMPSRVHRPAYPDFVSVREFDEAGRVVRECRFLGLFTSSVYTQSVRRIPFIRRKVETVVQRANFGSSAHLAKELVQVLEVLPRDELFQAPIDELFENAIAIVQIQERNRLRLFLRFDPYRRFCYCLVYVPRDSYSTETRLKIQQVLQERLEASDCEFSTYFSESVLTRVQFILRLDPSRAVQVDPVRLEQEVLQACRTWQDDYQSLVVERFGEAKGTHLLSEFPKGFPAGYRERFSPQSATVDMQHVLDLSEERPLVMSFYQPITAEENRLHCKLYHLNTPLPLSDILPIMENLGLRVLGEFPFRLRNRSGREYWIHDFAFTYAEGLEIDLLEINEALQDAFIHIYGGAAENDAFNRLVLTAGLAWREVALLRAYARYLKQIRMGFDLGYIASALLNHTDIARELVRLFKMRFYLARKLGDEDLADKQQRLEQAILSALDDVAVLNEDRILRRYLALIQATLRTNFYQPDANGRPKPYFSFKLDPRAIPEMPRPAPMYEIFVYSPRVEGVHLRGGKVARGGLRWSDREEDYRTEVLGLVKAQQVKNAVIVPGGAKGGFVPRRLPTTGTRDDIQAEAIACYRIFISGLLDITDNLREGQVAPPANVLRYDGDDPYLVVAADKGTASFSDIANGIAAEYDFWLGDAFASGGSAGYDHKKMGITARGAWVSVQRHFRERGINVQSDVISVIGIGDMAGDVFGNGLLMSETLQLVAAFNHLHIFIDPNPDPARSFLERKRLFDLPRSSWTDYDASLISEGGGIFPRSAKRVQISPQMKERFAIEADQLTPAELINALLKAPVDLLWNGGIGTYVKSSSESHAEVGDKANDAVRVNGAELRAKVVGEGGNLGMTQLGRVEYALHGGSSNTDFIDNAGGVDCSDHEVNIKILLNEVVSAGDMTAKQRNQLLFEMTDAVAELVLQNNYKQTQALSQAQHRSRERAAEYVRLINALEAAGQLDRALEFLPSDEALAERASIGKGLTRPELSVLISYSKIELKKALLDSRVPDDDYLAREMDSAFPQQLAEHFRAAMLQHRLKREIVATQIANDLVNNMGITFVQRLNEATGMSAANVAGAYVIVRDIFHLPHWFRQIEALDHKVPAELQLSLMDELMRLGRRATRWFLRNRRSELDAARDVAHFGPRVAALGLKLDELLQGSTRDHWQERYRRYTEAGVPELLARMVAGTNHLYTLLPILEAADETGQVPAQVAAAYFAVGGALELPWYLHQLTNMPVGNNWQALAREGFRDDLDSQQRSITVSVLQMENGAESISERVDAWLAQRPVPLARWRSMLAELRNASGNDYAIYAVASRELQGLAQSARHG Pseudomonas stutzeri RCH2 psRCH2 GFF1971 Psest_2014 Isocitrate lyase (EC 4.1.3.1) Specifically important for utilizing Sodium butyrate and Tween 20. Automated validation from mutant phenotype: the predicted function (ISOCIT-CLEAV-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Isocitrate lyase MSAYQDDIKAVAALKEQYGSSWAAINPESVARMRAQNRFKTGLEIAQYTADIMRKDMAEYDADSSVYTQSLGCWHGFIGQQKLISIKKHLKTTNKRYLYLSGWMVAALRSEFGPLPDQSMHEKTAVSDLIEELYTFLRQADSRELDLLFTALDAAREAGDNAKAAEIQNQIDNYETHIVPIIADIDAGFGNPEATYLLAKRMIEAGACCIQIENQVSDEKQCGHQDGKVTVPHADFLAKIAAVRYAFLELGIDNGVIVARTDSLGAGLTKQIAVTKEPGDLGDLYNSFLDCEEVSEAALGNGDVVIKREGKLLRPKRLPSNLFQFRAGTGEARCILDCITSLQNGADLLWIETEKPHVGQIAAMVDEIRKTIPNAKLVYNNSPSFNWTLNFRQQVFDAFVAEGKDVSAYDRAKLMSVEYDETELAQVADEKIRTFQRDGSAHAGIFHHLITLPTYHTAALSTDNLAKGYFADQGMLAYVKGVQRQELRQGIACVKHQNMAGSDIGDNHKEYFAGEAALKASGKDNTMNQFH Pseudomonas stutzeri RCH2 psRCH2 GFF2231 Psest_2276 Aldehyde dehydrogenase (EC 1.2.1.3) Specifically important for utilizing Ethanol. Automated validation from mutant phenotype: the predicted function (RXN66-3) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. NAD-dependent aldehyde dehydrogenases MIYAQPGTPGAVVSFKPRYGNYIGGEFVPPVKGEYFVNTSPVNGEVIAEFPRSGAEDIEKALDAAHAAADAWGKTSVQDRALILLKIADRIEANLEKLAVAETWDNGKAVRETLNADVPLAADHFRYFAGCIRAQEGSAAEINEHTAAYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCIVLKPAEQTPLSIMVFIEVVGDLLPPGVLNIVQGFGREAGQALATSTRIAKIAFTGSTPVGSHIMRCAAENIIPSTVELGGKSPNIFFEDIMNAEPAFIEKAAEGLVLAFFNQGEVCTCPSRALIQESIFEPFMEVVMKKIKAIKRGNPLDTDTMVGAQASEQQFDKILSYMEIAQQEGAQILTGGAAEKLEGSLSTGYYVQPTLIKGHNKMRVFQEEIFGPVVGVATFKDEAEALAIANDTEFGLGAGVWTRDINRAYRMGRGIKAGRVWTNCYHLYPAHAAFGGYKKSGVGRETHKMMLDHYQQTKNLLISYDINPLGFF Pseudomonas stutzeri RCH2 psRCH2 GFF2388 Psest_2436 Methylmalonate-semialdehyde dehydrogenase (EC 1.2.1.27) Specifically important for utilizing L-Valine. Automated validation from mutant phenotype: the predicted function (RXN-11213) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. methylmalonic acid semialdehyde dehydrogenase MTTSSSIPTVKLLIDGEFIESTTQDWRDVVNPATQEVLARVPFATAEEIDRAVASGQKAFKTWRKTPIGARARIFLKYQQLIRENMKELAAILTAEQGKTLADAEGDVFRGLEVVEHAAGIGNLQLGELANNVAAGVDTYTLLQPLGVCAGITPFNFPAMIPLWMFPMAIATGNTFVLKPSEQDPMVTMRLCELALEAGVPPGVLNVVHGGPDVVNAICDHPDIKAVSFVGSTKVGTHVYNRASQAGKRVQCMMGAKNHAIVLPDAHKEQTLNNLAGAAFGAAGQRCMALSVVVLVGEAQAWIPDLVAKAQTLKVNAGVEAGTDVGPLVSCAALDRVSGLIERGVREGAKLELDGRNPSVSGYENGNFVGPTIFSGVTREMSVYQEEIFGPVLCVMAAATMDEAIELINANPNGNGTAIFTRSGAAARHFQEEIDVGQVGINVPIPVPVPMFSFTGSRASKLGDLGPYGKQVVQFYTQTKTITERWFDENEVGGPVNTTINLK Pseudomonas stutzeri RCH2 psRCH2 GFF2389 Psest_2437 Enoyl-CoA hydratase [valine degradation] (EC 4.2.1.17) Specifically important for utilizing L-Isoleucine. Automated validation from mutant phenotype: the predicted function (METHYLACYLYLCOA-HYDROXY-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Enoyl-CoA hydratase/carnithine racemase MTFETLLVDIQERVALITLNRPQALNALNGQLISELNQALGQLEADPQIGCIVLTGSAKAFAAGADIKEMAELTYPQIYLDDFFADADRIATRRKPLIAAVAGYALGGGCELALLCDMIFAADNARFGQPEVNLGVLPGIGGTQRLTRAVGKAKAMDMCLTGRQMDAAEAERAGLVARVFPAESLLEETLKAARVIAEKSLPATMMIKESVNRAFETTLAEGIRFERRVFHAVFATADQKEGMAAFSEKRKPEFTNR Pseudomonas stutzeri RCH2 psRCH2 GFF2390 Psest_2438 3-hydroxyisobutyrate dehydrogenase (EC 1.1.1.31) Specifically important for utilizing L-Valine. Automated validation from mutant phenotype: the predicted function (3-HYDROXYISOBUTYRATE-DEHYDROGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 3-hydroxyisobutyrate dehydrogenase MHIGFIGLGNMGAPMAHNLLKAGHQLSVFDLNAAAVENLVGAGALPVDSPTAIAQGNAELIITMLPAAAHVKGVYLGVNGLIAHSRAGVMLIDCSTIDPHSAREVAKAAAEHGNPMLDAPVSGGTGGAAAGTLTFMVGGSDPDFDHAQPILAAMGKNIVHCGAAGNGQVAKVANNMLLGISMIGVAEAMALGVALGMDAKTLAGVINTSSGRCWSSDTYNPFPGVLDNVPSSRGYSGGFGSDLMLKDLGLATEAAKQVRQPVILGALAQQLYQSFSAQGHGGLDFSAIINQYRKDT Pseudomonas stutzeri RCH2 psRCH2 GFF2391 Psest_2439 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) Specifically important for utilizing L-Valine. Automated validation from mutant phenotype: the predicted function (3.1.2.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Enoyl-CoA hydratase/carnithine racemase MSVTERPVLAAVRNHVGHLTLNRPAGLNAVTLEMVRLLQQQLSAWAADPQIHAVVLRANGEKAFCAGGDIRSLYDSFQRGDTEHETFFEEEYALDQYIHAYPKPLLALMDGFVLGGGMGLVQGASLRVVTERVRMGMPEVGIGYFPDVGGSYFLSRLPGELGTYMGVTGLQIRAADALHVGLADWCVSHDQIAELDRCLDRMSWSVHPQEALRTLVATLGSNKLPGSELKALHQAIDEHFGKSDVVAIRASLAAETRPEFADWAEETVKVLDSRSPLAMCVTLEMLRRGRELPIADCFALELHLDRQWFAKGDIMEGVRALIIDKDKSPRWNPPTLAEVTPERVQAFFDGFKATTGKARRSATA Pseudomonas stutzeri RCH2 psRCH2 GFF3021 Psest_3079 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) Specifically important for utilizing L-Proline. Automated validation from mutant phenotype: the predicted function (1.2.1.88, 1.5.5.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain) MFKAGHVLDGAFANQKAAEFFPAISANYSVDEAQYLTELLQLADPGEAGIAAIRERARSLIEAVRGRDNAVDTLDALLRQYSLDTQEGLMLMCLAEALLRVPDAATADALIRDKLNAAEWERHLGQSDNVLVNFAAWGLVMTGKVVDPETADGRPKNVIGRLLKRSGEPVIRGAMNQAMKLMGKQFVLGRTISEALKNGRPEREKGYTYSFDMLGEAALTAEDAAKYMADYRQAVETVGAEPQVGKGPRPSVSIKLSALHPRYELAQRERVLTELFGSVRELAILARRLNVGITIDAEEADRLELSLELYEKLLRDPAIAGWGEFGLVIQAYSKRCLPVLVWLTLLGRELGERIPLRLVKGAYWDSEIKQCQVQGLDGYPVYTRKEGTDTSYLACARYLLSEHTRGVIYPQFASHNAHTVSCILAMAEETAQPREFEFQRLHGMGDALYDTVIEKYARNVRIYAPVGAHKDLLPYLVRRLLENGANSSFVHQLVDPRVPVESLIDHPVTQLRRFAAPGNPRIPLPPALFGNRKNSQGINMNIQNQWTELASAYQPFLERQWQAAPVISGRTLAGTPSEVRCPYELNKVVGQAQFASADQARQAIDRLAAYWPIWNATPVEARAAVLERLGDLLEQHRAELMALCTVEAGKSLQDGIDEVREAVDFCRYYAQQARLKLGREELKGPTGERNELFHEGRGVFVCVSPWNFPLAIYLGQITAALVAGNTVLAKPAEQTSLIAARALELMFEAGLPQEAIAFLPGDGATLGGVFCRDPRVVGVCFTGSTDTARIINRQLAEKEGPIATLIAETGGQNAMIVDSTALPEQVIKDAVGSAFTSAGQRCSALRVLYVQRDIADRVIDLLKGAMAELRVGPTHLRENDIGPVIDQEAREGLLAHIQQLKSEGRLIAEATVPAGLNGHFVAPVAFEIDGIHQLKKEHFGPVLHVVRYDAADLEKVVAAINGTGYGLTLGVHSRNEETAERIEQLARVGNLYVNRNQIGAVVGVQPFGGCRLSGTGPKAGGPSYLLRFANERTTSTNTTAVGGNASLLSLGDD Pseudomonas stutzeri RCH2 psRCH2 GFF3290 Psest_3354 1-phosphofructokinase (EC 2.7.1.56) Specifically important for utilizing D-Fructose. Automated validation from mutant phenotype: the predicted function (1PFRUCTPHOSN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 1-phosphofructokinase MARVLTVTLNPALDLTVQLPALRLGEVNRSDSLQVHAAGKGLNVAQVLADLGHQLTVTGFLGEGNPQAFEQLFSARGFTDEFVRVAGETRSNLKLAEADGRVTDINGPGLAVSEAQRAELLARLKRLVPAHELVVVAGSLPRGIDSQWFVQLLNSLKALGVRVALDTSGAALRDGLATRPWLIKPNEEELAEARGIELSGSSALAAEAQRLQEEGIEHVVVSQGADGVSWFSPGAALHASPPKVRVVSTVGAGDSLLAGMLHGLLEGWPAERTLTHATAIAAQAVGQVGFGITDTAQLAELQAAVRLQPLSQ Pseudomonas stutzeri RCH2 psRCH2 GFF3302 Psest_3366 Biosynthetic arginine decarboxylase (EC 4.1.1.19) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (ARGDECARBOX-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. arginine decarboxylase, biosynthetic MPVRRTRKDDGSQWTAADSRSIYGIRHWGAGYFAISDEGNVEVRPQGPSGEPIEFNGLIEQLREAGLSLPLLVRFPGILQDRVRRLTGAFDANIERMEYAGKYTALYPIKVNQQEAVVENIIATQNVSIGLEAGSKPELMAVLALAPKGGTIVCNGYKDREFIRLALMGQKLGHKVFIVIEKESEVGLVIEEANELKLTPQVGLRVRLSSLASSKWADTGGERSKFGLSAAQLLSVIERFRAAEMDQGIRLLHFHMGSQIANLADYRQGFREAIRYYAELRALNLPVDYIDVGGGLGVDYDGTHSRNASSINYDIDEYAGTVVGMLKEFCEAQGLPHPNIFSESGRAMTAHHAVLVMQVTDVERHNDELPVIENYDELPEIVQSLADLLGPTDPEMVTETYWRATHYMSESSAQYASGKLTLAQKALAEQSYFAICRRLYNQLKARQRSHRAVLDELNDKLADKYICNFSVFQSLPDTWAIDQILPIVPLQRLSEEPVRRAVLQDLTCDSDGKIKHYVDEQSIESSMPVHEVAPGEEYFLGVFLVGAYQEILGDMHNLFGDTDSVNVYQREDGSYYHAGIETHDTIEDMLRYVHLSPEELMTYYRDKVASAKLSAKERTQYIDALRLGLTRSSYLTP Pseudomonas stutzeri RCH2 psRCH2 GFF3446 Psest_3511 Maleylacetoacetate isomerase (EC 5.2.1.2) Specifically important for utilizing L-tyrosine disodium salt. Automated validation from mutant phenotype: the predicted function (MALEYLACETOACETATE-ISOMERASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. maleylacetoacetate isomerase MGTELTLYGYWRSSAAYRVRIALNLKGLAYRQVPVHLVKDGGQQRAADYRALNPQQLVPLLVDEGNGGARISQSLAILEYLDEVFPVPALLPADPVERAQVRSLAMHIACEIHPLNNLRVLQYLSAELGVDDEAKNAWYRHWVSQGLAAVEQGLETFGDKLSLNDRPGYLEACLVPQVYNARRFACDLAAYPRILEIVARCETLPAFQQAAPEVQPDAQ Pseudomonas stutzeri RCH2 psRCH2 GFF3448 Psest_3513 Homogentisate 1,2-dioxygenase (EC 1.13.11.5) Specifically important for utilizing L-tyrosine disodium salt. Automated validation from mutant phenotype: the predicted function (HOMOGENTISATE-12-DIOXYGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Homogentisate 1,2-dioxygenase MSRKWISFPIREGESSRQAHCDFPQGTYEREMGREGFFGPASHLHHKHPPTGWIDWEGPLRPHAFNFNQIPSEGDCPLQAPLALHNADVKLRLWKTNGAMRHLVRNGDGDELLFIHEGAGHLYCDFGHLEFRDGDYLMIPRGTAWRIEATQPVFMLLIENTDGAYQLPDKGLVGPHAIFDAAVLDHPRLDDAFRAQQDENPWQIRIKRRDQITTVTYPYNPLDVVGWHGDNTVVRLNWRDIRPLMSHRYHLPPSAHTTFVANGFVVCTFTPRPVESDPGALKVPFFHNNDDYDEVLFYHRGNFFSRDNIEQGMVTFHPCGFPHGPHPKALKKAQDDPATFADEVAVMIDTRRALEVGEAAAAVDVPEYVNSWRAPGKES Pseudomonas stutzeri RCH2 psRCH2 GFF3449 Psest_3514 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) Specifically important for utilizing L-tyrosine disodium salt. Automated validation from mutant phenotype: the predicted function (4-HYDROXYPHENYLPYRUVATE-DIOXYGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 4-hydroxyphenylpyruvate dioxygenase MNAVNKIEQHNPIGTDGFEFVEFTAPNAEGIEQLRTLFTQMGFTETAKHRSKEVWLFQQHDINIVLNGSPTGHVHAFAEKHGPSACAMAFRVKNAAQAAAYVESQGAKLVGSHANFGELNIPCVEGIGGSLLYLVDRYGDKSIYDVDFEYIEGRTPNDNAVGLMCIDHLTHNVMRGQMDVWSGFYERIANFREIRYFDIEGKLTGLFSRAMTAPCGKIRIPINESADDKSQIEEFIREYHGEGIQHIALSTDDIYATVRQLRANGVDFMTTPDTYYEKVDTRVAGHGEPTDVLRELNILIDGAPGDDGILLQIFTNTVIGPIFFEIIQRKGNQGFGEGNFKALFESIEEDQLRRGVIKADE Pseudomonas stutzeri RCH2 psRCH2 GFF3451 Psest_3516 Leucine dehydrogenase (EC 1.4.1.9) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (1.4.1.9) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Glutamate dehydrogenase/leucine dehydrogenase MSVFAHPDFDRHEQVVFCHDQASGLKAIIAIHDTRLGPALGGCRMFPYANDDDALRDVLRLSRGMTLKSSLAGLKLGGGKAVIIGDPHTGKSQTLLHAMGDFVDSLGGRYITAADSGTGDAEMQAFAQRTRHVVGATPRTTLDGSIASGDPSPSTAYGVFVGLKEAVRQRLGRDDLAGLKVAIQGVGHVGLGLARHLKAAGAELWVADIFDANVKQAMEEVGANVVRPQDIYGLDVDVFAPCAMGGILNEQTLEVLRAPVIAGAANNQLATAEIGIELQRRNQLYAPDYAINAGGIIDVYYQRTGGSAAQIDAHVKAIGDTLGEIFTRSAASGEPTSVIADRLALERLHAGGVPQTEAFKRQAS Pseudomonas stutzeri RCH2 psRCH2 GFF353 Psest_0354 Malate synthase G (EC 2.3.3.9) Specifically important for utilizing Sodium butyrate and Tween 20. Automated validation from mutant phenotype: the predicted function (MALSYN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. malate synthase G MTERVQVGGLQVAKVLYDFVNNEAIPGTGVDAAAFWAGADSVIHDLAPKNRALLAKRDDLQAQIDAWHQARAGQAHDAVAYKSFLQEIGYLLPEAEDFQATTENVDEEIARMAGPQLVVPIMNARFALNAANARWGSLYDALYGTDAISEADGASKGPGYNEIRGNKVIAYARNFLNEAAPLETGSHVDSTGYRIEGGKLVVSLKDGSTTGLKNPAQLQGFQGEASAPIAVLLKNNGIHFEIQIDPASPIGQTDAAGVKDILMESALTTIMDCEDSIAAVDADDKTVVYRNWLGLMKGDLVEELEKGGKRITRAMNPDRVYTKADGNGELTLHGRSLLFIRNVGHLMTNDAILDKEGNEVPEGIMDGLFTSLIAVHNLNGNTSRKNTRTGSMYIVKPKMHGPEEVAFATELFGRVEDVLGLPRNTLKVGIMDEERRTTINLKACIKEARERVVFINTGFLDRTGDEIHTSMEAGPMVRKAAMKAEKWISAYENNNVDVGLACGLQGKAQIGKGMWAMPDLMAAMLEQKVGHPMAGANTAWVPSPTAATLHAMHYHKIDVQARQVELAKREKASIDDILTIPLAQDTNWSEEEKRNELDNNSQGILGYMVRWVEQGVGCSKVPDINDIALMEDRATLRISSQHVANWMRHGVVTKDQVVESLKRMAPVVDRQNQGDPLYRPMAPDFDNSVAFQAALELVLEGTKQPNGYTEPVLHRRRREFKAKNGL Pseudomonas stutzeri RCH2 psRCH2 GFF3724 Psest_3793 D-alanine dehydrogenase (EC 1.4.99.-) Specifically important for utilizing D-Alanine. Automated validation from mutant phenotype: the predicted function (DALADEHYDROG-RXN) was linked to the condition via a SEED subsystem. A more specific reaction was selected manually. Glycine/D-amino acid oxidases (deaminating) MRVLVLGSGVVGTASAYYLARAGFEVVVVDRQPAVAMETSFANAGQVSPGYASPWAAPGVPLKAMKWLLQRHAPLAIKLTGDVDQYLWMAQMLRNCTAARYAVNKERMVRLSEYSRDCLDELRAETGIAYEGRQLGTTQLFRTQAQLDAAAKDIAVLERSGVPYELLDRAAIGRVEPALAKVAHKLSGALRLPNDQTGDCQMFTSRLAEMALALGVEFRFGQNIQRLEHAGDRIAGVWIDGKLETADRYVLALGSYSPQMLKPLGIRAPVYPLKGYSLTVPISDPAMAPQSTVLDETYKVAITRFDQRIRVGGMAEIAGHDLSLNPRRRETLEMVVGDLYPQGGDPAEAVFWTGLRPATPDGTPIIGATAYRNLYLNTGHGTLGWTMACGSGRVLADLLASKRPQISTDGLDIFRYGKHKETRKHAHPAAAH Pseudomonas stutzeri RCH2 psRCH2 GFF4008 Psest_4081 Glutaminase (EC 3.5.1.2) Specifically important for utilizing L-Glutamine. Automated validation from mutant phenotype: the predicted function (GLUTAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glutaminase A MQALLQEILDEVRPLLGQGRVASYIPALADVPAEQLGIAVCSADGEVFEAGDAQTPFSIQSISKVFSLVQAIGHRGESLWERLGHEPSGQPFNSLVQLEFERGRPRNPFINAGALVICDVNQSRFATPELSMRDFVRHLSGNRQIVSDTRVAESEYQHRARNAAMAYLMQAFGNFHNDVEAVLRSYFHHCALRMNCIDLARAFAFLAREGSCPQSGEVILAPRQAKQVNAIMATSGLYDEAGNFAYRVGLPGKSGVGGGIVAVVPGRFTVCVWSPELNAAGNSLIGMAALEALSQRIGWSVF Pseudomonas stutzeri RCH2 psRCH2 GFF4215 Psest_4288 Glutamate--putrescine ligase (EC 6.3.1.11) Specifically important for utilizing L-Arginine and Putrescine Dihydrochloride. Automated validation from mutant phenotype: the predicted function (RXN0-3901) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Glutamine synthetase MAPPRAVQLNEANAFLKEHPEVQYVDLLITDMNGVVRGKRIERASLHKVYEKGINLPASLFALDINGITVESSGLGMDIGDSDRTCFPIPNTLCKEPWQKRPTAQLLMTMHERDGDPFFADPREVLRQVVSKFDELGLTICAAFELEFYLIDQENINGRPQPPRSPISGKRPHSTQVYLIDDLDEYVDCLQDILEGAKEQGIPADAIVKESAPAQFEVNLHHVADPIKACDYAVLLKRLIKNIAYDHEMDTTFMAKPYPGQAGNGLHVHISLLDKNGNNIFATENPLESAPLRHAIGGLQETMAASMAFLCPNVNSYRRFGAQFYVPNAPCWGMDNRTVALRVPTDSPDAVRVEHRVAGADANPYLMLASILAGVHHGLTNKIEPDAPIEGNSYEQVEQSLPTNLRDALRELDDSEIMARYISPDYIDIFVACKESELAEFEHSISDLEYNWYLHTV Pseudomonas stutzeri RCH2 psRCH2 GFF445 Psest_0450 Branched-chain amino acid aminotransferase (EC 2.6.1.42) Specifically important for utilizing L-Isoleucine. Automated validation from mutant phenotype: the predicted function (BRANCHED-CHAINAMINOTRANSFERILEU-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. branched-chain amino acid aminotransferase, group I MSMADRDGVIWYDGELVQWRDATTHVLTHTLHYGMGVFEGVRAYNTPDGTAIFRLQAHTDRLFDSAHIMNMPMPYSKEEINEATRAAVRENNLESAYIRPMVFYGSEGMGLRASGLKVHVIVAAWHWGAYMGDEALELGIKVRTSSFTRHHVNITMTRAKSNGAYINSMLALQEAISGGADEALMLDPEGYVAEGSGENIFIIKDGVIYTPEVTACLNGITRGTVLTLAAEHGLKIVEKRITRDEVYIADEAFFTGTAAEVTPIREVDGRAIGIGRRGPITEKLQKAYFDLVTGKTDAHAEWRTLVK Pseudomonas stutzeri RCH2 psRCH2 GFF552 Psest_0557 Urease (EC 3.5.1.5) Specifically important for utilizing Urea. Automated validation from mutant phenotype: the predicted function (3.5.1.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. urease, alpha subunit MKISRQAYADMFGPTVGDKVRLADTDLWIEVEKDFTTYGEEVKFGGGKVIRDGMGQSQLCAAEVVDTLITNALILDHWGIVKADVGLKDGRIAAIGKAGNPDIQPDVTIAIGASTEVIAGEGMILTAGGIDSHIHFICPQQIEEALMSGVTTMIGGGTGPATGTNATTVTPGPWHMAMMLKAADAFPMNIGFTGKGNASLPEPLIEQVRAGAIGLKLHEDWGTTPAAIDNCLSVADQYDVQVAIHTDTLNESGFVETTLGAFKGRTIHTYHTEGAGGGHAPDIIKACGFANVLPSSTNPTRPFTRNTIDEHLDMLMVCHHLDPSIAEDVAFAESRIRRETIAAEDILHDLGAFSMISSDSQAMGRVGEVITRTWQTADKMKKQRGALPGDGAGNDNFRAKRYIAKYTINPAITHGVSHEVGSIEVGKWADLVLWRPAFFGVKPTLILKGGAIAASLMGDANASIPTPQPVHYRPMFASFGGSLHASSFTFISQAAFEAGVPEQLGLKKKIGVVKGCRSVQKKDLIHNDYTPDIQVDPQNYQVRADGQLLWCEPAEVLPMAQRYFLF Pseudomonas stutzeri RCH2 psRCH2 GFF555 Psest_0560 Urease (EC 3.5.1.5) Specifically important for utilizing Urea. Automated validation from mutant phenotype: the predicted function (3.5.1.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. urease, gamma subunit MDLSPREKDKLLIFTAGLVAERRLARGVRLNYPEAVAYISAALLEGARDGQTVADLMHYGTTLLSREQVMEGVPEMIPEIQVEATFPDGTKLVTVHQPIA Pseudomonas stutzeri RCH2 psRCH2 GFF856 Psest_0870 Alpha-glucosidase (EC 3.2.1.20) Specifically important for utilizing D-Maltose monohydrate. Automated validation from mutant phenotype: the predicted function (3.2.1.20) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Glycosidases MSEQLQNWWRGGVIYQVYPRSFFDSNGDGVGDLPGVLHKLDYIASLNVDAIWLSPFFTSPMKDFGYDVADYRGVDPLFGTLDDFVRLVEACHERGMRVLIDQVLNHSSDQHPWFAESRSSRDNDKADWYVWADPKPDGTVPNNWLSVFGGPAWSWDSRRRQYYLHNFLSSQPDLNFHCPAVQDQLLDDMEFWLKLGVDGFRLDAANFYFHDAELRDNPPNTEIREGSIGVRIDNPYAYQRHIYDKTRPENMDFLRRLRALLQRYPGASSVAEIGCDESLRTMAAYTSGGDTLHMAYSFDLLTEQCSPGYIRHTVEGIERELADGWSCWSMGNHDVVRVMTRWALNGRPDPERGRLLMALLLSLRGSVCMYQGEELGLPEAELRYEDLVDPYGITFWPEFKGRDGCRTPMPWESEAHHAGFTGSQPWLPVDDSHRSLSVAAQDADPHSMLNCYRRFLGWRREQRLLIEGDIHMVYHDDALLVFERRLGDEAWLCLFNLGDLSRSYELPAQAVPLVDVPASFAEYDGHWARLPAHGFGYVRLAG Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_1114 L-threonine aldolase (EC 4.1.2.5) Specifically important for utilizing L-Threonine. Automated validation from mutant phenotype: the predicted function (4.1.2.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Low-specificity L-threonine aldolase (EC 4.1.2.48) MTDKSQQFASDNYSGICPEAWAAMEQANHGHQRAYGDDEWTARASDGFRKLFETDCEVFFAFNGTAANSLALSSLCQSYHSVICSETAHVETDECGAPEFFSNGSKLLIARTENGKLTPDSIREVALKRQDIHYPKPRVVTLTQATEVGSVYTPDEIRAISATCKELGLNLHMDGARFSNACAFLGCTPADLTWKAGVDVLCFGGTKNGMAVGEAILFFNHKLAEDFDYRCKQAGQLASKMRFLSAPWVGILENDAWLKYANHANHCAQLLAELVSDIPGVELMFPVQANGVFLQLSEPAIAALTAKGWRFYTFIGNGGARFMCSWDTEQERVRELAKDIREVMSH Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_1170 5-aminopentanamidase (EC 3.5.1.30) Specifically important for utilizing L-Lysine. Automated validation from mutant phenotype: the predicted function (5-AMINOPENTANAMIDASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 5-aminopentanamidase (EC 3.5.1.30) MRVALYQCPPLPLDVAGNLQRLQQLALEAKGADLLVLPEMFLTGYNIGVDAVSVLAEVYNGESAQQVARIAKAAGIAILYGYPERTEDGQIYNAVQLIDSDGERVCNYRKTHLFGDLDHSMFSAGSDEFPIVELNGWKLGFLICYDLEFPENARRLALAGAELILVPTANMIPFDFVADVTVRARAFENQCYVAYANYCGHEGDIHYCGQSSIAAPDGSRIAQAGLDESLIVGELDRQLMVDSRAANRYLLDRRPELYGELNKS Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_1171 Lysine 2-monooxygenase (EC 1.13.12.2) Specifically important for utilizing L-Lysine. Automated validation from mutant phenotype: the predicted function (LYSINE-2-MONOOXYGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Lysine 2-monooxygenase (EC 1.13.12.2) MNKNNRHPADGKKPVTIFGPDFPFAFDDWIEHPAGLGSIPEHNHGAEVAIVGGGIAGLVAAYELMKLGLKPVVYEASKMGGRLRSQAFNGAEGIVAELGGMRFPVSSTAFYHYVDKLGLETKPFPNPLTPASGSTVIDLEGQTHYAQKLSDLPALFQEVADAWADALEAGSQFSDIQQAIRDRDVPRLKELWNTLVPLWDDRTFYDFVATSKAFAKLSFHHREVFGQVGFGTGGWDSDFPNSMLEIFRVVMTNCDDHQHLVVGGVEQVPQGIWRHVPERCAHWPAGTSLSSLHNGAPRTGVKKIAHAPGGRFAVTDNWGDTREYAAVLTTCQSWLLTTQIECDETLFSQKMWMALDRTRYMQSSKTFVMVDRPFWKDKDPETGRDLMSMTLTDRLTRGTYLFDNGDDKPGVICLSYSWMSDALKMLPQPVEKRVKLALDALKKIYPKVDIAARIIGDPITVSWEADPHFLGAFKGALPGHYRYNQRMYAHFMQDDMPAEQRGIFIAGDDVSWTPAWVEGAVQTSLNAVWGIMKHFGGATHAENPGPGDVFNEIGPIALPE Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_1866 Aminomethyltransferase (EC 2.1.2.10) Specifically important for utilizing Glycine. Automated validation from mutant phenotype: the predicted function (2.1.2.10) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Aminomethyltransferase (glycine cleavage system T protein) (EC 2.1.2.10) MSTEQLLKTPLHALHIELGARMVPFAGYDMPVQYPLGVMKEHQHTRDQAGLFDVSHMGQIRLTGANAAKALETLVPVDIIDLPVGMQRYAMFTNATGGILDDLMVANLGNDELFLVVNAACKDQDLAHLRKHIGDQCTIEPLFEERALLALQGPAAVTVLARLAPEVAKMTFMQFARVKLLGVDCFVSRSGYTGEDGFEISVPATNAEALARALLAEAEVAAIGLGARDSLRLEAGLCLYGHDMNTDTTPIEASLLWAISKPRRADGARAGGFPGAETVFAQQQAGVSRKRVGLLPQERTPVREGAEIVNEAGDIIGSVCSGGFGPTLGGPLAMGYVDSAYIALDTPVWAIVRGKKVPLLVSKMPFVPQRYYRG Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_1868 Glycine dehydrogenase (aminomethyl-transferring) (EC 1.4.4.2) Specifically important for utilizing Glycine. Automated validation from mutant phenotype: the predicted function (1.4.4.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Glycine dehydrogenase [decarboxylating] (glycine cleavage system P protein) (EC 1.4.4.2) MTQINLTTANEFIARHIGPRAGDEQAMLNSLGFDSLEALSASVIPDSIKGTSVLGLEDGLSEADALALIKSIATKNQLFKTFIGQGYYGTHTPSPILRNLLENPAWYTAYTPYQPEISQGRLEALLNFQTLISDLTGLPIANASLLDEATAAAEAMTFCKRLSKNKGSHAFFASVHCHPQTLDVLRTRAEPLGIDVVVGDERELTDVTPFFGALLQYPASNGDVFDYRELTERFHAANALVAVAADLLALTVLTAPGEFGADVAIGSAQRFGVPLGFGGPHAAYFSTKDAFKRDMPGRLVGVSVDRFGNPALRLAMQTREQHIRREKATSNICTAQVLLANIASMYAVYHGPKGLTQIANRVHHLTAILAKGLSALGLSVEQASFFDTLTVKAGAQTAALHDKAHAQRINLRVVDGERLGLSLDETTTQADVETLWSLLSDGKALPDFAALAASVQSAIPATLVRQSPILSHPVFNRYHSETELMRYLRKLADKDLALDRTMIPLGSCTMKLNAASEMIPVTWAEFGALHPFAPAEQSAGYQQLTDELEAMLCAATGYDSVSLQPNAGSQGEYAGLLAIRAYHQSRGEDRRDICLIPSSAHGTNPATAQMAGMRVVVTACDARGNVDIEDLRAKAIEHREHLAALMITYPSTHGVFEEGIREICGIIHDNGGQVYIDGANMNAMVGLCAPGKFGGDVSHLNLHKTFCIPHGGGGPGVGPIGVKSHLAPFLPGHAQMERKEGAVCAAPFGSASILPITWMYIRMMGGAGLKRASQLAILNANYISRRLEEHYPVLYTGSNGLVAHECILDLRPLKDSSGISVDDVAKRLIDFGFHAPTMSFPVAGTLMIEPTESESKEELDRFCDAMIRIREEIRAVENGTLDKDDNPLKNAPHTAKELVGEWSHPYSREQAVYPVASLIEGKYWPPVGRVDNVFGDRNLVCACPSIESYA Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_1974 Succinylglutamic semialdehyde dehydrogenase (EC 1.2.1.71) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (SUCCGLUALDDEHYD-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Succinylglutamic semialdehyde dehydrogenase (EC 1.2.1.71) MKSLYIAGEWLAGGGEAFESLNPVTQQVLWSGVGATAGQVESAVQAARQAFPDWARRTLEERISVLEAFAAALKNHADELAHTIGEETGKPLWEAATEVTSMVNKIAISVQSYRERTGEKSGPLGDATAVLRHKPHGVVAVFGPYNFPGHLPNGHIVPALLAGNSVLFKPSELTPKVAELTVKCWIEAGLPAGVLNLLQGARETGIALAANPGIDGLFFTGSSRTGNHLHQQFAGRPDKILALEMGGNNPLVVDQVADLDAAVYTIIQSAFISAGQRCTCARRLLVPQGAWGDSLLARLVAVSSTLSVGAFDQQPAPFMGSVVSLGAAKALMDAQEHLLANGAVALLEMTQPQAQSALLTPGILDVSAVADRPDEELFGPLLQVIRYADFEAAIAEANDTAYGLAAGLLSDSEARYQQFWLESRAGIVNWNKQLTGAASSAPFGGVGASGNHRASAYYAADYCAYPVASLETPSLVLPSALTPGVKMA Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_1977 Succinylglutamate desuccinylase (EC 3.5.1.96) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (SUCCGLUDESUCC-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Succinylglutamate desuccinylase (EC 3.5.1.96) MLALGKLLELTLAGREPAEKTQLTVEGVRMRWLSEGALEVRPPEARDNGLDLLLSAGIHGNETAPIELLDRLLHDIARGDLKPRARILFLFGNPEAIRKGERFVEQDVNRLFNGRHEQSSGCEALRACELERLAASFFSLPDRQRLHYDLHTAIRGSKIEQFALYPWKEDRQHSRQELARLRAAGMEAVLLQNKPSIVFSSYTYDKLGAEAFTLELGKARPFGQNDGVNVSLLEKRLKQIIEGTEPELTEDALDGLQLYSVAREIIKHSDSFRLNLPADIENFSELEVGYLLAEDIANTRWIIEEEGARIIFPNPRVKNGLRAGILVVPTTDENLA Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_2118 L-arabinolactonase (EC 3.1.1.15) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (L-ARABINONOLACTONASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-arabinolactonase (EC 3.1.1.15) MTWSVVTGHRARLGEGPFWDAPTQALYWVDIAGKQALRLIGANVQIWQMPEHVSAFIPCESGDALVALSSGVYRLDLDSPGLAPRLTLFCVADPQPGNRPNEARCDAQGRLWLGTMQNNIGANGEDLPIVHRSGGLFRIDRAGRVAPLLRNLGIPNTLLWSDDATSVYFGDSLDGTLYRHFIRTDGALDAPQVWFGPHERGVPDGSAMDAEGFIWNARWDGNCLLRLSLDGKVDRIIELPVSRPTSCVFGGSDLKTLYITSAASPLGHPLDGAVLSIAVDVPGKHCTRFAG Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_2411 Acetyl-CoA C-acetyltransferase (EC 2.3.1.9) Specifically important for utilizing L-Lysine. Automated validation from mutant phenotype: the predicted function (ACETYL-COA-ACETYLTRANSFER-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 3-ketoacyl-CoA thiolase (EC 2.3.1.16) @ Acetyl-CoA acetyltransferase (EC 2.3.1.9) MNTPEIYVVSAARTAIGTFGGSLKDVPLADLATTAVKAALERAAVDPALVGHLVMGNVIPTETRDAYISRVAAMNAGIPKETPAYNVNRLCGSGLQAIINAAQTLMLGDADIVVGAGAESMSRGPYLMPAARWGSRMGNAQVIDYMLGILHDPFHGIHMGITAENVAARNGITREMQDALAFEDQQRAAHAIANGYFSEQIATVEIQDRKGVKLFSVDEHPRATSLEQLAAMKPAFKKDGSVTAGNASGLNDGAAALVMASGNAVQANNLKPLARLVSYAHAGVEPEFMGLGPIPATRLALKRAGLTVADLDVIEANIAFAAQACAVSQELDLDPAKVNPNGSGIALGHPVGATGAIIATKAIHELHRTGGRYALVTMCIGGGQGIAAIFERV Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_2685 Glycine hydroxymethyltransferase (EC 2.1.2.1) Specifically important for utilizing Glycine. Automated validation from mutant phenotype: the predicted function (2.1.2.1) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Serine hydroxymethyltransferase (EC 2.1.2.1) MFSKHDQIKGYDDELLAAMNAEDARQEHHIELIASENYTSQRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDVVEQLAIDRARQLFGADYANVQPHSGSQANAAVYLALLQAGDTVLGMSLAHGGHLTHGAKVSFSGKLYNAVQYGIDTTTGLIDYDEVERLAVEHKPKMIIAGFSAYSKTLDFPRFRQIADKVGAYFFVDMAHVAGLVATGLYPNPLPYADVVTTTTHKTLRGPRGGLILAKANPELEKKLNAAVFPGGQGGPLMHVIAAKAVCFKEALEPAFKTYQSQVIRNAQAMAQVFIERGYDVVSGGTDNHLFLVSLIRQGLTGKDADAALGRAGITVNKNAVPNDPQSPFVTSGLRIGTPAITSRGFKEAQSIALAGWICDILDHLGDADIEANVARQAAALCADFPVYRD Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_2739 Anthranilate 1,2-dioxygenase (deaminating, decarboxylating) (EC 1.14.12.1) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (1.14.12.1-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Benzoate 1,2-dioxygenase beta subunit (EC 1.14.12.10) MSALQYSIEQFLYRKAELCDQQDWDAYITLFDEQSEFHLPQWESEHVYTTDPKRSMSLIYYSNRSGLEDRVFRLRTGKSAASTPMPRTLHQISNVRINELNNGLLEVKAAWVTLFTRQGLSEQFYGHVTYHLRPVADSWKITRKHIVLLNDTINSVLDFYHL Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_2740 Anthranilate 1,2-dioxygenase (deaminating, decarboxylating) (EC 1.14.12.1) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (1.14.12.1-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Benzoate 1,2-dioxygenase alpha subunit (EC 1.14.12.10) MNSAKSITQWQEYIQGCLDFRPAEGIYRVARDMFTEPELFDLEMELIFEKNWIYACHESEIANPNDFLTMRAGRQPMIITRDGNNQLHALINACQHRGATLTRVSKGNQSTFTCPFHAWCYKSDGRLVKVKAPGEYPEGFDKATRGLKKARIESYKGFVFISLDVNGSDSLEDYLGDAKVFFDMMVAQSPTGELEILPGKSTYSYDGNWKLQHENGLDGYHVSTVHYNYVSTVQHRQQVNAANGGVSDTLDYSKLGAGDAETDDGWFSFKNGHSLLFSDMPNPTVRAGYATVMPRLIEEYGQQQAEWMMHRLRNLNIYPSLFFMDQISSQLRIVRPVAWNKTEITSQCIGVKGESDADRENRIRQFEDFFNVSGMGTPDDLVEFREAQRGFQARLERWNEVSRGSEKWVEGPTPNSEVLGINPVLTGTEFTHEGLYINQHGSWQRFLLQGLEQKALKLKEV Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_2935 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (RXN-10815) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) MADLYENPMGLMGFEFIELASPTPNTLEPIFEIMGFTKVATHRSKDVHLYRQGAINLILNNEPHSVASYFAAEHGPSVCGMAFRVKDSQKAYKRALELGAQPIHIETGPMELNLPAIKGIGGAPLYLIDRFGEGSSIYDIDFVFIEGVDRHPVGAGLKIIDHLTHNVYRGRMAYWANFYEKLFNFREIRYFDIKGEYTGLTSKAMTAPDGMIRIPLNEESSKGAGQIEEFLMQFNGEGIQHVAFLSDDLIKTWDHLKSIGMRFMTAPPETYYEMLEGRLPNHGEPVDQLQARGILLDGSSESGDKRLLLQIFSETLMGPVFFEFIQRKGDDGFGEGNFKALFESIERDQVRRGVLSTD Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_2982 3-ketoacyl-CoA thiolase (EC 2.3.1.16) Specifically important for utilizing L-Isoleucine. Automated validation from mutant phenotype: the predicted function (METHYLACETOACETYLCOATHIOL-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 3-ketoacyl-CoA thiolase (EC 2.3.1.16) MTMSNDPIVIVSAVRTPMGGFQGELKSLTAPQLGAAAIKAAVERAGVASDSVDEVLFGCVLPAGLGQAPARQAALGAGLDKSTRCTTLNKMCGSGMEAAILAHDMLLAGSADVVVAGGMESMSNAPYLLDRARAGYRMGHGRVQDSMFLDGLEDAYDKGRLMGTFAEDCAETNGFSREAQDAFAIASTTRAQQAIKDGSFKAEIVPLTVTVGKEQVVISNDEQPPKARLDKIASLKPAFREGGTVTAANSSSISDGAAALVLMRQSQAQKQGLKPLAVIHGHAAFADTPGLFPVAPIGAIKKLMKKTGWSLNDVDLVEVNEAFAVVGMAAMTHLEIPHEKLNVHGGACALGHPIGASGARILVTLLSALRQKGLKRGVAAICIGGGEATAMAVECLY Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_2986 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) Specifically important for utilizing L-Valine. Automated validation from mutant phenotype: the predicted function (3.1.2.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) MDAMQNEVLAEVRNHIGHLTLNRPAGLNALTLDMVRNLHRQLDAWAQDSQVHAVVLRGAGEKAFCAGGDIRSLHDSFKSGDTLHEDFFVEEYALDLAIHHYRKPVLALMDGFVLGGGMGLVQGADLRVVTEKSRLAMPEVGIGYFPDVGGSYFLSRIPGELGIYLGVSGVQIRAADALYCGLADWYLESGKLGVLDEKLDQLEWHDTPLKDLQGLLAKFAVQQLPDAPLATLRPAIDHFFAQPDVPSIVEQLRQVTVADSHEWAVTTADLLETRSPLAMAVTLEMLRRGRELPLEQCFALELHLDRQWFERGDLIEGVRALLIDKDKTPRWNPPTLQALDAEHVASFFSEFDRSES Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_316 N-formylglutamate deformylase (EC 3.5.1.68) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (3.5.1.68) was linked to the condition via a SEED subsystem. This annotation was also checked manually. N-formylglutamate deformylase (EC 3.5.1.68) VDKVLNFKQGRVPLLISMPHAGVRLTPAVEAGLIPDAKSLPDTDWHIPQLYDFAAELGASTLAAEYSRFVIDLNRPSDDKPLYVGATTGLYPATLFDGIPLFREGLEPSKEERATYLEQIWTPYHSTLQQELARLKAEFGYALLFDAHSIRSIIPHLFDGKLPDFNLGTFNGASCDPQLATRLEAICALHDNYTHVLNGRFKGGHITRHYGNPAENIHAVQLELGQCTYMEEFEPFRYRPDLAEPTRLVLKELLQGLLAWGEKHYKR Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_317 Imidazolonepropionase (EC 3.5.2.7) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (IMIDAZOLONEPROPIONASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Imidazolonepropionase (EC 3.5.2.7) MKTLWQHCHVATMAQGVYSIIEDAAIVTSGAHIEWIGPRGELPAGEYPAVNDLNGAWVTPGLIDCHTHTVFGGNRSGEFEQRLQGVSYADIAASGGGIASTVRATRAASEDELFASAAKRLKSLMRDGVTSIEIKSGYGLDLANERKMLRVARRLGAELPVSVRSTCLAAHALPPEYKDRADDYIDHICADMLPALAAEGLVDAVDAFCEYLAFSPAQVERVFITAQALGLPVKLHAEQLSSLHGSSLAARYHALSADHLEFMTEDDAIAMAKSGTVAVLLPGAFYFLRETQLPPMEALRKHGVKIAIASDLNPGTSPALSLRLMLNMACTCFRMTPEEALAGATIHAATALGMADTHGSLEVGKVADFVAWQIDRPADLCYWLGGDLEKRVVRHGVESSL Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_320 Histidine ammonia-lyase (EC 4.3.1.3) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (HISTIDINE-AMMONIA-LYASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Histidine ammonia-lyase (EC 4.3.1.3) MTALNLIPGQLTLAQLRDVYQQPVKLTLDNSASAQIEASVACVEQILAENRTAYGINTGFGLLASTRIASEDLENLQRSLVLSHAAGVGQPISDELVRLIMVLKVNSLSRGFSGIRRVVIDALIALINAEVYPHIPLKGSVGASGDLAPLAHMSLVLLGEGKARYKGEWMEATEALKVAGLTPLTLAAKEGLALLNGTQVSTAFALRGLFEGEDLFAGALALGGLTVEAVLGSRSPFDARIHAARGQKGQIDAAAAYRDLLGERSEVSDSHENCEKVQDPYSLRCQPQVMGACLTQFRQAAEVLAIESNAVSDNPLVFAAEGDVISGGNFHAEPVAMAADNMALAIAEIGSLSERRISLMMDKHMSQLPPFLVANGGVNSGFMIAQVTAAALASENKALSHPHSVDSLPTSANQEDHVSMAPAAGKRLWEMAENTRGILAVEWLAAVQGLDLRNGLKTSPKLEKARAILRNEVPFYEKDRFFAPDINAASELLASRCLNELVSAKLLPSL Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_326 Urocanate hydratase (EC 4.2.1.49) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (UROCANATE-HYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Urocanate hydratase (EC 4.2.1.49) VTENKRTKFRDVEIRAARGNKLTAKSWLTEAPLRMLMNNLDPEVAENPKELVVYGGIGRAARNWECYDKIVESLTNLNDDETLLVQSGKPVGVFKTHSNAPRVLIANSNLVPHWASWEHFNELDAKGLAMYGQMTAGSWIYIGSQGIVQGTYETFVEAGRQHYNDNLTGKWVLTAGLGGMGGAQPLAATLAGACSLNIECQQVSIDFRLKSRYVDEQAKDLDDALARIAKYTAEGKAISIALLGNAAEILPELVKRGVRPDMVTDQTSAHDPLNGYLPAGWTWDEYRARAKTEPAAVIKAAKQSMAVHVKAMLDFQKQGIPTFDYGNNIRQMAQEEGVENAFDFPGFVPAYIRPLFCRGIGPFRWAALSGNAEDIYKTDAKVKELIPDDAHLHNWLDMARERISFQGLPARICWVGLGLRAKLGLAFNEMVRSGELSAPIVIGRDHLDSGSVSSPNRETESMQDGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGFSQHSGMVIVCDGTDEAAERIARVLHNDPATGVMRHADAGYQIAIDCAKEQGLNLPMITGK Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_330 Formiminoglutamic iminohydrolase (EC 3.5.3.13) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (FORMIMINOGLUTAMATE-DEIMINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Formiminoglutamic iminohydrolase (EC 3.5.3.13) MSAFFAERALLPSGWANNVRLEVSADGVLTHIQADSNADGAERLSGPLLPGMPNLHSHAFQRAMAGLAEVAGNPNDSFWTWRDLMYRLVGKISPEQLGVIARQLYIEMLKAGYTSVAEFHYVHHDISGQPYADPAELALRISQAAGSAGIGLTLLPVLYSHSGFGGQTPNEGQRRFINSTENYLKLQSRLQPLLAQQPAQALGLCFHSLRAVTPQQISEVLAASDKQCPVHIHIAEQQKEVDDCLTWSGRRPLQWLYENVEVDQRWCLVHATHANPEEVTSMARSRAIAGLCLTTEANLGDGIFPAVDFLAQGGRMGIGSDSHVSLSVVEELRWLEYGQRLRDQRRNRLYGADQPMVGRTLFDAALDGGAQALGQPIGALEVGKRADWLVLDGNDPYLATANGDGILNRWLFAGGDRQVRDVLVNGQWVVRDGRHADEEESNRAFTQVLRELLG Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_3320 L-arabonate dehydratase (EC 4.2.1.25) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (L-ARABINONATE-DEHYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-arabonate dehydratase (EC 4.2.1.25) MSDKKPTLRSAQWFGTADKNGFMYRSWMKNQGIADHQFHGKPIIGICNTWSELTPCNAHFRQIAEHVKRGVIEAGGFPVEFPVFSNGESNLRPTAMLTRNLASMDVEEAIRGNPIDGVVLLTGCDKTTPALLMGAASCDVPAIVVTGGPMLNGKHKGKDIGSGTVVWQLSEQVKAGTISIDDFLAAEGGMSRSAGTCNTMGTASTMACMAEALGTSLPHNAAIPAVDARRYVLAHMSGMRAVEMVREDLKLSKILTKEAFENAIRVNAAIGGSTNAVIHLKAIAGRIGVELDLDDWTRIGRGMPTIVDLQPSGRFLMEEFYYAGGLPAVLRRLGEANLIPNPNALTVNGKSIGENTRDAPIYGEDEVIRTLDNPIRADGGICVLRGNLAPLGAVLKPSAATPELMQHRGRAVVFENFDMYKARINDPELDVDANSILVMKNCGPKGYPGMAEVGNMGLPAKLLAQGVTDMVRISDARMSGTAYGTVVLHVAPEAAAGGPLAAVKEGDWIELDCASGRLHLDIADTELAARMADLQPPQNLIVGGYRQLYIDHVLQADQGCDFDFLVGCRGAEVPRHSH Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_3503 Beta-ureidopropionase (EC 3.5.1.6) Specifically important for utilizing Cytosine; Uridine. Automated validation from mutant phenotype: the predicted function (3.5.1.6) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Beta-ureidopropionase (EC 3.5.1.6) MNAAVDVLQSSHQHINRDRLWQSLMELARLGATVKGGVCRLALTDLDRQARDIFVKWCIDAGCTVSIDAVGNIFARRPGRNPDLPPVMTGSHIDTQPTGGKFDGCFGVLAGVEVLRTLNDLNIETEAPLEVVVWTNEEGSRFAPCMMGSGVFAEKFTLEETLAKVDAEGVTVGQALNAIGYAGPRKVSGHKVGAYFEAHIEQGPILEDERKTIGVVMGALGQKWFDLKLRGVEAHAGPTPMHLRKDALVGAAVIVGALNRAALSHQPHACGTVGCLQAYPGSRNVIPGEVRMTLDFRHLEPARLDSMIAEVREVIETTCDEHGLTFELTPTADFPPLYFDKGCVEAVRGAAQSLGLSHMDIVSGAGHDAIFLAELGPAGMIFVPCEGGISHNEIENAAPEDLAAGCAVLLRAMLAASAAIAKGELTA Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_3506 Dihydropyrimidinase (EC 3.5.2.2) Specifically important for utilizing Cytosine. Automated validation from mutant phenotype: the predicted function (3.5.2.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Dihydropyrimidinase (EC 3.5.2.2) MSLLIRGATLVTHDESYRADVYCADGVIKAIGENLDVPAGAEVLDGSGQYLMPGGIDPHTHMQLPFMGTVASEDFYSGTAAGLAGGTTSIIDFVIPNPQQSLLEAFHQWRGWAEKSASDYGFHVAITWWSEQVREEMAELVSQHGVNSFKHFMAYKNAIMAADDTLVASFERCLELGAVPTVHAENGELVYHLQRKLMAQGITGPEAHPLSRPSQVEGEAASRAIRIAETLGTPLYLVHVSTKEALDEITYARGKGQPVYGEVLAGHLLLDDSVYRDPDWQTAAGYVMSPPFRPRGHQEALWHGLQSGNLHTTATDHCCFCAEQKAAGRDDFSKIPNGTAGIEDRMAVLWDEGVNSGRFSMQQFVALTSTNTAKIFNLYPRKGAIRVGADADLVLWDPQGTRTISAKTHHQQVDFNIFEGKTVRGVPSHTISQGRVVWADGDLRAERGAGRYIERPAYPAVFDLLSKRAELHKPVAVKR Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_3508 Dihydropyrimidine dehydrogenase (NADP(+)) (EC 1.3.1.2) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (1.3.1.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Dihydropyrimidine dehydrogenase [NADP+] (EC 1.3.1.2) MADLSIVFAGIKAPNPFWLASAPPTDKAYNVVRAFEAGWGGVVWKTLGEDPAAVNVSSRYSAHFGANREVLGFNNIELITDRSLEINLREITQVKKDWPDRALIVSLMVPCVEESWKHILPLVEATGADGIELNFGCPHGMPERGMGAAVGQVPEYVEQVTRWCKTYCSLPVIVKLTPNITDIRVAARAAHRGGADAVSLINTINSITSVNLERMVANPMVGSQSTHGGYCGSAVKPIALNMVAEIARDPQTQGLPISGIGGIGNWRDAAEFIALGSGSVQVCTAAMLHGFRIVEDMKDGLSRWMDSQGYASISEFSGRAVGNTTDWKYLDINYKVIAKIDQEACIGCGRCHIACEDTSHQAVASLKQADGTHKYQVIDEECVGCNLCQITCPVQDCIEMVPVETGKPFLDWNHDPRNPYHVGP Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_3542 Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase (EC 2.3.1.168) Specifically important for utilizing L-Isoleucine; L-Valine. Automated validation from mutant phenotype: the predicted function (2.3.1.168) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Dihydrolipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex (EC 2.3.1.168) MGTHVIKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISIEVEGAGNVKESAQPAPVVKEAPVAATKVETVVESKPVAAPAPKAAVCQGPMVAREADERPLASPAVRKHALDLGIQLRLVRGTGPAGRVLHEDLDAYLAQGQSNASAPVAAAYAQRTDEQQIPVIGMRRKIAQRMQDATQRAAHFSYVEEIDVTAVEELRAHLNEKHGATRGKLTLLPFLVRALVVALRDFPQINARYDDEAQVITRLGAVHVGIATQADIGLMVPVVRHAEARSLWDSAAEISRLATAARNGKASRDELSGSTITLTSLGALGGIVSTPVLNLPEVAIVGVNKIVERPMVIKGQIVIRKMMNLSSSFDHRVVDGMDAALFIQAIRGLLEQPATLFVE Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_3543 Dihydrolipoyl dehydrogenase (EC 1.8.1.4) Specifically important for utilizing L-Isoleucine; L-Valine. Automated validation from mutant phenotype: the predicted function (1.8.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Dihydrolipoamide dehydrogenase of branched-chain alpha-keto acid dehydrogenase (EC 1.8.1.4) MQTLNTTLLIIGGGPGGYVTAIRAGQLGIPTILVEGQSLGGTCLNIGCIPSKALIHVAEQFHQTQHHSQHSALGISVSAPTLDIGKSVEWKDGIVDRLTTGVAALLKKNKVQVVQGWAKVVDGKTVEVGDTRIQCEHLVLATGSKSVNLPMLPIGGPIISSTEALAPTSVPKRLIVVGGGYIGLELGIAYRKLGAEVSVVEAQERILPAYDAELTQPVHDELKKLGVKLYLKHSVQGFDSSNNTLQVLAPNGETLNLETDQVLVAVGRKPNTQGWNLEALNLDMNGSSIKIDNRCQTSMRNVYAIGDLSGEPMLAHRAMAQGEMVAELISGKTREFNPTAIAAVCFTDPELVVVGKTPDEAKAAGWDCIVSSFPFAANGRAMTLESKSGFVRVVARRDNHVIVGWQAVGVGVSELSTAFAQSLEMGARLEDIGGTIHAHPTLGEAVQEAALRALGHALHL Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_3648 D-serine ammonia-lyase (EC 4.3.1.18) Specifically important for utilizing D-Serine. Automated validation from mutant phenotype: the predicted function (4.3.1.18) was linked to the condition via a SEED subsystem. This annotation was also checked manually. D-serine dehydratase (EC 4.3.1.18) MILGKTLESWYASYPLIRDLVALQETTWFNPAVAPVAESIGDVGLTAADVADASARLTRFASYLRRAFPETECSGGIIESDILPVPHLQQLLGERYGQALQGALWLKRDSHLPISGSIKARGGIYEVLKHAEDLALAANLLTLDDDYAVLDSDKARAFFGQYKIAVGSTGNLGMSIGIMGAALGFQVTVHMSADARQWKKDKLRSHGVTVIEYSSDYSVAVSQGRQQAESDPACHFVDDENSVSLFLGYSVAAERLKKQLAAADITVDAQHPLFVYLPCGVGGAPGGVAFGLKLAFGDAVHCIFAEPTHSPCMMLGVYSGLHDEVSVQDFGIDNVTAADGLAVGRASGFVGKAMQRLLDGFYTVSDEEMYSLLALMERSEGVRLEPSALAGVPGIARVQADQQGYLARARLDRQAMVQATHLVWATGGNMVPCDEMEAYLAKGRELLAKG Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_3822 Catechol 1,2-dioxygenase (EC 1.13.11.1) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (CATECHOL-12-DIOXYGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Catechol 1,2-dioxygenase (EC 1.13.11.1) MNVKISHTAEVQKFLEEASGLLNDAGNPRTKALVYRILRDSVNIIEDLAVTPEEFWKAVNYLNVLGARQEAGLVVAGLGLEHYLDLLMDAEDEQAGKSGGTPRTIEGPLYVAGAPLSQGEARLDDGVDPGVTLFMQGRVFNTAGEPLAGAVVDVWHANTGGTYSYFDTTQSEFNLRRRIVTDAEGRYRFRSIVPSGYGCPPDGPTQQLLDQLGRHGQRPAHVHFFISAPDHRHLTTQINLDGDQYLHDDFAYATRDELIAKITFSDDQQRAAAHGVSGRFAEIDFDFTLQSSAQPEEQQRHERVRALED Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_3823 Muconolactone isomerase (EC 5.3.3.4) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (MUCONOLACTONE-DELTA-ISOMERASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Muconolactone isomerase (EC 5.3.3.4) MLFHVKMTVNLPVDMNPEVAAKLKADEKALAQRLQEQGKWRHLWRIAGHYANYSVFDVDSVQELHDLLMQLPLFPYMAIEIDAMCRHPSSIRDDDR Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4101 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Nitrite reductase [NAD(P)H] large subunit (EC 1.7.1.4) MKKLKLVMIGNGMAGVRTLEELLKLSTELYDITVFGAEPHTNYNRILLSPVLAGEQTFEEIVLNDLDWYLENNIKLLLNRKVVEIDRVKRRVIAEDGSEAEYDRLLIATGSTPFILPIPGNTLDGVIGYRDIADTQAMIDTAKTHRHAVVIGGGLLGLEAANGLMLRGMHVTVVHIGEWLLERQLDKTSGQLLQTALESRGLHFRLCEQTQALHDAGNGRVGSVQFKNGDIIPADLVVMAAGIRPNTELAEKSGIPCSRGILVNDTMQTYDPRIYAIGECASHRGIAYGLVAPLFEQAKVCANHLAQLGFATYKGSVTSTKLKVTGIDLFSAGDFMGGEGTETITLSDPIGGIYKKLVIKDDVLVGACLYGDTADGGWYFRQIRENHAISEIRDHLMFGENALGDVGHQGQDKAMSMADNAEVCGCNGVCKGTIVKAIQEHGLFSVDDVKKHTKAASSCGSCAGLVEQILINTVGGAADVKPKSEKAICGCSDLNHGQIRQAIREQHLLTIAGTMSYLNWRTPNGCATCRPALNYYLISTWPGEAKDDPQSRLINERAHANIQKDGTYSVVPRMWGGVTNPSELRRIADVADKYNVPMVKVTGGQRIDLLGIRKQDLPGVWKDLDMPSGHAYGKSIRTVKTCVGSEFCRFGTQNSTQLGIELEHDLFNMWSPHKVKLAVSGCPRNCSEAGIKDVGIIGVDSGWEMYIGGNGGIKTEVAEFFVKLKTAEEVREYNGAFLQLYREEAFYLERTVHYLQRVGMEHIKKAVLEDPERRKALNDRLQFSLSFEQDPWKERLEQPQLKKEFDVIPVKNLEVLA Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4103 Nitrate reductase (EC 1.7.99.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.99.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Assimilatory nitrate reductase large subunit (EC:1.7.99.4) MDRQITASTCCYCGVGCGVLIEHDGEHILGVSGDPAHPANFGKLCSKGSTLHLTGDLTARALYPELRLGKSLARHRTDWDTALDHATSVFAATIAEHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYEDLELSDCVMIVGSNMAYAHPVLFRRLEAAKSRRPQMKVIVIDPRRTDTCDLADLHLAILPGTDVALFHGILHLLLWEDWIDRDFIRDHTEGLAELKNLVRDYTPQMVSQLCGISLGQLQQCAEWIGTSPSFLSLWCMGLNQSTAGSAKNSALINLHLATGQIGRPGAGPFSLTGQPNAMGGRETGSLSNLLPGHRDAANAQHRAQVASYWGVEQLPESPGLTAIELFEQVRNGKIKALWIACTNPAQSMPDQTAVRAALQACPFVVLQEAFSTTETAKFADLLLPAASWGEKEGCVTNSERRISHVRQAIVAPGEARPDWAITVDFAQRLEKHLRPGQASLFEFDNPAQVFDEYKQLTQGRDLDLSGISHALIDRLGPQQWPFPAGAVEGTARLYVDGVFATANGRAQFVADPYRAAKEQRDARFPLTLITGRLRDQWHGMSRTGTAAQLFGHVSEAELSLHPDELRRHRLQPGDLVSLKSRRGAIVVAVASDDSVRPGQAFLPMHWGDRFLKGGVNSLTLPAFDPLSKQPELKHSGVRLDPVDLPWKLFALIEGDVQRHFETLRPLCEAFSYVSLSLVGRERPALLVRAANTSAPSAELLSEIDKNLALDDGPVLAYDDPRRAIGKRVRIENGRITAIRLAGETLAQHWLQGLWLEGRADQQLRRWLLAPLSAPPGNLDMPFNSNKILCNCKNVGQNAICAGISRGLDLQGLKQELGCGTQCGSCVPEIKRLLAATAQPVTVFS Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4288 Kynureninase (EC 3.7.1.3) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (KYNURENINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Kynureninase (EC 3.7.1.3) MTTRNDCLALDAQDALAPLRQQFALPEGVIYLDGNSLGARPVAALARAQAVIAEEWGNGLIRSWNSAGWRDLPERLGNRLGGLIGAGDGEVVVTDTTSINLFKVLSAALRVQATRAPTRRVIVTETGNFPTDLYIAEGLADMLQQGYTLRLVDSPQELPQAIDQDTAVVMLTHVNYKTGYMHDMQALTTLTHECGALAIWDLAHSAGAVPVDLHQARADYAIGCTYKYLNGGPGSQAFVWVSPELCDLVAQPLSGWFGHSRQFAMESHYQPSSGIARYLCGTQPITSLAMVECGLDVFAQTDMASLRSKSLALTDLFIQLVEQRCAAHELTLVTPREHAKRGSHVSFEHPQGYAVIQALIARGVIGDYREPRIMRFGFTPLYTSFTEVWDAVQILGDILDQKTWSQEQFQIRHSVT Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4292 Tryptophan 2,3-dioxygenase (EC 1.13.11.11) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (RXN-8665) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Tryptophan 2,3-dioxygenase (EC 1.13.11.11) MSQCPYSPANQTEEWHNAELNFSDSMSYGDYLDLGRILSAQHPLSPDHNEMLFIIQHQTSELWMKLMLHELNAAREHVRLGELPPAFKMLARVSRIFDQLVHAWTVLATMTPTEYHAIRPFLGQSSGFQSFQYREIEFILGNKSATLLRPHAHRPELLQALEKAIATPSLYDEAIRLMASAGLTIDPQRFERDPTSPTAHDASVEAAWRVVYTDPSRYWDLYQLAEKLIDLEDSFRQWRFRHVTTVERIIGFQPGTGGTEGVGYLRKMLDTVLFPELWRVRSTL Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4293 Kynurenine formamidase, bacterial (EC 3.5.1.9) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (ARYLFORMAMIDASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Kynurenine formamidase, bacterial (EC 3.5.1.9) MKTTLSWWDISPPLSTTTPTWPGDTPFQEERVWSFGPECPVNVGRITLSPHTGAHVDAPLHYSADGAAIGDVSLDVYMGPCRVLHCLNSGRLVHPEQLEGRLQDLPERVLLRTWRQAPLSAWDPDFSAVAKETVDLLASLGVRLIGIDTPSLDPQQSKTMDSHNAVARHGMAILEGIVLDDVPEGDYELIALPLRFAHLDASPVRAILRPLNKPQLEEPTQ Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4394 Phenylalanine 4-monooxygenase (EC 1.14.16.1) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (1.14.16.1) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Phenylalanine-4-hydroxylase (EC 1.14.16.1) MKQTQYVAREPDAQGFIDYPAEEHAVWNTLITRQLKVIEGRACQEYLDGIEKLGLPHDRIPQLGEINKVLAETTGWQVARVPALIPFQTFFELLASKQFPVATFIRTREELDYLQEPDIFHEIFGHCPLLTNPWFAEFTHTYGKLGLKASKEERVYLARLYWMTIEFGLLDTPQGQRIYGGGILSSPKETVYSLSNEPEHQAFDPLECMRTPYRIDILQPLYFVLPNLKRLFDLAHEDIMGMVKQAMQMGLHTPKFPPKAA Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4830 N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (NAG6PDEACET-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) MSEDNILTAHGWVRGRLVHEHGKVVSIEGQPCDPADNDLPYLLPGFIDLHVHGGGGKDIMEGAPAFETITRTHVRFGTTSLLATTMTAPSEEISSVLQAVGEFCELRPQGCARVLGVHLEGPYINPGKLGAQPNFAHTALMAEVEAYLALAPIRVITIAPEIAGHDTLIRDLSSRGIRMQIGHTLGSYEEGVAALEAGASSFTHLYNAMSPLHHREPGIVGAALAHAKYAELIPDLLHVHPGAIRVALRSIPCLYCVTDSTAAAGMPDGEYKLGSHTVTKCLGGVRLPDGTLAGSTLTMDQALRNLVKIGLPIAEASQRLSQFPADYLGITERGRLQPGAWADCVRLDRSLKLTAVMVEGEDIDFKNA Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4831 Glucosamine-6-phosphate deaminase [isomerizing], alternative (EC 3.5.99.6) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (GLUCOSAMINE-6-P-DEAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Glucosamine-6-phosphate deaminase [isomerizing], alternative (EC 3.5.99.6) LTSKMLEEALSSFEAVQAQLQQLDPQMIEIAGRLRRQPPQVAMTVARGSSDHAASYFAYLTMQLLGIPVASLPMSVVTMQQAPLKVSGQVAFAFSQSGQSPDLVNSLRLLRKRGALSISLVNAEDSPLEAACEFSLPLCAGTESSVAATKSFIATLSASARLIGHWKEDTELLDACRALPEGLRDAAQQDWSQAIDALRDCQRLMVIGRGAGFAIAQEAALKFKETSAIQAEAFSSAEVRHGPMALIGDNYPLLVFAPRGAEQAGLLSLAADMRQRGALVLLAAPDDVLERDLTLTRAEHPALDPILAIQSFYVMAAGLAVARGMDPDQPRHLSKVTRTH Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_495 Glutarate-semialdehyde dehydrogenase (EC 1.2.1.20) Specifically important for utilizing L-Lysine. Automated validation from mutant phenotype: the predicted function (GLUTARATE-SEMIALDEHYDE-DEHYDROGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Succinate-semialdehyde dehydrogenase [NAD(P)+] (EC 1.2.1.16) MQLKDTQLFRQQAFIDGAWVDADNGQTIKVNNPATGEILGTVPKMGAAETRRAIEAADKALPAWRALTAKERATKLRRWYELIIENQDDLARLMTLEQGKPLAEAKGEIVYAASFIEWFAEEAKRIYGDVIPGHQPDKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSAFALAELAQRAGIPAGVFSVVSGSAGDIGSELTSNPIVRKLSFTGSTEIGRQLMSECAKDIKKVSLELGGNAPFIVFDDADLDKAVEGAIISKYRNNGQTCVCANRLYIQDGVYDAFAEKLKVAVAKLKIGNGLEAGTTTGPLIDEKAVAKVQEHIADALSKGATVLAGGKPMEGNFFEPTILTNVPNNAAVAKEETFGPLAPLFRFKDEADVIAMSNDTEFGLASYFYARDLGRVFRVAEALEYGMVGVNTGLISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYLCLGI Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4954 L-serine ammonia-lyase (EC 4.3.1.17) Specifically important for utilizing L-Serine. Automated validation from mutant phenotype: the predicted function (4.3.1.17) was linked to the condition via a SEED subsystem. This annotation was also checked manually. L-serine dehydratase (EC 4.3.1.17) MAISVFDLFKVGIGPSSSHTVGPMRAAATFAQALVDHGFLADVRRVEIRLYGSLSATGVGHATDRACVMGLMGEWPDRIDPTTIDSRIHTLRETGKLCLAGVAQIAFDWQRDLLLLDESLPYHPNAMSLTAFGETGELFEQTYYSVGGGFIIEAAEAESGIAPAGDVVLPYDFSSAAELLKLCNEHGLRVGELMMANERAWRSDAEIRQGLLHIWSVMRECVEQGLRHEGILPGGLSVPRRAAKLHRSLQEIGKPNVITSTLSAMEWVNLYALAVNEENAAGGRMVTAPTNGAAGIIPAVLHYYMKFNADASDDDVVAFFLGAAAVGILCKKNASISGAEVGCQGEVGSACAMAAAGLAEVLGATPEQLENAAEIGLEHNLGLTCDPVGGLVQVPCIERNAIAAVKAINATQMALRGDGKHFISLDRVIRTMRDTGADMHDKYKETSRGGLAVNWVEC Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4962 Homogentisate 1,2-dioxygenase (EC 1.13.11.5) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (1.13.11.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Homogentisate 1,2-dioxygenase (EC 1.13.11.5) MNPDSTTPALAYQSGFGNEFSSEALPGALPVGQNSPQKAPYGLYTELFSGTAFTMARSEARRTWMYRIQPSANHPAFFKLDRQLTGGPLGEVTPNRLRWNPLDIPAEPTDFIDGLVSMAANSGAEKPAGISIYNYRANRSMERAFFNADGEMLLVPELGRLRIATELGVLELEPLEIAVLPRGLKFRIELLDPQARGYVAENHGAPLRLPDLGPIGSNGLANPRDFLTPVAAYENLQQPTTLVQKFLGQLWACELNHSPLNVVAWHGNNVPYKYDLRRFNTIGTVSFDHPDPSIFTVLTSPTSVHGLANLDFVIFPPRWMVAEKTFRPPWFHRNLMNEFMGLIQGEYDAKAEGFVPGGASLHSCMSAHGPDGETCTKAINAELKPAKIDNTMAFMFETSQVLRPSRFALDCPQLQNTYDACWATLPATFDPTRR Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_5145 3-hydroxyisobutyrate dehydrogenase (EC 1.1.1.31) Specifically important for utilizing L-Valine. Automated validation from mutant phenotype: the predicted function (3-HYDROXYISOBUTYRATE-DEHYDROGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 3-hydroxyisobutyrate dehydrogenase (EC 1.1.1.31) MKIAFIGLGNMGAPMARNLIKAGHALRLVDLNKAVLAELEQLGGSISASAREAAEGAELVITMLPAAVHVRSVWLGEDGVLAGIGKGVPAVDCSTIDPQTARDVAAAAAKQGVAMADAPVSGGTGGAAAGTLTFMVGATPELFATLQPVLAQMGRNIVHCGEVGTGQIAKICNNLLLGISMVGVSEAMALGDALGIDTKVLAGIINSSTGRCWSSEMYNPWPGIVETAPASRGYTGGFGAELMLKDLGLATEAARQAHQPVVLGAVAQQLYQAMSLRGEGGQDFSAIINGYRKPQ Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_5146 Methylmalonate-semialdehyde dehydrogenase (EC 1.2.1.27) Specifically important for utilizing L-Valine. Automated validation from mutant phenotype: the predicted function (RXN-11213) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Methylmalonate-semialdehyde dehydrogenase (EC 1.2.1.27) MNVSLTPNDTTVQKVKLLIDGQWVESKTTEWHDIINPATQQVLAKVPFATAEEVDAAISAAHRAFQTWKLTPIGARMRIMLKLQALIREHSKRIAAVLSAEQGKTIADAEGDIFRGLEVVEHACSIGSLQMGEFAENVAGGVDTYTLRQPIGVCAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSEQDPMSTMLLVELAIEAGIPAGVLNVVHGGKDVVDGLCTHKDIKAVSFVGSTAVGTHVYDLAGKHGKRVQSMMGAKNHAVVLPDANREQALNALVGAGFGAAGQRCMATSVVVLVGAAKQWLPDLKALAQKLKVNAGSEPGTDVGPVISKKAKARILDLIESGIKEGAKLELDGREISVPGYEKGNFVGPTLFSGVTTDMQIYTQEIFGPVLVVLEVNTLDEAIALVNANPFGNGTGLFTQSGAAARKFQNEIDVGQVGINIPIPVPVPFFSFTGSRGSKLGDLGPYGKQVVQFYTQTKTVTSRWFDDDSVNDGVNTTINLR Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_740 L-asparaginase (EC 3.5.1.1) Specifically important for utilizing L-Asparagine. Automated validation from mutant phenotype: the predicted function (ASPARAGHYD-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-asparaginase (EC 3.5.1.1) MNSSTYPAAQHVMVLYTGGTIGMQASANGLAPASGFEARMRDYLHSQPELVVPQWRFREMSPLIDSANMTPTYWQQLREAVVDAVDVQGCDSVLILHGTDTLAYSAAAMSFQLLGLHARVCFTGSMLPAGVTDSDAWENLGGALVAMGQGLAPGVHLYFHGELLDPTRCAKVRSFGRHPFKRLVRQGGGVKAASIPAQLNYNQPKQLAKVAVLPLFPGISAEVLDGLLDSGIQGLVLECYGSGTGPSDNPEFLASLGRARDNGVVVVAVTQCHEGGVKLDVYEAGSRLRGVGVLSGGGMTREAAFGKLHGLLGAGLEAAEVRRLVELDLCGELS Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_1013 L-serine ammonia-lyase (EC 4.3.1.17) Specifically important for utilizing L-Serine. Automated validation from mutant phenotype: the predicted function (4.3.1.17) was linked to the condition via a SEED subsystem. This annotation was also checked manually. L-serine dehydratase (EC 4.3.1.17) MAISVFDLFKVGIGPSSSHTVGPMRAAATFAQALIDQHLLADVRRVEIRLYGSLSATGVGHATDRACVMGLMGEWPDSIDPNSIDSRIQTLRETGELSLAGKSTIAFNWQRDLLLLDESLPYHPNAMSLTAFGETGELFEQTYYSVGGGFIIEAAEAESGIAPASDVVLPYDFSSAAELLKLCNQHGLRVSELMMANERAWRSDAEIRQGLLHIWSVMRECVEQGLRHEGILPGGLNVPRRAAKLHRSLLEIGKPNVISSTLSAMEWVNLFALAVNEENAAGGRMVTAPTNGAAGIIPAVLHYYMKFNPDASDDDVVAFFLGAAAVGILCKKNASISGAEVGCQGEVGSACAMAAAGLADILGATPEQLENAAEIGLEHNLGLTCDPVGGLVQVPCIERNAIAAVKAINATQMALRGDGKHFISLDRVIRTMRDTGADMHDKYKETSRGGLAVSWVEC Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_1110 5-dehydro-4-deoxyglucarate dehydratase (EC 4.2.1.41) Specifically important for utilizing D-Galacturonic Acid monohydrate. Automated validation from mutant phenotype: the predicted function (4.2.1.41) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 5-dehydro-4-deoxyglucarate dehydratase (EC 4.2.1.41) MNPQELKSILSSGLLSFPVTDFNAQGDFHRAGYIKRLEWLAPYGASALFAAGGTGEFFSLAASEYSEIIKTAVDTCATSVPILAGVGGATRQAIEYAQEAERLGAKGLLLLPHYLTEASQDGVAAHVEAVCKSVKIGVVVYNRNVCRLTAPLLERLAERCPNLIGYKDGLGDIELMVSIRRRLGDRFSYLGGLPTAEVYAAAYKALGVPVYSSAVFNFIPKTAMDFYHAIAREDHATVGKIIDDFFLPYLDIRNRKAGYAVSIVKAGAKIAGYDAGPVRAPLTDLTGEEYEMLAALIDKQGAQ Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_1229 Methylmalonate-semialdehyde dehydrogenase (EC 1.2.1.27) Specifically important for utilizing L-Valine. Automated validation from mutant phenotype: the predicted function (RXN-11213) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Methylmalonate-semialdehyde dehydrogenase (EC 1.2.1.27) MNASLETTVQKVKLLIDGEWVESQTTEWHDIVNPATQQVLAKVPFATAAEVDAAISAAHRAFQTWKLTPIGARMRIMLKLQALIREHSKRIAVVLSNEQGKTIADAEGDIFRGLEVVEHACSIGSLQMGEFAENVAGGVDTYTLRQPIGVCAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSEQDPMSTMLLVELAIEAGIPPGVLNVVHGGKDVVDALCTHKDIKAVSFVGSTAVGTHVYDLAGKHGKRVQSMMGAKNHAVVLPDANREQALNALVGAGFGAAGQRCMATSVVVLVGAAKQWLPDLKALAQKLKVNAGSEPGTDVGPVISKRAKARILDLIESGIKEGAKLELDGRDISVPGYEKGNFVGPTLFSGVTPEMQIYTQEIFGPVLVVLEVDTLDQAIALVNANPFGNGTGLFTQSGAAARKFQTEIDVGQVGINIPIPVPVPFFSFTGSRGSKLGDLGPYGKQVVQFYTQTKTVTARWFDDDSVNDGVNTTIHLR Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_1296 Biosynthetic arginine decarboxylase (EC 4.1.1.19) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (ARGDECARBOX-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Biosynthetic arginine decarboxylase (EC 4.1.1.19) MSVRRTRKDDGSQWTVADSRSVYGIRHWGAGYFAINDAGRVEVRPNGPTSSPIDLFEQVDQLRKSGLSLPLLVRFPDILQDRVRQLTGAFDANIERLEYQSKYTALYPIKVNQQEAVIENIIATQNVSIGLEAGSKPELLAVLALAPKGGTIVCNGYKDREFIRLALMGQKLGHNVFIVIEKESEVGLVIEEAASLKVKPQVGLRVRLSSLASSKWADTGGEKSKFGLSAAQLLSVVERFRAAGLDQGIRLLHFHMGSQIANLADYQHGFKEAIRYYGELRNLGLPVDHIDVGGGLGVDYDGTHSRNASSINYDMDDYAGVVVGMLKEFCDAQSLPHPNIFSESGRSLTAHHAMLVVQVTDVEKHNDDVPKIDNKEELPETVQWLVDLLGPTDIEMVTETYWRATHYMSDVATQYADGKLTLAQKALAEQCYFAVCRRLHNSLKARQRSHRQVLDELNDKLADKYICNFSVFQSLPDTWAIGQVLPILPLHRLDEEPLRRAVLQDLTCDSDGKIKQYVDEQSIETSLPVHGLNEGEDYLLGIFLVGAYQEILGDMHNLFGDTDSVNIYQNADGSVYHAGIETHDTIEDMLRYVHLSPEELMTHYRDKCASARISAAERTQFLDALRLGLTRSSYLSS Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_1578 N-formylglutamate deformylase (EC 3.5.1.68) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (3.5.1.68) was linked to the condition via a SEED subsystem. This annotation was also checked manually. N-formylglutamate deformylase (EC 3.5.1.68) VDKVLNFKQGRVPLLISMPHAGLRLTPVVEAGLIPDAKSLPDTDWHIPRLYEFAAELGASTLAAEYSRFVIDLNRPSDDKPLYVGATTGLYPATLFDGIPLFREGMEPSATERATYLEQIWTPYHRTLQEELARLKAEFGYALLFDAHSIRSIIPHLFDGKLPDFNLGTFNGASCDPQLASQLEAICARHGDYSHVLNGRFKGGHITRHYGNPAENIHAVQLELGQCTYMEEFEPFRYRPDLAAPTQVVLRELLQGLLAWGEKHYR Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_1579 Imidazolonepropionase (EC 3.5.2.7) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (IMIDAZOLONEPROPIONASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Imidazolonepropionase (EC 3.5.2.7) MKTLWQHCHVATMAQGAYSIIEDAAIVTSGAHIEWIGPRGELPPGEYPAVNDLNGAWVTPGLIDCHTHTVFGGNRSGEFEQRLQGVSYAEIAAAGGGIASTVRATRAASEDELFASAAKRLKSLMRDGVTSIEIKSGYGLDLANERKMLRVVRRLGAELPVSVRSTCLAAHALPPEYTDRADAYIDHICTEMLPALAAEGLVDAVDAFCEYLGFSPEQVERVFVAAQNLGLPVKLHAEQLSSLHGSSLAARYHALSADHLEFMTEDDAIAMAKSGTVAVLLPGAFYFLRETQLPPMEALRKHGVKIAIASDLNPGTSPALSLRLMLNMACTCFRMTPEEALAGATIHAATALGMAETHGSLEAGKVADFVAWQIDRPADLSYWLGGDLEKRVVRHGVETSV Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_1582 Histidine ammonia-lyase (EC 4.3.1.3) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (HISTIDINE-AMMONIA-LYASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Histidine ammonia-lyase (EC 4.3.1.3) MSQAEKIVIADAPLRWQDVVAVARHGAQLELSPQIWTRIENAQAIVQRIVASGERAYGVNTGLGALCNVSLKGEQLSQLSRNTLLSHACGVGAPLADEQTRAIICAAIRNYSHGKSGIHRRVVEALLALLNRGITPQVPSQGSVGYLTHMAHIGITLLGVGNVSYRGQIVTAQQALSEEGLQPVQLGAKDGLCLVNGTPCMTGLSCLAIADATRLVQWADVIGAMSFEAQRGQIAAFDAEIIALKPHLGMQQVGINLRALLDGSEVIASSKGIRTQDALSIRSIPQVHGAARDQLEHAKKQIETELNSVTDNPMLLGTPDNFRVMSQANPHGQSVALAADLLAIAMAEIGSIAERRLDRLINPHVSGLPAFLVANPGVNSGMMIVQYVAASLCAENRQLAQPAVLDNYVTSGLQEDHLSMGTNAALKLHRALENCTQILAIEYLLAAQAFEFLKEQRFGAGTDTAWRLLRERVPAYDQDRWLAPDIAAAAGVLKDPILLHKALPNLN Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_1587 Urocanate hydratase (EC 4.2.1.49) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (UROCANATE-HYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Urocanate hydratase (EC 4.2.1.49) VTDNKPTKYRNVEIRAARGNKLTAKSWLTEAPLRMLMNNLDPEVAENPKELVVYGGIGRAARNWECYDKIVESLTNLNDDETLLVQSGKPVGVFKTHSNAPRVLIANSNLVPHWANWEHFNELDAKGLAMYGQMTAGSWIYIGSQGIVQGTYETFVEAGRQHYNDDLKGRWVLTAGLGGMGGAQPLAATLAGACSLNIECQQVSIDFRLNSRYVDEQATDLDDALARIAKYTKEGKAISIALLGNAAEILPELVKRGVRPDMVTDQTSAHDPLNGYLPAGWTWEEYRARAKTEPAAVVKAAKQSMAVHVKAMLDFQKMGIPTFDYGNNIRQMAQEEGVENAFDFPGFVPAYIRPLFCRGIGPFRWAALSGDPQDIYKTDAKVKELIPDDAHLHNWLDMARERISFQGLPARICWVGLGLRAKLGLAFNEMVRSGELSAPIVIGRDHLDSGSVSSPNRETESMQDGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGFSQHSGMVIVCDGTDEAAERIARVLHNDPATGVMRHADAGYQIAIDCAKEQGLNLPMITGK Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_1591 Formiminoglutamic iminohydrolase (EC 3.5.3.13) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (FORMIMINOGLUTAMATE-DEIMINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Formiminoglutamic iminohydrolase (EC 3.5.3.13) MSAFFAERALLPSGWANNVRLEVSADGVLTHIQADSHADDAERLSGPLLPGMPNLHSHAFQRAMAGLAEVAGNPNDSFWTWRDLMYRLVGKISPDQLGVIARQLYIEMLKAGYTSVAEFHYVHHDTSGQPYADPAELALRISQAASSAGIGLTLLPVLYSHSGFGGQAPNEGQRRFINSTENYLKLQSRLQPILAQQPAQALGLCFHSLRAVTPQQISEVLAASDKQCPVHIHIAEQQKEVDDCLSWSGRRPLQWLYENTDVDQRWCLVHATHANPEEVTLMAKSRAIAGLCLTTEANLGDGIFPAVDFLAQGGRMGIGSDSHVSLSVVEELRWLEYGQRLRDQRRNRLYGADQPMVGRTLYDAALDGGAQALGQPIGALEVGKRADWLVLDGNDPYLATASGDGILNRWLFAGGDRQVRDVLVNGQWVVRDGRHAGEEESNRAFTQVLRDLLG Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_2023 L-asparaginase (EC 3.5.1.1) Specifically important for utilizing L-Asparagine. Automated validation from mutant phenotype: the predicted function (ASPARAGHYD-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-asparaginase (EC 3.5.1.1) MNSSTFPAAQHVMVLYTGGTIGMQASAHGLAPASGFEARMREYLHSQPELVVPQWRFREMAPLIDSANMTPAYWQQLREAVVDAVDVQGCDSVLILHGTDTLAYSAAAMSFQLLGLHARVVFTGSMLPAGVTDSDAWENLSGALVALGQGLAPGVHLYFHSELLDPTRCAKVRSFGRHPFKRLERQGGGVKATSVPAQLNYNQPKQLAKVAALPLFPGIGAEQLDGLLNSGIQGLVLECYGSGTGPSDNPAFLASLERARDKGVVVVAVTQCHEGGVQLDVYEAGSRLRDAGVLSGGGMTREAAFGKLHALLGAGLETTEVRRLVELDLCGELS Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_2429 Carnitine 3-dehydrogenase (EC 1.1.1.108) Specifically important for utilizing Carnitine Hydrochloride. Automated validation from mutant phenotype: the predicted function (CARNITINE-3-DEHYDROGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Carnitine 3-dehydrogenase (EC 1.1.1.108) @ 3-hydroxybutyryl-CoA dehydrogenase (EC 1.1.1.157) @ 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) MSFITDIKTFAALGSGVIGSGWVSRALAHGLDVVAWDPAPGAEAALRKRVANAWGALEKQGLAPGASQDRLRFVATIEECVRDADFIQESAPERLELKLELHSKISAAAKPNALIGSSTSGLLPSEFYESSTHPERCVVGHPFNPVYLLPLVEVVGGKNTAPQAVQAAMKVYESLGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLAGGDAGMRHFMAQFGPALQLPWTYLPAPELTDKLIDDVVDGTSEQLGKHSISALERYRDDCLLAVLEAVKTTKEKHGMAFSE Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_2504 5-aminopentanamidase (EC 3.5.1.30) Specifically important for utilizing L-Lysine. Automated validation from mutant phenotype: the predicted function (5-AMINOPENTANAMIDASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 5-aminopentanamidase (EC 3.5.1.30) MRVALYQCPPLPLDVAGNLQRLHQLALEAKGADLLVLPEMFLTGYNIGIDAVSVLAEVHNGESAQQIARIAKTTGIAILYGYPERTEDGQIYNAVQLIDANGERLCNYRKTHLFGDLDHSMFSPGPDEFPLVELNGWKLGFLICYDLEFPENARRLALAGAELILVPTANMIPYDFIADVTVRARAFENQCYVAYANYCGHEGEIQYCGQSSIAAPDGSRIAQAGLDEALIVGELDRQLMIDSRAANRYFLDRRPELYGELNKR Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_2505 Lysine 2-monooxygenase (EC 1.13.12.2) Specifically important for utilizing L-Lysine. Automated validation from mutant phenotype: the predicted function (LYSINE-2-MONOOXYGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Lysine 2-monooxygenase (EC 1.13.12.2) MNKNNRHPADGKKPVTVFGPDFPFAFDDWIEHPAGLGSIPAHNHGAEVAIVGAGIAGLVAAYELMKLGLKPVVYEASKMGGRLRSQAFNGAEGIIAELGGMRFPVSSTAFYHYVDKLGLQTKPFPNPLTPASGSTVIDLEGKTHYAQKLADLPALFQEVADAWADALEAGSQFSDIQQAIRDRDVPRLKELWNTLVPLWDDRTFYDFVATSEAFAKLSFHHREVFGQVGFGTGGWDSDFPNSMLEIFRVVMTNCDDHQHLVVGGVEQVPLGIWRHVPERCVHWPEGTSLSSLHSGAPRSGVKKIAHAPNGRFTVTDNYGDTREYAAVLTTCQSWLLTTQIECDESLFSQKMWMALDRTRYMQSSKTFVMVDRPFWKDKDPETGRDLMSMTLTDRLTRGTYLFDNGDDKPGVICLSYSWMSDALKMLPHPVEKRVKLALDALKKIYPKVDIAARIIGDPITVSWEADPHFLGAFKGALPGHYRYNQRMYAHFMQDDMPAEQRGIFIAGDDVSWTPAWVEGAVQTSLNAVWGIMKHFGGETHAENPGPGDVFNEIGPIALPE Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_3440 Succinylornithine transaminase (EC 2.6.1.81) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (SUCCORNTRANSAM-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Succinylornithine transaminase (EC 2.6.1.81) MSVEHAAVERADFDQVMVPNYAPAAFIPVRGAGSRVWDQSGRELIDFAGGIAVNVLGHAHPALVAALTEQANKLWHVSNVFTNEPALRLAHKLVDATFAERVFFCNSGAEANEAAFKLARRVAHDRFGTEKYEIVAALNSFHGRTLFTVNVGGQSKYSDGFGPKITGITHVPYNDLAALKAAVSDKTCAVVLEPIQGEGGVLPAELSYLQGARELCDAHNALLVFDEVQTGMGRSGKLFAYQHYGVTPDILTSAKSLGGGFPIAAMLTTEDLAKHLVVGTHGTTYGGNPLACAVAEAVIDVINTPEVLNGVNAKHDKFKTRLEQIGEKYGLFTEVRGLGLLLGCVLSDAWKGKAKDIFNAAEREGLMILQAGPDVIRFAPSLVVEDADIDAGLDRFERAAAKLTQA Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_3835 Nitrate reductase (EC 1.7.99.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.99.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Assimilatory nitrate reductase large subunit (EC:1.7.99.4) MNQITASTCCYCGVGCGVLIEHDGERILGVSGDPAHPANFGKLCSKGSTLHLTGDLTARALYPELRLGKGLARSRTDWDTALDHAANVFAETIAEHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCNYEDLELSDCVMIVGSNMAYAHPVLFRRLEEAKSRRPQMKVIVIDPRRTDTCDLADMHLAILPGTDVALFHGILHLLLWEDWVDRDFIKAHTEGLAELKNLVRDYTPTMVSQLCGISVEQLQQCAQWVGTSPSFLSLWCMGLNQSTAGSAKNSALINLHLATGQIGRPGAGPFSLTGQPNAMGGRETGSLSNLLPGHREAANAEHRAQVADYWGVDQLPANTGLTAIELFEQMRSGKIKALWIACTNPAQSLPDQTAVREALQACPFVVLQEAFRTTETAAFADLLLPAASWGEKDGTVTNSERRISHVRRAIGAPGEARSDWAITVDFAQRLEKHLRPGATSLFAFETPAQVFDEYKHLTRGRDLDLSGISHALIDQLGPQQWPFPAGAREGTARLYLDGVFPTASGRAQFITDPYRAAKEQRDARFPLTLITGRLRDQWHGMSRTGTAAQLFGHVSEAVLSLHPDELRRHRLQPGDLINLKSRRGSVIVPVSSDDSVRPGQAFLPMHWGDRFLKGGVNTLTLPAFDPLSKQPELKHSGVRLEPVQLPWQLFALIEGDVQQHLETLRPLCEAFSYASLSLTGRERPALLIRAASAAAPEPQLLRDIDQCLGLNEGPVLAYDDPRRSIGKRVRIENGRITAIRLAGETLAQHWLQSLWLEGRADEQLRRWLLAPLSAPPGSAGGPASGTKTLCNCMNVSQNAVCAGIGRGLDLQGLKQELGCGTQCGSCVPEIKRLLAATAQPVAVIS Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_4042 Isocitrate lyase (EC 4.1.3.1) Specifically important for utilizing Tween 20. Automated validation from mutant phenotype: the predicted function (ISOCIT-CLEAV-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Isocitrate lyase (EC 4.1.3.1) MALTREQQIAALEKDWAENPRWKGVTRNYSAADVVRLRGSVQPEHTFAKMGADKLWNLVTQGAKPSFRPEKDFVNCMGALTGGQAVQQVKAGIQAIYLSGWQVAADNNSAESMYPDQSLYPVDSVPTVVKRINNSFRRADQIQWKAGKNPGDEGYIDYFAPIVADAEAGFGGVLNAYELMKSMIEAGAAGVHFEDQLASVKKCGHMGGKVLVPTQEAVQKLTAARLAADVAGTPTIILARTDANAADLLTSDCDPYDQPFVTGERTQEGFYKVRAGLDQAIARGLAYAPFADLIWCETAKPDLDEARRFAEAIKKEYPDQLLSYNCSPSFNWKKNLDDATIAKFQRELSAMGYKHQFITLAGIHNMWHSMFNLAHDYARNDMTAYVKLQEQEFADAAKGYTFVAHQQEVGTGYFDDMTTVIQGGTSSVTALTGSTEEEQFH Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_413 L-arabinolactonase (EC 3.1.1.15) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (L-ARABINONOLACTONASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-arabinolactonase (EC 3.1.1.15) MVNVTASSRASPLPHKSNKKGGFMTWTAVTGHRAQLGEGPFWDAPTQALYWVDIAGKQALRLIGANVEIWQMPEHVSAFIPCESGDALVTLSSGVYRLDLASPGLEPRLTLFCVADPQPGNRPNEARCDAQGRLWLGTMQNNIGEQGEDLPVVRRSGGLFRIDRDARVTPLLRGLGIPNTLLWSDDGTTLYFADSLDSTLYRHFIHTDGNLDTAYVWFGPHERGGPDGSAMDAEGYVWNARWDGSCLLRLNPDGYVDRVIELPVSRPTSCVFGGEDFKTLYITSAASPLNHPLDGALLSIRVDVPGKACQRFAG Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_4790 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) Specifically important for utilizing L-Valine. Automated validation from mutant phenotype: the predicted function (3.1.2.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) MDATQNEVLAEVRNHIGHLTLNRPAGLNAITLDMVRSLQQQLDAWAQDPQVHAVVLRGAGEKAFCAGGDIRSLYDSFKSGDTLHEDFFVEEYALDLAIHHYRKPVLALMDGFVLGGGMGLVQGADLRVVTERSRLAMPEVAIGYFPDVGGSHFLPRVPGELGIYLGVSGVQIRAADALYCGLADWYLESNKLGTLDEQLDQLQWHETPLKDLQGLLAKLAVQQLPAAPLAALRPAIDHFFALPDVPSMVEQLRAVTVADSHEWATATADLLESRSPLAMGVTLEMLRRGRHLSLEQCFALELHLDRQWFERGDLIEGVRALLIDKDKNPRWSPPTLQALDAGHVASFFTGFDPSWS Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_5116 Sucrose alpha-glucosidase (EC 3.2.1.48) Specifically important for utilizing Sucrose. Automated validation from mutant phenotype: the predicted function (3.2.1.48-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Sucrose-6-phosphate hydrolase (EC 3.2.1.B3) MSAALEIAQHALSDGLSRVTDDYRPGYHLAPPAGWMNDPNGVVYFRGEYHVFYQHHPFDAKWGPMYWGHAKSADLVHWQHLPIALAPGDDFDRDGCFSGSAVVCGDTLALIYTGHTWLGEVGDERYIRQVQCLATSTDGIQFVKHGAVIDTAPQDTIMHFRDPKVWQEDDGWYLIAGARLGDVPLLPLYRSTDLHSWEFLDYVSSGSEGDGYMWECPDLFRLNGRDVLLYSPQGMQPEGYERLNKYQTGYRVGRLDSQWHFTGGPFIELDNGHDFYAAQTLLAADGRRLVWAWLDMWESPMPSQAHHWCGMLGVPRELELHADRLCVYPARELTALRMAPLPGVSWWEGSGSRWVPEVNGDMLEIHVHLDLRGCTSGHLGIALRCSDDGHEETLLYYDASLQRLVLDRSRAGAQVTGQRSVSIDPTQERLELRVFLDRSSIEVFDENGRFSLSSRLYPRPDSLGVKLFANGSGGRVSIPKAWPLASGWL Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_6031 Ribokinase (EC 2.7.1.15) Specifically important for utilizing D-Ribose. Automated validation from mutant phenotype: the predicted function (RIBOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Ribokinase (EC 2.7.1.15) MPAKVVVIGSLNMDLVTRAPRLPRGGETLIGKSFATVSGGKGANQAVAAARLGAQVSMVGCVGNDAYGEALRGALLAEQIDCQAVSTVEDSSGVALIVVDDNSQNAIVIVAGANGALTPEVIDRFDAVLQAADVIICQLEVPDATVGHALKRGRELGKTVILNPAPASRPLPVDWYAAIDYLIPNESEASVLSGLPVDSLSTAETAATRLIAMGAGKVIITLGSQGSLFADGQRFEHFPAAKVKAVDTTAAGDTFVGGFAAALAAGKGEADAIRFGQVAAALSVTRAGAQPSIPTLSDVQAFKAP Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_00805 AO353_00805 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrite reductase MKKLKLVMIGNGMAGVRTLEELLKLSSELYDITVFGAEPHTNYNRILLSPVLAGEQTFEEIVLNDLDWYLENNIKLLLNRKVVEIDRVKRRVIAEDGSEAEYDRLLIATGSTPFILPIPGNTLEGVIGYRDIADTQVMIDTAKTHKHAVVIGGGLLGLEAANGLMLRGMHVTVVHLGEWLLERQLDKTSGQLLQTALEGRGLHFRLCEQTQALHDAGNGRVGSVQFKNGDIIPADLVVMAAGIRPNTELAEKSGIPCNRGILVNDTLQTYDPRIYAIGECASHRGIAYGLVAPLFEQAKVCANHLAQLGFARYSGSVTSTKLKVTGIDLFSAGDFMGGEGTETITLSDPIGGVYKKLVIKDDVLVGACLYGDTADGGWYFRQIRENHAIGEIRDHLMFGENALGDVGHQGQDKAMSMADNAEVCGCNGVCKGTIVKAIQEHGLFSVDEVKKHTKAASSCGSCAGLVEQILINTVGGAADVKPKSEKAICGCSDLNHGQIRQAIREEHLLTIAGTMSYLNWRTPNGCATCRPALNYYLISTWPGEAKDDPQSRLINERAHANIQKDGTYSVVPRMWGGVTNPSELRRIADVADKYNVPMVKVTGGQRIDLLGIKKQDLPGVWKDLDMPSGHAYGKSIRTVKTCVGSEFCRFGTQNSTQLGIELEHDLFNMWSPHKVKLAVSGCPRNCSEAGIKDVGIIGVDSGWEMYIGGNGGIKTEVAEFFVKLKTAEEVREYNGAFLQLYREEAFYLERTVHYLQRVGMEHIKKAVLEDPERRKALNDRLQFSLSFEQDPWKERLEQPLLKKEFDVIPVKNLEVPA Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_00810 AO353_00810 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrite reductase MNWLDICALEEINALGSRIVSGPKGDIAIFRTSDDEVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQIDLESGQALAPDVGCAHHHPARVENGRVMLALREAG Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_00815 AO353_00815 Nitrate reductase (EC 1.7.99.4) Specifically important for utilizing Sodium nitrate and Sodium nitrite. Automated validation from mutant phenotype: the predicted function (1.7.99.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. nitrate reductase MSRQTTASTCCYCGVGCGVLIEHDGEQILGVSGDPTHPANFGKLCSKGSTLHLTGDLAARALYPELRLGKGMARSRTDWDTALDHATSVFADTIAEHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYEDLELSDCVMIVGSNMAYAHPVLFRRLEEAKSRRPQMKVIVIDPRRTDTCDLADLHLAILPGTDVALFHGILHLLLWEDWVDREFIKAHTEGLAELKSLVRDYTPQMVAQLCGISVEQLQQCAEWVGTSSSFLSLWCMGLNQSTAGSAKNSALINLHLATGQIGRPGTGPFSLTGQPNAMGGRETGSLSNLLPGHREAANAQHRAEVAAYWGVEKLPDTTGLTAIELFEQVQSGKIKALWIACTNPAQSLPDQQTVRAALQACPFVVLQEAFRTTETAPFADLLLPAASWGEKEGTVTNSERRISHVRRAINAPGEARPDWAITVDFAQRLERRLRPGQPSLFAFEQPAQVFDEYKQLTRGRDLDLCGISHALLDRLGPQQWPFPDGASSGTPRLYADGIFPTESGRAQFVADPYRAAKEQRDARFPLTLITGRLRDQWHGMSRTGTAAQLFGHVSEALLSLHPDELRRYRLQTGDLVNLKSRRGSVIVAIGSDDSVRPGQAFLPMHWGDRFLKGGVNTLTQPAFDPLSKQPELKHSGVRIEPVKLPWHLFALVEGDVQQHFETLRPLCEDFSYASLSLTGRERPALLIRAASAQAPDPQRLHAIDQQLGLNDGPVLAYDDPRRAIGKRVRIEQGRITAIRLAGETLAQHWLQNLWLEGRADEQLRRWLLAPLSTPPGSAGSSVSTTKTLCNCKNVSESAVCAGIRSGLDLQGLKQQLGCGTQCGSCVPEIKRLLAANVQPIAITS Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_03060 AO353_03060 Acetyl-coenzyme A synthetase (EC 6.2.1.1) Specifically important for utilizing Ethanol. Automated validation from mutant phenotype: the predicted function (ACETATE--COA-LIGASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. acetyl-CoA synthetase MSAASLYPVRPEVAANTLTDEATYKAMYQQSVVNPDGFWREQAKRLDWIKPFTTVKQTSFDDHHVDIKWFADGTLNVSYNCLDRHLAERGDQIAIIWEGDDPAESRNITYRELHEQVCKFANALRGQDVHRGDVVTIYMPMIPEAVVAMLACTRIGAIHSVVFGGFSPEALAGRIIDCKSKVVITADEGLRAGKKISLKANVDDALTNPETSSIQKVIVCKRTGGNIKWNQHRDIWYEDLMKVAGTVCAPKEMGAEEALFILYTSGSTGKPKGVQHTTGGYLLYAALTHERVFDYRPGEIYWCTADVGWVTGHTYIVYGPLANGATTLLFEGVPNYPDITRVAKIIDKHKVNILYTAPTAIRAMMAQGTAAVEGADGSSLRLLGSVGEPINPEAWEWYYKNVGQSRCPIVDTWWQTETGATLMSPLPGAHGLKPGSAARPFFGVVPALVDNLGNIIEGVAEGNLVILDSWPGQARTLYGDHDRFVDTYFKTFRGMYFTGDGARRDADGYWWITGRVDDVLNVSGHRMGTAEIESAMVAHPKVAEAAVVGVPHDIKGQGIYVYVTLNGGEEPSEALRLELKNWVRKEIGPIASPDVIQWAPGLPKTRSGKIMRRILRKIATGEYDGLGDISTLADPGVVQHLIDTHKTMNVA Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_03500 AO353_03500 Glycine dehydrogenase (aminomethyl-transferring) (EC 1.4.4.2) Specifically important for utilizing Glycine. Automated validation from mutant phenotype: the predicted function (1.4.4.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. glycine dehydrogenase MTQVNLSTANEFIARHIGPRAGDEQAMLNSLGFDSLEALSASVIPDSIKGTSVLGLEDGLSEAEALASIKAIAAKNQLFKTYIGQGYYNCHTPSPILRNLLENPAWYTAYTPYQPEISQGRLEALLNFQTLISDLTGLPIANASLLDEATAAAEAMTFCKRLSKNKGSHAFFASIHSHPQTLDVLRTRAEPLGIDVVVGDERELTDVSAFFGALLQYPASNGDLFDYRELTERFHAVNALVAVAADLLALTVLTPPGEFGADVAIGSAQRFGVPLGFGGPHAAYFSTKDAFKRDMPGRLVGVSVDRFGKPALRLAMQTREQHIRREKATSNICTAQVLLANIASMYAVYHGPKGLKQIANRIHHLTAILAKGLSALGLNVEQANFFDTLTLATGANTAALHDKARAQRINLRVIDGERLGLSLDETTTQADIETLWSVLADGKALPDFAALAASVQSRIPAELVRQSPILSHPVFNRYHSETELMRYLRKLADKDLALDRTMIPLGSCTMKLNAASEMIPVTWAEFGALHPFAPPAQSAGYQQLTDELEAMLCAATGYDAISLQPNAGSQGEYAGLLAIRAYHQSRGEERRDICLIPSSAHGTNPATANMAGMRVVVTACDARGNVDIEDLRAKAIEHREHLAALMITYPSTHGVFEEGIREICGIIHDNGGQVYIDGANMNAMVGLCAPGKFGGDVSHLNLHKTFCIPHGGGGPGVGPIGVKSHLTPFLPGHAAMERKEGAVCAAPFGSASILPITWMYIRMMGGAGLKRASQLAILNANYISRRLEEHYPVLYTGSNGLVAHECILDLRPLKDSSGISVDDVAKRLIDFGFHAPTMSFPVAGTLMIEPTESESKEELDRFCDAMICIREEIRAVENGTLDKDDNPLKNAPHTAAEIVGEWTHPYSREQAVYPVASLIEGKYWPPVGRVDNVFGDRNLICACPSIESYA Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_04450 AO353_04450 N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (NAG6PDEACET-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-acetylglucosamine-6-phosphate deacetylase MSEDNILTAQGWIRGRLIHEHGKIVRIEGQPCDPADNDLPYLLPGFIDLHVHGGGGKDIMEGTPAFDTITKTHVRFGTTSLLATTMTAPPEEISRVLAEVGEFCEQRPKGCARVLGVHLEGPYINPGKLGAQPNFAHTALMAEVEAYLALAPIRVITIAPEIAGHDKLIRALSDRGIRMQIGHTLGSYEEGVAALEAGASSFTHLYNAMSPLHHREPGIVGAALAHAKYAELIPDLLHVHPGAIRVALRSIPCLYCVTDSTAAAGMPDGEYKLGSHTVTKCLGGVRLPDGTLAGSTLTMDQALRNLVKIGLPLAEASQRLSQFPADYLGIQERGRLQPGAWADCVRLDRSLTLTAVMVEGEDIDFKNA Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_04455 AO353_04455 Glucosamine-6-phosphate deaminase [isomerizing], alternative (EC 3.5.99.6) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (GLUCOSAMINE-6-P-DEAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. iron dicitrate transport regulator FecR MLEEALSSYKAVDAQLQQLDPLMIEIAGRLNRQPPQVAMTVARGSSDHAASYFAYLTMQHVGIPVASLPMSVVTMQQAPLKVSGQAVFAFSQSGQSPDLVNSLRLLRKRGALSISMVNAENSPLEAACEFSLPLCAGTESSVAATKSFIATLSASARLIAYWKQDPELLQAGLALPEGLRDAATQDWSLAVDVLRDCQRLMVIGRGAGFAIAQEAALKLKETSAIQAEAFSSAEVKHGPMALIDDNYPLLVFAPRGAEQAGLLSLAAEMRQRGARVLLAAPDDVSERDLTLSRAEHPALDPILAIQSFYVMAAGLAVARGMDPDQPRHLSKVTRTH Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_05935 AO353_05935 Kynureninase (EC 3.7.1.3) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (KYNURENINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. kynureninase MITRNDCLALDAQDPLAHLRHQFALPEGVIYLDGNSLGARPVAALERAQAVIAEEWGNGLIRSWNSAGWRDLPERLGNRLAGLIGAGEGEVVVTDTTSINLFKVLGAALRVQAMRAPTRRVIVSESSNFPTDLYIAEGLMDLLQQGYSLRLVDSPEELAQAIDQDTAVVMLTHVNYKTGYMHDMQAVTALIHECGALAIWDLAHSAGAVPVDLRQAGADYAIGCTYKYLNGGPGSQAFVWVAPQLCDLVTQPLSGWFGHSRQFDMASGYEPSSGIARYLCGTQPITSLAMVECGLEIFAQTDMPSLRRKSLALTDLFIQLVEQRCAAHDLKLITPREHARRGSHVSFEHPQGYAVIQALIAQGVIGDYREPRIMRFGFTPLYTSFTEVFDAVQILGEILDQQTWSQAQFQVRHSVT Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_05950 AO353_05950 Anthranilate 1,2-dioxygenase (deaminating, decarboxylating) (EC 1.14.12.1) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (1.14.12.1-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. anthranilate 1,2-dioxygenase large subunit MSGEKNVEQWKAFIEGCLDFRPAEGVFRIARDIFTEPQLFDLEMELIFEKNWIYACHESELANNHDFITMRAGRQPMIITRDGDGQLNALINACQHRGTTLTRVGKGNQSTFTCPFHAWCYKSDGRLVKVKAPGEYPEGFDKATRGLKKARIQSYKGFVFISLDVHGDNSLEDFLGDAKVFFDMMVAQSPTGELEVLPGKSAYTYDGNWKLQNENGLDGYHVSTVHYNYVATVQHRQQVDSKNGTRASGTLDYSKLGAGDANTDDGWFAFNNGHSVLFSDMPNPTVRSGYATIMPRLIEEHGQEKAEWMMHRLRNLNIYPSLFFLDQISSQLRIIRPVAWNKTEIISQCLGVKNESDADRENRIRQFEDFFNVSGLGTPDDLVEFREAQRGFQARLERWSDISRGSHQWATGATPNSEAIGIAPAMTGTEFTHEGLYVNQHSNWQKFLLDGLDAKSLKLREV Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_05955 AO353_05955 Anthranilate 1,2-dioxygenase (deaminating, decarboxylating) (EC 1.14.12.1) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (1.14.12.1-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. benzoate 1,2-dioxygenase small subunit MNPQLQYQIEQFFYRKSELCDAKDWDAYIQLFDEQSEFHLPQWDSEHVYTRDPKREMSLIYYANRSGLEDRVFRLHTGKAASATPMPRTLHLINNVRISELEAGELEVRLNWHTLFYRLATSEQFYGDATYRLKPHADSWLITRKHVLLLNDTINSVLDFYHL Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_05970 AO353_05970 Tryptophan 2,3-dioxygenase (EC 1.13.11.11) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (RXN-8665) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. tryptophan 2,3-dioxygenase MSQCPYSSDQSPSNPPEEWHNAELNFSDSMSYGDYLDLGKILSAQHPLSPDHNEMLFIIQHQTSELWMKLMLHELKAAREHVRLGELPPAFKMLARVSRIFDQLVHAWTVLATMTPTEYHAIRPFLGQSSGFQSFQYREIEFILGNKSATLLRPHAHRPELLAELEKAIATPSLYDESIRLMVSAGLAIDPQRFERDPASPTAYDASVEAAWRVVYTDPSRYWDLYQLAEKLIDLEDSFRQWRFRHVTTVERIIGFQPGTGGTEGVGYLRKMLDTVLFPELWRVRSTL Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_05975 AO353_05975 Kynurenine formamidase, bacterial (EC 3.5.1.9) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (ARYLFORMAMIDASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. kynurenine formamidase MKKTMSWWDISPPLSTATPTWPGDTPFQEERVWTFGPECPVNVGRITLSPHTGAHVDAPLHYSADGAAIGDVSLDVYIGPCRVLHCLDSGRLVQPEQLEGRLADLPERVLLRTYQQAPLTAWDPDFTAVAKETVDLLSSLGVRLIGIDTPSLDPQQSKTMDSHNAVARHGMAILEGIVLDDVPEGDYELIALPLRFANLDASPVRAILRPLNKPPLEEPAQ Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_05985 AO353_05985 3-hydroxyisobutyrate dehydrogenase (EC 1.1.1.31) Specifically important for utilizing L-Valine. Automated validation from mutant phenotype: the predicted function (3-HYDROXYISOBUTYRATE-DEHYDROGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 3-hydroxyisobutyrate dehydrogenase MKIAFIGLGNMGAPMARNLIKAGHSLNLVDLNKAVLAELAQLGGTISATAREAAQGAELVITMLPAAVHVRSVWLGEDGVLAGIAKGVPAVDCSTIDPQTARDVAAAAAKQGVAMADAPVSGGTGGAAAGTLTFMVGATPELFATLQPVLAQMGRNIVHCGEVGTGQIAKICNNLLLAISMVGVSEAMALGDALGIDTQVLAGIINSSTGRCWSSEMYNPWPGIVETAPASRGYTGGFGAELMLKDLGLATEAARQAHQPVMLGAVAQQLYQAMSQRGEGGKDFSAIINSYRKP Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_05990 AO353_05990 Methylmalonate-semialdehyde dehydrogenase (EC 1.2.1.27) Specifically important for utilizing L-Valine. Automated validation from mutant phenotype: the predicted function (RXN-11213) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. methylmalonate-semialdehyde dehydrogenase MNASLTPETTVQKVKLLIDGQWVESQTTEWHDIVNPATQQVLAKVPFATPAEVDAAISAAHRAFQTWKLTPIGARMRIMLKLQALIREHSKRIAVVLSAEQGKTIADAEGDIFRGLEVVEHACSIGSLQMGEFAENVAGGVDTYTLRQPIGVCAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSEQDPMSTMLLVELAIEAGIPAGVLNVVHGGKDVVDALCTHKDIKAVSFVGSTAVGTHVYDLAGKHGKRVQSMMGAKNHAVVLPDANREQALNALVGAGFGAAGQRCMATSVVVLVGAAKQWLPDLKALAQKLKVNAGSEPGTDVGPVISKRAKARILDLIESGIKEGAKLELDGRDITVPGYEKGNFVGPTLFSGVTTDMQIYTQEIFGPVLVVLEVDTLDQAIALVNANPFGNGTGLFTQSGAAARKFQNEIDVGQVGINIPIPVPVPFFSFTGSRGSKLGDLGPYGKQVVQFYTQTKTVTSRWFDDDSVNDGVNTTINLR Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_07420 AO353_07420 Lysine 2-monooxygenase (EC 1.13.12.2) Specifically important for utilizing L-Lysine. Automated validation from mutant phenotype: the predicted function (LYSINE-2-MONOOXYGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. amine oxidase MNKNNRHPADGKKPVTIFGPDFPFAFDDWIEHPAGLGSIPAHNHGAEVAIVGAGIAGLVAAYELMKLGLKPVVYEASKMGGRLRSQAFEGAEGIIAELGGMRFPVSSTAFYHYVDKLGLETKPFPNPLTPASGSTVIDLEGQTHYAQKLADLPALFQEVADAWADALEDGSRFGEIQQAIRDRDVPRLKELWNTLVPLWDDRTFYDFVATSKAFAKLSFHHREVFGQVGFGTGGWDSDFPNSMLEIFRVVMTNCDDHQHLVVGGVEQVPLGIWRHVPKRCAHWPEGTSLSSLHNGAPRTGVKRIARAADGRFSVTDNWGDTREYAAVLTTCQSWLLTTQIECEESLFSQKMWMALDRTRYMQSSKTFVMVDRPFWKDKDPETGRDLMSMTLTDRLTRGTYLFDNGDDKPGVICLSYSWMSDALKMLPQPIEKRVKLALDALKKIYPKVDIAARIIGDPITVSWEADPHFLGAFKGALPGHYRYNQRMYAHFMQQDMPAEQRGIFIAGDDVSWTPAWVEGAVQTSLNAVWGIMNHFGGKTHVENPGPGDVFHEIGPIALPE Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_07425 AO353_07425 5-aminopentanamidase (EC 3.5.1.30) Specifically important for utilizing L-Lysine. Automated validation from mutant phenotype: the predicted function (5-AMINOPENTANAMIDASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. carbon-nitrogen hydrolase MRVALYQCPPLPLDVAGNLQRLQKLATEAKGADLLVFPEMFLTGYNIGAEAVGALAEAQDGTCAQYIASIAKASGIAIVYGYPERAEDGQIYNAVQLIDSRGQRLANYRKTHLFGELDHSMFSVGPDEFPLVELNGWKLGFLICYDLEFPENARRLALAGAELILVPTANMIPYDFIADVTVRSRAFENQCYVAYANYCGHEGEIHYCGQSSIAAPDGSRIAQAGLDEALIVGTLDRQLMVDSRAANRYFLDRRPELYGELNKR Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_07670 AO353_07670 L-threonine aldolase (EC 4.1.2.5) Specifically important for utilizing L-Threonine. Automated validation from mutant phenotype: the predicted function (4.1.2.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. threonine aldolase MTDKSQQFASDNYSGICPEAWAAMEQANQGHQRAYGDDEWTARASDDFRKLFETDCEVFFAFNGTAANSLALSSLCQSYHSVICSETAHVETDECGAPEFFSNGSKLLIARTENGKLTPESIREIALKRQDIHYPKPRVVTLTQATEVGSIYTPEEIRAISATCKELGLNLHMDGARFSNACAFLNCSPADLTWKAGVDVLCFGGTKNGMAVGEAILFFNHKLAEDFDYRCKQAGQLASKMRFLSAPWVGLLENDAWLKHARHANYCAQLLAELVSDIPGVELMFPVQANGVFLQLSESAVAALTAKSWRFYTFIGKGGARFMCSWDTEVERVRELAADIREVMAG Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_09960 AO353_09960 L-asparaginase (EC 3.5.1.1) Specifically important for utilizing L-Asparagine. Automated validation from mutant phenotype: the predicted function (ASPARAGHYD-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. asparaginase MIPATYPAAQHVMVLYTGGTIGMQASANGLAPASGFEARMRDYLHSQPDLVVPNWRFREMTPLIDSANMTPAYWQRLRDAVIEAVDVDGCDSVLILHGTDTLAYSAAAMSFQLLGLHARVLFTGSMLPAGVPDSDAWENLGGALVALGQGLAPGVQLYFHGELLDPTRCAKIRSFGRHPFARLQRQGGGVKAPALPTALEYRQSKQLAKVGVLPLFPGIGAEQLDGVLNSGIQGLVLECFGSGTGPSDNPEFLASLARARDQGVVVVAITQCHEGGVELDVYEAGSRLRGVGVLSGGGMTREAAFGKLHALLGADLDTAEVRRLVELDLCGELS Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_12235 AO353_12235 Formiminoglutamic iminohydrolase (EC 3.5.3.13) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (FORMIMINOGLUTAMATE-DEIMINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-formimino-L-glutamate deiminase MSAFFAERALLPSGWANNVRLEVSADGLLTHIQADASAEGAERLSGPLLPGMPNLHSHAFQRAMAGLAEVAGNPNDSFWTWRDLMYRLVGKISPEQLGIIARQLYIEMLKAGYTSVAEFHYVHHDHNGHPYADPAELSLQISQAASASGIGLTLLPVLYSHSGFGGLAPNEGQRRFINSTENYLKLQARLQPLLAQQPAQQLGLCFHSLRAVTPQQISEVLAASDKHCPVHIHIAEQQKEVDDCLIWSGRRPLQWLYENTDVDQRWCLVHATHANPEEVSLMAKSRAIAGLCLTTEANLGDGIFPAVDFLAQGGRMGIGSDSHVSLSVVEELRWLEYGQRLRDQRRNRLYGADQPMVGRTLYDAALDGGAQALGQPIGALEVGKRADWLVLDGNDPYLATASGDGILNRWLFAGGDRQVRDVLVNGKWVVRDGHHAGEEDSNRAFTQVLRELLG Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_12250 AO353_12250 Urocanate hydratase (EC 4.2.1.49) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (UROCANATE-HYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. urocanate hydratase VTDNTQKPTPVTFTKHRDVEIRAPRGNKLTAKSWLTEAPLRMLMNNLDPEVAENPKELVVYGGIGRAARNWECYDKIVESLTNLNDDETLLVQSGKPVGVFKTHSNAPRVLIANSNLVPHWASWEHFNELDAKGLAMYGQMTAGSWIYIGSQGIVQGTYETFVEAGRQHYNDNLTGRWVLTAGLGGMGGAQPLAATLAGACSLNIECQQVSIDFRLKSRYVDEQAKDLDDALARIAKYTKEGKAISIALLGNAAEILPELVRRGVRPDMVTDQTSAHDPLNGYLPAGWTWEEYRARAKTEPAAVIKAAKQSMAVHVKAMLDFQKQGIPTFDYGNNIRQMAQEEGVENAFDFPGFVPAYIRPLFCRGIGPFRWAALSGNAEDIYKTDAKVKELIPDDAHLHNWLDMARERISFQGLPARICWVGLGLRAKLGLAFNEMVRSGELSAPIVIGRDHLDSGSVASPNRETESMQDGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGFSQHSGMVIVCDGTDEAAERIARVLHNDPATGVMRHADAGYQIAIDCAKEQGLNLPMITGK Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_12280 AO353_12280 Imidazolonepropionase (EC 3.5.2.7) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (IMIDAZOLONEPROPIONASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. imidazolonepropionase MKTLWQHCHVASMAQGTYSIIEDAAIVTSGAHIEWIGPRSELPSGEYLEVHDLAGAWVTPGLIDCHTHTVFGGNRSGEFEQRLQGVSYAEIAAAGGGIASTVRATRAATEDELFASAKKRLKSLMRDGVTSIEMKSGYGLDLASERKILRVIRRLGAELPISVRSTCLAAHALPPEYVDRADDYIEHICSEMLPALAAEGLVDAVDAFCEYLAFSPAQVERVFVAAQKLGLPLKLHAEQLSSLHGSSLAARYHALSADHLEFMTEEDAIAMAASGTVAVLLPGAFYFLRETQLPPMDALRKHGVKIAIASDLNPGTSPALSVRLMLNMACTCFRMTPEEALAGATIHAATALGMERTHGSLEVGKVADFVAWQIDRPADLSYWLGGDLEKRVVRHGVEVEL Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_12810 AO353_12810 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) Specifically important for utilizing L-Proline. Automated validation from mutant phenotype: the predicted function (1.2.1.88, 1.5.5.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. transcriptional regulator MATTTLGVKLDDPTRERLKAAATSIDRTPHWLIKQAIFNYLEKLEGGATLTELSGLTRSEADEGAEVHVDHAHQCFLEFAESILPQSVLRASITAAYRRPEPEVVPMLIEQARLPAPMAEATNKLAASIAEKLRNQKSAGGRAGIVQGLLQEFSLSSQEGVALMCLAEALLRIPDKGTRDALIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVATHNEAGLTSSLSRIIGKSGEPMIRKGVDMAMRLMGEQFVTGETIAEALANASKFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHGRGIYEGPGISIKLSALHPRYSRAQYERVMDELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPQLTGWNGIGFVIQAYQKRCPYVIDYVIDLARRSRHRLMIRLVKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYIACARKLLSVPEVIYPQFATHNAHTLSAIYHIAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVSEGKLNRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNRIADQSISIQELVADPVSSIEQMATLEGGFGLPHPRIPLPRDLYGSERANSSGIDLANEHRLASLSCALLATAHNNWKAAPMLGCAASAETPVPVLNPSDLRDVVGHVQEATVTDADNAIQCALNAAPIWQATPPAERAAILERAADLMESEIQPLMGLLAREAGKTFANAIAEVREAVDFLRYYAVQARNDFTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRILLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNVAGRLDAQGRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAECRLGNPERLSVDIGPVIDAEAKAGIEKHIQAMRDKGRNVYQVAIADMEECKRGTFVMPTLIELESFDELQREIFGPVLHVVRYKRKDIDQLIGQINASGYGLTLGVHTRIDETIAKVIDNVNAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPTDAIEQSFARGDTLSAPDVRLRDAMSKPLTALKTWADSHKLTELSALCAQFATQSQSGITRTLNGPTGERNSYAILPREHVLCLAEVESDLLSQLAAVLAVGGSAVWPEGELSKALLARLPKDVQARIKLVADWNKDEVVFDAVLHHGHSDQLRAVCQQVAKRAGAIIGVQGLSQGETNIALERLVIERALSVNTAAAGGNASLMTIG Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_13495 AO353_13495 Urease (EC 3.5.1.5) Specifically important for utilizing Urea. Automated validation from mutant phenotype: the predicted function (3.5.1.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. urease subunit alpha MKISRQAYADMFGPTVGDKVRLADTELWIEVEKDFTTYGEEVKFGGGKVIRDGQGQSQLLAAEVVDTLITNALIIDHWGIVKADVGLKDGRIAAIGKAGNPDVQPNVTIAVGASTEVIAGEGMILTAGGVDTHIHFICPQQIEEALMSGVTTMIGGGTGPATGTNATTCTSGPWHLARMLQAADAFPMNIGLTGKGNASLPEPLIEQVKAGAIGLKLHEDWGTTPASIDNCLNVADQFDVQVAIHTDTLNESGFVETTLAAFKGRTIHTYHTEGAGGGHAPDIIKACGFANVLPSSTNPTRPFTRNTIDEHLDMLMVCHHLDPSIAEDVAFAESRIRRETIAAEDILHDLGAFSMISSDSQAMGRVGEVITRTWQTADKMKKQRGALAGDGEGNDNFRVKRYIAKYTINPAITHGISHEVGSIEVGKWADLVLWRPTFFGVKPTLILKGGAIAASLMGDANASIPTPQPVHYRPMFASYGGSLHATSLTFISQAAQEAGLPEALGLKKKIAVVKGCREVQKTDLIHNDYLPKIDVDPQTYQVKADGVLLWCEPADVLPMAQRYFLF Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_13515 AO353_13515 Urease (EC 3.5.1.5) Specifically important for utilizing Urea. Automated validation from mutant phenotype: the predicted function (3.5.1.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. urease subunit gamma MDLTPREKDKLLIFTAGLVAERRLARGVKLNYPEAMAYISAALLEGARDGQTVAELMHYGTTLLNREQVMEGIPEMIPEIQVEATFPDGTKLVTVHQPIV Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_15500 AO353_15500 L-serine ammonia-lyase (EC 4.3.1.17) Specifically important for utilizing L-Serine. Automated validation from mutant phenotype: the predicted function (4.3.1.17) was linked to the condition via a SEED subsystem. This annotation was also checked manually. serine dehydratase MAISVFDLFKVGIGPSSSHTVGPMRAAATFAQALFDQGLLEQTRRVEVRLYGSLSATGVGHATDRACVMGLMGEWPDSIDPSCIGPRIQQLRESGELLLAGRRSIAFDWQRDLLLLDESLPYHPNAMSLTAFGESGQLWEQTYYSVGGGFIVEAAEAESGVPASSDVVLPYEFSSAVELLSLCNQHGLRVSELMMANERAWRSDAEIRSGLLHIWSVMRECVEQGLRHEGILPGGLDVPRRAAKLHRSLLEIGKPNVISSTLSAMEWVNLFALAVNEENAAGGRMVTAPTNGAAGIIPAVLHYYMKFNPDASDDDVVAFFLAAASVGILCKKNASISGAEVGCQGEVGSACAMAAAGLADVLGATPEQLENAAEIGLEHNLGLTCDPVGGLVQVPCIERNAIAAVKAINATQMALRGDGKHFISLDRVIRTMRDTGADMHDKYKETSRGGLAVSWVEC Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_15550 AO353_15550 Homogentisate 1,2-dioxygenase (EC 1.13.11.5) Specifically important for utilizing L-tyrosine disodium salt. Automated validation from mutant phenotype: the predicted function (HOMOGENTISATE-12-DIOXYGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. homogentisate 1,2-dioxygenase MNLDSTAPALVYQSGFGNEFSSEALPGALPVGQNSPQKAPYGLYTELFSGTAFTMARSEARRTWMYRIQPSANHPAFVKLERQLAGGPLGDVTPNRLRWNPLEIPGEPTDFIDGLVRMAANSGSEKPAGISIYHYRANRSMERVFFNADGEWLLVPEQGRLRIATELGVLELEPLEIAVLPRGLKFRIELLDPQARGYLAENHGAPLRLPDLGPIGSNGLANPRDFLTPVAHYEDLKQPTTLVQKFLGELWGCELDHSPLNVVAWHGNNVPYKYDLRRFNTIGTVSFDHPDPSIFTVLTSPTSVHGLANLDFVIFPPRWMVAENTFRPPWFHRNLMNEFMGLIQGTYDAKAEGFLPGGASLHSCMSAHGPDGETCTKAINAELAPSKIDNTMAFMFETSQVLRPSRFALDCPQLQNNYDACWASLPVTFNPNRR Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_15560 AO353_15560 Maleylacetoacetate isomerase (EC 5.2.1.2) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (5.2.1.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. maleylacetoacetate isomerase MELFTYYRSTSSFRVRIALALKGLEYQALPINLIAPQGGEHQQPAYLHINPQGRVPALRTDEGELLIQSPAIIEYLEERYPQVPLLSKDLARRAHERGVAALIGCDIHPLHNVSVLNQLRQLGHDEPQVVHWIGHWITQGLAAVEHLIGDEGYCFGNAPGLADVYLIPQLYAAERFNISLEAYPRIRRVAALAVQHPAFIKAHPANQPDTP Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_15985 AO353_15985 Alpha,alpha-phosphotrehalase (EC 3.2.1.93) Specifically important for utilizing D-Trehalose dihydrate. Automated validation from mutant phenotype: the predicted function (3.2.1.93) was linked to the condition via a SEED subsystem. This annotation was also checked manually. trehalose-6-phosphate hydrolase MQDWQRSVIYQIYPKSFHSHAGNPTGDLLGVVAKLDYLQWLGVDCLWITPFLRSPQRDNGYDISDYYAIDPSYGTMADCELLIAEAGKRGIKLMLDIVVNHTSIEHSWFQQARSSLDNPYRDFYIWRDQPNNWESKFGGSAWEYEAQTGQYFLHLFDHTQADLNWDNPQVRAEVFKLMRFWRDKGVGGFRLDVINLISKPADFPEDHTDGRRFYTDGPNVHEYLQEMHREVFEGHDLINVGEMSSTSLEHCIRYSRPDSKELSMTFNFHHLKVDYPNMQKWVRADFDFLELKRILSDWQTGMQAGGGWNALFWCNHDQPRVVSRFGDDGEHRVVSAKMLGTALHFLQGTPFIYQGEELGMTNPGFERIEQYRDVETLNIYRLKREAGESEASSMAAIMQKSRDNSRTPMQWSALPNAGFSSSEPWIGVPANAMQINVENQLDDTTSVLHHYRQLIALRRSEPLIQDGVYRQLLPTHKQVWVYLREGEGERLLVVNNFYGTACEVELPERVITDCMLQRLVISNYPDSEVRKQQLFLRPYESFVLHLTDH Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_17230 AO353_17230 Beta-ketoadipate enol-lactone hydrolase (EC 3.1.1.24) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (3-OXOADIPATE-ENOL-LACTONASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 3-oxoadipate enol-lactonase VGFVQLADGELKYQLDGPEHAPVLVLSNSLGTNLHMWDVQIPAFTKHFRVLRFDTRGHGRSLVTPGPYSIEQLGRDVLALLDALNIERAHFCGLSMGGLIGQWLGINAGERLHKLVVCNTAAKIGDPSVWNPRIETVLRDGPAAMVALRDASIARWFTPDFAQANPAVAKQITDMLAATSPQGYAANCAAVRDADFREQLASITVPTLVIAGTEDAVTPPSGGRFIQERVRGAEYAEFYAAHLSNVQAGSAFSDRVLSFLLAEKSI Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_18585 AO353_18585 Phenylalanine 4-monooxygenase (EC 1.14.16.1) Specifically important for utilizing L-Phenylalanine; L-tyrosine disodium salt. Automated validation from mutant phenotype: the predicted function (1.14.16.1) was linked to the condition via a SEED subsystem. This annotation was also checked manually. phenylalanine 4-monooxygenase MKQTQYVAREPDAQGFIHYTAEEHAVWNTLITRQLKVLEGRACQEYMDGIEKLGLPHDRIPQLDEINKVLGETTGWQVARVPALIPFQTFFELLASKQFPVATFIRTREELDYLQEPDIFHEIFGHCPLLTNPWFAEFTHTYGKLGLQASKEERVYLARLYWMTIEFGLVDTPQGKRIYGGGILSSPKETVYSLSGEPEHQAFDPLEAMRTPYRIDILQPLYFVLPNLKRLFDLAHEDIMGMVHQGMQLGLHAPKFPPKPKAA Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_20350 AO353_20350 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (RXN0-2301) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. isovaleryl-CoA dehydrogenase MSYPTLNFALGETIDMLRDQVRAFVSKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGTHEQKAKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDANTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEENILGVLNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_20835 AO353_20835 Ribokinase (EC 2.7.1.15) Specifically important for utilizing D-Ribose. Automated validation from mutant phenotype: the predicted function (RIBOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. ribokinase MPAKVVVVGSLNMDLVTRAQRLPHAGETLHGESFATVSGGKGANQAVASARLGAQVSMIGCVGDDAYGEQLRAALLAEQIDCQALTSVEGSSGVALIVVDDNSQNAIVIVAGANGQLTPGMVAGFDAVLAAADVIICQLEVPMHTVGYVLKRGRELGKTVILNPAPATSPLPADWYSSIDYLIPNESEASALSGLPVDSLESAELAASRLIAAGAGKVIITLGPQGSLFANGQSCEHFPAPKVKSVDTTAAGDTFVGGFAAALAAGKSEVEAIRFGQVAAALSVTRAGAQPSIPSLSDVQAFKAS Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_21340 AO353_21340 Myo-inosose-2 dehydratase (EC 4.2.1.44) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (MYO-INOSOSE-2-DEHYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. myo-inosose-2 dehydratase MPAIRIGINPISWSNDDLPALGGETPLSTALSEGKEIGYEGFELNGKFPKDAKGVGDVLRPYDLALVSGWYSSRLARRSVAEEIEAIGSHVELLAKNGAKVLVYGEVADSIQGQRIPLVERPRFHTEQAWQEYADKLNELARFTLSQGVRLAYHHHMGAYVESPADIDKLMSLTGSEVGLLFDSGHCYMGGGEPLEVLRKHIGRICHVHFKDVRKPVVQLARNNLWSFPDCIINGTFTVPGDGDIDFAALLDVLLAADYHGWLVVEAEQDPAVAPSYVYAKKGYETLRALLDQRTGQ Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_21365 AO353_21365 Inositol 2-dehydrogenase (EC 1.1.1.18) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (1.1.1.18) was linked to the condition via a SEED subsystem. This annotation was also checked manually. inositol 2-dehydrogenase MSLKLGVIGTGAIGQDHIRRCSQTLLNSQVVAVTDINLQQAAKVVADLKLTAEVYPDGHALIKAPDVEAILVTSWGPSHEEFVLAAIAAGKPVFCEKPLAVTAEGCRKIVEAEVAHGKRLVQVGFMRPYDEGYRALKAVIDSGQIGEPLMLHCAHRNPTVGENYKTDMAITDTLIHELDVLRWLLDDDYVSVQVVFPRKTSKAHAHLKDPQIVLLETAKGTRIDVEVFVNCQYGYDIQCEVVGETGIAKLPEPSQVQMRSGAKLSNAILMDWKDRFIAAYDVELQAFIDGVRAGQVGGPSAWDGFAAAVAADACIEAQQSGAIVNVALPDRPRFYG Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_23525 AO353_23525 Catechol 1,2-dioxygenase (EC 1.13.11.1) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (CATECHOL-12-DIOXYGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. catechol 1,2-dioxygenase MNAKISHTASAQKFLEEASGLLNDAGNPRAKALIYRILRDSVNIIEDLEVTPEEFWKAVNYLNELGARQEAGLLVAGLGLEHYLDLLMDAEDAQAGKTGGTPRTIEGPLYVAGAPLSNGEARLDDGVDPGVVLFMQGQVKNTDGKPLAGAVVDVWHANTGGTYSYFDGSQSEFNLRRRIVTDAEGRYRFRSIVPSGYGCPPDGPTQQLLDQLGRHGQRPAHIHFFISADDHRHLTTQINLDGDKYLHDDFAYATRDELIAKITFSDDQQRAREHGVSGRFAEIEFDFTLQSSAQPEEQHRHERVRALED Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_25210 AO353_25210 D-serine ammonia-lyase (EC 4.3.1.18) Specifically important for utilizing D-Serine. Automated validation from mutant phenotype: the predicted function (4.3.1.18) was linked to the condition via a SEED subsystem. This annotation was also checked manually. D-serine dehydratase MIQGKTLDAWYESHPIIKELVSLQEITWFNPAIASVSIALGDVGLNHNDVKDASERLRRFAPYIAKVFPETAAADGIIESGIQPLKKFQQRLLSEAGLPGVGSLWLKKDSDLPISGSIKARGGIHEVLKHAEDLALQAGLIKLDDNYEALASDSALEFFSRYKIAVGSTGNLGLSIGIMSAKLGFQATVHMSSDARQWKKDKLRASGVTVVEYESDYSVAVENGRLQAEKDPACYFIDDENSPHLFLGYAVAAERLARQFEFAGVRVDADHPLFVYLPCGVGGGPGGVAFGLKLAFGDAVHCVFAEPTHSPCMMLGVYTGLHDEVSVQEFGIDNVTAADGLAVGRPSGFVGKAMQRLIDGYYTVTDEELYRLMFLAHELENVKLEPSALAGAPGVVRVLNDEKYLERIGVSTAKLANATHLIWGTGGSMVPAAEFATYLDKGRALQHPAQ Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_26560 AO353_26560 Beta-ureidopropionase (EC 3.5.1.6) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (3.5.1.6) was linked to the condition via a SEED subsystem. This annotation was also checked manually. allantoate amidohydrolase MNAAVDVLQSSHQHIDRDRLWQSLMELAKLGATVKGGVCRLALTDLDRQARDIFVRWCEEAGCTVSIDAVGNIFARRAGRNPQLPPVMTGSHIDTQPTGGKFDGCFGVLAGVEVLRTLNDLGVETEAPLEVVVWTNEEGSRFAPCMMGSGVFAEKFTLEETLAKTDASGVTVGEALNAIGYAGSRKVSGHAVGAYFEAHIEQGPILEDERKTIGVVMGALGQKWFDLKLRGVEAHAGPTPMHLRKDALVGAAAIVAAVNRTALGHQPHACGTVGCLQAYPGSRNVIPGEVRMTLDFRHLEPARLDSMIAEVRQVIDSTCDEHGLTYELTPTADFPPLYFDKGCVEAVRSAAQGLGLSHMDIVSGAGHDAIFLAELGPAGMIFVPCEGGISHNEIENATPDDLAAGCAVLLRAMLAASAAIASGELAA Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_26570 AO353_26570 Dihydropyrimidinase (EC 3.5.2.2) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (3.5.2.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. phenylhydantoinase MSLLIRGATVITHDESYRADVLCADGVIKAIGNNLDTPAGCEVLDGSGQYLMPGGIDPHTHMQLPFMGTVASEDFFSGTAAGLAGGTTSIIDFVIPNPQQSLLEAFHQWRGWAEKSASDYGFHVAITWWSEQVREEMAELVSHHGVNSFKHFMAYKNAIMAADDTLVASFERCLELGAVPTVHAENGELVYHLQRKLMAQGITGPEAHPLSRPSQVEGEAASRAIRIAETLGTPLYLVHVSTKEALDEITYARSKGQPVYGEVLAGHLLLDDSVYQHPDWQTAAGYVMSPPFRPRGHQEALWHGLQSGNLHTTATDHCCFCAEQKAAGRDDFSKIPNGTAGIEDRMAVLWDEGVNTGRLSMQDFVALTSANTAKIFNLYPRKGSIRVGADADLVLWDPQGTRTISAKTHHQNVDFNIFEGKTVRGVPSHTVSQGRLVWADGDLRAERGAGRYIERPAYPAVFDLLSKRAELHKPTAVKR Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_26580 AO353_26580 Dihydropyrimidine dehydrogenase (NADP(+)) (EC 1.3.1.2) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (1.3.1.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. dihydropyrimidine dehydrogenase MADLSIVFAGIKAPNPFWLASAPPTDKAYNVVRAFEAGWGGVVWKTLGEDPAAVNVSSRYSAHFGANREVIGINNIELITDRSLEINLREITQVKKDWPDRALIVSLMVPCVEESWKNILPLVEATGADGIELNFGCPHGMPERGMGAAVGQVPEYVEQVTRWCKTYCSLPVIVKLTPNITDIRVAARAAHRGGADAVSLINTINSITSIDLDRMVAHPMVGSQSTHGGYCGSAVKPIALNMVAEIARDPQTQGLPICGIGGIGSWRDAAEFMALGSGAVQVCTAAMLHGFRIVEEMKDGLSRWMDSQGYSSVQDFSGRAVGNTTDWKYLDINYQVIAKIDQQACIGCGRCHIACEDTSHQAIASLKQPDGTHKYEVIDDECVGCNLCQITCPVQDCIAMVPVDNGKPFLDWDHDPRNPYHVAG Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_26790 AO353_26790 Glutaminase (EC 3.5.1.2) Specifically important for utilizing L-Glutamine. Automated validation from mutant phenotype: the predicted function (GLUTAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glutaminase A MQALLNEILDTVRPLIGQGKVANYIPALGSVPADQLGIAVYGNDGELYCAGDAHTLFSVQSISKVFSLVQAIEHSGEAIWERLGHEPSGQPFNSLVQLEFERGRPRNPFINAGALVICDINQSRFAAPALSMRDFVRRLSGNPQVMVDSKVAESEYQHRARNAAMAYLMQSFGNFHNDVEAVLRSYFSHCALRMSCVDLARAFCFLANDGFCKHSGEQILTARQTKQVNSIMATSGLYDEAGNFAYRVGLPGKSGVGGGIVAVVPGRFTVCVWSPELNPAGNSLAGMAALELLSQRIGWSVF Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_26925 AO353_26925 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (1.13.11.27) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 4-hydroxyphenylpyruvate dioxygenase MADLYENPMGLMGFEFIELASPTPNTLEPIFEIMGFTKVATHRSKDVHLYRQGQINLILNNEPHSVASYFAAEHGPSVCGMAFRVKDSQKAYKRALELGAQPIHIETGPMELNLPAIKGIGGAPLYLIDRFGEGSSIYDIDFVFIEGVDRHPVGAGLKIIDHLTHNVYRGRMAYWANFYEKLFNFREIRYFDIKGEYTGLTSKAMTAPDGMIRIPLNEESSKGAGQIEEFLMQFNGEGIQHVAFLSDDLIKTWDHLKKIGMRFMTAPPDTYYEMLEGRLPNHGEPVNELQARGILLDGSSEAGDKRLLLQIFSETLMGPVFFEFIQRKGDDGFGEGNFKALFESIERDQVRRGVLSTE Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_00035 AO356_00035 Fructokinase (EC 2.7.1.4) Specifically important for utilizing D-Sorbitol. Automated validation from mutant phenotype: the predicted function (FRUCTOKINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. sugar kinase MQLPSVVVFGEALTDVVQHSPGRWQGYPGGAPWNVARAMSRLGVPTAFAGSISTDSLGDELAQQSKAAGLDMRFLQRVDADPLVAIVPSSHPPRYFFAGEADLLFDVDQLPAGWLDAVRLCHFSCISLARQPLGDRLVEVARRVKEEDKLISYDPNWRNLMDTRYRELTFPAMVELADIIKLSDEDLRQIYPGLNEEQALHTLRTMNASAQILFTRGAKGMALYAADVKFEQPAIAVEVADTVGAGDSSMAGWLASTLLGIQEPHARLEFSAACASVSCSHAGAYAPSREEVEDLLSNRMQHQR Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_00950 AO356_00950 Ribokinase (EC 2.7.1.15) Specifically important for utilizing D-Ribose. Automated validation from mutant phenotype: the predicted function (RIBOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. ribokinase MPAKVVVIGSLNMDLVTRAPRLPRGGETLIGESFATIPGGKGANQAVAAARLGAQVSMVGCVGDDAYGEQLRGALLAEGIDCQAVRVEQGSSGVALIVVDDNSQNAIVIVAGANGALTAEVLDGVDDVLQSADVIICQLEVPDATVGHALKRGRALGKIVILNPAPASHALPADWYACIDYLIPNESEAAVLSGLAVDSLETAEAAAAHLIAAGAGKVIVTLGAQGLMFANGASFEHFPAPRVKAVDTTAAGDTFVGGFAAALACGKSEVDAIRFGQVAAALSVTRAGAQPSIPTLLEVQAFKS Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_01580 AO356_01580 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (RXN0-2301) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. isovaleryl-CoA dehydrogenase MSYPSLNFALGETIDMLRDQVQAFVKAELAPRAAQIDIDNLFPADMWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNHEQKTKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDANTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEENILGALNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_01590 AO356_01590 Methylglutaconyl-CoA hydratase (EC 4.2.1.18) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (METHYLGLUTACONYL-COA-HYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. gamma-carboxygeranoyl-CoA hydratase MDNFNTLELHSDPRGVATLWLSRESKNNAFNAEMIRELILALDHVSSDPNLRFLLIRGRGKHFSAGADLAWMQQSAELDYHTNLDDARELAELMYNLAKLKIPTLAVVQGAAFGGALGLISACDMAIGADEAQFCLSEVRIGLAPAVISPFVVQAIGERAARRYALTAERFDGQRAKEIGLLSESYPVETLDQQVEQWIDNLLLNSPAAMRASKELLREVGNGALTPALRRYTENAIARIRVSPEGQEGLRAFLQKRAPNWQAESNNNKEPRR Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_02560 AO356_02560 Xanthine dehydrogenase (EC 1.17.1.4) Specifically important for utilizing Inosine. Automated validation from mutant phenotype: the predicted function (1.17.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. FAD-binding molybdopterin dehydrogenase VIQFLLNQELRSEHALDPNLTVLNYLREHVGKPGTKEGCASGDCGACTVVVGELETDANGRERIRYRSLNSCLTFVSSLHGKQLISVEDLKHQGQLHSVQQAMVDCHGSQCGFCTPGFVMSLFALQKNSEQPDAHKAHEALAGNLCRCTGYRPILAAAEQACCGKQPDQFDARAAETIARLKAIAPTETGELNSGDKRCLVPLTVADLADLYDAYPQARLLAGGTDLALEVTQFHRTLPVMIYVGNVTELKRIERFDDRLEIGAATALSDCYEALKAEYPDFGELLQRFASLQIRNQGTLGGNIGNASPIGDSPPLLIALGAQIVLCKGQSRRTLALEDYFIDYRVTARQESEFIEKIIVPRASAEQAFRAYKVSKRLDDDISAVCAAFNLCIDNGVVRDARVAFGGMAATPKRAKHCEAALIGAPWTDSTVERACAALAEDFTPLSDFRASKEYRLLSARNLLRKYFIELQTPHIETRVTAYV Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_02565 AO356_02565 Xanthine dehydrogenase (EC 1.17.1.4) Specifically important for utilizing Inosine. Automated validation from mutant phenotype: the predicted function (1.17.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. xanthine dehydrogenase MSNHHAVEKTQAELAELFARDLTTGVGRSVKHDSAAKHVSGEAQYIDDRLEFPNQLHVYARLSDRAHARIIRIDTAPCYAFEGVRIAITHADIPGLKDIGPLLPGDPLLAIDDVQFVGQPVLAVAARDLETARKAAMAAIVEYEDLEPVLDVVEALRKRHFVLDSHTHQRGDSATALASAEHRLQGSLHIGGQEHFYLETQISSVMPTEDGGMIVYCSTQNPTEVQKLVAEVLGVSMNKVVVDMRRMGGGFGGKETQAASPACLCAVVAHLTGQPTKMRLPRVEDMLMTGKRHPFYIEYDVGFDSRGRLHGIALELAGNCGCSPDLSASIVDRAMFHADNAYYLGDATINGHRCKTNTASNTAYRGFGGPQGMVAIEEVMDAIARHLGLDPLAVRKANYYGKTERNVTHYYQTVEHNMLEEMTAELEESSQYAERREAIRRYNANSPILKKGLALTPVKFGISFTASFLNQAGALIHVYTDGSIHLNHGGTEMGQGLNTKVAQVVAEVFQVEMDRVQITATNTDKVPNTSPTAASSGADLNGKAAQNAAETIKRRLVEFAARQYKVSEEDVAFHNGHVRVRDHILSFEALVQQAYFAQVSLSSTGFYKTPKIYYDRSQARGRPFYYYAYGAACAEVIVDTLTGEYKMLRTDILHDVGASLNPAIDIGQVEGGFIQGMGWLTMEELVWNDKGKLMTNGPASYKIPAVADMPLDLRVKLVENRKNPEDTVFHSKAVGEPPFMLGIAAWCAIKDAVASLGDYRHQPNIDAPATPERVLWGCEQMRGLKAVKAEEAEVEVASL Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_03975 AO356_03975 Phenylalanine 4-monooxygenase (EC 1.14.16.1) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (1.14.16.1) was linked to the condition via a SEED subsystem. This annotation was also checked manually. phenylalanine 4-monooxygenase MKQTQYVAREPDAQGFIHYTAEEHAVWNTLITRQLKVIEGRACQEYLDGIDKLGLPHDRIPQLDEINKVLGQTTGWQVARVPALIPFQTFFELLASKQFPVATFIRTREELDYLQEPDIFHEIFGHCPLLTNPWFAEFTHTYGKLGLQASKEERVYLARLYWMTIEFGLVQTPQGRRIYGGGILSSPKETVYCLSDEPEHQAFDPLEAMRTPYRIDILQPVYFVLPELKRLFDLAHEDIMGMVKRGRELGLHAPKFPPKAA Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_07330 AO356_07330 1-phosphofructokinase (EC 2.7.1.56) Specifically important for utilizing D-Fructose. Automated validation from mutant phenotype: the predicted function (1PFRUCTPHOSN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 1-phosphofructokinase MAKILTLTLNPALDLTVELARLEPGQVNRSDAMHAHAAGKGVNVAQVLADLGHTLTVSGFLGEDNAQVFETLFAQRGFVDAFIRVPGETRSNIKLAEQDGRITDLNGPGPMVDAAAQQALLARLEQIAPGHDVVVVAGSLPRGVSPQWLQALIARMKALGLNVALDTSGEALRVALAAGPWLIKPNTEELADALGCEVVSETAQAQAAQRLHAQGIEHVVISHGADGVNWFSVGAALHASPPKVSVASTVGAGDSLLAGMLHGLLSADTPEQTLRTATAIAAMAVTQIGFGIHDTALLASLEQGVRVRPLTEQ Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_08390 AO356_08390 Urease (EC 3.5.1.5) Specifically important for utilizing Urea. Automated validation from mutant phenotype: the predicted function (3.5.1.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. urease subunit alpha MKISRQAYADMFGPTVGDKVRLADTELWIEVEKDFTTYGEEVKFGGGKVIRDGMGQSQLLAAEVVDTLITNALIIDHWGIVKADVGLKDGRIAAIGKAGNPDIQPDVTIAIGASTEVIAGEGMILTAGGIDTHIHFICPQQIEEALMSGVTTMIGGGTGPATGTNATTCTSGPWHLARMLQAADAFPMNIGFTGKGNASLPEPLIEQVKAGAIGLKLHEDWGTTPAAIDNCLSVADQYDVQVAIHTDTLNESGFVETTLAAFKGRTIHTYHTEGAGGGHAPDIIKACGFPNVLPSSTNPTRPFTRNTIDEHLDMLMVCHHLDPSIAEDVAFAESRIRRETIAAEDILHDLGAFSMISSDSQAMGRVGEVITRTWQTADKMKKQRGALPGDGEGNDNFRIKRYIAKYTINPAITHGISHEVGSIEVGKWADLVLWRPAFFGVKPTLILKGGAIAASLMGDANASIPTPQPVHYRPMFASYGGSRHATSLTFISQAAAEAGLPEQLGLKKRIAVVKGCRDVQKTDLIHNDYLPSIDVDPQTYQVKADGVLLWCEPAEVLPMAQRYFLF Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_09595 AO356_09595 Imidazolonepropionase (EC 3.5.2.7) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (IMIDAZOLONEPROPIONASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. imidazolonepropionase MKTLWQNCHAATMAQGVYSIIEDAAIVTQGEHIHWIGPRAELPMGDYPAVNDLKGAWVTPGLIDCHTHTVFGGNRSGEFEQRLQGVSYAEIAAAGGGIASTVRATRAASEDELFASAAKRLKGLMHDGVTTVEIKSGYGLDLASERKILRVIRRLGAELPVSVRSTCLAAHALPPEYKDRADDYIEHICTEMLPALAAEGLVDAVDAFCEYLAFSPAQVERVFITARQLGLPVKLHAEQLSSLHGSSLAARYQALSADHLEFMTEDDAKAMAASGTVAVLLPGAFYFLRETQLPPMDALRKHGVKIAVASDLNPGTSPALSLRLMLNMACTCFRMTPEEALAGATIHAAQALGMAQTHGSLEVGKVADFVAWHIDRPADLAYWLGGDLEKRVVRHGVEID Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_09605 AO356_09605 Histidine ammonia-lyase (EC 4.3.1.3) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (HISTIDINE-AMMONIA-LYASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. histidine ammonia-lyase MSQAEKIVITGAPLRWQDVVAVARFGAELELSTQTWARIDNAQAIVQRIVESGERAYGVNTGLGALCNVSLKDEQLSQLSRNTLLSHACGVGAPLTDEQTRAILCAAILNYSQGKSGIHRRVVEALLALLNRGITPQVPSQGSVGYLTHMAHIGIALLGVGQVSYRGQIVPAQQALVAEGLQPVQLGAKDGLCLVNGTPCMTGLSCLALADATRLVQWADVIGAMSFEAQRGQIAAFDAEIIALKPHPGMQQVGVNLRALLDGSEVIAASRGIRTQDALSIRSIPQVHGAARDQLAHARQQIETELNAVTDNPLLLGTPENFRVMSQANPHGQSVALAADLLAIAMAEIGSIAERRLDRLINPHVSGLPAFLVANPGVNSGMMIVQYVAASLCAENKQLAQPAVLDNFVTSGLQEDHLSMGTNAALKLHRALENCTQILAIEYLLAAQAFEFLKAQRFGAGTDIAWKLLRERVPPYDQDRWLAPDIASAAGLLKDPNVLHNVLPNLN Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_09630 AO356_09630 Urocanate hydratase (EC 4.2.1.49) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (UROCANATE-HYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. urocanate hydratase VTDATRKPEKYRDVEIRAPRGNTLTAKSWLTEAPLRMLMNNLDPEVAENPKELVVYGGIGRAARNWECYDKIVESLTNLNDDETLLVQSGKPVGVFKTHSNAPRVLIANSNLVPHWASWEHFNELDAKGLAMYGQMTAGSWIYIGSQGIVQGTYETFVEAGRQHYDSNLKGRWVLTAGLGGMGGAQPLAATLAGACSLNIECQQVSIDFRLKTRYVDEQAKDLDDALARIEKYTAEGKAISIALCGNAAEILPEMVRRGVRPDMVTDQTSAHDPLNGYLPAGWTWDEYRARAKTEPAAVVKAAKQSMAVHVKAMLAFQKMGVPTFDYGNNIRQMAQEEGVENAFDFPGFVPAYIRPLFCRGIGPFRWAALSGDPQDIYKTDAKVKELIPDDAHLHNWLDMARERISFQGLPARICWVGLGQRAKLGLAFNEMVRSGELSAPIVIGRDHLDSGSVASPNRETESMQDGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGFSQHSGMVIVCDGTDEAAERIARVLHNDPGTGVMRHADAGYQIAIDCAKEQGLNLPMITGK Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_09645 AO356_09645 Formiminoglutamic iminohydrolase (EC 3.5.3.13) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (FORMIMINOGLUTAMATE-DEIMINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-formimino-L-glutamate deiminase MSAFFAERALLPSGWAHDVRLEVDAKGVLTHIQAGSHADGAERLGGPLLPGMPNLHSHAFQRAMAGLAEVAGNPNDSFWTWRDLMYRLVGKISPDQLGIIARQLYIEMLKAGYTSVAEFHYVHHDTDGAPYADPAELALRISHAASAAGIGLTLLPVLYSHSGFGGQAPNDGQRRFINSTENYLKLQSRLQPILAGQPAQALGLCFHSLRAVTPGQIQDVLAASDRDCPVHIHIAEQQKEVDDCLSWSGARPLQWLYENTEVDQRWCLVHATHANAQEVSLMAKSRAIAGLCLTTEANLGDGIFPAVDFLAQGGRLGIGSDSHVSLSVVEELRWLEYGQRLRDQRRNRLYRADQPMVGRTLFDAALEGGAQALGQPVGALDIGKRADWLVLDGNDPYLATANGDGILNRWLFAGGDRQVRDVMVGGRWVVRDGRHAGEEESARAFTQVLRELLD Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_10030 AO356_10030 Agmatine deiminase (EC 3.5.3.12) Specifically important for utilizing L-Arginine. Automated validation from mutant phenotype: the predicted function (AGMATINE-DEIMINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. agmatine deiminase MTTLHSTPRADGFHMPAEWATQTQVWMIWPERPDNWRLGGKPAQAAHVAVAKAIARFEPVTVAVSAAQYENARARLDVPNIRLVEMSSDDAWVRDTGPTFVINDSGEVRGVDWDFNAWGGFDGGLYAPWNRDSQVASKVLEIERSPRYRTEGFVLEGGSIHVDGEGTVITTEECLLNRNRNPHMSREQIEAVLSAQLAVDKVIWLPDGLFNDETDGHVDNFCCYVRPGEVLLAWTDDPQNPNYTRCHAAMDVLQNSTDAKGRPFTVHKMPIPGPMYATEEECAGVDAVEGSQERNPTVRLAGSYVNFLIVNGGIIAPSFDDPLDAPARDILQNLFPQHEVVMVPGRELLLGGGNIHCLTQQQPAPYVK Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_11100 AO356_11100 L-asparaginase (EC 3.5.1.1) Specifically important for utilizing L-Asparagine. Automated validation from mutant phenotype: the predicted function (ASPARAGHYD-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. asparaginase MNPSTYPAAQHVMVLYTGGTIGMQASAHGLAPASGFEARMRDYLHSQPELVVPQWRFREMSPLIDSANMTPAYWQQLREAVVDAVDVQGCDSVLILHGTDTLAYSAAAMSFQLLGLHARVCFTGSMLPAGVTDSDAWENLSGALVALGQGLAPGVHLYFHGELLAPTRCAKVRSFGRHPFKRLERQGGGTPAPTLPTQLNYNQPKQLTNIAALPLFPGISAQILDGLLGSGIQGLVLECYGSGTGPSDNPAFLASLERARDSGVVVVAVTQCHEGGVELDVYEAGSRLRGVGVLSGGGMTREAALGKLQALIGAGLPVEEVRRLVELDLCGELI Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_13845 AO356_13845 Carnitine 3-dehydrogenase (EC 1.1.1.108) Specifically important for utilizing Carnitine Hydrochloride. Automated validation from mutant phenotype: the predicted function (CARNITINE-3-DEHYDROGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 3-hydroxybutyryl-CoA dehydrogenase MSFITDIKTFAALGSGVIGSGWVSRALAHGLDVVAWDPAPGAEAALRKRVANAWGALEKQGLAPGASQDRLRFVATIEECVRDADFIQESAPERLELKLELHGQISAAAKPNALIGSSTSGLLPSEFYEGCTHPERCVVGHPFNPVYLLPLVEVVGGKHTAPEAVQAAMQVYESLGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLAGGDAGMRHFMAQFGPALQLPWTYLPAPELTEKLIDDVVDGTSEQLGSHSISALERYRDDCLLAVLEAVKTTKAKHGMAFEE Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_16835 AO356_16835 Maleylacetoacetate isomerase (EC 5.2.1.2) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (5.2.1.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. maleylacetoacetate isomerase MELYTYYRSTSSYRVRIALALKGLDYQALPVNLIAAPGGEHRQPAYLAINPQGRVPALRTDEGALLVQSPAIIEYLEERYPQVPLLSADLAVRAHERGVAALIGCDIHPLHNVSVLNQLRQWGHDEAQVTEWIGHWISQGLAAVEQLIGDDGYCFGALPGLADVFLIPQLYAAERFNVSLQGYPRIRRVAALAAVHPAFQQAHPAKQPDTP Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_17550 AO356_17550 N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) Specifically important for utilizing N-Acetyl-D-Glucosamine. Automated validation from mutant phenotype: the predicted function (NAG6PDEACET-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. N-acetylglucosamine-6-phosphate deacetylase MSEDNILTCDGWVRGRLLHEHGRVVAIEGQPCDPASNDLPYLLPGFIDLHVHGGGGKDIMQGASAFETIARTHLRFGTTALLATTMTAPSEEIASVLQALGEFCEQRPNGSARVLGVHLEGPYINPGKLGAQPNFAHTALLAEVESYLALAPIRVITIAPEIAGHDALIRALSARGVRMQIGHTLGSYEEGVAALAAGASSFTHLYNAMSPLHHREPGIVGAALAHAQYAELIPDLLHVHPGAMRVALRSIPCLYCVTDSTAAAGMPDGEYKLGSHTVTKCLGGVRLADGTLAGSTLTMDQALRNLVKIGLPIAEASQRLSQFPADYLGLPERGRLQPGAWADCVRLDRSLTLTDVMVEGEAIDFQNA Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_18695 AO356_18695 Acetyl-coenzyme A synthetase (EC 6.2.1.1) Specifically important for utilizing Ethanol. Automated validation from mutant phenotype: the predicted function (ACETATE--COA-LIGASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. acetyl-CoA synthetase MSAASLYPVRPEVAASTLTDEATYKAMYQQSVVNPDGFWREQAKRLDWIKPFTTVKQTSFDDHHVDIKWFADGTLNVSYNCLDRHLAERGDQIAIIWEGDDPSESRNITYRELHEEVCKFANALRGQDVHRGDVVTIYMPMIPEAVVAMLACTRIGAIHSVVFGGFSPEALAGRIIDCKSKVVITADEGVRAGKKIPLKANVDDALTNPETSSIQKVIVCKRTAGNIKWNQHRDIWYEDLMKVAGTVCAPKEMGAEEALFILYTSGSTGKPKGVQHTTAGYLLYAALTHERVFDYKPGEVYWCTADVGWVTGHSYIVYGPLANGATTLLFEGVPNYPDITRVAKVIDKHKVSILYTAPTAIRAMMASGTAAVEGADGSSLRLLGSVGEPINPEAWDWYYKNVGKERCPIVDTWWQTETGGVLISPLPGATALKPGSATRPFFGVVPALVDNLGNLIEGAAEGNLVILDSWPGQARTLYGDHDRFVDTYFKTFSGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESAMVAHPKVAEAAVVGVPHDIKGQGIYVYVTLNAGEETSEALRLELKNWVRKEIGPIASPDVIQWAPGLPKTRSGKIMRRILRKIATAEYDGLGDISTLADPGVVAHLIETHKTMNVA Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_21690 AO356_21690 Glutaminase (EC 3.5.1.2) Specifically important for utilizing L-Glutamine. Automated validation from mutant phenotype: the predicted function (GLUTAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. glutaminase A MQALLNEILDAVRPLIGQGKVADYIPALGTVVPNQLGIAVYGNDGELYCAGDAETAFSVQSISKVFSLVQAIGHSGEAIWERLGHEPSGQPFNSLVQLEFERGRPRNPFINAGALVICDINQSRFAAPALSMRDFVRRLSGNPQVMVDGKVAESEYQHRARNAAMAYLMQSFGNFHNDVEAVLRSYFSHCALRMSCIDLARAFCFLANDGFCKHSGEQILSARQTQQVNSIMATSGLYDEAGNFAYRVGLPGKSGVGGGIVAVVPGRFTVCVWSPELNAAGNSLAGMAALELMSQRIGWSVF Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_22845 AO356_22845 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (1.13.11.27) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 4-hydroxyphenylpyruvate dioxygenase MADLYENPMGLMGFEFIEFASPTPNTLEPIFEIMGFTKVATHRSKDVHLYRQGAINLILNNEPHSVASYFAAEHGPSVCGMAFRVKDSQLAYKRALELGAQPIHIETGPMELNLPAIKGIGGAPLYLIDRFGEGSSIYDIDFVFLEGVDRNPVGAGLKIIDHLTHNVYRGRMAYWAGFYEKLFNFREIRYFDIKGEYTGLTSKAMTAPDGMIRIPLNEESSKGAGQIEEFLMQFNGEGIQHVAFLTDDLIKTWDHLKSIGMRFMTAPPDTYYEMLEGRLPNHGEPVNELQSRGILLDGASEQGDKRLLLQIFSETLMGPVFFEFIQRKGDDGFGEGNFKALFESIERDQVRRGVLATE Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_22970 AO356_22970 Branched-chain amino acid aminotransferase (EC 2.6.1.42) Specifically important for utilizing L-Isoleucine. Automated validation from mutant phenotype: the predicted function (BRANCHED-CHAINAMINOTRANSFERILEU-RXN, BRANCHED-CHAINAMINOTRANSFERLEU-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. branched-chain amino acid aminotransferase MGNESINWDKLGFDYIKTDKRYLSHWRDGAWDAGTLTDDNVLHISEGSTALHYGQQCFEGLKAYRCKDGSINLFRPDQNAARMQRSCARLLMPQVETEQFVEACKQVVRANERFIPPYGTGGALYLRPFVIGVGDNIGVRTAPEFIFSIFCIPVGAYFKGGLTPHNFLISSFDRAAPQGTGAAKVGGNYAASLMPGSQAKKASFADCIYLDPMTHSKIEEVGSANFFGITHDNTFVTPRSPSVLPGITRLSLIELAKSRLGLEVIEGDVFIDKLSDFKEAGACGTAAVITPIGGISYKDKLHVFHSETEVGPITQKLYKELTGVQTGDVEAPAGWIVKV Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_22975 AO356_22975 Dihydrolipoyl dehydrogenase (EC 1.8.1.4) Specifically important for utilizing L-Isoleucine; L-Leucine. Automated validation from mutant phenotype: the predicted function (1.8.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. dihydrolipoamide dehydrogenase MQQTLNTTLLIIGGGPGGYVAAIRAGQLGISTILVEGQALGGTCLNIGCIPSKALIHVAEQFHQTRHHSQGSALGITVAAPTLDIGKSVEWKDGIVDRLTTGVAALLKKHKVQVIHGWAKVIDGKTVEVGDTRIQCEHLLLATGSKSVNLPMLPLGGPIISSTEALAPTSVPKHLVVVGGGYIGLELGIAYRKLGAEVSVVEAQERILPAYDGELTQPVHEALKQLGVKLYLKHSVEGFDAQASTLQVRDPNGDTLNLETDRVLVAVGRKPNTQGWNLAALDLAMNGSAVKIDSRCQTSMRNVWAIGDLSGEPMLAHRAMAQGEMVAELIAGQHREFNPTAIAAVCFTDPELVVVGKTPDEAKAAGLDCLVSSFPFAANGRAMTLESKSGFVRVVARRDNHLIVGWQAVGVGVSELSTAFGQSLEMGARLEDIAGTIHAHPTLGEAVQEAALRALGHALHL Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_23085 AO356_23085 Dihydropyrimidine dehydrogenase (NADP(+)) (EC 1.3.1.2) Specifically important for utilizing Cytosine. Automated validation from mutant phenotype: the predicted function (1.3.1.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. dihydropyrimidine dehydrogenase MADLSIVFAGIKAPNPFWLASAPPTDKAYNVVRAFEAGWGGVVWKTLGEDPAAVNVSSRYSAHYGVNREVLGINNIELITDRSLEINLREITQVKKDWPDRALIVSLMVPCVEESWKRILPLVEATGADGIELNFGCPHGMPERGMGAAVGQVPEYVEQVTRWCKTYCSLPVIVKLTPNITDIRVAARAAHRGGADAVSLINTINSITSVDLDRMVALPSVGSQSTHGGYCGSAVKPIALNMVAEIARDPQTQGLPICGIGGIGSWRDAAEFIALGSGAVQVCTAAMLHGFRIVDEMKDGLSRWMDEHGHANLQAFSGRAVGNTTDWKYLDINYQVIAKIDQEACIGCGRCHIACEDTSHQAIASLKQADGTHVYEVIDEECVGCNLCQITCPVQDCIEMVTVDTGKPFLDWNHDPRNPYHVTA Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_23095 AO356_23095 Dihydropyrimidinase (EC 3.5.2.2) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (3.5.2.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. phenylhydantoinase MSLLIRGATVITHDESYRADVFCADGVIKAIGDNLDVPAAVEVLDGSGQYLMPGGIDPHTHMQLPFMGTVASEDFFSGTAAGLAGGTTSIIDFVIPNPQQSLMEAFHQWRGWAEKSASDYGFHVAITWWSEQVREEMAELVSHHGVNSFKHFMAYKNAIMAADDTLVASFERCLELGAVPTVHAENGELVYHLQRKLLAQGITGPEAHPLSRPSQVEGEAASRAIRIAETLGTPLYLVHVSTKEALDEITYARSKGQPVYGEVLAGHLLLDDSVYRDPDWQTAAGYVMSPPFRPRGHQEALWHGLQSGNLHTTATDHCCFCAEQKAAGRDDFSKIPNGTAGIEDRMAVLWDEGVNSGKLSMQDFVALTSTNAAKIFNLYPRKGAIRVGADADLVLWDPQGSRTISAKTHHQQVDFNIFEGKTVRGVPSHTISQGRLVWADGDLRAERGAGRYIERPAYPAVFDLLSKRAELHRPVAVKR Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_23105 AO356_23105 Beta-ureidopropionase (EC 3.5.1.6) Specifically important for utilizing Uridine. Automated validation from mutant phenotype: the predicted function (3.5.1.6) was linked to the condition via a SEED subsystem. This annotation was also checked manually. allantoate amidohydrolase MNAAIDVLQSTQPHINRDRLWQSLMDLAQLGATVKGGVCRLALTDLDRQARDLFVQWTQAAGCTVSIDGVGNIFARRPGRNPNLPPVMTGSHIDTQPTGGKFDGCFGVLSGLEVLRTLNDLNIETEAPLEVVVWTNEEGSRFAPCMMGSGVFAEKFTLEETLAKTDAEGISVGQALNAIGYAGPRPVSGHPVGAYFEAHIEQGPILEDEGKTIGVVMGALGQKWFDLTLRGVEAHAGPTPMHLRKDALVGASVIVGAVNRAALGHQPHACGTVGCLQAYPGSRNVIPGEVRMTLDFRHLEPARLDSMIAEVKQVIEDTCRQHGLTFDLKPTADFPPLYFDQGCVDAVRGAAQGLGLSHLDIVSGAGHDAIFLAELGPAGMIFVPCEGGISHNEIENAAPDDLAAGCAVLLRAMLAASQAIAEGRMAA Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_23165 AO356_23165 Myo-inosose-2 dehydratase (EC 4.2.1.44) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (MYO-INOSOSE-2-DEHYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. myo-inosose-2 dehydratase MPAIRIGINPISWSNDDLPSLGGETPLSTALSEGKAIGYEGFELNGKFPKDAKGVGDVLRPYDLALVSGWYSSRLARRSAAEEIDAIASHVELLAQNGANVLVYGEVADSIQGQRIPLVERPRFHTDEAWQAYADKLTELARFTLSQGVRLAYHHHMGAYVESPADIDKLMALTGSEVGLLFDSGHCYMGGGEPLQVLRKHIERVCHVHFKDVRKPVVQLARNNLWSFPDCIINGTFTVPGDGDIDFAALLDVLLAADYQGWLVVEAEQDPAVAPSYAYAKKGYDTLRALLQERSAS Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_23190 AO356_23190 Inositol 2-dehydrogenase (EC 1.1.1.18) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (1.1.1.18) was linked to the condition via a SEED subsystem. This annotation was also checked manually. inositol 2-dehydrogenase MSLKLGVIGTGAIGQDHIRRCSQTLLNSQVVAVTDINLQQAAKVVADLKLTAEVYPDGHALIKAPDVEAILVTSWGPSHEEFVLAAIAAGKPVFCEKPLAVTAEGCRKIVEAEVAHGKRLVQVGFMRPYDEGYRALKAVIDSGQIGEPLMLHCAHRNPSVGENYKTDMAITDTLIHELDVLRWLLADDYVSVQVVFPRKTSKALAHLRDPQIVLLETARGTRIDVEVFVNCQYGYDIQCEVVGETGIAKLPEPSQVQLRSGAKLSNAILMDWKDRFIAAYDVELQAFIDGVRAGQVGGPSAWDGFAAAVAADACVEAQQSGQIVKVELPERPRFYG Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_24205 AO356_24205 Alpha,alpha-trehalase (EC 3.2.1.28) Specifically important for utilizing D-Trehalose dihydrate. Automated validation from mutant phenotype: the predicted function (TREHALA-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. trehalase MRPIELTSLSFATLLCVACSSQPPATWSYVDAQGRANLPPDQAYPELFEAVQRGQVFTDQKHFVDALPNRDPAQIRADYLARRDHDGFDIKAFVKDNFIESGQAESPAPKPGAPIQEHIDSLWPILSRSYSQVPAYSSLLPLPQPYVVPGGRFREMYYWDSYFTMLGLEQSGDKARVRQMTDNFAYMIDTYGHIPNGNRTYYLSRSQPPFFAYMVALQARIEGDQAYGRYLPQLQKEYAYWMAGAQALKPGAADRHVVKLADGSVLNRYWDASPTPRQESWLQDVRTAEQAPDRPKEEVWRDLRAGAESGWDFSSRWLDDGQNLASIRTTAIVPVDLNSLIYHLEQTIAKACETVQNAPCVQAYGRRAELRQRAIEQHLWNADKGFYVDYDWQRQQQRQQLTAATLFPLYTGLASAEHAHRTADAVRDGLLRVAGIATTQVNTGQQWDEPNGWAPLQWVAVEGLDRYGHTALAQQVGSRFLQQVENLYRKENKLVEKYDLSGRGDGGGGGEYELQDGFGWTNGVTLKLLGKYGKTSSTLGE Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_27695 AO356_27695 Xylulose kinase (EC 2.7.1.17) Specifically important for utilizing D-Xylose. Automated validation from mutant phenotype: the predicted function (XYLULOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. xylulose kinase MANQQLFLGIDCGTQGTKALILDTISGQVLGQGAAAHSMISGANGRREQDTQQWLDAFTQATHQALAAAGVDGQAILGIGVSGQQHGLVLLDDQGQVLRPAKLWCDTETTPENDRLLAYLGGEDGSLERLGVVIAPGYTVSKLLWTREQHPQVFERIASVLLPHDFLNYWLTGRHCSEYGDASGTGYFNVRTRQWDVQLLQHIDPSARLQAALPELIEAHQPVGRILPAIAAHLGINPDAVVASGGGDNMMGAIGTGNIQPGVITMSLGSSGTVYAYAAEPAVSPQPSVATFCSSNGGWLPLICTMNLTNATGAIRELLDLDIDAFNALVVQAPIGAEGVCMLPFLNGERVPALPHATASLLGLTTTNLTRANLCRAVVEGTTFGLRYGLDLLRANGLKAQSIRLIGGGSKSPVWRQIVADIMDTTVICTEQSEAAALGAAIQAAWCHSGAQDSLAELCERCVKLDPASETRPVTAHVTASQQAYERYRQHVATL Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_28500 AO356_28500 Xylose isomerase (EC 5.3.1.5) Specifically important for utilizing D-Xylose. Automated validation from mutant phenotype: the predicted function (XYLISOM-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. xylose isomerase MPYFPGVDKIRYEGPASDSPLAFRHYDANRLVLGKPMREHLRMAVCYWHTFVWPGSDVFGAGTFKRPWQHAGDPMEVAIGKAEAAFEFFSKLGIDYYCFHDTDVAPEGGSLKEYRNHFAQMIDHLERHQEQTGIKLLWGTANCFSNPRFAAGAASNPDPEVFACAAAQVFSAMNATQRLKGANYVLWGGREGYETLLNTDLKHEREQLGRFMRMVVEHKHKIGFKGDLLIEPKPQEPTKHQYDYDSATVFGFLQQFGLENEIKVNIEANHATLAGHSFHHEIATAVSLGIFGSIDANRGDPQNGWDTDQFPNSVEEMTLATYEILKAGGFGNGGFNFDSKVRRQSVDDIDLFHGHVAAMDVLALALERAAAMVQNDQLQQFKDQRYAGWQQPFGKAVLAGDFSLESLAEHAFTNELNPQAVSGRQEMLENVVNRFIYP Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_28760 AO356_28760 Xylonate dehydratase (EC 4.2.1.82) Specifically important for utilizing D-Xylose. Automated validation from mutant phenotype: the predicted function (XYLONATE-DEHYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. dihydroxy-acid dehydratase MSDTPERRLRSEQWFNDPAHADMTALYVERYMNYGMTREELQSGRPIIGIAQTGSDLTPCNRHHLELAQRVKAGIRDAGGIPMEFPVHPIAEQSRRPTAALDRNLAYLGLVEILHGYPLDGVVLTTGCDKTTPACLMAAATTDLPAIVLSGGPMLDGHHKGELIGSGTVLWHARNLMAAGEIDYEGFMEMTTAASPSVGHCNTMGTALSMNALAEALGMSLPGCASIPAPYRERGQMAYATGKRICELVLQDIRPSQIMTRQAFENAIAVASALGASSNCPPHLIAIARHMGVELSLDDWQRIGEDVPLLVNCMPAGKYLGEGFHRAGGVPSVMHELQKAGRLHEDCATVSGRTIGEIVSSSLTSNADVIHPFDTPLKHRAGFIVLSGNFFDSAIMKMSVVGEAFRKTYLSEPGAENSFEARAIVFEGPEDYHARIDDPALDIDERCILVIRGVGTVGYPGSAEVVNMAPPAALIKQGIDSLPCLGDGRQSGTSASPSILNMSPEAAVGGGLALLQTNDRLKVDLNTRTVNLLIDDEEMARRRLEWTPNIPPSQTPWQELYRQLVGQLSTGGCLEPATLHLRVIARSGEPRHSH Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_1650 Sucrose alpha-glucosidase (EC 3.2.1.48) Specifically important for utilizing Sucrose. Automated validation from mutant phenotype: the predicted function (3.2.1.48-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Sucrose-6-phosphate hydrolase (EC 3.2.1.B3) MTVSVNAMNAPMPSPLEHAQQALSEGQSRLIGDYRPAYHLAPVAGWMNDPNGVVFFRGEYHVFYQHHPFDAKWGPMYWGHAKSTDLVHWQHLPLALAPGDDFDRHGCFSGSAVVCGDTLALIYTGHTWLGEVGDERFIRQVQCLATSDDGIRFVKHGAVIENAPQETIMHFRDPKVWREDGYWYLIAGARLGDKPLLPLYRSTDLHTWDFLDYVSSGNEGDGYMWECPDLFRLNGCDVLLYSPQGMKPEGYERLNKYQTGYRIGRLDSEWHFTGGPFIELDNGHDFYAAQTLETADGRRLVWAWLDMWESPMPSQAHHWCGMLGLPRELELQGDRLGVFPARELTALRQAPLPSVAPWGESGSRWVPQVKGDRLEIHVHLDLLDCTEGHLGIALRCSTDEQEQTLLYYDASLQRLVLDRSRSGAQVSGQRSVSIVPSQTQLHLRVFLDRSSIEVFEENGRFSFSSRLYPRPDSLGVKLLANGTGGRVAIPKAWPLDSGWL Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_1668 Xylonate dehydratase (EC 4.2.1.82) Specifically important for utilizing D-Xylose. Automated validation from mutant phenotype: the predicted function (XYLONATE-DEHYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Xylonate dehydratase (EC 4.2.1.82) MSDTPKHRLRSEQWFNDPAHADMTALYVERYMNYGMTREELQSGRPIIGIAQTGSDLTPCNRHHLELAQRVKAGIRDAGGIPMEFPVHPIAEQSRRPTAALDRNLAYLGLVEILHGYPLDGVVLTTGCDKTTPACLMAAATTDLPAIVLSGGPMLDGHHKGELIGSGTVLWHARNLMAAGEIDYEGFMEMTTAASPSVGHCNTMGTALSMNALAEALGMSLPGCASIPAPYRERGQMAYATGKRICDLVRQDIRPSQIMTRQAFENAIAVASALGASSNCPPHLIAIARHMGVELSLEDWQRIGEDVPLLVNCMPAGKYLGEGFHRAGGVPSVMHELQKAGRLHEDCATVSGKTIGEIVSNSLTSNTDVIHPFDTPLKHRAGFIVLSGNFFDSAIMKMSVVGEAFRKTYLSEPGAENSFEARAIVFEGPEDYHARIDDPALDIDERCILVIRGVGTVGYPGSAEVVNMAPPAALIKQGIDSLPCLGDGRQSGTSASPSILNMSPEAAVGGGLALLKTNDRLKVDLNTRTVNLLIDDAEMAQRRREWIPNIPPSQTPWQELYRQLVGQLSTGGCLEPATLHLRVIARSGEPRHSH Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_1965 Fructokinase (EC 2.7.1.4) Specifically important for utilizing D-Sorbitol. Automated validation from mutant phenotype: the predicted function (FRUCTOKINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Fructokinase (EC 2.7.1.4) MNMQLPSVVVFGEALTDVVQHSPGRWQGYPGGAPWNVARAMSRLGVPTAFAGSISTDSLGDELAQQSKAAGLDMRFLQRVDADPLVAIVPSSHPPRYFFAGEADLLFDVDQLPAGWLDAARLCHFSCISLARQPLGDRLVEVARRVKEEDKLISYDPNWRNLMDTRYRELTFPAMVELADIIKLSDEDLRQIYPGLNEEQALHTLRTMNASAQILFTRGAKGMALYAADVKFEQPAIAVEVADTVGAGDSSMAGWLASTLLGIQEPHARLEFSAACASVSCSHAGAYAPSREEVEDLLSNRMQHQR Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2102 Glutaminase (EC 3.5.1.2) Specifically important for utilizing L-Glutamine. Automated validation from mutant phenotype: the predicted function (GLUTAMIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Glutaminase (EC 3.5.1.2) MQALLNEILDAVRPLIGQGKVADYIPALGTVAPNQLGIAVYGNDGELYCAGDAETAFSVQSISKVFSLVQAIGHSGEAIWERLGHEPSGQPFNSLVQLEFERGRPRNPFINAGALVICDINQSRFAAPALSMRDFVRRLSGNPQVMVDGKVAESEYQHRARNAAMAYLMQSFGNFHNDVEAVLRSYFSHCALRMSCIDLARAFCFLANDGFCKHSGEQILSARQTQQVNSIMATSGLYDEAGNFAYRVGLPGKSGVGGGIVAVVPGRFTVCVWSPELNAAGNSLAGMAALELMSQRIGWSVF Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2191 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (RXN0-2301) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) MSYPSLNFALGETIDMLRDQVQAFVNAELAPRAAQIDIDNLFPADMWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNHEQKTKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDKYVLNGSKTWITNGPDANTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEDNILGALNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2193 Methylglutaconyl-CoA hydratase (EC 4.2.1.18) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (METHYLGLUTACONYL-COA-HYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Methylglutaconyl-CoA hydratase (EC 4.2.1.18) MDNFNTLELHSDPRGVATLWLSRESKNNAFNAEMIRELILALDHVSSDPNLRFLLIRGRGKHFSAGADLAWMQQSAELDYHTNLDDARELAELMYNLAKLKIPTLAVVQGAAFGGALGLISACDMAIGADEAQFCLSEVRIGLAPAVISPFVVQAIGERAARRYALTAERFDGQRAKEIGLLSESYPAEVLDQQVEQWIDNLLLNSPAAMRASKELLREVGNGALTPALRRYTENAIARIRVSPEGQEGLRAFLQKRAPNWQAESNNKEPRR Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2378 Nitrite reductase (NAD(P)H) (EC 1.7.1.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Nitrite reductase [NAD(P)H] large subunit (EC 1.7.1.4) MKKLKLVMIGNGMAGVRTLEELLKLSNELYDITVFGAEPHTNYNRILLSPVLAGEQTFEEIVLNDLSWYLDNNIKLLLNRKVVEIDRVKRRVIAEDGSEAEYDRLLIATGSTPFILPIPGNTLDGVIGYRDIADTQAMIDTAKTHKHAVVIGGGLLGLEAANGLKLRGMDVTVVHLGEWLLERQLDKTSGQLLQTALENRGLKFRLSEQTQALHDAGNGRVGSVQFKNGDIIPADLVVMAAGIRPNTELAEKSGIPCNRGILVNDTMQTYDPRIYAIGECASHRGTAYGLVAPLFEQAKVCANHLAQLGFATYKGSVTSTKLKVTGIDLFSAGDFMGGEGTETITLSDPIGGVYKKLVIKDDVLVGACLYGDTADGGWYFRQIRENHGISEIRDHLMFGENALGDVGHQGQDKAMSMADSAEVCGCNGVCKGTIVKAIQEHGLFSVDDVKKHTKAASSCGSCAGLVEQILINTVGGAADVKPKSEKAICGCSDLNHGQIRQAIRDQHLLTIAGTMSYLNWRTPNGCATCRPALNYYLISTWPGEAQDDPQSRLINERAHANIQKDGTYSVVPRMWGGVTNPAELRRIADVADKYNVPMVKVTGGQRIDLLGIKKQDLPGVWKDLDMPSGHAYGKSIRTVKTCVGSEFCRFGTQNSTQLGIELEHDLFNMWSPHKVKLAVSGCPRNCSEAGIKDVGIIGVDSGWEMYIGGNGGIKTEVAEFFVKLKTAEEVREYNGAFLQLYREEAFYLERTVHYMQRVGMEHIKKAVLEDPERRKALHERLKFSLSLEQDPWKQRLEQPQLKKEFEVIPVKNLEVLA Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2380 Nitrate reductase (EC 1.7.99.4) Specifically important for utilizing Sodium nitrate. Automated validation from mutant phenotype: the predicted function (1.7.99.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Assimilatory nitrate reductase large subunit (EC:1.7.99.4) MNRQITASTCCYCGVGCGVLIEHDGERILGVSGDPAHPANFGKLCSKGSTLHLTGDLAARALYPELRLGKGLARARSDWDSALDHAASVFAETIAEHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYEDLEMSDCVMIVGSNMAYAHPILFRRLEEAKSRRPQMKIIVIDPRRTDTCDLADLHLAILPGTDVALFHGILHLLLWEDWVDRDFIKAHTEGLADLKNLVRDYIPSMVAQLCGISVEQLHLCAEWVGTSPSFLSLWCMGLNQSTAGSAKNSALINLHLATGQIGRPGAGPFSLTGQPNAMGGRETGSLSNLLPGHREAANPEHRADVARYWGVEQLPATTGLSAIELFEQVRSGKIKALWIACTNPAQSMPDQTAVREALQACPFVVLQEAFRTTETAAFADLLLPAASWGEKEGSVTNSERRISHVRRAIGAPGEARADWAITVDFAQRLEKRLRPGQPSLFAFETPAQLFDEYKQLTRGRDLDLSGISHALIDQLGPQQWPFPEGATVGTARLYVDGIFPTDSGRARFVADPYRAAKELRDARYPLTLNTGRLRDQWHGMSRTGTAAQLFGHVNEAVLSLHPDELQRHRLQAGDLVSLKSRRGSVIVAVDSDDSVRPGQAFLPMHWGDRFLKGGVNTLTQPAFDPLSKQPELKHSGVRLEPVNLPWQFFALIEGDVQQHLEALRPLCEAFSYVSLSLTGRERPALLIRAASAVTPEPQLLQAIDEQLGLIDGPVLAYDDPRRSIGKRVRIENGRITAIRLAGETLARHWLQNLWLEGRANEQLRRWLLAPLSAPPGNVGAATGGSKTLCNCMNVSQRAICAGIERGLDLQGLKQELGCGTQCGSCVPEIKRLLVATAQPLAAIS Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2630 Phenylalanine 4-monooxygenase (EC 1.14.16.1) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (1.14.16.1) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Phenylalanine-4-hydroxylase (EC 1.14.16.1) MKQTQYVAREPDAQGFIHYTAEEHAVWNTLITRQLKVIEGRACQEYLDGIDKLGLPHDRIPQLDEINKVLGETTGWQVARVPALIPFQTFFELLASKQFPVATFIRTREELDYLQEPDIFHEIFGHCPLLTNPWFAEFTHTYGKLGLQASKEERVYLARLYWMTIEFGLVQTPQGRRIYGGGILSSPKETVYCLSDEPEHQAFDPLEAMRTPYRIDILQPVYFVLPELKRLFDLAHEDIMGMVKRGRELGLHAPKFPPKAA Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2914 4-hydroxybenzoate 3-monooxygenase (EC 1.14.13.2) Specifically important for utilizing 4-Hydroxybenzoic Acid. Automated validation from mutant phenotype: the predicted function (1.14.13.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. P-hydroxybenzoate hydroxylase (EC 1.14.13.2) MKTLKTQVAIIGAGPSGLLLGQLLHNAGIDTVILERQTPEYVLSRIRAGVLEQGMVELLRQAGVGQRMDAEGLPHDGFELVLNDRRVHIDLKGLTGGKNVMVYGQTEVTRDLMAAREAAGARTLYLASNAQPHDMQTQTPFVTFEHEGETWRLDCDYIAGCDGFHGVARQSIPAEKLKVFERVYPFGWLGVLADTPPVHEELVYARHTRGFALCSMRSKTRTRYYLQVPAEEQVADWPDERFWGELKNRLPADLAAALVTGPSIEKSIAPLRSFVVEPMQYGRMFLVGDAAHIVPPTGAKGLNLAASDVSTLFNILLKVYRDGRVELLEKYSAICLRRVWKAERFSWWMTSMLHRFDDDAFNQRISEAELEYFVDSEAGRKTIAENYVGLPYEAIE Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_3553 Urease (EC 3.5.1.5) Specifically important for utilizing Urea. Automated validation from mutant phenotype: the predicted function (3.5.1.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Urease gamma subunit (EC 3.5.1.5) MDLTPREKDKLLIFTAGLVAERRLARGLKLNYPEAMAYISAALLEGARDGQTVAELMHYGTTLLSREQVMEGIPEMIPEIQVEATFPDGTKLVTVHQPIA Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_3556 Urease (EC 3.5.1.5) Specifically important for utilizing Urea. Automated validation from mutant phenotype: the predicted function (3.5.1.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Urease alpha subunit (EC 3.5.1.5) MIPGQYQVQPGDIELNVGRRTLTLKVANSGDRPIQVGSHYHFFETNDALTFDRAASRGMRLNIPAGTAVRFEPGQSREVELVELAGHRRVFGFAGRVMGDLDCHAFVARELAPAGARSGRVFGVCCAAQREQAPSPQWIAHFDFEFQGKHMKISRQAYADMFGPTVGDKVRLADTELWIEVEKDFTTYGEEVKFGGGKVIRDGMGQSQLLAAEVVDTLITNALIIDHWGIVKADVGLKDGRIAAIGKAGNPDIQPDVTIAIGASTEVIAGEGMILTAGGIDTHIHFICPQQIEEALMSGVTTMIGGGTGPATGTNATTCTSGPWHLARMLQAADAFPMNIGFTGKGNASLPEPLIEQVKAGAIGLKLHEDWGTTPAAIDNCLSVADQYDVQVAIHTDTLNESGFVETTLAAFKGRTIHTYHTEGAGGGHAPDIIKACGFPNVLPSSTNPTRPFTRNTIDEHLDMLMVCHHLDPSIAEDVAFAESRIRRETIAAEDILHDLGAFSMISSDSQAMGRVGEVITRTWQTADKMKKQRGALPGDGEGNDNFRIKRYIAKYTINPAITHGISHEVGSIEVGKWADLVLWRPAFFGVKPTLILKGGAIAASLMGDANASIPTPQPVHYRPMFASFGGSRHATSLTFISQAAAEAGLPEQLGLKKRIAVVKGCRDVQKTDLIHNDYLPSIDVDPQTYQVKADGVLLWCEPAEVLPMAQRYFLF Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_3797 N-formylglutamate deformylase (EC 3.5.1.68) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (3.5.1.68) was linked to the condition via a SEED subsystem. This annotation was also checked manually. N-formylglutamate deformylase (EC 3.5.1.68) VEKVLNFMQGRVPLLISMPHAGLRLTPAVQAGLIPEAQSLPDTDWHIPRLYEFAAELGASTLAAEYSRFVVDLNRPSDDKPMYVGATTGLYPATLFDGVPLFRQGLEPSAEERARYLQQIWMPYHQALQQELARLKAEFGYALLFDAHSIRSVIPHLFDGKLPDFNLGTFNGASCDPTLASQLEAICARHGQFTHVLNGRFKGGHITRHYGNPAEDIHAVQLELCQSTYMEEYEPFNYRADLAEPTQVVLRQLLEGLLAWGRQAYKH Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_3798 Imidazolonepropionase (EC 3.5.2.7) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (IMIDAZOLONEPROPIONASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Imidazolonepropionase (EC 3.5.2.7) MKTLWQNCHAATMAQGVYSIIEDAAIVTQGKHIQWIGPRAELPTGDYPAVNDLKGAWVTPGLIDCHTHTVFGGNRSGEFEQRLQGVSYAEIAAAGGGIASTVRATRAASEDELFASAAKRLGSLMRDGVTTVEIKSGYGLDLASERKILRVIRRLGAELPVSVRSTCLAAHALPPEYKDRADDYIEHICSEMLPALAAEGLVDAVDAFCEYLAFSPAQVERVFITAQQLGLPVKLHAEQLSSLHGSSLAARYQALSADHLEFMTEDDAKAMAASGTVAVLLPGAFYFLRETQLPPMEALRKHGVKIAVASDLNPGTSPALSLRLMLNMACTCFRMTPEEALAGVTIHAAQALGMAQTHGSLEAGKVADFVAWHIDRPADLAYWLGGDLEKRVVRHGVEID Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_3799 Histidine ammonia-lyase (EC 4.3.1.3) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (4.3.1.3) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Histidine ammonia-lyase (EC 4.3.1.3) MTALNLIPGQLSLAQLRDIYQQPVTLSLDASASAQIEASVACVEQILAENRTAYGINTGFGLLASTRIASEDLENLQRSLVLSHAAGVGEPISDALVRLVMVLKVNSLSRGFSGIRRQVIDALIALINAEVYPHIPLKGSVGASGDLAPLAHMSLVLLGEGKARYKGEWLPAVEALKVAGLAPLTLAAKEGLALLNGTQVSTAFALRGLFEGEDLFAGALALGGLTVEAVLGSRSPFDARIHAARGQKGQIDAAAAYRDLLGERSEVSDSHQNCDKVQDPYSLRCQPQVMGACLTQFRQAAEVLVIEANAVSDNPLVFAAEGDVISGGNFHAEPVAMAADNMALAIAEIGSLSERRISLMMDKHMSQLPPFLVANGGVNSGFMIAQVTAAALASENKALSHPHSVDSLPTSANQEDHVSMAPAAGKRLWEMAENTRGILAVEWLAACQGLDLRGGLKTSTKLERARGLLRAQVPFYEKDRFFAPDINAASELLASRCLNELVTAQLLPSL Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_3805 Urocanate hydratase (EC 4.2.1.49) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (UROCANATE-HYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Urocanate hydratase (EC 4.2.1.49) VTDATRKPEKYRDVEIRAPRGNTLTAKSWLTEAPLRMLMNNLDPEVAENPKELVVYGGIGRAARNWECYDKIVESLTNLNDDETLLVQSGKPVGVFKTHSNAPRVLIANSNLVPHWASWEHFNELDAKGLAMYGQMTAGSWIYIGSQGIVQGTYETFVEAGRQHYDSNLKGRWVLTAGLGGMGGAQPLAATLAGACSLNIECQQVSIDFRLKTRYVDEQATDLDDALARIEKYTAEGKAISIALCGNAAEILPEMVRRGVRPDMVTDQTSAHDPLNGYLPAGWTWDEYRARAKTEPAAVVKAAKQSMAIHVKAMLAFQKMGVPTFDYGNNIRQMAQEEGVENAFDFPGFVPAYIRPLFCRGIGPFRWAALSGDPQDIYKTDAKVKELIPDDAHLHNWLDMARERISFQGLPARICWVGLGQRAKLGLAFNEMVRSGELSAPIVIGRDHLDSGSVASPNRETESMQDGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGFSQHSGMVIVCDGTDEAAERIARVLHNDPGTGVMRHADAGYQIAIDCAKEQGLNLPMITGK Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_3808 Formiminoglutamic iminohydrolase (EC 3.5.3.13) Specifically important for utilizing L-Histidine. Automated validation from mutant phenotype: the predicted function (FORMIMINOGLUTAMATE-DEIMINASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Formiminoglutamic iminohydrolase (EC 3.5.3.13) MSAFFAERALLPSGWAHDVRLEVDAEGVLTHIQAGSHADGAERLGGPLLPGMPNLHSHAFQRAMAGLAEVAGNPNDSFWTWRDLMYRLVGKISPDQLGIIARQLYIEMLKAGYTSVAEFHYVHHDTDGAPYADPAELALRISHAASAAGIGLTLLPVLYSHSGFGGQAPNDGQRRFINSTENYLKLQSRLQPILAGQPSQALGLCFHSLRAVTPGQIQDVLAASDRECPVHIHIAEQQKEVDDCLSWSGARPLQWLYENTEVDQRWCLVHATHANAQEVSLMARSRAIAGLCLTTEANLGDGIFPAVDFLAQGGRLGIGSDSHVSLSVVEELRWLEYGQRLRDQRRNRLYRADQPMVGRTLFDAALEGGAQALGQPIGALDIGKRADWLVLDGSDPYLATAQGDAILNRWLFAGGDRQVRDVMVGGRWVVRDGRHAGEEESARAFTQVLRELLG Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4013 5-aminovalerate transaminase (EC 2.6.1.48) Specifically important for utilizing L-Lysine. Automated validation from mutant phenotype: the predicted function (2.6.1.48) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 5-aminovalerate aminotransferase (EC 2.6.1.48) / Gamma-aminobutyrate:alpha-ketoglutarate aminotransferase (EC 2.6.1.19) MSKTNADLMARRTAAVPRGVGQIHPIFAESAKNATVTDVEGREFIDFAGGIAVLNTGHVHPKIIAAVTEQLNKLTHTCFQVLAYEPYVELCEKINAKVPGDFAKKTLLVTTGSEAVENAVKIARAATGRAGVIAFTGAYHGRTMMTLGLTGKVVPYSAGMGLMPGGIFRALYPNELHGVSIDDSIASIERIFKNDAEPRDIAAIIIEPVQGEGGFYVAPKEFMKRLRALCDQHGILLIADEVQTGAGRTGTFFAMEQMGVAADLTTFAKSIAGGFPLAGVCGKAEYMDAIAPGGLGGTYAGSPIACAAALAVMEVFEEEHLLDRCKAVGERLVAGLKAIQKKYPVIGDVRALGAMIAVELFENGDSHKPNAAAVAQVVAKARDKGLILLSCGTYGNVLRVLVPLTAPDEQLDKGLAILEECFSEL Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4087 L-asparaginase (EC 3.5.1.1) Specifically important for utilizing L-Asparagine. Automated validation from mutant phenotype: the predicted function (ASPARAGHYD-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-asparaginase (EC 3.5.1.1) MNGSTYPAAQHVMVLYTGGTIGMQASAHGLAPASGFEARMRDYLHSQPELVVPQWRFREMSPLIDSANMTPAYWQQLREAVVDAVDVQGCDSVLILHGTDTLAYSAAAMSFQLLGLHARVCFTGSMLPAGVIDSDAWENLSGALVALGQGLAPGVHLYFHGELLAPTRCAKVRSFGRHPFKRLERQGGGLKASSLPAQLNYNQPKQLANIAALPLFPGISAEILDGLLGSGIQGLVLECYGSGTGPSDNPAFLASLERARDSGVVIVAVTQCHEGGVELDVYEAGSRLRGVGVLSGGGMTREAAFGKLQALIGAGLPVEEVRRLVELDLCGELA Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_456 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (RXN-10815) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) MADLYENPMGLMGFEFIEFASPTPNTLEPIFEIMGFTKVATHRSKDVHLYRQGAINLILNNEPHSVASYFAAEHGPSVCGMAFRVKDSQKAYKRALELGAQPIHIETGPMELNLPAIKGIGGAPLYLIDRFGEGSSIYDIDFVFIEGVDRNPVGAGLKIIDHLTHNVYRGRMAYWAGFYEKLFNFREIRYFDIKGEYTGLTSKAMTAPDGMIRIPLNEESSKGAGQIEEFLMQFNGEGIQHVAFLTDDLVKTWDHLKSIGMRFMTAPPDTYYEMLEGRLPNHGEPVDELQSRGILLDGASEQGDKRLLLQIFSETLMGPVFFEFIQRKGDDGFGEGNFKALFESIERDQVRRGVLATE Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4777 5-aminopentanamidase (EC 3.5.1.30) Specifically important for utilizing L-Lysine. Automated validation from mutant phenotype: the predicted function (5-AMINOPENTANAMIDASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. 5-aminopentanamidase (EC 3.5.1.30) MRVALYQCPPLPLDPAGNLHRLHQVALEARGADVLVLPEMFMTGYNIGVDAVNVLAEVYNGEWAQQIARIAKAAGLAIVYGYPERGEDGQIYNAVQLIDAQGERLANYRKSHLFGDLDHAMFSAGDAALPIVELNGWKLGLLICYDLEFPENARRLALAGAELILVPTANMQPYEFIADVTVRARAIENQCFVAYANYCGHEGELQYCGQSSIAAPNGSRPALAGLDEALIVAELDRQLMDDSRAAYNYLHDRRPELYDDLHKH Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4778 Lysine 2-monooxygenase (EC 1.13.12.2) Specifically important for utilizing L-Lysine. Automated validation from mutant phenotype: the predicted function (LYSINE-2-MONOOXYGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Lysine 2-monooxygenase (EC 1.13.12.2) MNKNNRHPADGKKPITIFGPDFPFAFDDWIEHPAGLGSIPAHNHGTEVAIVGAGIAGLVAAYELMKLGLKPVVYEASKMGGRLRSQAFNGAEGVIAELGGMRFPVSSTAFYHYVDKLGLETKPFPNPLTPASGSTVIDLEGQTYYAQKLADLPALFQEVADAWADALEDGSRFGDIQQAIRDRDVPRLKALWNTLVPLWDDRTFYDFVATSKAFAKLSFQHREVFGQVGFGTGGWDSDFPNSMLEIFRVVMTNCDDHQHLVVGGVEQVPHGIWNHVPERCAHWPQGTSLNSLHLGAPRSGVKRIARAADGRFSVTDVWDNTREYAAVLVTCQSWLLTTQIECEEALFSQKMWMALDRTRYMQSSKTFVMVDRPFWKDKDPETGRDLMSMTLTDRLTRGTYLFDNGDDKPGVICLSYSWMSDALKMLPHPVEKRVKLALDALKKIYPKVDIAARIIGDPITVSWEADPHFLGAFKGALPGHYRYNQRMYAHFMQDDMPAEQRGIFIAGDDVSWTPAWVEGAVQTSLNAVWGIMKHFGGETHAENPGPGDVFHEIGPIALPE Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_478 Dihydrolipoyl dehydrogenase (EC 1.8.1.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (1.8.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Dihydrolipoamide dehydrogenase of branched-chain alpha-keto acid dehydrogenase (EC 1.8.1.4) MQQTLNTTLLIIGGGPGGYVAAIRAGQLGIPTILVEGQALGGTCLNIGCIPSKALIHVAEQFHQTRHHSQGSALGITVSAPSLDIGKSVEWKDGIVDRLTTGVAALLKKHKVQVIHGWAKVIDGKTVEVGDTRIQCEHLLLATGSKSVDLPMLPVGGPIISSTEALAPTSVPKHLVVVGGGYIGLELGIAYRKLGAEVSVVEAQERILPAYDGELTQPVHEALKQLGVKLYLKHSVEGFDAQASTLQVRDPAGDTLNLDTDRVLVAVGRKPNTQGWNLEALNLAMNGAAVKIDQRCQTSMRNVWAIGDLSGEPMLAHRAMAQGEMVAELIAGQHREFNPTAIAAVCFTDPELVVVGKTPDEAKAAGLDCIVSSFPFAANGRAMTLESKSGFVRVVARRDNHLIVGWQAVGVGVSELSTAFGQSLEMGARLEDIAGTIHAHPTLGEAVQEAALRALGHALHL Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_479 Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase (EC 2.3.1.168) Specifically important for utilizing L-Leucine; L-Isoleucine. Automated validation from mutant phenotype: the predicted function (2.3.1.168) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Dihydrolipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex (EC 2.3.1.168) MGTHVIKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGRVIALGGEPGEVMAVGSELIRIEVEGAGNLKESAQQAPTPTPAAQAPKPAPVATPEPVLEKTAAPRCAPQAPVARDPDERPLASPAVRKHALDLGIQLRLVQGSGPAGRVLHEDLEAYLAQGPSVQAKGGSGYAERHDEQQIPVIGMRRKIAQRMQEATQRAAHFSYVEEIDITALEELRVHLNEKHGASRGKLTLLPFLVRALVVALRDFPQMNARYDDEAQVIHRSGAVHVGVATQSDVGLMVPVVRHAEARSLWDNAAEISRLATAARTGKASRDELSGSTITLTSLGALGGIVSTPVLNLPEVAIVGVNKIVERPVVIKGQIVIRKMMNLSSSFDHRVVDGMDAAQFIQALRGLLEQPATLFVE Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_480 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) (EC 1.2.4.4) Specifically important for utilizing L-Isoleucine. Automated validation from mutant phenotype: the predicted function (1.2.4.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Branched-chain alpha-keto acid dehydrogenase, E1 component, beta subunit (EC 1.2.4.4) MNDHNTNIALDTAMTTTTMTMIQALRSAMDVMLERDDNVVVFGQDVGYFGGVFRCTEGLQNKYGTSRVFDAPISESGIVGVAVGMGAYGLRPVAEIQFADYVYPASDQIISEAARLRYRSAGEFTAPMTLRMPCGGGIYGGQTHSQSIEAMFTQVCGLRTVMPSNPYDAKGLLIASIENDDPVIFLEPKRLYNGPFDGHHDRPVTPWSKHPSAQVPDGYYTVPLDVAAITRPGKDVTVLTYGTTVYVSQVAAEETGIDAEVIDLRSLWPLDLETIVKSVKKTGRCVVVHEATRTCGFGAELVALVQEHCFHHLEAPIERVTGWDTPYPHAQEWAYFPGPSRVGAALKRVMEV Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_496 Dihydropyrimidine dehydrogenase (NADP(+)) (EC 1.3.1.2) Specifically important for utilizing Cytosine. Automated validation from mutant phenotype: the predicted function (1.3.1.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Dihydropyrimidine dehydrogenase [NADP+] (EC 1.3.1.2) MADLSIVFAGIKAPNPFWLASAPPTDKAYNVVRAFEAGWGGVVWKTLGEDPAAVNVSSRYSAHYGANREVLGINNIELITDRSLEINLREITQVKKDWPDRALIVSLMVPCVEESWKRILPLVEATGADGIELNFGCPHGMPERGMGAAVGQVPEYVEQVTRWCKTYCSLPVIVKLTPNITDIRVAARAAHRGGADAVSLINTINSITSVDLDRMVALPSVGSQSTHGGYCGSAVKPIALNMVAEIARDPQTQGLPICGIGGIGSWRDAAEFIALGSGAVQVCTAAMLHGFRIVDEMKDGLSRWMDEHGHANLQAFSGRAVSNTTDWKYLDINYQVIAKIDQEACIGCGRCHIACEDTSHQAIASLKQADGTRKYEVIDEECVGCNLCQITCPVQDCIEMVTVDTGKPFLDWNHDPRNPYHVAV Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_498 Dihydropyrimidinase (EC 3.5.2.2) Specifically important for utilizing Cytosine. Automated validation from mutant phenotype: the predicted function (3.5.2.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Dihydropyrimidinase (EC 3.5.2.2) MSLLIRGATVITHDESYRADVFCADGVIKAIGDNLDVPAAVEVLDGGGQYLMPGGIDPHTHMQLPFMGTVASEDFFSGTAAGLAGGTTSIIDFVIPNPQQSLMEAFHQWRGWAEKSASDYGFHVAITWWSEQVREEMAELVNHHGVNSFKHFMAYKNAIMAADDTLVASFERCLELGAVPTVHAENGELVYHLQRKLLAQGITGPEAHPLSRPSQVEGEAASRAIRIAETLGTPLYLVHVSTKEALDEITYARSKGQPVYGEVLAGHLLLDDSVYRDPDWQTAAGYVMSPPFRPRGHQEALWHGLQSGNLHTTATDHCCFCAEQKAAGRDDFSKIPNGTAGIEDRMAVLWDEGVNSGKLSMHDFVALTSTNTAKIFNLYPRKGAIRVGADADLVLWDPQGSRTISAKTHHQQVDFNIFEGKTVRGVPSHTISQGRLVWADGDLRAERSAGRYIERPAYPAVFDLLSKRAELNKPTAVKR Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_513 Myo-inosose-2 dehydratase (EC 4.2.1.44) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (MYO-INOSOSE-2-DEHYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Inosose dehydratase (EC 4.2.1.44) MPAIRIGINPISWSNDDLPSLGGETPLSTALSEGKAIGYEGFELNGKFPKDAKGVGDVLRPYDLALVSGWYSSRLARRSAAEEIDAIASHVELLAQNGATVLVYGEVADSIQGQRIALIERPRFHTDEAWQAYADKLTELARFTLSQGVRLAYHHHMGAYVESPADIDKLMALTGSEVGLLFDSGHCYMGGGEPLQVLRKHIERICHVHFKDVRKPVVQLARNNLWSFPDCIINGTFTVPGDGDIDFAALLDVLLAADYQGWLVVEAEQDPAVAPSYAYAKKGYDTLRALLQERNPS Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_517 Epi-inositol hydrolase (EC 3.7.1.-) Specifically important for utilizing m-Inositol. Automated validation from mutant phenotype: the predicted function (RXN-14149) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Epi-inositol hydrolase (EC 3.7.1.-) MTTTRLTMAQALVKFLDNQYIEVDGVQSKFVAGVFTIFGHGNVLGLGQALEQDSGDLVVHQGRNEQGMAHAAIGFAKQHLRRKIYACSSSVGPGAANMLTAAATATANRIPLLLLPGDVYASRQPDPVLQQIEQFHDLSISTNDAFKAVSKYWDRINRPEQLMTAAIHAMRVLTDPAETGAVTLALPQDVQAEAYDYPDYFLQKRVHRIDRRPATEAMLGDALALLKGKRRPLIICGGGVRYSEANAALQAFAERFDIPFAETQAGKSAVVSSHPLNVGGVGETGCLAANLLAKKADLIIGIGTRYSDFTTGSKWLFQHPDVQFLNLNISPCDALKLDGVQLLADARSGLESLSAALGDYRAEWGGQIADAKVQLDAEVDRIYQADYQAEDFLPEIDDHMDPAVFREFIELTGSCLTQSRVLGTLNETLADDAIIVAAAGSLPGDLQRAWRSKGVNTYHVEYGYSCMGYEVNAALGVKLAEPDKEVYALVGDGSYMMLHSELATSIQERRKINVVLLDNMAFGCINNLQMGNGMDSFGTEFRFRNPDTGKLDGAFVPVDFAMSAAAYGCKTYRVKTLDELHAALADARLQTVSTLIDIKVLPKTMIHSYLSWWRVGVAQVSTSARTDAVAKTLNERLAKARQY Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5290 Homogentisate 1,2-dioxygenase (EC 1.13.11.5) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (1.13.11.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Homogentisate 1,2-dioxygenase (EC 1.13.11.5) MNLVSPASDLAYQSGFGNEFASEALPGALPVGQNSPQKVPYGLYAELFSGTAFTMARSEARRTWMYRIRPSANHPAFTRLERQLAGGPLGEVTPNRLRWNPLEIPAEPTDFIDGLVCMAANAGADKPAGISLYQYQANRSMERVFFNADGEWLIVPQLGRLRITTELGVLELAPLEIVVLPRGLKFRIELLDPQARGYLAENHGAPLRLPDLGPIGSNGLANPRDFLTPVAHYENLAQPTSLVQKFLGELWGCELDHSPLDVVAWHGNNVPYKYDLRRFNTIGTVSFDHPDPSIFTVLTSPTSVHGLANLDFVIFPPRWMVAENTFRPPWFHRNLMNEFMGLIQGAYDAKAEGFLPGGASLHSCMSAHGPDGETCTKAINAELQPVKIDNTMAFMFETSQVLRPSRFALDCPQLQTDYDACWASLPVTFDPTRR Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5292 Maleylacetoacetate isomerase (EC 5.2.1.2) Specifically important for utilizing L-Phenylalanine. Automated validation from mutant phenotype: the predicted function (5.2.1.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Maleylacetoacetate isomerase (EC 5.2.1.2) @ Glutathione S-transferase, zeta (EC 2.5.1.18) MELYTYYRSTSSYRVRIALALKGLDYQALPVNLIAAPGGEHRQPAYLAINPQGRVPALRTDEGALLVQSPAIIEYLEERYPQVPLLSADLTVRAHERGVAALIGCDIHPLHNVSVLNKLRQWGHDETQVTEWIGHWISQGLAAVEQLMGDDGYCFGAAPGLADVYLIPQLYAAERFNVSLQAYPRIRRVAALAAGHPAFQQAHPANQPDTP Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5556 Aminomethyltransferase (EC 2.1.2.10) Specifically important for utilizing Glycine. Automated validation from mutant phenotype: the predicted function (2.1.2.10) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Aminomethyltransferase (glycine cleavage system T protein) (EC 2.1.2.10) MSTEQLLKTPLHALHLELGARMVPFAGYDMPVQYPLGVMKEHQHTRDQAGLFDVSHMGQIRLTGAGAAKALETLVPVDIIDLPVGMQRYAMFTNENGGILDDLMVANLGNDELFLVVNAACKDQDLAHLRAHIGAQCSIEPLFEARALLALQGPAAVTVLARLAPDVAKMTFMQFQRVTLLGMDCYVSRSGYTGEDGFEISVPAAEAEKLARALLAEPEVAAIGLGARDSLRLEAGLCLYGHDMNTETTPIEASLLWAISKVRRADGARAGGFPGAETVFAQQQGGVKRKRVGLLPQERTPVREGAEIVNEAGEIIGTVCSGGFGPTLGGPLAMGYLDSAYVALDTPVWAIVRGKKVPLLVSKMPFVPQRYYRG Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5557 L-serine ammonia-lyase (EC 4.3.1.17) Specifically important for utilizing Glycine. Automated validation from mutant phenotype: the predicted function (4.3.1.17) was linked to the condition via a SEED subsystem. This annotation was also checked manually. L-serine dehydratase (EC 4.3.1.17) MSLSVFDLFKIGIGPSSSHTVGPMRAAARFAEGLRRDDLLNCTTSVKVELYGSLGATGKGHGSDKAVLLGLEGEHPDTVDTETVDARLQAIRSSGRLNLLGEHSIEFNEKLHLAMIRKPLAFHPNGMIFRAFDAAGLQVRSREYYSVGGGFVVDEGAAGADRIVEDATPLTFPFKSAKDLLGHCSTYGLSISQVMLTNESAWRPEAETRAGLLKIWQVMQDCVAAGCRNEGILPGGLKVKRRAAALHRQLCKNPEAALRDPLSVLDWVNLYALAVNEENAYGGRVVTAPTNGAAGIIPAVLHYYMRFIPGASEDGVVRFLLTAAAIGILYKENASISGAEVGCQGEVGVACSMAAGALCEVLGGSVQQVENAAEIGMEHNLGLTCDPIGGLVQVPCIERNAMGSVKAINAVRMAMRGDGHHFVSLDKVIRTMRQTGADMKSKYKETARGGLAVNIIEC Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5558 Glycine dehydrogenase (aminomethyl-transferring) (EC 1.4.4.2) Specifically important for utilizing Glycine. Automated validation from mutant phenotype: the predicted function (1.4.4.2) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Glycine dehydrogenase [decarboxylating] (glycine cleavage system P protein) (EC 1.4.4.2) MTVNLGTANEFIARHIGPRASDEQAMLERLGYDSLEALSASVIPESIKGTSVLDMGDGQSEADALASIKAIAAKNQLFKTYIGQGYYNCHTPAPILRNLLENPAWYTAYTPYQPEISQGRLEALLNFQTLISDLTGLPIANASLLDEATAAAEAMTFCKRLSKNKGSNAFFASVHSHPQTLDVLRTRAEPLGIDVVVGDERELSDVSGFFGALLQYPASNGDLFDYRELTERFHTANALVAVAADLLALTLLTPPGEFGADVAIGSAQRFGVPLGFGGPHAAYFSTKDAFKRDMPGRLVGVSVDRFGKPALRLAMQTREQHIRREKATSNICTAQVLLANIASMYAVYHGPKGLVQIANRIHHLTAILAKGLGALGLSVEQESFFDTLTLRTGAQTAALHDKARAQRINLRVVDAERLGLSLDETTSQADVEALLRLIGNLMADGKAVPDFAALAASVQSHIPAELVRQSAILSHPVFNRYHSETELMRYLRKLADKDLALDRTMIPLGSCTMKLNAASEMIPVTWAEFGALHPFAPAEQSAGYQQLTDELEAMLCAATGYDAVSLQPNAGSQGEYAGLLAIRAYHQSRGEDRRDICLIPSSAHGTNPATAHMAGMRVVVTACDARGNVDIEDLRAKAIEHREHLAALMITYPSTHGVFEEGIREICGIIHDNGGQVYIDGANMNAMVGLCAPGKFGGDVSHLNLHKTFCIPHGGGGPGVGPIGVKSHLAPFLPGHASMERKQGAVCAAPFGSASILPITWMYIRMMGGAGLKRASQLAILNANYIARRLEEHYPVLYSGSNGLVAHECILDLRPLKDSSGISVDDVAKRLIDFGFHAPTMSFPVAGTLMIEPTESESKEELDRFCDAMICIREEIRAVENGSLDKDDNPLKNAPHTAAEIVGEWTHPYSREQAVYPVASLIDGKYWPPVGRVDNVFGDRNLVCACPSIESYA Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5966 L-arabinolactonase (EC 3.1.1.15) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (L-ARABINONOLACTONASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-arabinolactonase (EC 3.1.1.15) MTWTAVTEHRAILGEGPFWDEPTQALYWVDIAGKQALRLIGANVQIWQMPEHVSAFIPTQSGDALVTLSSGVYRLDLDSPGLEPRLTLLCMADPQLGNRANEARCDALGQLWLGTMQNNIGENAEDLPIERRSGGLFRVSGDGRVMPLLRGLGIPNTLLWSPDGTTVYFGESLDGTLYRHFIHPDGSLAPAEVWFGPHPRGGPDGSAMDARGYIWNARWDGSCLLRLNPQGQVDRVIELPVSRPTSCVFGGDDLKTLYITSAASPLGHPLDGAVLSMRVDIPGVACTRFAG Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_6061 Methylisocitrate lyase (EC 4.1.3.30) Specifically important for utilizing Sodium propionate. Automated validation from mutant phenotype: the predicted function (4.1.3.30) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Methylisocitrate lyase (EC 4.1.3.30) MSNSTPGQRFRDAVANEHPLQVVGTINANHALLAKRAGFKAIYLSGGGVAAGSLGVPDLGITGLDDVLTDVRRITDVCDLPLLVDVDTGFGSSAFNVARTVKSMIKFGAAAIHIEDQVGAKRCGHRPNKEIVSQQEMVDRIKAAVDARTDDSFVIMARTDALAVEGLESALDRAAACIEAGADMIFPEAITELEMYKLFASRVKAPILANITEFGATPLYTTEQLAGADVSLVLYPLSAFRAMNKAAENVYTAIRRDGTQQNVIDTMQTRMELYDRIDYHTFEQKLDALFAAKK Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_6062 2-methylcitrate synthase (EC 2.3.3.5) Specifically important for utilizing Sodium propionate. Automated validation from mutant phenotype: the predicted function (2.3.3.5) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 2-methylcitrate synthase (EC 2.3.3.5) MAEAKVLSGAGLRGQVAGQTALSTVGQSGAGLTYRGYDVRDLAADAQFEEVAYLLLYGELPTQAQLDAYTGKLRQLRDLPQALKEVLERIPADAHPMDVMRTGCSFLGNLEPEQDFSQQHDKTDRLLAAFPAIMCYWYRFSHQGQRIECVTDEVSIGGHFLHLLHGKKPSELHVKVMNVSLILYAEHEFNASTFTARVCASTLSDLFSCITAAIGSLRGPLHGGANEAAMEMIERFSSPQEAIEGTLGMLARKDKIMGFGHAIYKDNDPRNEVIKGWSKKLADEVGDTVLFPVSEAIDKTMWEQKKLFPNADFYHASAYHFMGIPTKLFTPIFVCSRLTGWAAHVFEQRANNRIIRPSAEYTGVEQRKFVPIEQR Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_609 L-arabonate dehydratase (EC 4.2.1.25) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (L-ARABINONATE-DEHYDRATASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. L-arabonate dehydratase (EC 4.2.1.25) MSDKKPSLRSAQWFGTADKNGFMYRSWMKNQGIADHQFHGKPIIGICNTWSELTPCNAHFRQIAEHVKRGVIEAGGFPVEFPVFSNGESNLRPTAMLTRNLASMDVEEAIRGNPIDGVVLLTGCDKTTPALLMGAASCDVPAIVVTGGPMLNGKHKGQDIGSGTVVWQLSEQVKAGTITIDDFLAAEGGMSRSAGTCNTMGTASTMACMAEALGTSLPHNAAIPAVDARRYVLAHMSGMRAVEMVREDLKLSKILTKEAFENAIRVNAAIGGSTNAVIHLKAIAGRIGVQLDLDDWTRIGRGMPTIVDLQPSGRFLMEEFYYAGGLPAVLRRLGEANLIPHPNALTVSGKSIGENTKDAPIYGQDEVIRTLDNPIRADGGICVLRGNLAPLGAVLKPSAATAELMQHRGRAVVFENFDEYKARINDPELDVDASSILVMKNCGPKGYPGMAEVGNMGLPAKLLAQGVTDMVRISDARMSGTAYGTVVLHVAPEAAAGGPLAAVKEGDWIELDCTSGRLHLDIPDAELAARLADIVPPQQLLVGGYRQLYIDHVLQADQGCDFDFLVGCRGAEVPRHSH Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_612 Ketoglutarate semialdehyde dehydrogenase (EC 1.2.1.26) Specifically important for utilizing L-Arabinose. Automated validation from mutant phenotype: the predicted function (25-DIOXOVALERATE-DEHYDROGENASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Ketoglutarate semialdehyde dehydrogenase (EC 1.2.1.26) MNQILGHNYIGGARSAAGQTRLQSVDASTGEALPHDFIQATAEEVDAAAKAAAAAYPAYRSLSAVRRAEFLEAIADELDALGDEFVAVVCRETALPAARIQGERGRTSGQMRLFAKVLRRGDFYGARIDRALPERTPLPRPDLRQYRIGLGPVAVFGASNFPLAFSTAGGDTASALAAGCPVVFKAHSGHMATAEHVADAIIRAAEKTLMPAGVFNMIYGGGVGEWLVKHPAIQAVGFTGSLKGGRALCDMAAARPQPIPVFAEMSSINPVIVLPQALETRAESVARDLTASVVQGCGQFCTNPGLVIGIRSPQFTAFTQQVAALIGDQAPQTMLNAGTLQSYGKGLQKLLAHPGIEHLAGRQQQGNQAQPQLFKADASLLINGDEALQEEVFGPTTVFVEVADQAQLTAALNGLHGQLTATMIGEPADFERFSELTPLLEQKVGRILLNGYPTGVEVCDSMVHGGPYPATSDARGTSVGTLAIDRFLRPVCFQNYPDSLLPEPLKNANPLGILRLVDGVPGREAL Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_805 Xylulose kinase (EC 2.7.1.17) Specifically important for utilizing D-Xylose. Automated validation from mutant phenotype: the predicted function (XYLULOKIN-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Xylulose kinase (EC 2.7.1.17) MANQQLFLGIDCGTQGTKALILDATSGQVLGLGAAAHSMISGANGRREQDTQQWLDAFTQATHQALAAAGVDGQAILGIGVSGQQHGLVLLDDQGQVLRPAKLWCDTETTPENDRLLAHLGGEDGSLERLGVVIAPGYTVSKLLWTREQHPQVFERIASVLLPHDFLNYWLTGRHCSEYGDASGTGYFNVRTRQWDVQLLQHIDPSARLQAALPELIEAHQPVGRILPAIAAHLGINPEAVVASGGGDNMMGAIGTGNIQPGVITMSLGSSGTVYAYAAEPAVSPQPSVATFCSSSGGWLPLICTMNLTNATGAIRELLDLDIDAFNALVAKAPIGAEGVCMLPFLNGERVPALPHATGSLLGLTTTNLTRANLCRAVVEGTTFGLRYGLDLLRANGLQAQSIRLIGGGSKSAQWRQIVADTMDTTVICTEQSEAAALGAAIQAAWCHSGSQTGLAELCERCVKLDPSSETRPIAAHVAASQQAYERYRQHVATL Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_4787 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) Important for isoleucine utilization. 2-methylbutaonyl-CoA is an intermediate in the standard pathway and no other gene for the methylbutanoyl-CoA dehydrogenase was apparent in the fitness data. Butyryl-CoA dehydrogenase (EC 1.3.99.2) MIPNDEQLQISDAARQFAQERLKPFAAEWDREHRFPKEAIGEMAGLGFFGMLVPEQWGGCDTGYLAYAMALEEIAAGDGACSTIMSVHNSVGCVPILKFGNDDQKERFLKPLASGAMLGAFALTEPQAGSDASSLKTRARLDGDHYVLNGCKQFITSGQNAGVVIVFAVTDPSAGKRGITALIVPTDSPGYKVARVEDKLGQHASDTCQILFEDVKVPVANRLGEEGEGYKIALANLEGGRVGIASQSVGMARAAFEAARDYARERESFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGKPALVEASMAKLFASEMAEKVCSSALQTLGGYGYLNDFPLERIYRDVRVCQIYEGTSDIQRMVISRNL Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_26355 AO356_26355 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) Important for isoleucine utilization. 2-methylbutaonyl-CoA is an intermediate in the standard pathway and no other gene for the methylbutanoyl-CoA dehydrogenase was apparent in the fitness data. acyl-CoA dehydrogenase MLPTEEQTQIRDMARQFAQERLKPFAAEWDREHRFPREAIAEMAELGFFGMLVPEQWGGCDTGYLAYAMTLEEIAAGDGACSTIMSVHNSVGCVPILKFGNDEQKAKFLTPLASGAMLGAFALTEPQAGSDASSLKTRARLEGDHYVLNGCKQFITSGQNAGVVIVFAVTDPSAGKRGISAFIVPTDSPGYSVARVEDKLGQHASDTCQILFEEVKVPVGNRLGEEGEGYKIALANLEGGRVGIAAQAVGMARAAFEAARDYARERSSFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGQPALVEASMAKLFASEMAEKVCSMALQTLGGYGYLNDFPLERIYRDVRVCQIYEGTSDIQRMVISRNL Shewanella oneidensis MR-1 MR1 200844 SO1679 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) # Specifically important in carbon source L-Isoleucine; nitrogen source L-Isoleucine (EC 1.3.8.5). Similar to ACAD8_HUMAN (Isobutyryl-CoA dehydrogenase, mitochondrial). acyl-CoA dehydrogenase family protein (NCBI ptt file) MDFNFNEDQRQFAELARQFATDELAPFAAKWDEEHHFPKDVIQKAGELGFCSLYSPESEGGMGLSRLDASIIFEELSKGCTATTAMLTIHNMATWMVTTWGTETLRQAWSEPLTTGQMLASYCLTEPGAGSDAASLQTKAVPDGDEYVVSGSKMFISGAGSTELLVVMCRTGQAGPKGISAIAIPADSEGIIYGKAEDKMGWNAQPTRLVTFDNVRVPVANLLGEEGQGFTFAMKGLDGGRINIATCSVGTAQAALERASQYMNERQQFGKPLAAFQALQFKLADMATELVAARQMVRLAAFKLDSGDPEGTAYCAMAKRFATDVGFQVCDAALQIHGGYGYIREYPLERHFRDVRVHQILEGTNEIMRLIIARRLLDENAGQIL Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_25680 AO353_25680 2-methylbutanoyl-CoA dehydrogenase / butanoyl-CoA dehydrogenase / isobutyryl-CoA dehydrogenase (EC 1.3.8.1; EC 1.3.8.5) Specifically important for: Sodium butyrate. SEED has it as butyryl-CoA dehydrogenase. Also important on isoleucine and valine, which implies that it acts on the other substrates as well acyl-CoA dehydrogenase MLPTDEQLQISDAARQFAQERLKPFAAEWDREHRFPKEAIGEMAELGFFGMLVPEQWGGCDTGYLAYAMALEEIAAGDGACSTIMSVHNSVGCVPILKFGNDDQKERFLKPLASGAMLGAFALTEPQAGSDASSLKTRARLNGDHYVLNGCKQFITSGQNAGVVIVFAVTDPSAGKRGISAFIVPTDSPGYKVARVEDKLGQHASDTCQILFEDVQVPVANRLGEEGEGYKIALANLEGGRVGIASQSVGMARAAFEAARDYARERESFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGKPALVEASMAKLFASEMAEKVCSTALQTLGGYGYLSDFPLERIYRDVRVCQIYEGTSDIQRMVISRNL Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_1146 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) Specifically important for: L-Isoleucine. 2-methylbutanoyl-CoA is an intermediate in isoleucine catabolism. Butyryl-CoA dehydrogenase (EC 1.3.99.2) MLATEEQTQIRDMARQFAEERLKPFAAEWDREHRFPREAIDEMAELGFFGMLVPEQWGGCDTGYLAYAMTLEEIAAGDGACSTIMSVHNSVGCVPILKFGNDEQKAKFLTPLASGAMLGAFALTEPQAGSDASSLKTRARLEGDHYVLNGCKQFITSGQNAGVVIVFAVTDPSAGKRGISAFIVPTDSPGYSVARVEDKLGQHASDTCQILFEDLKVPVGNRLGEEGEGYKIALANLEGGRVGIAAQAVGMARAAFEAARDYARERSSFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGQPALVEASMAKLFASEMAEKVCSMALQTLGGYGYLNDFPLERIYRDVRVCQIYEGTSDIQRMVISRNL Pseudomonas stutzeri RCH2 psRCH2 GFF2397 Psest_2445 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) Specifically important for: L-Isoleucine. SEED has it as butyryl-CoA dehydrogenase, which is also expected to perform this reaction. 2-methylbutanoyl-CoA is an intermediate in isoleucine catabolism Acyl-CoA dehydrogenases MLPNEDQNAIAEMARQFAQERLKPFAEQWSREHRYPAEAIGEMAALGFFGMLVPEQWGGSDTGYLAYAMALEEIAAGDGACSTIMSVHNSVGCVPILRFGNEQQKSDFLTPLARGEQIGAFALTEPQAGSDASSLRTRARRDGDHYVLNGAKQFITSGKHAGTVIVFAVTDPDAGKGGISAFIVPTDSPGYQVVRVEDKLGQHASDTCQIAFEDLRVPVANRLGEEGEGYRIALANLEGGRIGIAAQAVGMARAAFEAARDYARDRETFGKPIIEHQAVAFRLADMATQIAVARQMVHHAAALREVGRPALVEASMAKLFASEMAEKVCSAAIQTLGGYGYLADFPVERIYRDVRVCQIYEGTSDIQRLVISRNLGGPV Pseudomonas simiae WCS417 WCS417 GFF2715 PS417_13850 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) Specifically important for: L-Isoleucine. SEED has it as butyryl-CoA dehydrogenase, which is also expected to perform this reaction in isoleucine catabolism acyl-CoA dehydrogenase MLPNEEQLQISDAARQFAQERLKPFAAEWDREHRFPKEAIGEMAELGFFGMLVPEQWGGCDTGYLAYAMALEEIAAGDGACSTIMSVHNSVGCVPVLKFGNDQQKEQFLKPLASGAMLGAFALTEPQAGSDASSLKTRARLEGDHYVLNGCKQFITSGQNAGVVIVFAVTDPAAGKRGISAFIVPTDSPGYSVARVEDKLGQHASDTCQILFEDVKVPVANRLGEEGEGYKIALANLEGGRVGIASQAVGMARAAFEAARDYARERESFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGKPALVEASMAKLFASEMAEKVCSAALQTLGGYGYLSDFPLERIYRDVRVCQIYEGTSDIQRMVISRNL Shewanella amazonensis SB2B SB2B 6937588 Sama_1743 Acyl-CoA dehydrogenase (EC 1.3.8.-) Specifically important in carbon source Tween 20. This confirms that it is an acyl-CoA dehydrogenase and not a biosynthetic acyl-ACP dehydrogenase (as suggested by KEGG). Since Tween 20 is hydrolyzed to a C12 fatty acid, this may act on long chain acyl-CoAs, or it might act on medium-chain acyl-CoA intermediates. acyl-CoA dehydrogenase family protein (RefSeq) MNPYQAPLGEMRFLLEHVFNAQATWQGLASLDGMVDMDTALAILEEAAKLNSELVHPINRAGDEEGVGFSDGRVTTPKGYKEAYNAFVEGGWVGLSGDPEYGGMGMPKMLGVLVDEMGYSACNAFNLYGSLTAGAALAINAHGTEELKSTYLPKLYSGEWAGAMDMTEPQAGSDLRHIRTRAEPQEDGSYLITGSKIFITGGDQDLTENVIHLVLAKISGSNTLSLFLVPKIGVDDQGNLTEPNGVSVGSIEHKMGLKGSATCVMNFDSARGWLIGRENKGLACMFTMMNYERLAIGIQGLGSAQAAVQMASDYARERLQGNAVGSTAAADPILVHGDVRRMLLTTRTLTDAGRALAVHTGKQLDLAKFADDDAVKTKAGRYVGLLTPVAKAFLTDRGLDITIMAQQVFGGHGYIRETGIEQLVRDTRIAQIYEGTNGIQAIDFLGRKVTGDNLATVKEFIAEHIEVLSDTCDKANSLRVGFADFVAVATWINDNKLSRPALINSVAVEMLDAFGYLLYGYYHLLMRDAARAADSEFAAAKAAYCDYYFAKLMPRADALLRAAKAGDELLMSLPETCF Shewanella amazonensis SB2B SB2B 6936606 Sama_0794 gamma-glutamyl-gamma-aminobutyrate hydrolase (EC: 3.5.1.94) Specifically important for: Putrescine Dihydrochloride. Similar to puuD (PUUD_ECO57), a step in putrescine catabolism. Also, is cofit with other genes from the gamma-glutamyl-putrescine pathway. However another homolog of puuD (Sama_2645) is also important in putrescine utilization and it is not clear why. Both of the homologs in S. amazonensis have conserved active site residues (see aliignments against puuD in PaperBLAST). hypothetical protein (RefSeq) MPLQQESARQERKPVILMSMGQQDRNGHAYQVMTHKYMQPVVDISDCIPLLIPTCFGVADIEQYLDMADGVYLSGAASNIDPSLYGQENLTPEKKQDLARDLVDIALIKGAVKRGLPILGICRGMQEMNIAFGGDLYQKVHDEDHLNDHREDPDTPPDVQYGASHSISMVKGSWLHKLLGDTIEVNSLHGQGIKTLGKGLEALALAEDGLVEALHAPYLPQFTLGVQWHPEWKALENPDSIKIFKAFGEACRRRAGSALDLRIDKAS Azospirillum brasilense Sp245 azobra AZOBR_RS05755 AZOBR_RS05755 Butyryl-CoA dehydrogenase (EC 1.3.8.1) Specifically important for: Sodium butyrate. KEGG's annotation of azl:AZL_005040 has been updated to 3-(methylthio)propanoyl-CoA dehydrogenase [EC:1.3.8.-], which is questionable; phenotype indicates that butyryl-CoA is a substrate (SEED_correct) acyl-CoA dehydrogenase MIPYTAPVDDLRFVLNEVVGLETVAALPNCDSAAPDLVDAVLEEAGKFASGVLAPLNRVGDKEGSVLENGVVRTPTGWKDAYSQFTESGWNSLPFEPEYGGQGLPWTVAFAVNEMWQAANLSFGLCPLLTQGAVDLLTEHASAEQKALYLPKMIAGEWNGTMNLTEPQAGSDLAAVRTRAVRADDGTYRITGQKIFITYGEHDLTDNIVHLVLARLPDAPPGIKGISLFIVPKFLPNADGTPGARNDLRCASLEHKLGIMASPTAVMAFGDDGGAVGFLVGQENRGIEYMFTMMNNARLGVGIQGVAIAERAYQQARDYAKGRVQSKDLADPKGSGVAIIRHPDVRRMLLDMRAKTEAARALALYAGTQLDVSRHHEDATVRAAATARVDILTPIVKAWSTDIGCDVASTGVQIHGGMGFIEETGAAQHYRDARITPIYEGTNGIHANDLTFRKTGRDGGESARTFIAEMRATVAELESIPGDDMEAIRTNLSAGLDALEQAVAWVVKTQADGDLRAAAAGAVNYLKLWGTVAGGWMLARSAAKALEGLRQPGANAPFLEAKLVTARFYAEQILAQGPGLLLPILTAHRTVMALSEDQF Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS04580 RR42_RS04580 Butyryl-CoA dehydrogenase (EC 1.3.8.1) # Specifically important in carbon source Sodium butyrate. This indicates that butyryl-CoA is a substrate. acyl-CoA dehydrogenase MTYRAPLKDMLFVMNELADLDAVSKLPGFEDATPETAQAVLDEAAKFNEQVVAPLNRIGDTDPSSWKDGVVTTTPGFKDAFRQFGEGGWQGVLHPQEFGGQGLPKLIATACNEMLNTANLSFALCPLLTDGAIEALLTAGSDAQKATFLPKLISGEWTGTMNLTEPQAGSDLAAVRTRAEPQGDGTYKVFGTKIFITYGEHDMAQNIVHLVLARTPTAPEGVKGISLFIVPKFLVNEDGSLGARNDAHCVSIEHKLGIKASPTAVLQFGDHGGAIGTLVGEENRGLEYMFIMMNSARFSVGMQGIAVSERAYQQAVNFARERVQSRPVDGSAREAVAIIHHPDVKRMLMTMRSLIEGARAVAYVAAAACDTAHQHADDAVRKQSQAFYEFMVPIVKGWSTELSIDVTSLGVQVHGGMGFIEETGAAQHYRDARILPIYEGTTAIQANDLVGRKTLRDGGAVARAICAQIAETEAALGKHGGAAFTAVQAQLAKGRAALETVVAFVVANAKSDPNAVFAGSVPYLKLCGIVFSGWQLGRAMLAADAKRGEDPSFHDAKISTAHFFAEHILSQASGLRDAIVAGAVPVNALSEAQF Caulobacter crescentus NA1000 Caulo CCNA_01356 CCNA_01356 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92); possible 5-dehydro-2-deoxyphosphogluconate aldolase DUF2090 (EC 4.1.2.29) Important for utilizing m-Inositol. This protein is a fusion of 5-keto-deoxygluconate kinase and DUF2090. As DUF2090 has distant similarity to aldolases, it may provide the missing 5-dehydro-2-deoxyphosphogluconate aldolase activity. 5-dehydro-2-deoxygluconokinase IolC MAQDAKTLDLIAVGRSSVDLYGQQVGGRLEDMGSFAKYLGGSPTNTAAGGARLGLKTGLLTRVGADHMGRFIREQLEREGVDVAGVLSDPDRLTALVILGIRDRVNFPLIFYRENCADMALEPSDVDEAWFAQAGAVLINGTHLSQPNVYETSLKAARAVKAAGGRVAFDIDYRPVLWGLTGKDAGENRFVENQQVTAKLQEVVALCDLIVGTEEEIHILGGSTDTIAALRAIRRASDALLVCKRGPEGCVAFPGAIPDALDEGVSARGFKVEVFNVLGAGDAFMAGFLRGWLRHESVETCCEWGNACGAIVVSRHGCTPAMPTWIELQAFLSERERPFRLREDAELEHIHWATTRERVYDELTVLAIDHRSQFEDLIAETGGDAERIPDFKRLALRAVQMVAGRDETRFGMLLDGRFGFEALAEAADHDYWIARPIELPKSRPLEFECSADVATELLEWPLNQVVKCLAFYHPDDESDLRERQERQLLRLADACRKTRHELLLELILPRGMSSDSRTVARAIRRLYALGIRPDWWKLEPLTDPDAWREIEIAIAENDPLCRGVVLLGLSAPEAELVASFEVVAPFPIVKGFAVGRTIFYDVARAWLSNQIDDDAAVTALAAKFKVLVDAWRRLRGSVEKAA Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS12125 HSERO_RS12125 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92); possible 5-dehydro-2-deoxyphosphogluconate aldolase DUF2090 (EC 4.1.2.29) Specifically important for utilizing m-Inositol. This protein is a fusion of 5-keto-deoxygluconate kinase and DUF2090. As DUF2090 has distant similarity to aldolases, it may provide the missing 5-dehydro-2-deoxyphosphogluconate activity. 5-dehydro-2-deoxygluconokinase MQATHTPSTSTPRRFAADRRLDLICIGRLAVDLYAQQVGAPLSDVSSFAKYLGGSSANIAFGCARLGLKSAMLARIGDEANGQFLKAELAAEGCDVSHVTVDPQRLTALVMLGLKDKDSFPLIFYRDNCADMALAPEDIDEAFIASSKALLITGTHFSTPQVHRSSSLALQYARRHNVRTVLDIDYRPVLWGLTSKGDGETRFIASDGVTQHLQGILPQFDLVVGTEEEFMIAGGSTDIMAALRAVRALCAATLVVKRGPLGCVVLHGAIPERLDDGFHYRGVQVEVLNVLGAGDAFISGFLKGWLNEEDDEHCCRYANACGALVVSRHACAPAMPGPIELDYFLQHAHRLQRPDRDAHLQRLHRVVSRRRHWDEVNVFAFDHRNQFFELAVEAGVSQDKLPALKRLLVEAVAQTEAKLGLQGKTGVLIDDRYGQDALNAATGRGWWVGRAVELPLSNPLEFDFGRSIGTHLQTWPQEQVVKCLVQFHPDEQVEKRLEQEAQIRALYQAVQRSGHELLLEIIPSKTLPQEEDTVLRALKRLYNLDIYPEWWKLESMSARQWEAIDALIAERDPYCRGVVLLGLAAPVSELAAGFAASRHSKTCRGFMVGRTIFHESSRAWLQGRIDDATLIAQVRTTFEELIGLWRASRVTPAREAA Pseudomonas simiae WCS417 WCS417 GFF2324 PS417_11850 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92); possible 5-dehydro-2-deoxyphosphogluconate aldolase DUF2090 (EC 4.1.2.29) Specifically important in carbon source m-Inositol. This protein is a fusion of 5-keto-deoxygluconate kinase and DUF2090. As DUF2090 has distant similarity to aldolases, it may provide the missing 5-dehydro-2-deoxyphosphogluconate aldolase activity. 5-dehydro-2-deoxygluconokinase MGQTRFASGRQLDLICLGRLGVDLYAQQVGARLEDVSSFAKYLGGSSANIAFGTARLGLRSAMLSRVGDDHMGRFLVESLAREGCDVSGIKVDPERLTALVLLGLKDRETFPLVFYRENCADMALRAEDISEAFIASSKALLITGTHFSTDGVYKASIQALDYAAKHNVQRVLDIDYRPVLWGLAGKADGETRFVADQNVSQHVQKILPRFDLIVGTEEEFLIAGGSEDLLTALRKVRELTQATLVVKLGPQGCTVIHGAIPARLEDGAIYPGVRVEVLNVLGAGDAFMSGFLSGWINDASDERCSQLANACGGLVVSRHACAPAMPTPAELEYLFNSPVPITRPDQDLTLQRLHRVTVPRKAWKQLFVFAFDHRWQLVDLAQKGGQDLARISDAKQLFIQAIERVEKKLAEQGVEADVGLLADQRFGQDALNAASGRGWWIARPVEVQNSRPLAFEHGRSVGSNLIAWPQEQIIKCLVQFHPDDEPLLRLEQEAQLKAVYEASIVSGHELLLEVIPPKDHPSTYPDVLYRSLKRLYNLGIYPAWWKIEAQSAEDWKKLDELIQERDPYCRGVVLLGLNASAEFLADGFQQASQSTTCRGFAVGRTIFQEPSRAWMAGEIDDEVLIQQVQATFEQLINAWRSARN Caulobacter crescentus NA1000 Caulo CCNA_00866 CCNA_00866 2-keto-3-deoxyxylonate dehydratase XylX (EC 4.2.1.141) Important for utilizing D-Xylose. It was previously reported to be involved in xylose catabolism and named xylX (see CC0823 and PMC1855722). It is distantly related to the characterized 2-keto-3-deoxyxylonate dehydratase from Haloferax volcanii (PMC2785657) fumarylacetoacetate hydrolase family protein MGVSEFLPEDWKAATLLGRIDFGEGPTPVLVRGGRVEDVSKIAPTVADLMNAFQPGAVIPRGEDKGPLEALDIRPVWEDPDGAAPVKLLAPVDLQCLKAAGVTFAVSTLERVIEERARGDAGEALKIRTLLAERMGGDLKSVEPGSQGAQRLKDALIADGLWSQYLEVAIGPDAEIFTKGPTLSSMGWGDQVGVRYDSHWNNPEPEVVLLCDGSGLIRGAALGNDVNLRDFEGRSALLLSKAKDNNASCAIGPFFRLFDETFGLDDVRSAEVELKITGRDNFVLDGKSNMSLISRDPAVLAGQAYGKQHQYPDGFALFLGTMFAPIQDRDTPGQGFTHKVGDRVRVSTPKLGVLENEVTTCDKAKPWTFGISALIRNLAGRGLL Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1895 Ga0059261_1895 2-keto-3-deoxyxylonate dehydratase (EC 4.2.1.141) # Specifically important in carbon source D-Xylose. 31% identical to HVO_B0027, which is 2-keto-3-deoxyxylonate dehydratase (see PMC2785657). Ga0059261_1895 is also 61% identical to xylX from Caulobacter crescentus, which is also required for xylose utilization (PMC1855722) and is believed to have this activity as well. Fumarylacetoacetate (FAA) hydrolase family protein VPEAFDVSALPEDAGQATLAGRVMLAEGPVPVIVREGRVHDVSTVAATTADLFDLPDPASAAGKYLCDVTDLTIGGGAYALLAPIDLQCVKACGVTFAVSALERVIEERARGDAGQAAAIRAELEEKIGGGIRSVVPGSADAAKLKAVLIDAGMWSQYLEVAIGPDAEVFTKAPVLSSVGWGAEIGIRSDSSWNNPEPEVVVIANAAGKVIGATLGNDVNLRDFEGRSALLLGKAKDNNAACAIGPFVRLFDAQFGIDDVRNAELDLLIEGPEGYRLEGHSSMNQISRDPLELVRQTLSEHQYPDGFALFLGTLFAPVQDRDDPGRGFTHKIGDTVRIRSRKLGTLTNRVTTSKDAAPWTFGIRELYRSIAARTAA Phaeobacter inhibens BS107 Phaeo GFF3567 PGA1_c36210 L-asparaginase (EC 3.5.1.1) # Specifically important in carbon source L-Asparagine. This protein is homologous to characterized asparaginases (i.e. Q9RFN5, see PMID:22450783) L-asparaginase II MMTNPVPMTEVWRGPLLESLHLGHAVVCNAKGEIVRSWGDPDAVIYPRSSAKMIQALPLITSGAAAKYGLTSEQLALACASHNGAEIHTSRVNAWLDQLSMTDHDFRCGPQLPDDIPARNALIKTDTSPCQVHNNCSGKHAGFLTLSQHLGAGPEYVEIDHPVQQACRSAFEQVTEEVSPGYGIDGCSAPNFATSVKGLARAMAWFAAASDRSDRDADAAQELVSAMMAHPELVAGETRACTNLMRAMGGTVAIKTGAEAVFIAILPEQKLGVALKITDGATRASECAIASILVGLGVLDADHPATLKYRNAPLINRRGIDCGSIRPSAEMTF Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_25670 AO353_25670 isobutyryl-CoA dehydrogenase (EC 1.3.8.5) Specifically important for: L-Valine. SEED has it as butyryl-CoA dehydrogenase, which is also expected to perform this reaction in valine catabolism acyl-CoA dehydrogenase MHDIELTEEQVMIRDMARDFARGEIAPHAQAWEKAGWIDDALVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATGALMSIHNSVGCGPVLNYGTEEQKQTWLADLASGQAIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSNGRRAKLAIVFAVTDPDLGKKGLSAFLVPTDTPGFIVDRSEHKMGIRASDTCAVTLNNCTIPEANLLGERGKGLAIALSNLEGGRIGIAAQALGIARAAFEAALAYARDRVQFDKPIIEHQSVANMLADMHTRLNAARLLILHAARLRSAGKPCLSEASQAKLFASEMAEKVCSSAIQIHGGYGYLEDYPVERYYRDARITQIYEGSSEIQRMVIARELKNYLV Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_2985 isobutyryl-CoA dehydrogenase (EC 1.3.8.5) Specifically important for: L-Valine. Isobutyryl-CoA is an intermediate in valine degradation. SEED annotates it as butyryl-CoA dehydrogenase, which is also expected to perform this reaction Butyryl-CoA dehydrogenase (EC 1.3.99.2) MHDIELSEEQVMIRDMARDFARGEIAPHAQAWEKAGWIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATGAFMSIHNSVGCGPVLNYGSEEQKQTWLADLASGQVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSNGKRAKLAIVFAVTDPDLGKRGISAFLVPTDTAGFIVDRTEHKMGIRASDTCAVTLNNCTIPEANLLGERGKGLAIALSNLEGGRIGIAAQALGIARAAFEAALAYSRDRVQFGKAINEHQSIANLLADMHMQLNAARLMILHAARLRTAGKPCLSEASQAKLFASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIARELKNYLI Pseudomonas simiae WCS417 WCS417 GFF2713 PS417_13840 isobutyryl-CoA dehydrogenase (EC 1.3.8.5) Specifically important for: L-Valine. SEED annotates it as butyryl-CoA dehydrogenase, which is also expected to perform this reaction in valine catabolism acyl-CoA dehydrogenase MQDIEYTEEQVMIRDMARDFARGEIAPYAQAWEKAGWIDDALVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATGALMSIHNSVGCGPILNYGTESQKQTWLADLASGQAIGCFCLTEPQAGSEAHNLRTRAELRDGHWVITGAKQFVSNGKRAKLAIVFAITDPELGKKGISAFLVPTATPGFVVDRTEHKMGIRASDTCAVTLNQCTVPEANLLGERGKGLAIALSNLEGGRIGIAAQALGIARAAFEAALAYARDRVQFDKAIIEHQSVANLLADMQTQLNAARLLILHAARLRSAGKPCLSEASQAKLFASEMAEKVCSSAMQIHGGYGYLEDYPVERYYRDARITQIYEGTSEIQRMVIARELKHYQL Desulfovibrio vulgaris Miyazaki F Miya 8499492 DvMF_0262 Homocysteine formation from aspartate semialdehyde (NIL/ferredoxin component) Mutants in all three genes of this putative system are rescued by casamino acids or methionine but not by threonine. We propose that these three genes act together to enable the formation of homocysteine from asparate semialdehyde (the pathway proposed by Allen et al 2015 (PMID:25938369)). (auxotroph) 4Fe-4S ferredoxin iron-sulfur binding domain protein (RefSeq) MTEQQTKPYRKNIHLTFPPEISGKPIVSDLVRRYDLTVNILKAQITPRKEGYLTLEISGGEDNCLKGIAYLREQDVTVTDVSQRISRDEDSCMHCGMCTAICPTSALAMDIEARVVVFDKDRCTACGLCTRVCPVGAMNVEVENGGL Pseudomonas putida KT2440 Putida PP_5260 PP_5260 2-oxoadipate decarboxylase/hydroxylase (2-hydroxyglutarate synthase) Specifically important in carbon source L-Lysine; carbon source D-Lysine. This is part of the pathway from D-lysine to 2-oxoglutarate. For biochemical evidence that this enzyme forms 2-hydroxyglutarate, see https://doi.org/10.1101/450254 metalloprotein, putative enzyme MPANDFVSPDSIRAQFSAAMSLMYKQEVPLYGTLLELVSEINQQVMAQQPEVAEALRWTGEIERLDQERHGAIRVGTAEELATIARLFAVMGMQPVGYYDLSSAGVPVHSTAFRAVHEQSLHVSPFRVFTSLLRLELIDNPQLRELAQSILAKRQIFTSRALELIAQCEREGGLDAADAETFVQEALHTFRWHQDATVTAEQYQQLHDQHRLIADVVAFKGPHINHLTPRTLDIDAIQLGMPAKGIPPKAVVEGPPTRRHPILLRQTSFKALQETVAFRDQQGREGSHTARFGEIEQRGAALTPKGRQLYDKLLDATRVALGGAPAEANAERYMALLQANFAEFPDDLAQMREQGLAYFRYFATEKGLAARDQEGRPTTLQGLIDAGHVHFEALVYEDFLPVSAAGIFQSNLGDDAQAEYGSNANREAFEAALGLQVQDELALYAQSERRSLQACAQALNLGSM Pseudomonas putida KT2440 Putida PP_2909 PP_2909 glutarate hydroxylase Specifically important in carbon source 2-Piperidinone; carbon source 5-Aminovaleric acid. This is part of the pathway from L-lysine and 5-aminovalerate to succinate. For detailed rationale and biochemical evidence, see https://doi.org/10.1101/450254 carbon starvation induced protein MNAFTQIDELVMPLPLEPQGYTIAPSKQSPRLLELTFARETVEAFVQAVAQWPVQALEYKSFLRFRVGEILDELCQGTLRPVLLNTILDRATGGMLITPIGLDDVSQAEDMVKFTTACAHLIGRSNYDAMSGQFYARFVVVNSDNSDSYLRQPHRVMELHNDGTFVNQITDYVLMLKIDEKNMEGGNSLLLHLDDWEQCEAFFRHPLARREMRWTAPPSKKVAEDVFHSVFDTDAEGRPTMRYIDQFVQPENYEEGIWLNALSESLEGSGKKVSVPVGVGSFLLINNLFWLHGRDRFTPHEGLRRELMRQRGYVAFPKPLYQRGQ Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_11510 AO353_11510 5-aminovalerate transaminase (EC 2.6.1.48) Specifically important for utilizing L-Lysine. This confirms that it is involved in L-lysine catabolism via 5-aminovalerate. A milder phenotype on putrescine suggests that it is also likely to be a 4-aminobutyrate transaminase. 4-aminobutyrate aminotransferase MSKTNASLMKRREAAVPRGVGQIHPIFADHAKNSTVTDVEGREFIDFAGGIAVLNTGHLHPKVIAAVTEQLNKLTHTCFQVLAYEPYVELCEKINAKVPGDFAKKTLLVTTGSEAVENSIKIARAATGRAGVIAFTGAYHGRTMMTLGLTGKVVPYSAGMGLMPGGIFRALYPNELHGVSIDDSIASIERIFKNDAEPRDIAAIIIEPVQGEGGFYVAPKEFMKRLRALCDQHGILLIADEVQTGAGRTGTFFAMEQMGVAADLTTFAKSIAGGFPLAGVCGKAEYMDAIAPGGLGGTYAGSPIACAAALAVMEVFEEEHLLDRCKAVGERLVTGLKAIQAKYPVIGEVRALGAMIAVELFENGDSHKPNAAAVAKVVAKARDKGLILLSCGTYGNVLRVLVPLTAPDEQLDKGLAIMEECFSEL Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS05225 HSERO_RS05225 L-arabinolactonase (EC 3.1.1.15) Important for L-arabinose utilization, and no other good candidates for this activity were found in the genome. This gene also has other phenotypes and may act on other substrates. gluconolaconase MNVQLLVDGHHELGEGVLWCDRSQSVFWTDIHASRLWNHDPQTGLTRSWGMPERLCCYAFTADPQQLLIGLESRLAFFNLSTGTIAPICRIEDDLPSTRLNDGRCDRQGRFVFGTLNEDAGRAPIASFYRLNTDLTLERLSLPSIAISNSICFSLDGKLMYHCDSMAGKIMVCDYDTASGAVGGQRVFADVAQPGGPDGSTIDAEGYLWNAQWGGARVVRYAPDGRIDRVVAIPTSQPSCVAFGGAQFDTLYVTTAHEGMSAEQRAADPQAGALFAVALADVRGLPEVRFAG Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS05210 HSERO_RS05210 L-arabinose 1-dehydrogenase (EC 1.1.1.46) Specifically important in carbon source L-Arabinose. Similar to characterized L-arabinose 1-dehydrogenases such as B8H1Z0. 3-oxoacyl-ACP reductase MSNTPQNVQLASFPSLKGKRVFITGGGTGIGAAIVEAFAQQGAHVAFVDIATEASEALCNEVAAAGHPKPLFRHCDLRDIPAFQATIAELQAQLGDFDVLVNNAANDQRHKLEEVTLEYWNDRIAINQRPSFFAVQSVVEGMKRRGGGSIINFSSISWHQSGGGFPVYTTAKASTLGLTRGLARDLGPHKIRVNTVTPGWVMTERQIKLWLDEEGKKAIARNQCLQGDLLPWHLARMVLFLAADDSAMCTAQEFIVDAGWV Pseudomonas simiae WCS417 WCS417 GFF2133 PS417_10880 cytochrome c component of deoxyribose dehydrogenase Specifically important in carbon source 2-Deoxy-D-Ribose. This gene is in a conserved cluster with the iorAB-like subunits of deoxyribose dehydrogenase and has a similar (if weaker) fitness pattern. It is probably the electron acceptor in vivo. alcohol dehydrogenase MNNRRFARTAGWLALPCLVAAGLLAWYVTREPATPFEQEQAGATFEPALVSRGEYVARLSDCVACHSLAGKAPFAGGLEMATPLGAIHATNITPDKSTGIGTYSLADFDRAVRHGVAPGGRRLYPAMPYPSYVKLSDDDIKALYAFFMQGIKPANQPNIPSDIPWPLNMRWPIALWNGVFAPTATYAAKPDQDALWNRGAYIVQGPGHCGSCHTPRGLAFNEKALDEAGAPFLAGALLDGWYAPSLRQDPNTGLGRWSEPQIVQFLKTGRNAHAVVYGSMTEAFNNSTQFMQDDDLAAIARYLKSLPGDPQRDGAPWQYQAVAAVQDAPGAHTYATRCASCHGLDGKGQPEWMPPLAGATSALAKESASAINITLNGSQRVVASGVPDAYRMPAFREQLSDTEIAEVLSYVRSTWGNNGGAVDANAVGKLRGHTDPASSSPIILHMR Pseudomonas simiae WCS417 WCS417 GFF1425 PS417_07245 2-deoxy-D-ribonate 3-dehydrogenase Specifically important in carbon source 2-Deoxy-D-Ribose; also important for deoxyribonate utilization, so this is the second dehydrogenase in the pathway 3-ketoacyl-ACP reductase MSVLQRLQPYPGLRVLISGGAAGIGEVLAAAYLEAGAQVHVCDVSESALAVFRDKYPGTVATRADVSDAAQIEAVFKVQREHLGGLDVLVNNAGIAGPTGGIDAISDAEWQATININLTAQYRFAHHAVPMLKESSHGHLLHIASVAGRLGYAWRTPYAATKWAIVGLMKSLASELGESDIRVNALLPGIVEGPRMDGVIRARAEQVGVPEAEMRQEYLNKISLKRMVTAEDVAAMALFLCSPAARNVTGQAISVDGNVEYL Pseudomonas simiae WCS417 WCS417 GFF1429 PS417_07265 2-deoxy-D-ribonate transporter 1 Specifically important for utilization of deoxyribose and deoxyribonate. Because deoxyribose is probably oxidized in the periplasm, this is probably a deoxyribonate transporter. It belongs to the MFS superfamily, and is in conserved proximity to other deoxyribonate utilization genes. Another putative transporter (PS417_07260) is also important for utilizing deoxyribose and deoxyribonate, which is not explained. membrane protein MTTTPSARTPQALNKLMFVKLMPLLIIAYILSFLDRTNIALAKHHLDVDLGISAAAYGLGAGLFFLTYALSEIPSNLIMHKVGARFWIARIMVTWGLISAAMAFVQGETSFYVLRLLLGIAEAGLFPGVMLYLTYWFNREQRARATGYFLLGVCFANIIGGPVGAALMRMDGMLGWHGWQWMFMLEGLPAVAFAWVVWRKLPDRPSKAPWLSAEEARGIEQRIAQETEEGAGEGGHSLKNWLTPQILLAIFVYFCHQITIYTVIFFLPSIISKYGELSTMSVGLLTSLPWIAAALGALLIPRFATTPGRCRRLLVTGLLTMALGLGIASVSGPVFSLLGFCLSAVMFFVVQSIIFLYPASRLKGVALAGGLGFVNACGLLGGFVGPSVMGVIEQSTGNAMNGLKVIALVLVVAALAALRLRMGHEPERGAQASEASYT Pseudomonas simiae WCS417 WCS417 GFF1428 PS417_07260 2-deoxy-D-ribonate transporter 2 Specifically important for utilization of deoxyribose and deoxyribonate. Because deoxyribose is probably oxidized in the periplasm, this is probably a deoxyribonate transporter. It belongs to the MFS superfamily, and is in conserved proximity to other deoxyribonate utilization genes. Another MFS transporter, PS417_07265, is also important for utilizing deoxyribose and deoxyribonate, which is not explained.. MFS transporter MATIKKASLRSIHRHSWVSLLVCWMIWILNAYDREIVLRLGPTISKHFDLSADQWGTVATVVMLALALLDIPGSMWSDRYGGGWKRARFQVPLVLGYTAISFLSGFKALSGNLATFIALRVGVNLGAGWGEPVGVSNTAEWWPVERRGFALGAHHTGYPIGAMLSGIVASFVITVFGEENWRYVFYFAFVVALPLMIFWARYSTAERISALYVDIAAKGMTPPDNAPASSVKGEAWRTFVATLRNRNIALTAGNTMLTQVVYMGVNIVLPAYLYNIAGLSLAESAGMSVVFTLTGILGQLVWPSLSDIIGRRTTLIICGLWMAASVGAFYFANTLTLIVVVQLLFGLVANAVWPIYYAVACDSAEPSATSTANGIITTAMFIGGGLAPVLMGSLIAMGGGWTTLHGYTVCFFVMAGCALGGALLQLFSHRPQALVVQLDS Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_00640 H281DRAFT_00640 putative regulator of deoxyribonate oxidation Conserved next to and has similar phenotypes as the deoxyribonate oxidation cluster. It is probably a transcriptional activator. AraC-type DNA-binding protein LASTRPLLNERIYAPYKIAALVEVLAEQGIAAETSLKGSGLTVDQLNDASVMTSVRQYAVVARNAVLLSRDPATPFKVGSRLHLSAYGMYGYALMSCLSLRDYFRLGVKYHRLATPTVTIDWTEYPDKAVWSFPDAFVSSPSRELREFIIEQQFTQHVTHLQDVAGHSCPPLKACFSYPAPPHAGIYSQYLGCPCFFDAPQCELIYDSAILNQKPQLAHKLTATLLQETCDRLIGQAKTSVGTSGEVYQILMSTPGVFPGMEEVATRLNLTSRTLRRHLETEGTSFVAIVDDVRCSLAIEYLQSTRMSTEDVAMLLGFSDAANFRRALKRWTGKGPGELRR Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_00641 H281DRAFT_00641 2-deoxy-3-keto-D-ribonate cleavage enzyme Important for utilization of deoxyribose and deoxyribonate. This is expected to be the next step after the oxidation of deoxyribonate. It would release glyceryl-CoA and acetoacetate. Uncharacterized conserved protein, DUF849 family MSDTSRKVIISCAITGATHVPSMSEFLPITPEQIRDQAIEAAQAGAAIIHLHARDPVDGRPTPSPEIFKAFVPAIAEATDAVINITTGGSTRMTLEERLAYPRLARPEMCSLNMGSMNFSIHPVAAKISSWRYGWEKDYIEGMEDMIFRNTFRDIRNILLELGESGTRFEFECYDVGHLYNLAHFVDQGLVKPPFFIQSVFGILGGLGADPENMLLMRSTADRLFGRENYHFSVLGAGRHQMPLVTMSAIMGGNVRVGLEDSVYLAKGVKAETNAQQVRKIRRILEELSLEIATPADARKMLGLKGADQVNL Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_00642 H281DRAFT_00642 2-deoxy-D-ribonate transporter Important for utilization of deoxyribonate and, to some extent, deoxyribose. This may be a deoxyribose transporter as well, or, deoxyribose might be oxidized in the periplasm. Sugar phosphate permease MDTASADQRVGQLHRIATRKAMARLIPLMCAIYFMSFLDRTNVALAKLQLAADVGISAAAYGFGSGIFFLGYALLEVPSNLAAHKVGPRRWIARIAVTWGILSTAMMFVQGTSSFYVLRVLLGIAEAGLFPALMYMVTLWFAPHDRPVVVGWIYIAPALALMLGNPLGGALMQLDGFGGLHGWQWMFMLEGIPSVIVGIVLFFKMPERPRDARWLSAAERDVLETHAVIDGHGRADYSSANWIAALKRPTTVLIGLIYFLNQVAFVGLYFFTPAIIHQMHVDSSLVVGFLSASVGLGFLLGVLVLPRIHRRTDRDCVFLGILTAGLILGACAYLAVTNPAARIALLTVTAFFAGGVLPSYWAIAMKRLQGIQAAAGLAFVNTIGLIGGFVGPYLFGIAETSSGRSDAGFTVILIAGVLGLALVPVLARAMRSEAGVLASSGSAAQMKP Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_00644 H281DRAFT_00644 2-deoxy-D-ribonate 3-dehydrogenase Important for utilization of deoxyribonate and deoxyribose. Similar to the deoxyribonate dehydrogenase of P. simiae (PS417_07245). NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family MSIIDLLKPRPGLRVFVSAGAAGIGLAIAEAFIEAQAEVYICDVNQAAIDEATSRFPKLHAGIADVSKQAQVDQIIDDARRKLGGLDVLVNNAGIAGPTGAVEELDPAQWESTVSTNLNSQFYFLRKAVPVLKETSDCASIIAMSSVAGRLGYPFRTPYASTKWAIVGLVKSLAAELGPSNVRVNAILPGVVEGERMDRVISARADALGIPFNAMREEYLKKISLRRMVTVDDIAAMALFLASPAGSNVTGQAISVDGNVEYL Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_01117 H281DRAFT_01117 acetaldehyde dehydrogenase (EC 1.2.1.3) Important for utilization of deoxyribose and deoxynucleosides. The acetaldehyde would be formed by deoxyribose 5-phosphate aldolase (H281DRAFT_01118) aldehyde dehydrogenase (NAD+) MSVAEYFSSMDYGPAPEDDQPARQWLAQHEARFGHFIGGAWHAPASGAQFVSHAPASGERLADIAQGDAADIDAALAAARAAQPGWLALGGKGRARHLYALARMVQRHSRLFAVLEALDNGKPIRETRDLDVPLVARHFLHHAGWAQLQDSEFADHAPLGVIGQIVPWNFPLLMLAWKIAPAIATGNCVVLKPAEYTPLTALLFAELAHQAGLPAGVLNVVTGDGSTGAALVEHPQVDKIAFTGSTEVGKLIRSVTAGSGKSLTLELGGKSPFIVFDDADLDGAVEGVVDAIWFNQGQVCCAGSRLLVQEGIEARFIAKLKRRMETLRVGPSLDKSIDMGAIVDPVQLERIHSLVETGRREGCAIWQAADTPLPANGCFYPPTLVTNVAPASTLAQEEIFGPVLVTMSFRTPDEAIALANNSRYGLAASVWSETIGRALDVAPRLAAGVVWVNATNLFDAAVGFGGYRESGYGREGGREGIHEYLKPRAWLNLPKRQPVSAATNASDDRQVSNLALVDRTAKLFIGGKQVRPDSGYSLPVHAPDGTRVGEVGEGNRKDIRNAVQAARAAQKWSQASTHNRAQVLFYLAENLAVRADEFAHQLTVRNGATDAAAHAEVEASVTRLFTYAAWADKFDGAVHTPPLRGVALAMHEPLGVIGIACPDEAPLLAFVSLAAPALAMGNRVVVLPGEACPLAVTDFYQVVETSDVPGGVVNIVTGKREALLPALARHDDVDAVWCFGSAADATLIERESVGNLKRTFTDYGRQFDWFDRASEGLPFLRQAVQVKNIWIPYGD Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_01116 H281DRAFT_01116 deoxyribose kinase (EC 2.7.1.15) Important for utilization of deoxyribose and deoxynucleosides. Deoxynucleosides might be hydrolyzed to deoxyribose. ribokinase MSSQPQQSGRVVILGIYVTDLTFRAARMPLVGETIAGSAFAMGPGGKGSNQAVAAARAGAEVVFCTRIGNDAFGSIAQATWAREGITARASVVEGVSTGAAHIFVDDTTGMNAIIVAAGAAGTLSAADVDAIEADIAGSRVFVTQLEQPLAAARRGLEVARKHGVTTVFNPAPALPLDDDIFPLCDYITPNETEAAALTGVPIANVDDARRAADVLLAKGVGTVIVTLGEGGALLHDATQSIWLPAFRCGAVVETAGAGDGFTGGFAAALARGEDAISAMRFGCALAGISVTRAGTAPSMPTLAEVNRVLSESAQPAQAS Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_01115 H281DRAFT_01115 deoxynucleoside transporter, permease component 1 Important for utilization of dAMP and deoxyinosine. Because the fitness profiles for these compounds are very similar, dAMP is likely hydrolyzed before uptake, but this could also be a transporter for deoxynucleotides. monosaccharide ABC transporter membrane protein, CUT2 family MKSSFAAGKLFADRQLNFLLIVNVLVVLVATWLSRGQFVDIDNLQSMGGQLPELGLLALGIMLSMVSGNGGIDLSGVGLANLSGMVAAMLVPRLVNGDDSPVLYTSLFCAIVLMMGLLGGLLNGVVIARLRLTPILCTLGTQLLFTGFAVVISNGASVHVDYVEPLSDIGNGTVLQVPIAFCIFLAAVIVLGWLLKRSPFGLRLYLMGTNPKAAFYAGIPRARMLITTYAMCGVLASLAGLISATHTSSAKWDYGNSYLLIAILIAVMGGVNPAGGHGRIICVFFAATVLQFLSSLFNLLGVSQFFGDCAWGFLLLLSLAFAGGERVRAIFGLGGGGGSTQPAKPPASGSAGATQRR Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_01114 H281DRAFT_01114 deoxynucleoside transporter, substrate-binding component Important for utilization of dAMP and deoxyinosine. Because the fitness profiles for these compounds are very similar, dAMP is likely hydrolyzed before uptake, but this could also be a transporter for deoxynucleotides. monosaccharide ABC transporter substrate-binding protein, CUT2 family MKLTRLGAALAAAALTVGVIAAAQAATNETIVTVVKVTGINWFNRMDEGVKEFAKDNPGVTAYQTGPGRADAAQQLKIIEDLIAKKVNAIAVVPYDPPTLEPALKKAMDRGIKVVTHEADNAKNTMVDIEAFDNTAYGAGLNERLASCMHNEGKWAVLVGSLGSRSQVQWADGGIGNAKAKYAKMNLVEPKLETNNDGERAYEVAKEVLRKHPDLKGFQGSSSLDVIGIGRAVEEAGMQGKICVYGTGLPTEAGKFLESGAINGIAFWDPKLAGIAMNKVAKMLVDGKTVENGADLGIPGYTKVTVAKGPGKGIIVRGQGWVNVDKSNYKQYPF Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_01113 H281DRAFT_01113 deoxynucleoside transporter, ATPase component No fitness data for this gene; it was reannotated based on the mutant phenotypes of its neighbors. monosaccharide ABC transporter ATP-binding protein, CUT2 family MNQQEVSSAPLSQPFLEVVGVHKRFTGVHALRGVSLSFQRGQIYHLLGENGCGKSTLIKIISGAQPPDEGQLVIEGVPHARLSALEALAAGIETVYQDLSLLPNMSVAENVALTSELATHEGRLARTFDRRVLAATAARALEAVGLPGNSEFQSTLIEQLPLATRQLVAIARAIASEAKFVIMDEPTTSLTQKEVDNLIAVLANLRAQGVTVLFVSHKLDECYAIGGEVIVLRDGQKMAQGPIAEFTKAQISELMTGRHLSNERYRESAHAQDIVLDVRGFTRAGQFSDVSFKLHGGEILGVTGLLDSGRNELARALAGVAPAQSGDVLLDGQQIALRTPSDAKRHRIGYVPEDRLNEGLFLDKPIRDNVITAMISSLRDRFGQIDRTRAQALAEQTVKELQIATPGVDKPVQSLSGGNQQRVLIGRWLAIDPRVLILHGPTVGVDVGSKDIIYRIMQRLSQRGIGIILISDDLPELLQNCDRILMMKKGHVSAEYRADELSEADLYHALLSEAA Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_01112 H281DRAFT_01112 deoxynucleoside transporter, permease component 2 Important for utilization of dAMP and deoxyinosine. Because the fitness profiles for these compounds are very similar, dAMP is likely hydrolyzed before uptake, but this could also be a transporter for deoxynucleotides. monosaccharide ABC transporter membrane protein, CUT2 family MNSRIPSRTDPRTDPPSASPMKQTMTTPTVVEIAPSVEAPGLRTRLARNPEWFTVALIVVTCLIVGAINPRFFQFATLFDLLHSATTMSLFALGTLVVLASGGIDVSFTAIAALTMYGITKAVFAWWPDAPFALILVTGALGGVVLGMVNGLLVHRLKAPSLIVTIGTQYLYRGLLLTFIGTTFFMNIPHSMDRFGRIPLFFYHTADGLRAVLPVSVLALVAAAVVTWWLLNRTMMGRAVYAMGGSLAIAERLGYNLRAIHLFVFGYTGMLAGIAGILHVSNNRLANPFDLVGSELDVIAAVILGGARITGGTGTVVGTLLGVVLVTLIKSVLILVGVPSTWQKVIIGAFILLAGTLFALQRKR Burkholderia phytofirmans PsJN BFirm BPHYT_RS04765 BPHYT_RS04765 2-deoxy-D-ribonate transporter Important for the utilization of deoxyribonate. Similar to the putative deoxyribonate transporter in several other bacteria. major facilitator transporter MTTQSAGPAGNALHRIATHKAMLRLIPLMCVIYFMSYLDRTNVSLAKARLATDLGISAAAYGLGAGIFFIGYALLEVPSNLVAHRVGPRRWIARIAITWGALSASMMFVQGEWSFYAIRVLLGIAEAGLFPALMYMVTMWFAPQDRSVAVGWIYTAPALALVIGNPLGGAFMQMDGLGGLHGWQWLFLLEGLPTIFVGVLLWFKLPEKPSDARWLSADEARALEARAVPDAAHPGMFSQDWVAALKRPATVLIGLIYFLNQVAFVGLVFFTPAMIQQMHVKSPLMIGVLSSSVGIGFLLGVLVLPRIHRRVTNDCLYLGVLTLGLVTSAILFMSTSVLSTQLLLFVATAFFAGGVLPLYWAIAMKRLHGIQAAAGLAFINTIGLIGGFVGPYLFGLAESASGHSASGFSVVVGASVLGLVLVPLLAKAIQSEGRAASLAEPLLNTES Burkholderia phytofirmans PsJN BFirm BPHYT_RS04775 BPHYT_RS04775 2-deoxy-D-ribonate 3-dehydrogenase Important for deoxyribonate utilization. Similar to the deoxyribonate dehydrogenase of P. simiae (PS417_07245) 3-ketoacyl-ACP reductase MKTIDLLRPTPGLRVLISGAAAGIGAAIAQAFLDVGANVYICDVDPAAIDRARTAHPQLHAGVADVSDCAQVDRIIDDARSKLGGLDLLINNAGIAGPTGAVEDLDPAEWERTIGTNLNSQFYFLRKAVPLLKETSANPGIIAMASVAGRLGYAFRTPYAASKWAIVGMVKSLAIELGPNNVRVNAILPGVVEGERMDRVISARAESLGIGFDQMKGEYLQKISLRRMVTVHDVAAMALFLASPAGQNISGQAISVDGNVEYL Burkholderia phytofirmans PsJN BFirm BPHYT_RS25810 BPHYT_RS25810 acetaldehyde dehydrogenase (EC 1.2.1.3) Specifically important in carbon source 2-Deoxy-D-Ribose. Acetaldehyde is expected to be produced by the deoxyribose 5-phosphate aldolase. aldehyde dehydrogenase MSVAEYFSSMEYGPAPEDDQPARAWLAQHEDGFGHFIGGAWHAPAAGERFASNAPATGEQLAQVAQGDAADIDAAVAAARAAQPGWLALGGAGRARHLYALARMVQRHSRLFAVLEALDNGKPIRETRDIDVPLVARHFLHHAGWAQLQESEFADYAPLGVVGQIVPWNFPLLMLAWKIAPAIATGNCVVLKPAEYTPLTALLFAELAHRAGLPAGVLNVVTGDGRTGAALVEHPQVDKIAFTGSTEVGRLIRSATAGSGKSLTLELGGKSPFIVFDDADLDGAVEGVVDAIWFNQGQVCCAGSRLLVQEGIEARFIAKLKRRMETLRVGTSLDKSIDLGAIVDPVQLERIQSLVETGRREGCSVWQSPDTTIPSGGCFFPPTLVTGVAPASTLAQEEIFGPVLVTMSFRTPDEAIALANNSRYGLAASVWSETIGRALDVAPRLASGVVWINATNLFDAAVGFGGYRESGYGREGGREGIYEYLKPRAWLKLAERRAAQDVVRDAAALDPLSNVTSIDRTAKLFIGGKQARPDSGYSLPVLAPDGTPVGEVAAGNRKDIRNAVEAARAAQKWSQASTHNRAQVLFYLAENLAVRADEFVRQLVVRNGATEAAARAEVDASVQRLFTYAAWADKFDGAVHTPPLRGVALAMHEPLGVIGIACPDEAPLLGFVSLAAPALAMGNRVVVLPSEASPLTVTDFYQVAETSDVPGGVLNIVTGERGALLPALVKHDDVDAVWCFGSAADSTLVERESVGNLKRTFVDYGRQFDWFDRASEGRPFLRQAVQVKNIWIPYGD Burkholderia phytofirmans PsJN BFirm BPHYT_RS25805 BPHYT_RS25805 deoxyribose kinase (EC 2.7.1.15) Specifically important in carbon source 2-Deoxy-D-Ribose ribokinase MNTPAQLNGKGRVVILGIYVTDLTFRAGRMPQIGETIAGTAFAMGPGGKGSNQAVAAARVGADVVFCTRIGNDAFGSIARATWAAEGITARASVIDGVSTGAAHIFVDDNTGMNAIIVASGAAGTMEAADVDAIEADIAAARVFVTQLEQPLAAARRGLEVARKHGVITVFNPAPAMPLDDAIFPLCDYITPNETEATALTGVPIANADDARRAADVLLAKGVGTAIITLGEGGALLHSANQSLLVPAYHCGRVVETAGAGDGFTGGFAAALARGDDAITALRFGCALAGISVTRPGTAPSMPTLDEVNQVLNQPSQPNQAAGVSQPS Klebsiella michiganensis M5al Koxy BWI76_RS21985 BWI76_RS21985 acetaldehyde dehydrogenase (EC 1.2.1.3) Specifically important for utilizing deoxynucleotides/deoxnucleosides (dAMP, dC), D-lactate, and succinate. Deoxynucleosides are metabolized via deoxyribose 5-phosphate aldolase which produces acetaldehyde. It is not obvious what aldehyde would be an intermediate in lactate or succinate catabolism. aldehyde dehydrogenase MRYAHPGTPGALVALKSAYGNFIDGKFVEPIGGEFFMNTSPVDGSNIGQFPRSDAKDIDFALDAAHRAADAWGKTSAQHRANLLLQVADRIEANLEYLAVAESWDNGKPIRETLNADLPLAVDHFRYFAGCLRAQEGSTAEIDETTVAYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTPLSITLLLEIIGDLFPAGVLNVVQGFGKEAGEALATSKRIAKIAFTGSTPVGRHIMACAAENIIPCTVELGGKSPNIYFADVMEGEEEYIEKAVEGLVLGFFNQGEVCTCPSRALIQESIYEPFMARVMDKVAQIRRGDPFDTDTMIGAQASRQQFDKILSYIKIARDEGGKILTGGERASISAELDNGFYIQPTLIQGRNDMRSFQEEIFGPVIGVTTFKDEAEALSIANQTQFGLGAGVWTRDTNLAYRMGRGIKAGRVWTNCYHIYPAHAAFGGYKQSGVGRETHKMALNAYQQTKNLLVSYGTAPLGLF Klebsiella michiganensis M5al Koxy BWI76_RS23695 BWI76_RS23695 deoxyribonyl-CoA synthetase Specifically important in carbon source 2-Deoxy-D-ribonic acid lithium salt. K. michiganensis appears to metabolize deoxyribonate via acyl-CoA intermediates. putative acyl-CoA synthase MSSTSADFQNLYQALSRSAARSPDALALAFEDRRYLYRDFHLRVQRAMAQLDRIWSLRKGDRILLAWGNHPAFCEVLFAALGLGIEVVPFSTKLKQAESEELVGHIAPRAVLFDATVQDWLKQTPDALCVSLSEWQALSLPDPLTRLPTPVNRDDTAVMMFTSGTTGEPKGAIITHHNLLCAIDAYAQKLNLTAADSTILAVPIYHITGLSALLALFISLGASLWLQHRFNAPQVINTLREQNITFLHGSPTIFILLCQAAREQSASHPGDFPALRTIACGAGHLSDGLIAELKTLFPHTAIQPIYGLTETTSPATIFPGDVWGSDKCGSSGQAIPGLAIAIRNDRQQPLPAGQIGHIWLKGDVVIREYWQHSERRPSCDAQGWFCTGDLGYLDDEGWLYIKDRSKDMINRGGEKIYSLELENILSTYRGVREVAVIPTPSPVYGEEPVAFIVPDGQHHLTSEEILGWLKVKIARFKLPARIIFTRVLPRTHNGKVSKQQLKARLAESIITLSTEDKK Klebsiella michiganensis M5al Koxy BWI76_RS23700 BWI76_RS23700 glycerate CoA-transferase Specifically important in carbon source 2-Deoxy-D-ribonic acid lithium salt. After oxidization and cleavage to glyceryl-CoA, this enzyme would form glycerate. This protein is 42% identical to a propionate CoA-transferase (Q9L3F7) that uses propionyl-CoA and acetate as substrates, so it is likely that acetate is the CoA-acceptor. acetyl-CoA--acetoacetyl-CoA transferase subunit alpha/beta MSSKFIDAHQAAQWVASGDTVCTVGMTLIGAAESILSAIEARFLTAGEPRDLTLLHAAGQSDRQRGIQHFAHPGMVTRLIGSHWGLAPRWMAMINNNEVEAWCLPQGQIVHLYSAMAAGLAGRLSPVGLGTFVDPRMEGGRMNARTRERPDLIEHVTFRGAEYLFYPAIPLDVVIVRGTHADEDGNLTTDEEVMKLEVLHAVLAARRYGAKVLAQVKYRVAKGSLHPKSVTVPGNLIDAIVVCEEPQMDHRQTSSWDFDPALCGDIQLPAAQSAPLPLDLRKLIGRIACRYLTPGCVINLGTGIPNDVIGAIIHEERLGEQVTITVESGIYGGQQAGGVDFGIGRNLSAMIGHQDQMLYYNGAGVDITFMGAGEMDPHGHVNATRLGASCPGAGGFIDITQNARHVVFCSSFTAKGLEIACEQGALHIRREGEVRKFVAGVNQISYNGELARAKGQTMHYVTERAVFELRPEGPVLTEIAPGIDLERDILAHMDFRPTIAADLQVMDSRLFTPQPCGLAEHLSRNSSSDSQGN Klebsiella michiganensis M5al Koxy BWI76_RS23705 BWI76_RS23705 2-deoxy-D-ribonyl-CoA 3-dehydrogenase Important for deoxyribonate utilization. Although the closest characterized homolog is a 3-oxoacyl-CoA reductase (fabG or P0A0H9), an ACP-attached substrate is normally part of biosynthesis, which is difficult to reconcile with this gene's mutant phenotype or its presence in the deoxyribonate utilization cluster. 3-oxoacyl-ACP reductase MKLASKTAIVTGAARGIGFGIAQVLAREGARVIIADRDAHGEAAAASLRESGAQALFISCNIGDKAQVEALFSQAEEAFGAVDIVVNNAGINRDAMLHKLSEADWDTVIDVNLKGTFLCMQQAAIRMRERGAGRIINIASASWLGNVGQTNYSASKAGVVGMTKTACRELAKKGVTVNAICPGFIDTDMTRGVPENVWQIMINKIPAGYAGEAKDVGECVAFLASDGARYINGEVINVGGGMVL Klebsiella michiganensis M5al Koxy BWI76_RS23710 BWI76_RS23710 3-keto-2-deoxy-D-ribonyl-CoA thiolase Specifically important in carbon source 2-Deoxy-D-ribonic acid lithium salt. This gene would form glyceryl-CoA and acetyl-CoA. acetyl-CoA acetyltransferase MTQANDIVVVSGVRTAIGTFNGSLKHTHQHDLGAAVIREAVNRAGLAPQDIDETIVGNVGQIAESGFIARICQLRAGIPQESTAYSVNRQCGSGLQALADGMMQLQSGQAEVVVACGTENMTQLPYYLRKARDGYRMGHGELEDGLISILTWPEGPYHNGITAENVAQRFGITREAMDDFAWSSQQKALKAIAEERFREQILALEVPDGKKATRLFATDEHPRDTPREKLAALRPAFKADGVVTAANSSGINDGAAALVMMTRQQAEKRGLTPRMRIRGWAVAGCGAEIMGFGPSPATRRLMDRLNMDVHAIDLIELNEAFAAQALAVMNDLRLDPARVNVNGGAIALGHPVGASGAILPVKLMYEMARSGARTGLVTMCIGGGQGISMLFEREGA Klebsiella michiganensis M5al Koxy BWI76_RS23715 BWI76_RS23715 2-deoxy-D-ribonate transporter 1 Specifically important in carbon source 2-Deoxy-D-ribonic acid lithium salt. Similar to deoxyribonate transporters in other bacteria. However it is not clear why this organism has two deoxyribonate transporters (this gene and BWI76_RS23725) MFS transporter MSAINEKAVNGTQLQRTHKKIYRHLMPLLIVAYIISFIDRTNIGMAKATMSVDIGLSATAFGLGAGLFFLTYAVLEIPSNLFLTRIGARRWIARIMITWGIISCGMAFVTGPTSFYVMRLLLGAAEAGLYPGIIYYLTLWFGREERAKATGLFLLGVCLANIIGAPLGGLLLSLDGMSGWHGWQWMFFIEGLPAIALAFVVWRRLPDKPADARWLDSHDVQAITAVLEKEAEETRHTPSRFSLKTALTTRVFLLLVLIYFTHQFSVYGLSYFLPGIIGSWGQLTPLQIGLLTAIPWIAAAAGGILLPRFARTEQRSRSMLMAGYLVMATGMAIGAIAGHGVALLGFSLAAFMFFAMQSIIFNWLPSIMSGHMLAGSFGLLNCLGLCGGFLGPFILGAFEDRTGAATSGLWFAVALLIVGALASLLIKSSSSSTPASAKQARGENA Klebsiella michiganensis M5al Koxy BWI76_RS23725 BWI76_RS23725 2-deoxy-D-ribonate transporter 2 Important in carbon source 2-Deoxy-D-ribonic acid lithium salt. Similar to deoxyribonate transporters in other bacteria. However it is not clear why this organism has two deoxyribonate transporters (this gene and BWI76_RS23715) MFS transporter MTTINQTPAGEQGAKKRLIHRFSWVSLLVCWLIWVLNAYDREMILRLGPVISKEFSLSPEQWGNVVALIMVALAVLDIPGSIWSDRYGSGWKRARFQVPLVLGYTALSFISGIKAISHGLTAFVLLRVGVNLGAGWGEPVGVSNTAEWWPKEKRGFALGVHHTGYPIGALLSGVVASLVLSAFGEGSWRYCFLLALIVAIPLMIFWAKYSTADRINTLYQHIDSQGMTRPATQESSHVAKGEGMKTFLRTLRNRNISLTAGNTLLTQIVYMGINVVLPPYLYHVSGLSLAASAGLSIIFTLTGTLGQIIWPWLSDSFGRKRTLIVCGLWMSIGIALFYFATNMPRLIAIQLFFGLVANAVWPIYYAMASDSAEERATSTANGIITTAMFIGGGLSPLLMGWLIQFGGGWENPAGYIYAFFTMAGCALLGMLLQLMTTDKTPRKAH Pseudomonas putida KT2440 Putida PP_3621 PP_3621 vanillin dehydrogenase, iorA-like component Specifically important in carbon source Vanillin. This gene cluster is probably the major vanillin dehydrogenase in P. putida. This system is expected to use a molybdopterin cofactor, which explains why molybdate uptake is required for growth on vanillin (PMID:24136472). isoquinoline 1-oxidoreductase subunit alpha MELRINQKTYQVEADADTPLLWVIRDDLGLTGTKYGCGLAQCGACSVLVDGNVVRACVTPVAGVVGREVTTIEAIEADPVGKRVVAAWVEHQVAQCGYCQSGQVMAATALLKHTPKPSDAQIDAAMVNLCRCGTYNAIHAAVHDLAQGEQA Pseudomonas putida KT2440 Putida PP_3622 PP_3622 vanillin dehydrogenase, iorB-like component Specifically important in carbon source Vanillin. This gene cluster is probably the major vanillin dehydrogenase in P. putida. This system is expected to use a molybdopterin cofactor, which explains why molybdate uptake is required for growth on vanillin (PMID:24136472). putative Isoquinoline 1-oxidoreductase, beta subunit MNTPVDTPAELLRLQRGETVNLSRRRFLAGTAVGALVLGFGLPMGSARVQAAAAAAATAERGTQVPAFLEIRPDGTVRLLSPFMEGGQGPFTAMAQIVGEELDVDPAHFVVDSAPPGEAYVVMENGMRITGGSMSVRMSYPTMRRLGALARGMLLQAGAEHLGVPVDELSTTPGNVVHTTTGRSVPYGELAGRAMDLPVPDPASVKLRDPSQFRWIGKPVRRLDAYDKSTGKAQYCIDIKVDGMLHAAVQHAPRLGMTVGSLRNEDQIKAMKGVHSVHQLPGAVAVVAERWWHAKRAVEAIQVDWKEPAADSKVRPMPADFSSDAWREHLATVQGPSRDEENEGDIAGALANAKTKVEASYHNQYLNHAQLEPPSALARFNPDGSLDVWLPNQAPDMFRDDIARRTGLEPAQINLHSPLLGGFFGRHFLYDSANPYPQAIALAKAVGRPVKLIWSREEEFLRDVLRPVAVVKFRAGLDADGMPVALEAVSATEGPTEALAGKQGEKIDPTALEGLSGKSYAIANKRIAQIYVKGPAMLGYWRSVGNSLNDFFYESFLDELADKGGKDPFELRLHLLRDNPRLTNLLNAVADLSGGWKRGPFTAEDGSKRARGVAMASPFGSEAAVIAEVSIDNGQVRVHDIWQAIDPGSIVNPAIIEHQVNGAVALGLSQTLVEEAVYVDGKPRARNYDLYPILPPSRMARVHVRIIESGAKMGGIGEPPLPAVAPAVANAVAQLTGQRVRSLPLSRHTFS Pseudomonas putida KT2440 Putida PP_3623 PP_3623 vanillin dehydrogenase, cytochrome c component Specifically important in carbon source Vanillin. This gene cluster is probably the major vanillin dehydrogenase in P. putida. This system is expected to use a molybdopterin cofactor, which explains why molybdate uptake is required for growth on vanillin (PMID:24136472). Alcohol dehydrogenase cytochrome c subunit MTHRFARTAGWLALPCLVAAGLLAWYVTREPASPFADAQATAADPALVSRGEYVARLSDCVACHSLPGGKPFAGGLEMATPLGAIHATNITPDRDSGIGNYTLADFDRAVRQGVAPGGRRLYPAMPYPSYAKLSDDDVKALYAFFMHGVQPARQANLGSDIPWPLNLRWPIALWNGLFAATTPYTDKAGQDAQWNRGAYIVQGPGHCGSCHTPRGLAFNEKALDDSGKPFLSGALLDGWYAPSLRADHNTGLGRWSEAEIAQFLKTGRNRHAVVYGSMTEAFNNSTQFMHDDDLAAIAHYLKSLPGDPQRDGAPWHYQAESLATRLDSPGARTYVTRCASCHGLDGKGQAEWMPPLAGATSALAKESASAINITLNGSQRVVAAGVPDAYRMPALREQLSDQEIADVLSFVRTAWGNQGGAVDAQAVGKLRGHTDPASSSPIILHMR Pseudomonas putida KT2440 Putida PP_3356 PP_3356 p-coumarate CoA-ligase (EC 6.2.1.12) Specifically important in carbon source p-Coumaric acid. This is the first step in its catabolism. feruloyl-CoA-synthetase MNNEARSGSTDPGQRPRYRQVAIGHPQVQVSHVDDVLRMQPVEPLAPLPARLLERLVHWAQVRPDTTFIAARQADGAWRSISYVQMLADVRTIAANLLGLGLSAERPLALLSGNDIEHLQIALGAMYAGIAYCPVSPAYALLSQDFAKLRHVCEVLTPGVVFVSDSQPFQRAFEAVLDDSVGVISVRGQVAGRPHISFDSLLQPGDLAAADAAFAATGPDTIAKFLFTSGSTKLPKAVITTQRMLCANQQMLLQTFPTFAEEPPVLVDWLPWNHTFGGSHNLGIVLYNGGSFYLDAGKPTPQGFAETLRNLREISPTAYLTVPKGWEELVKALEQDPALREVFFARIKLFFFAAAGLSQSVWDRLDRIAEQHCGERIRMMAGLGMTEASPSCTFTTGPLSMAGYVGLPAPGCEVKLVPVGDKLEARFRGPHIMPGYWRSPQQTAEAFDEEGFYCSGDALKLADARQPELGLMFDGRIAEDFKLSSGVFVSVGPLRNRAVLEGSPYVQDIVVTAPDRECLGLLVFPRLPECRRLAGLAEDASDARVLANDTVRSWFADWLERLNRDAQGNASRIEWLSLLAEPPSIDAGEITDKGSINQRAVLQRRAAQVEALYRGEDPDALHAKVRP Pseudomonas putida KT2440 Putida PP_3357 PP_3357 p-hydroxybenzaldehyde dehydrogenase vdh (EC 1.2.1.64) Specifically important in carbon source p-Coumaric acid. This gene is known as vdh and has vanillin dehydrogenase activity, but it is not required for growth on vanillin (PMID:25026441). Instead, its primary substrate in vivo seems to be p-hydroxybenzaldehyde (which is the product of hydroxycinnamoyl-CoA hydratase-lyase) vanillin dehydrogenase MLQVPLLIGGQSRPASDGRTFERCNPVTGEVVSQAAAATLADADAAVAAASAAFPAWAALAPGERRSRLLAGADLLQARAAEFIAAAGETGAMANWYGFNVKLAANMLREAAAMTTQITGEVIPSDVPGSFAMALRAPCGVVLGIAPWNAPVILATRAIAMPLACGNTVVLKASELSPAVHRLIGQVLHDAGIGDGVVNVISNAPQDAPAIVERLIANPAVRRVNFTGSTHVGRIVGELAARHLKPALLELGGKAPLLVLDDADLDATVEAAAFGAYFNQGQICMSTERLVVDSCIADAFVDKLAVKIAGLRAGDPQASTSVLGSLVSAAAGERIKALIDDAVAKGARLVSGGQLEGSILQPTLLDNVDASMRLYREESFGPVAVVLRAEGDEALLQLANDSEFGLSSAIFSRDTSRALALAQRVESGICHINGPTVHDEAQMPFGGVKSSGYGSFGSRTAIDQFTQLRWVTLQHGPRHYPI Pseudomonas putida KT2440 Putida PP_4108 PP_4108 2-aminoadipate transaminase (EC 2.6.1.39) Specifically important in carbon source D-Lysine. D-lysine. This is part of the pathway from D-lysine to 2-oxoglutarate. For detailed rationale and biochemical evidence, see https://doi.org/10.1101/450254 putative 4-aminobutyrate aminotransferase MNQESISQSIAIVHPITLSHGRNAEVWDTDGKRYIDFVGGIGVLNLGHCNPAVVEAIQAQATRLTHYAFNAAPHGPYLALMEQLSQFVPVSYPLAGMLTNSGAEAAENALKVARGATGKRAIIAFDGGFHGRTLATLNLNGKVAPYKQRVGELPGPVYHLPYPSADTGVTCEQALKAMDRLFSVELAVEDVAAFIFEPVQGEGGFLALDPAFAQALRRFCDERGILIIIDEIQSGFGRTGQRFAFPRLGIEPDLLLLAKSIAGGMPLGAVVGRKELMAALPKGGLGGTYSGNPISCAAALASLAQMTDENLATWGERQEQAIVSRYERWKASGLSPYIGRLTGVGAMRGIEFANADGSPAPAQLAKVMEAARARGLLLMPSGKARHIIRLLAPLTIEAEVLEEGLDILEQCLAELN Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_25685 AO353_25685 acetyl-CoA:acetyl-CoA C-acetyltransferase / acetyl-CoA:propanoyl-CoA 2-C-acetyltransferase (EC 2.3.1.9; EC 2.3.1.16) Specifically important for: Sodium butyrate; L-Isoleucine. Degradation of acetoacetyl-CoA (EC 2.3.1.9) is consistent with a role in butyrate degradation. The role in Ile degradation suggests that 2-methylacetoacetyl-CoA is also a substrate (conversion to propionyl-CoA + acetyl-CoA). Hence the broader EC # 2.3.1.16. acetyl-CoA acetyltransferase MTMSHDPIVIVSAVRTPMGGFQGELKSLSAPQLGAAAIRAAVERAGVAADAVEEVLFGCVLSAGLGQAPARQAALGAGLDKSTRCTTLNKMCGSGMEAAILAHDMLLAGSADVVVAGGMESMSNAPYLLDRARSGYRMGHGKVLDHMFLDGLEDAYDKGRLMGTFAEDCAEANGFTREAQDEFAIASTTRAQQAIKDGSFNAEIVPLQVIVGKEQKLITDDEQPPKAKLDKIASLKPAFRDGGTVTAANSSSISDGAAALLLMRRSEAEKRGLKPLAVIHGHAAFADTPGLFPVAPVGAIKKLLKKTGWSLDEVELFEVNEAFAVVSLVTMTKLEIPHSKVNVHGGACALGHPIGASGARILVTLLSALRQKGLKRGVAAICIGGGEATAMAVECLY Phaeobacter inhibens BS107 Phaeo GFF329 PGA1_c03400 acetyl-CoA:acetyl-CoA C-acetyltransferase / acetyl-CoA:propanoyl-CoA 2-C-acetyltransferase (EC 2.3.1.9; EC 2.3.1.16) Specifically important for utilizing Potassium acetate amd threonine. EC 2.3.1.9 (acetoacetyl-CoA) was linked to acetate via a SEED subsystem. The phenotype on threonine suggests that propanyl-CoA is also a substrate, hence the broader EC # 2.3.1.16. acetyl-CoA acetyltransferase PhaA MTNVVIASAARTAVGSFGGAFAKTPAHDLGAAVLQAVVERAGIDKSEVSETILGQVLTAAQGQNPARQAHINAGLPQESAAWSLNQVCGSGLRAVALAAQHIQLGDAAIVCAGGQENMTLSPHAANLRAGHKMGDMSYIDTMIRDGLWDAFNGYHMGQTAENVAEKWQISREMQDEFAVASQNKAEAAQKAGKFADEIAAFTVKTRKGDIIVDQDEYIRHGATIEAMQKLRPAFAKDGSVTAANASGLNDGAAATLLMSADDAEKRGIEPLARIASYATAGLDPSIMGVGPIYASRKALEKAGWSVDDLDLVEANEAFAAQACAVNKDMGWDPAIVNVNGGAIAIGHPIGASGCRVLNTLLFEMKRRDAKKGLATLCIGGGMGVAMCVERP Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_2711 Ga0059261_2711 homoserine dehydrogenase (EC 1.1.1.3) Divergent from characterized homoserine dehydrogenases but has the expected phenotype: important for fitness in the absence of amino acids and is most cofit with homoserine O-acetyltransferase Ga0059261_2301 homoserine dehydrogenase (EC 1.1.1.3) MTEPLRVALAGLGTVGAGVIRLIDANAELIARRAGRPIEIVAVSARDRAKDRGVDITRFDWVDDMTELARHPKADVVVELIGGSDGPALALARATLAAGKGLVTANKAMIAHHGLELAQVAEKSDTPMKFEAAVAGGVPVIKGLREGAAANQIDRVYGILNGTCNFILSKMEAEGRDFGEVLAEAQAAGFAEADPSFDIDGVDAAHKLSILASIAFGTQPAFGDVAIGGIRHLLAADIAEAAALGYRIRLLGIADLSGNGLFQRVHPHLVPLSHPLAHVLGPTNAVVAEGNFVGRLLFQGAGAGDGPTASAVVADLIDIARTEFGPPYAMPATSLAAEPVAPTGERRGRAYLRFTVADKVGVLAEIAAAMRDAGVSIESLIQRGAMADGSVLVAIVTHEVPERSIAQALEKLRGSPSLAGEPMWMHILGE Bacteroides thetaiotaomicron VPI-5482 Btheta 350116 BT0588 BexA: efflux pump for ciprofloxacin, lomefloxacin, and paraquat Specifically important in stress Paraquat dichloride; stress Lomefloxacin hydrochloride; and potentially important during growth in ciprofloxacin, which is reported to be a substrate of this efflux pump (PMCID:PMC90835), along with norfloxacin and ethidium bromide. BexA, multidrug efflux pump (NCBI ptt file) MKTKYTYKQIWTIAYPILISLIMEQLIGMTDTAFLGRVGEIELGASAIAGVYYLAIFMMAFGFSVGAQILIARRNGEGNYKEIGPIFYQGIYFLVVVAAILFTLSIVFSPFILKNIISSPHIYDAAESYIHWRVYGFFFSFVGVMFRAFFVGTTQTKTLTLNSIVMVLSNVVFNYILIFGKFGFPQLGIAGAAIGSSLAELVSVIFFIIYTWKRIDCKKYALNILPKFQSRTLKRILNVSVWTMIQNFVSLSTWFMFFLFVEHLGERSLAIANIIRNVSGIPFMIAMAFAATCGSLVSNLIGAGEKDCVRGTINQHIRIGYVFVLPILIFFCLFPDLILRIYTDMPDLRDASIPSLWVLCAAYVVLVPANVYFQSVSGTGNTRTALAMELCVLTIYVAYATYFILYLKMDIAFAWTTESVYGIFIFLFCYWYMKKGNWQKKQI Bacteroides thetaiotaomicron VPI-5482 Btheta 350646 BT1118 outer membrane binding protein for D-galacturonate and 1,4-beta-D-galactobiose (SusD-like) Specifically important in carbon source D-Galacturonic Acid monohydrate and carbon source 1,4-B-D-Galactobiose along with the adjacent SusC-like protein (BT1119). This is a SusD-like protein that is probably on the outer membrane and binds the substrates. putative outer membrane protein, probably involved in nutrient binding (NCBI ptt file) MVALATMMTSCLTEDPRDQLYEEDIYNNANNIYINAVAVLYNYIGGSADSEGLQGTCRGIYDYNTLTTDEAMIPIRGGDWYDGGLWTNMYQHKWSPNDLPLYNTWKYLYKVVVLSNKSLHIIDKYSHNLSEEQRVAYEAEVRALRALFYYYIMDMYGRVPIVTSYEQPQDEVVQSERSEVFRFIVNELQEVAELLPNERSNKMGNYYGRITTPVANFLLAKLALNAEIYCDDNWTDGVPRNGKEIFFTVDGEKLNAWQTCIKYCNKLAEVGYRLEDDYSYNFSVHNENSNENIFTIPLDKNLYAAQFWYLFRSRHYNHGGALGGSSENGTSANISTVLANGYGTDDVDARFEKNFYAGIVEVDGKPVMMDNGQQLEYFPLELKLNLTGSSYVKTAGARMAKYEVDRTSHSDGRQPDNDIVLFRYADALLMKSEAKVRNGEDGSLELNEVRGRVGMPYREATLENILKERLLELVWEGWRRQDMVRFGVYHKSYDQRVQLADEKNGYTTVFPIPQKSIDLNPKLKQNVGYK Bacteroides thetaiotaomicron VPI-5482 Btheta 350647 BT1119 TonB-dependent receptor for D-galacturonate and 1,4-beta-D-galactobiose (SusC-like) Specifically important in carbon source D-Galacturonic Acid monohydrate and perhaps 1,4-beta-D-galactobiose, along with the adjacent SusD-like protein (BT1118). This is a SusC-like protein that is probably a TonB-dependent receptor for uptake through the outer membrane. putative outer membrane protein, probably involved in nutrient binding (NCBI ptt file) MGRVSLCLVIMFFICSAQKIDAQVQNIREKQDTISATKSLEHIRPENIKKGPLNNALDVLSGQSAGVNVTTNGTDRLAMLNSIRVRGTTSIMGGNDPLVIIDGVTSDIATLSTIYPADIESFTILKNATETAMYGSRGASGVIEIKTKKGTGRGFEISYDGNYGFESMYKHLQMLNGPEYIATAEALGLDYNNGGYNTNFHDVITRTGLIHQHHLAFSGGSENSNYRASFGFMDHNTIVKVNDYRNLVVKLDATQKAFDGRLVGDFGVYGYSSKIHDIFDTRMLFYSAAAQNPTYPAGTDVNGNWVKNSAASHINHPGALLYEKNDSEERNFNTHLGLKFNILDNLILSAFGSYSYSSTGNAQFCPTWVWAQGNVYRGEFKGEDYFTNVSLSYNNAWGDSHLDAVVGAEYLKQVRTGLWVQAKGITTNDFSYNNIGATSSRPFGGTSSSYEDQSLASIMGSVTYSYKDRYSIAAALRGDGSSMVSDNNTFGFFPSVSLGWDVKKEGFLSDTDFITMLKLRTGYGRSGNLGGITSYTTLNTVKENGIVSINGAPTVTMGSIRNTNPDLKWETRSTFNIGFDLGIWDNRLMLTSELYYSKTTDMLYEYDVPVPTFAFDKLMANIGSMSNQGVELGISVVPIQRKDMEMNINFNMSYQKNKLLSLSGEYNGMHMTASDITPIGSLYGAGQNGGDNNVVYQIVGQPLGVFYLPHCKGLKENELGGYSYDIEDLNDDGEIDFSDGGDRYIAGQATPKVTIGSNISFRYKSFDIAMQINGAFGHKIFNGTGLAYTNMSIFPDYNVLKGAPEKNIIDQNVSDYWLEKGDYVNIEHITIGYNIPMKSKAVKSLRLSAGISNLATITGYSGLTPMINSYVVSNTLGIDDKRTYPLYRTYSLGLSIQF Bacteroides thetaiotaomicron VPI-5482 Btheta 351687 BT2159 predicted 3-ketohexose reductase Specifically important in carbon source D-Trehalose dihydrate; carbon source palatinose hydrate; carbon source D-Raffinose pentahydrate; carbon source D-Leucrose. Distant homologs in other organisms that seem to be involved in the 3-ketoglycoside pathway (i.e., Echvi_3375). It is expected to be cytoplasmic and might reduce 3-ketohexoses. putative oxidoreductase (NCBI ptt file) MDAQFSLDTKIKVGIIGFGRMGRFYWEAMRKSGRWEIAYICDTDPTTRELAKKISPESLVVENDQKIFEDESVQVVGLFTLADSRLEQIEKAIRYGKHIIAEKPVADTMEKEWKVVDMIENSNVLSTVNLYLRNSWYHNLMKEYIQKGEIGELAIIRICHMTPGLAPGEGHEYEGPAFHDCGMHYVDIVRWYAESEYRTWNAQGVNMWNYKDPWWVQCHGTFQNGVVFDITQGFVYGQLSKDQTHNSYVDIIGTEGIVRMTHDFKTAVVDLHGVHQTLRVEKPFGGKNIDVLCDLFADSILTGKRNPRLPLMYDSTIASEYAWKFLQDARMNDLPAIGNLQTLEQIRERRKNMKNGYGLLHSNPPQITNSLK Bacteroides thetaiotaomicron VPI-5482 Btheta 351688 BT2160 SusR4: regulator of disaccharide catabolism (SusR4) Specifically important in carbon source D-Trehalose dihydrate; carbon source palatinose hydrate; carbon source D-Raffinose pentahydrate; carbon source D-Leucrose. Predicted to regulate the operon BT2160:BT2156 (PMCID:PMC3878776) putative regulatory protein (NCBI ptt file) MDKSLFFIIFANNMKFNRCYLKRIVLLFLVALGIGNALYANNELKILADSLHKMIDAKPLFVQKKEQRIARIKCLLKDSGLTPDREYKVNLQLYNEYKKFNIDSAIHYVDRNLEIARQLNRNYLKYQSSLQLSLVYSMCGRYRDAELLLEKMKPSEFPRSLLATYYDTYARFWEYYSISATNNQYGKKREAYQDSLYALMDHTSFDYKLSRAYSYAGHDSTKAIKILDELLNAEEVGTPNYAMITHSYAMLSRYLKREDDAKKYLMMSAIADIQNATRETASLQALALIQYEENNLADAFKFTQSAIDDVVSSGIHFRAMEIYKFYSIINTAYQTEEARSKSNLITFLISTSVSLFLLIVLVVFIYIQMKKTLRMKRALAQSNEELLRLNDKLNSMNSELNDKNDELCEINNIKEHYIAQFFDVCFSYIHKMEKYQNMLYKIAINKCYEELIKKLKSSALIDDELDALYTRFDRVFLNLYPTFVSDFNALLKDDEKIILKQDALLNRELRIYALLRLGITDSGKIANFLRCSTSTVYNYRTKMRNKAAVDRDEFENEIMKI Bacteroides thetaiotaomicron VPI-5482 Btheta 352319 BT2792 regulator of the bile salt efflux system Specifically important in stress Bile salts; stress Deoxycholic acid; stress Chenodeoxycholic acid. In a putative operon with the bile salt efflux system. This is a two-component response regulator of the yesN superfamily (CDD) and is probably the regulator of the operon. AraC/XylS family transcriptional regulator (NCBI ptt file) MQGLGLIVCRQGSFQFSLDNKCASAKAGETLFIHEESWVQVLQETEDVEILILAYQIEPIRDIIGNSVVSMYMYSKLTPELSCVWNTGEEDEIMKYMSLIDSVLEMEESVFSLYEQKLLLLALTYRICSVYNRKLISAGQETGGRKNEIFVRLIQLIEQYYMQERSVEFYADKLCLSPKYLSALSKSICGYTVQELVFKAIIRKCISLLKNTQKNIQEISNEFGFPNASYFGTFFKKQMGMSPQQYRRNL Bacteroides thetaiotaomicron VPI-5482 Btheta 352320 BT2793 bile salt tripartite efflux system, inner membrane component Specifically important in stress Bile salts; stress Deoxycholic acid; stress Chenodeoxycholic acid. This protein is distantly related to emrB-type efflux pumps (see CDD). putative MFS transporter (NCBI ptt file) MPSCPRNYPFYNWVPKPIGIIILLFFFLPILSVGGVYSVNSTEMMSGLGIISEHIQFANFVTSIGMAAFAPFLYELVCIRREKLMCIAGFALMYVFSYVCAKTDSIFLLALCSLLTGFLRMVLMMVNLFTLIKYAFGMEATRNITPGMEPKDATGWNKLDIEKCISQPVVYLFFMILGQMGTALTAWLAFEYEWKYVYYFMMGILLLSILILFITMPNHGFAGRFPINFRKFGNVTAFCISLTCITYVLVYGKVLDWYDDPSICWATAISILFAGIFLYMDVTRRSSYFILGALRLRTIRMGALLYLLLMIINSSAMFVNVYAGVGMHLDNLQNASLANWCMVGYFIGALISIVLGSKGVHLKYLFALGFFFLALSAGFMYFEVQTAGLYERMKYPVIIRTIGMMILYALTAAYANQRMPFKYLSTWICIMLTVRMVLGPGIGGAIYSNVLQERQQHYITRYAQNVDLVNPEASASYTNTVQGMQYQGKSETEAHNMAAMSVKGRIQVQATLSAVKEMAGWTIYAGVICMIFVLVVPYPKRKLLT Bacteroides thetaiotaomicron VPI-5482 Btheta 352321 BT2794 bile salt tripartite efflux system, membrane fusion component Specifically important in stress Bile salts; stress Deoxycholic acid; and perhaps stress chenodeoxycholate. This protein belongs to the EmrA/HlyD family of membrane fusion proteins. putative multidrug resistance protein (NCBI ptt file) METMDNNTISSTHQEKAKKMRKLRRWQIIVSLFGVAVIVWGVIEIVFLFLGYKQTETSNDAQIEQYVSPVNLRASGYINKIYFTEHQQVRKGDTLLVLDDREYKIRVMEAEAALKDAQAGATVINATLQTTQTTASVYDASIAEIEIRLAKLEKDRQRYENLVKRNAATPIQLEQITTEYEATFKKLEATRRQREAALSGVNEVSHRRENTEAAIQRATAALEMARLNLSYTVVLAPCDGKLGRRSLEEGQFITAGQCITYILPDTQKWIIANYKETQIENLRIGQEVAITVDAISKKEFTGKVTAISGATGSKYSLVPTDNSAGNFVKIQQRIPVRIDFTDLSKEDNDKLAAGMMVVVKAKL Bacteroides thetaiotaomicron VPI-5482 Btheta 352322 BT2795 bile salt tripartite efflux system, outer membrane component Specifically important in stress Bile salts; stress Deoxycholic acid; and perhaps chenodeoxycholate. This protein belongs to the TolC family of outer membrane export proteins. outer membrane efflux protein precursor (NCBI ptt file) MDSPILSQPIKFVPEYRAIIMKRLLFIFTFFCLLAIHGGAQNILTLENCLRIGIENNLSLQGKRKAMQKSKYGISENRVKLLPQINGFANFNDNIDPPVSVTDGSSYGVPYNITRTLQYSANAGIELQMPLYNQTLYTSISIAEIVDEMSRLSYEKAREDLILQISKMYYLGQVTAEQIALIKANITRLEELRDITQAFFDNGMAMEVDLKRVNINLENLKVQYDNAQAMMTQQLNMLKYIMDYPAEKEIGLLPVNTDSIATVALTGLSENLYELQLLQSQVQLAERQKRLISNGYIPSLNLTGNWRFAAYTDEAYHWFHSGPSNHWFRSYGVGLTLRIPIFDGLDKKYKIRKAMIDIETMKLSRLDTRKNLQTQYLNAVNDLMNNQRNFKKQKDNYLLAEEVYTVTTDRYREGITSMTEVLQDEMRMSEAQNNYISAHYNYRVTNLMLLKLTGQISSLFK Bacteroides thetaiotaomicron VPI-5482 Btheta 352329 BT2802 conserved protein required for D-ribose utilization Specifically important in carbon source D-Ribose. This protein is in conserved proximity to ribose kinase. It has no apparent homology to characterized proteins. It is often divergent from the ribose kinase, which hints that it has a regulatory role. hypothetical protein (NCBI ptt file) MKRVDSVISLIYSLSKSEKKHFSLQVIKDKEEKDYLVIYDIIIKSKQPNGNTVKEEFYRRKPNGSFEVSIQYLYEKLTDTLLTLRKKKDIYYDLLNNLCKARMLYERSLFEECFEILSNTIEQAQFYENNEILTIALKLELEYLLRLNFPNMTEQELFHKHFIQNEALKKIRKITEQSSLHNLLKYRLSHIGSIRTVKQKQDMNDLMVNELYIAASSDSEGNFELTRNHKLFQANYLMGAGDYRAALNSYKELDSLFEQNQQFWSNPPIYYLSVLEGVLGSLRSVSNYDEIPYFLDKLRKLISDSTSLEFKVNATCLLFQYELFPYLDKGDFSKCTQLMADYQEILYDKEAWLGPIRKSELLLYTTLVHIGNQEYKTAKKYISNAIIDHNIKYLPLMRTIRLVRLIVFYEVQEHELIQYESRSITRSLSSPKEQTFKTERIILWFLNKRNIPILKKDREAFWEKLSPEIHELYNNKYESQLLRLFDFTAWMESKIRKEKLSEVLRARASAKEC Bacteroides thetaiotaomicron VPI-5482 Btheta 352330 BT2803 ribokinase (EC 2.7.1.15) Specifically important in carbon source D-Ribose. An adjacent protein (BT2804) is also expected to be a ribokinase and is also required. It is not clear why both proteins are required. ribokinase (NCBI ptt file) MIIAFICIVLIFNTMETISIHRPKIVVIGSCNTDMVVKANRLPVPGETILGGTFYMNPGGKGANQAIAAARLGAEVTFISKIGYDLFGLQALEIYRSEKINTEYIFTDQKSPSGVALISVDSFGENSIIVAPGASRSLSIEDINKAEEKIKEADIILMQLEIPIDTVEYAATIACKYGKKVILNPAPASSLSNSFLMNVHTILPNRIEAEMLSGIKVMNIESAHRAAQAIGEKGIENVVITLGKDGAYVKEKDEYTMIPAKEVETIDTTGAGDVFCGAFSVCLSEGHSLAKSVKFANAAAAIAVTRIGAQSAIPYKREVVL Bacteroides thetaiotaomicron VPI-5482 Btheta 352331 BT2804 ribokinase (EC 2.7.1.15) Specifically important in carbon source D-Ribose. An adjacent protein (BT2803) is also expected to be a ribokinase and is also required. It is not clear why both proteins are required. ribokinase (NCBI ptt file) MKVVVIGSSNIDMVAQVNHLPAPGETVGDASFMQSLGGKGANQAVAAARLGGSVTFITSLGNDMYAEILKKHFKKEGITTDYIIDDVNQPTGTALIFVADSGENCIAVAPGANYSLLPGSIIHFSKVIDEADIIVMQAEIPYETIKRIALLAKQKGKKVLFNPAPACLIDEELMKAIDILVVNELEAAFISGIEYTGNNLEEIALSLLQAGARNAVITLGSQGVYMKNDKEIIQLPGYKVNAIDTIAAGDTFCGALAVICAQREIDRDALSFANAAAAIAVTRSGAQPSIPTLDEVKHFMLEKELALSFNF Bacteroides thetaiotaomicron VPI-5482 Btheta 352336 BT2809 D-ribose transporter Specifically important in carbon source D-Ribose. It belongs to a family of sugar transporters. It probably moves D-ribose through the inner membrane. putative integral membrane protein (NCBI ptt file) MYIVNSYTLAIIFCFITMICWGSWGNTQKLASKNWRYELYYWDYTIGILLFALLLVFTLGSFGDSGRGFLEDIQQVEAAYIASALIGGAIFNASNILLSASVSIAGMAVAFPLGVGLALVLGVFINYFSSPKGDPFWLFTGVVLIVIAIICNGIAAGKNQKAGTNNSKKGIILAAIAGILMSFFYRFVAAAMDLNNFESPTTGMATPYTAFFIFAIGIFLSNFLFNTLVMKRPFVGLPVTYKEYFAGKASTHMVGILGGCIWGLGTALSYIAAGKAGAAISYALGQGAPMIAALWGVFIWKEFTGSSKATNRLLGVMFILFILGLTFIVISGGS Bacteroides thetaiotaomicron VPI-5482 Btheta 352760 BT3233 predicted glycosaminoglycan binding protein (DUF4861) Specifically important in carbon source Heparin sodium salt from porcine intestinal mucosa; carbon source Chondroitin sulfate A sodium salt from bovine trachea; and perhaps carbon source hyaluronic acid. Belongs to the galactose mutarotase-like domain superfamily, which are thought to be carbohydrate-binding proteins (see InterPro IPR011013). Also, this family (PF16153) is predicted by the PFam curators to bind carbohydrates because of its conserved proximity to glycosyl hydrolyase family 88. hypothetical protein (NCBI ptt file) MKKIFILAAIALMGFASCADSKQSMTVTVTNPLALERTGEMVEVPMSDVTAKLQLADTAQIVVLGEDGQQVPYQVTYDEKVVFPATVKANGTATYTIQSGTPDPYNVIACGRYYPERLDDVAWENDLGGYRAYGPALQKRGERGFGYDLFTKYNTTEPILESLYAEELDKEKRARIAELKKTDPKAAAELQNAISYHIDHGYGMDCYAVGPTLGCGTAALMAGDTIIYPYCYRTQEILDNGPLRFTVKLEFNPLTVRGDSNVVETRVITLDAGSYLNKTVVSYTNLKEAMPVTTGIVLREPDGVVTADAANGYITYVDPTTDRSGGNGKIFIGAAFPSLVKEAKTVLFPEKEKKELRGGADGHVLAISEYEPGSEYTYYWGSAWDKAAIKTVDAWNAYMAEYAQKVRTPLTVTY Bacteroides thetaiotaomicron VPI-5482 Btheta 352855 BT3328 hyaluronic acid endo-lyase (PL29) Specifically important in carbon source Hyaluronic acid sodium salt from Streptococcus equi. In vitro, it also degrades other glycosaminoglycans such as chondroitin sulfate and dermatan sulfate (PMCID:PMC6240882), but it is not important for utilizing chondroitin sulfate. We do not have fitness data for dermatan sulfate. hypothetical protein (NCBI ptt file) MKKVISIICITLLVALYSCDERDDLRSDIDNLKERVANLEASIEQMNSDISNYQQMVEGKILVVGYSKDEQDNYTIELSNGETVTIYSGKVDMNDMPLFSVNASGHWAYTINDMTTELLVNDKPVSAIPEAGTAGVTPKLKVDANGFWLISIDNGSTWNKLGNNQIADGTQAVANASSLFSNVTIDEATGQITFTIRADNSQVKVPIYGKDFYLTIKYEGTATFGLGQKQEFLVEQANVETATIENQTWGVKLTENKLIVTAPKTNVQGKEYEEQIYIKIFSKEGYCRVVKLPVKLLTTEIDANSALAWQRFRQGEDNVLPDYSYAGYNHGESAPQGAFSLGYQVINVKERMTAKNMTAREALISILQEKGMTRVNGTNKLNANAKIVIYFPAGDYILHNDDDNTRDESKQKDAVDSKNNNVSSGIEIYGGNFVIKGDGPDKTRLIMETPNLPTSISNLSSSPILLAIKHTNGPNNAGNSPKLASVTENAKRGDFTVKVSGTTGISSGQWVQLRLRSGDRELVKKEIGPIALNENWAIAKAPISINQSSDDLYGVKITEFHQVKSASNGKITFYEPIMHDIDIKYNDTEGWEIRTYKYLENVGVEDLSFVGNALDGYAHHGEGHAEQAKVGWQYDGAYKPLLLQRVVNSWVRNVHFESVSEALTFAESANSSAYDIRISGKRGHSAVRSQGSSRVFIGKVRDESAGNDVYGKSCQGQFHGCGVSKPSVGTVLWNVTWGNDACFESHATQPRATLIDNCSGGLVYYRAGGDENEVPNHLGDLTLWNLNVTGTDSHASNFAWWSDSDTWWKIFPPIVVGTHGMNVKFSGKEQQQVTYEESTGMKVSPESLYEAQLRERLGYVPGWLNALK Bacteroides thetaiotaomicron VPI-5482 Btheta 352864 BT3337 RND efflux system for fusidic acid, chlorpromazine, and thioridazine, outer membrane component Specifically important in stress Fusidic acid sodium salt; stress Chlorpromazine hydrochloride; stress Bile salts; stress Thioridazine hydrochloride; stress Rifampicin; stress Cefoxitin sodium salt. This protein belongs to the NodT family of outer membrane exporters. outer membrane protein oprM precursor, multidrug resistance protein (NCBI ptt file) MKKQILYMLCATALLSSCHIYKSYDRPEDITASGLYRDPAADNDTLASDTTNFGNLPWREVFTDPQLQSLIEQGLKQNTDLLSAALNVKAAEASLMSARLAYAPSIGLSPQGTISSFDKNAATKTYSLPVTASWQVDLFGQLLNSKRNAQVTLKQTKAYRQAVQTQVIANIANMYYTLLMLDRQLEITQATAEVLKRNAETVQALSERSTYTSAALAQSKAAYAQVVASIPDIEQSIRETENALSTFLGEAPHAIKRGVLEAQALPEELSAGIPLQLLSNRPDVKAAEMSLASCYYNTNSARAAFYPQITLSGSAGWTNSAGSAIINPGKLLASAIGSLTQPLFYRGTNIARLKAAKAQEEQAKLSFQQTLYNAGSEVSNALSLYQNTSKKAESRQMQVESAKKASEDTKELFNLGTSTYLEVLSAQQSYLSAQISQVSDCFDKMQAVVSLYQALGGGRED Bacteroides thetaiotaomicron VPI-5482 Btheta 352865 BT3338 RND efflux system for fusidic acid, chlorpromazine, and thioridazine, inner membrane component Specifically important in stress Fusidic acid sodium salt; stress Chlorpromazine hydrochloride; stress Thioridazine hydrochloride; stress Cefoxitin sodium salt. This protein belongs to the RND family of inner membrane transporters. AcrB/AcrD family multidrug resistance protein (NCBI ptt file) MKLDKFINRPVLSTVISILIVILGAIGLATLPITQYPDIAPPTVSVRATYTGASASTVLNSVIAPLEEQINGVENMMYMTSNASNTGSGDISIYFKQGTDPDMAAVNVQNRVSMAQGLLPAEVTRIGVTTQKRQTSMLVVFSLYDETDTYTDAFIENYAKINLIPQVQRVQGVGDASVMGQDYSMRIWLRPDVMAQYKLIPNDVSTALAEQNIEAAPGQFGERSNQTFQYTIRYKGRLQQPEEFENIVIKSLPNGEVLRLNDIAEIQLDRLGYNFTNRVNGHKAVTCIVYQMAGTNATQTITDIQKLLDEASTTLPSGLKINVSMNANDFLFASIHEVLKTLIEAFILVFIVVYIFLQDLRSTLIPTIAIPVALIGTFFVLSLIGFSLNLLTLCALVLAIAIVVDDAIVVVEGVHAKLDQGYTSARLASIDAMNELGGAIVSITLVMMSVFIPVSFMGGTAGTFYRQFGLTMAIAIGLSALNALTLSPALCAVLLKPHTDHGDKKQTLVSRFHTSFNAAYDSILKRYKKRVLFFIQKKWLSMGLVVLSIVLLIFFMNTTPTGMVPNEDTGTLMGAVTLPPGTSQDRSEQILARVDSLIAADPAVASRTLISGFSFIGGQGPSYGSFIIKLKDWDERSMIQNSDVIVGSLYMRAQKIIKEAQVLFFAPPMIPGYSASTDIEVNMQDKTGGDLNKFFDVANNYTAALEARPEINSAKTTFNPNFPQYMIDIDAAACKKAGISPSDILSTMQGYYGGLYASNFNRFGKMYRVMIQSDPLSRKNLESLNNVKVRNNQGEMAPISQFISVEKVYGPDIISRFNLYTSMKVMVAPASGYTSGQALAALAEVAKENLPAGYTYELGGMAREEAQSSGSTTGLIFILCFVFVYLLLSAQYESYILPLAVLLSIPFGLLGSFLFVNGMSAIGSISALKMILGTMSNNIYMQIALIMLMGLLAKNAILIVEFALDRRKMGMSITWAAVLGAGARLRPILMTSLAMVVGLLPLMFAFGVGAHGNRTLGTASIGGMLIGMICQIFIVPALFVIFQYLQEKVKPMEWEDIDNTDAVTEIEQYAK Bacteroides thetaiotaomicron VPI-5482 Btheta 352866 BT3339 RND efflux system for fusidic acid, chlorpromazine, and thioridazine, membrane fusion component Specifically important in stress Fusidic acid sodium salt; stress Chlorpromazine hydrochloride; and perhaps thioridazine. This protein belongs to the hlyD/MFP family of membrane fusion proteins. AcrA/AcrE family multidrug resistance protein (NCBI ptt file) MKSRIVFFAFCLALLSSCGNKGNDTGKVPEYAVQELQKTTANLMKAYPATIKGRQDVEIRPQVSGFITKLCVDEGATVRKGQLLFIIDPTQYEAAVRTAKASVATAEAAVNTQQMTVDNKIELNKKQIISDYDLSMAKNSLAQAQAQLAQAKAQLTTAQQNYSFTQVKSPSDGVINDIPYRLGALVSPSMATPMTTVSEIDEVYVYFSTTEKELLAMTKTGGTIKEEISKIPAIKLQLIDGTTYDAEGKVDAITGVIDQSTGSVSMRAIFPNKEHMLRSGGTANVLIPYNMENVISIPQSATVEIQDKKFVYVLQPDNTVKYTEIGIFNLDNGKEYLVTSGLNPGDKIVIEGVQSLKDGQKIQPITPAQKEANYQQHLKDQHDGNLATAFN Bacteroides thetaiotaomicron VPI-5482 Btheta 352875 BT3348 unsaturated glucuronide lyase acting on chondroitin/heparin disaccharides (EC 3.2.1.180) Specifically important in carbon source Hyaluronic acid sodium salt from Streptococcus equi; carbon source Chondroitin sulfate A sodium salt from bovine trachea; carbon source Heparin sodium salt from porcine intestinal mucosa. It is 51% identical to C6Y0D8 which preferentially cleaves 1,4-type unsaturated glucuronides that arise during heparin degradation (PMC3931040). B. thetaiotaomicron is believed to degrade chondroitin sulfate via unsaturated 1,3-glucoronides (PMID:25041429). This in combination with the mutant phenotypes suggest that BT3348 has a broader specificity. putative unsaturated glucuronyl hydrolase (NCBI ptt file) MKTILSALGLSLLIFTSCGGQKKVEVDFIQDNIDNAVAQNTIQTDIIEKSGKILNPRTINADGSISYIPIDDWCSGFFPGSMWLTYNLTGDKKWLPLAEKYTEALDSVKYLKWHHDVGFMIGCSYLNGYRFADKKEYKDVIVEAAKSLSTRFRPGAGVIQSWDADKGWQGTRGWKCPVIIDNMMNLELLFEATAFSGDSTFYNIAVKHADTTMAHHFRPDNSCYHVVDYDPETGEVRKRQTAQGYADESSWARGQAWALYGYTACYRYTKDKKYLDQAQKVYNFIFTNKNLPEDLVPYWDYDAPNIPNEPRDASAAACTASALYELDGYLPGNHYKETADKIMESLGSPAYRAKVGTNGNFILMHSVGSIPHGQEIDVPLNYADYYFLEGLMRKRDLEKK Bacteroides thetaiotaomicron VPI-5482 Btheta 352876 BT3349 chondroitin disaccharide sulfatase Specifically important in carbon source Chondroitin sulfate A sodium salt from bovine trachea. It probably acts on unsaturated chondroitin disaccharides (see PMID:25041429) putative sulfatase yidJ (NCBI ptt file) MGGLTLFAAQGCKAPKQVAEQAEHPNIIYVFPDQYRNQAMGFWNQEGFRDKVNFRGDPVHTPNIDTFARESMVLTSAQSNCPLSSPHRGMLLTGMYPNRSGVPLNCNSTRPISSLRDDAECIGDVFSKAGYDCAYFGKLHADFPTPNDPENPGQYVETQRPVWDAYTPKEQRHGFNYWYSYGTFDEHKNPHYWDTDGKRHDPKEWSPLHESGKVVSYLKNEGNVRDTKKPFFIMVGMNPPHSPYRSLNDCEEQDFNLYKDQPLDSLLIRPNVDLNMKKAESVRYYFASVTGVDRAFGQILEALKQLGLDKNTVVIFASDHGETMCSQRTDDPKNSPYSESMNIPFLVRFPGKIQPRVDDLLLSAPDIMPTVLGLCGLGDSIPSEVQGRNFAPLFFDEKAEIVRPAGALYIQNLDGEKDKDGLVQSYFPSSRGIKTARYTLALYIDRKTKQLKKSLLFDDVNDPYQLNNLPLDENKEVVEQLYREMGTMLKEIDDPWYTEKILSDRIPY Bacteroides thetaiotaomicron VPI-5482 Btheta 353095 BT3568 outer membrane binding protein for laminaribiose (SusD-like) Specifically important in carbon source Laminaribiose. An adjacent SusC-like protein (BT3569) has similar phenotypes. BT3568 probably binds laminaribiose and promotes transport by BT3569 through the outer membrane. putative outer membrane protein, probably involved in nutrient binding (NCBI ptt file) MKLNKYLFSTFIAASALLISSCSDFLDRSPQGQFTEDDNPNALVNGKIYNVYTMMRSFDITAGTPAIAIHYLRSEDSEKGSIPSDGSDVAEMYDDFLYTPTNGLLGSYWGKNYAIIYQCNDILDAIAEKETAGQTETEDIINKGEASFFRAYCYFNLVRAFGEVPLVTYKINDASEANIPKTTADKIYEQIDTDLKTAEESLPETWSTEYTGRLTWGAARSLHARTYMMRSDWDNMYKASTDVINKGLYNLKTPYNEIFTDDGENSGGSIFELQCTATAALPQSDVIGSQFCEVQGVRGAGQWDLGWGWHMATQLMADAYETGDPRKNATLLYFRKTDDEPITPENTNEPYGESPISPAMGAYFNKKAYTDPALRKEYTNKGFWVNIRLIRYSDVVLMAAEAANEKNIPGEAVDYLEMVRARARGTNTNILPKITTNDQGELREAIRHERRVELGLEPDRFYDLVRWGIASEVLHAAGKVNYQDKNALLPLPQSEIDKSKGVLVQNPDY Bacteroides thetaiotaomicron VPI-5482 Btheta 353096 BT3569 TonB-dependent receptor for laminaribiose (SusC-like) Specifically important in carbon source Laminaribiose. An adjacent SusD-like protein (BT3568) has similar phenotypes. BT3569 probably moves laminaribiose through the outer membrane. putative outer membrane protein, probably involved in nutrient binding (NCBI ptt file) MEKFNAMRTRLLQDLQKKTIRFKSIVALTCLLLTSVSAFAQTKTVTGTVTDAANEPLIGASVLVQGTSTGTITDMDGKYSISVTPEDVLVFSYVGMTTQSVKVGAQNVINVTLKEDSQVLAETVVIGYGSAKKRDLTGSITNVKGEEIANKPATNPLSSLQGKVAGVQIVNSGRAGADPEIRIRGTNSINGYKPLYVVDGLFNDNINFLNPEDIESMEILKDPSSLAIFGVRGANGVIIITTKKAKEGQTLVNINTSFGFKKVVDKVDLVNGPQFQELYSEQLANQKDTPFDFSGWNANTNWQDEIFQTAFITNNNISITGASPKHSFYLGVGYSHEQGNIKHEKFSKVTINASNDYKITDFLKVGFQFNGARTLPADSKQVLGALRAAPIAPVYNKEYGLYSVLPEFQKAQINNPMVDVDLKANTTKAENYRASGNIYGEVDFLKHFNFKAMFSMDYASNNGRTYLPVMKVYDDTAAGDVVTLGTGKTEVSQFKENETKVQSDYLLTYTNSFDHGNHNLTATVGFTTYYNSLSRLDGARKQGVGLVIPDDPDKWFVSIGDAATATNGSTQWERTTVSMLARVIYNYKGKYLFNGSFRRDGSSAFSYTGNEWQNFFSLGGGWLMTEEEFMKDIKWLDMLKIKASYGTLGNQNLDRAYPAEPLLSNAYSAVFGKPSIIYPGYQLSYLPNPNLRWEKVEAWEAGFETNVLRNRLHFEGVYYKKRTKDLLAEVPGISGTVPGIGNLGEIENMGVEMAASWRDQIGDWGYSVSANLTTIKNKVKSLVQDGYSIIAGDKQQSYTMAGYPIGFFYGYKVAGVYQSQADIDASPENTLATVTPGDLKFADVNRDGKITPEDRTMIGNPTPDFTYGLSLGVNYKNWSLGIDMMGQHGNEIFRTWDNYNFAQFNYLSQRMDRWHGEGTSNSQPLLNSKHSINNLNSEYYIEDGSFFRIRNVQLAYSFDKALLAKIRLQALKVYVNIQNLKTWKHNTGYTPELGGSATTFGVDDGSYPVPAVYTFGINLTF Bacteroides thetaiotaomicron VPI-5482 Btheta 353225 BT3699 SusF SusF: Outer membrane amylopectin-binding protein Specifically important in carbon source amylopectin from maize. It is part of the starch utilization system (Sus) and binds starch (PMCID:PMC3464567). Given the phenotypic information, it probably binds specifically to the amylopectin part of starch. outer membrane protein SusF (NCBI ptt file) MKKHLIYTGMFLAAIGFSACNEDFKDWADPQSNPQEESAGQLTATFTAGKDASIVMDAATADSVEIAKLSSTTAEEGSKIAVNSLTLNENHTIPFSMTEDHVFKVALAQLDSVTQEAYKSRASVVRELKISINASAVTPSGEGIQLVGNEVSITLQPATTPAVDPDGYYIVGDFTGWDGNSAQQMKKDALDENLYILEAEIESTSNFKIFPASAINGNDIDWTKALGSSVDGDDSGDNFVSWTNAGAINTALDGKIKISFDAFNYRFTVKDNSAPTELYMTGSAYNWGTPAGDPNAWKALVPVNGTKGTFWGIFYFAANDQVKFAPQANWGNDFGFVDAISQESKDLAGLSDEGGNLKVGIAGWYLVYVSVIGDDKVIEFEKPNVYLMGDTSYNGWDAQLVEQDLFTVPGTADGEFVSPAFLKDGAVRICVNPKAVSAGDWWKTEFIIFDGQIAYRGNGGDQAAVQGKTGQKVYLNFGNGTGRIE Bacteroides thetaiotaomicron VPI-5482 Btheta 353226 BT3700 SusE SusE: Outer membrane amylopectin-binding protein Specifically important in carbon source amylopectin from maize. It is part of the starch utilization system (Sus) and binds starch (PMCID:PMC3464567). Given the phenotypic information, it probably binds specifically to the amylopectin part of starch. outer membrane protein SusE (NCBI ptt file) MKKISNILLAVTFALPLFTACETDNDSNPILNEPDTFTLNTPAYAANNVYDLKNAQTVELTCSQPDYGFPAATTYTVQASFEQDFIEATDESKANYTVLESTSPTAKINVDASELNNALLDLWTAVNGEQAELPTEPVAVYIRLKANITSSGKGVCFSNVIELPNVLISKSTSSLTPPKTMFIVGSMLDTDWKVWKPMAGVYGMDGQFYSMIYFDANSEFKFGTKENEYIGINDNRVTVTDKAGAGVSGSDNFVVENAGWYLFYVKAAVKGDDYQFTITFYPAEVYLFGNTTGGSWAFNDEWKFTVPATKDGNFVSPAMTASGEVRMCFKTDLDWWRTEFTLHDGEIFYRDFNLIDSWTEKGDGYSIQGSAGNVIHLNFTAGTGEKK Bacteroides thetaiotaomicron VPI-5482 Btheta 353230 BT3704 SusA SusA: alpha-amylase / neopullulanase / cyclomaltodextrinase (EC 3.2.1.135; EC 3.2.1.54) Specifically important in carbon source a-Cyclodextrin SusA. Some homlogs are also specifically required for utilizing cyclodextrin. SusA was previously shown to account for most of the neopullulanase activity of cell extracts (PMCID:PMC178630) alpha-amylase (neopullulanase) SusA (NCBI ptt file) MKRNLLFIILLLLLPGLHQVFATSTIKKVAPTFWWAGMKNPELQILLYGDRISSADVSLSADNITLQEVVKQENPNYLVLYLDLSKAAPQNFDIILKQGKKQTKIPYELKQRRPNASAVEGFDSSDVLYLIMPDRFANGNPSNDIIPGMLEGNVDRNEPFARHGGDLKGIENHLDYIADLGVTSIWLNPIQENDMKEGSYHGYAITDYYQVDRRFGSNEEFRKLTQEANAKGLKVVMDMIFNHCGSDNYLFKDMPSKDWFNFEGNYVQTSFKTATQMDPYASDYEKKIAIDGWFTLTMPDFNQRNRHVATYLIQSSIWWIEYAGINGIRQDTHPYADFDMMARWCKAVNEEYPKFNIVGETWLGNNVLISYWQKDSRLAYPKNSNLPTVMDFPLMEEMNKAFDEETTEWNGGLFRLYEYLSQDIVYSHPMSLLTFLDNHDTSRFYRSEADTKNLDRYKQALTFLLTTRGIPQIYYGTEILMAADKANGDGLLRCDFPGGWPNDTKNCFDAANRTPQQNEAFSFMQKLLQWRKGNEVIAKGQLKHFAPNKGVYVYERKYGDKSVVVFLNGNDREQTIDLVPYQEILPASSAFDLLTEKKVELRNELTLPSREIYLLSF Bacteroides thetaiotaomicron VPI-5482 Btheta 353314 BT3788 TonB-dependent receptor for alpha-mannan (SusC-like) Specifically important in carbon source Mannan from Saccharomyces cerevisiae. Part of a polysaccharide utilization locus that is induced by mannan and is required for mannan utilization (see PMCID:PMC4978465). putative outer membrane protein, probably involved in nutrient binding (NCBI ptt file) MKNTQKYFILLLMLILLVPSNIWGQETKKEIIVKGVVEDDLGPIIGASVVAKNQAGVGVITNTEGKFSLKVGPYDVLVVTFVGYQPYELPVLKMNDPNNVTIKLLEDVGKIDEVVITASGLQQKKTLTGAITNVDVKQLNAVGSSSLSNSLAGVVPGIIAMQRSGEPGENTSEFWIRGISTFGAKSGALVLIDGVERNFDEILPQDIESFSVLKDASATAIYGQRGANGVILITTKRGEKGKVKINVKAGFDWNTPVKVPEYASGYDWARLANEARLGRYDSPIYTPEELEIIRSGLDTDLYPNIDWRDLMLKSGAPRYYANISFSGGSDNVRYYVSGQYTSEQGRYKTFSSENKYNTNTTYERYNYRANVDMNITKTTVLKVSVGGWLVNRTTPTRSTGDIWEDFAKFTPLSTPRKWSTGQWPRVDGQDTPEYHMTQRGYHTKWESKVETSVKLEQDLKFITPGLKFEGVFAFDTYNENIIKREKKEEVWEAQKYRDENGKLILKRVVNRSPMNQNKEVRGDKRYYFQASLDYNRLFAHAHRVGVFGMVYQEEKTDVNFDSSDLIGSIPRRNLAYSGRFTYAYKDKYLAEFNWGCTGSENFEHGKQFGFFPAVSAGYVISEEAFMKKALPWIDQFKIRASYGEVGNDVLDGRRFPYVSLIDTDDGGSYSFGEFGTNRVQAYRIRTLGTPNLTWEIAKKYDVGVDFSFFNGKISGALDWFLDKRDDIFMQRKHMPLTTGLADQTPMANVGKMKSYGWEGNIGFTQSIGQVNLQLRANFTYQTTDIIDKDEAANELWYKMDKGFQLNQSRGLIALGLFKDQDEIDRSPKQTSNRPILPGDIKYKDVNGDGVINDDDIVPLGYREVPGLQYGVGLSANWRNWNLSVLFQGTGKCDFFIGGNGPHAFRSERYGNILQAMVDGNRWIPKEISGTTATENPNADWPLLTYGNNDNNNRKSTFWLYERKYLRLRNVEVSYDFPQTWTRKFFVSNLRLGFVGQNLLTWAPFKMWDPEGTREDGSNYPINKTFSCYLQISF Bacteroides thetaiotaomicron VPI-5482 Btheta 353315 BT3789 Outer membrane binding protein for alpha-mannan (SusD-like) Specifically important in carbon source Mannan from Saccharomyces cerevisiae. Part of a polysaccharide utilization locus that is induced by mannan and is required for mannan utilization (see PMCID:PMC4978465). hypothetical protein (NCBI ptt file) MKKLVYYILLSISALSFSACTDYINVDKYFYDQVSLDSAFSKRIYVDGWLSSAYSVMNKLGEYKEPFRWASDDLYHPDMKEYVEGSYSADKPKGDENAGESRLWKYYEGIRKASTFLDNVDRCPELTMDEIADMKGQARFLRAYCYWALIRVFGPVPLIPLEGLDADLSYEELSLPRTHFDEIVSFIDTELAETARLLPMRRTVNNLGRPTRGAALGLRARVLLYAASPLYNGNLDFFNVVDNKGNQLISQTYDESKWAKAAAAAKDVIELAKTSGLYELYTIAPKIGTLDMYRPPVHPEYSTKDYPDGWANIDPLLSYKSNFDGSVQGSKNPELIFTRTSDGTGTINDWMYQALPRTISGNNRLCVTQKQVNAYAMNDGRTISEAANTGDYVTTGFTTEAYSENNPFLPAKVSLMYNKREPRFYASIAYNGSVWEAASASEPRYRNQQIFYYRGTEDGKQGFKEECPLTGMTLKKFYNSEDSRTDGGYVIEKTEMTIRYAEILLIYAEALNELSEGEVYHLKTYSNEDVEIKRDEDEMRYAIKRIRMRAGVPDYTNETYKNQADFRVKLKRERQVELLGENSMRYFDLRRWKDALTEENQLLQGCNINISDDDTYIADFYKETPVSSVHKVFEQRMYLFPFPTYELKRNVNLTQNPGW Bacteroides thetaiotaomicron VPI-5482 Btheta 353713 BT4187 exo-alpha-D-galacturonosidase for catabolism of rhamnogalacturonan I and polygalacturonate Specifically important in carbon source Rhamnogalacturonan - from potato; carbon source polygalacturonic acid. Rhamnogalacturonan I is a polymer of D-galacturonate and L-rhamnose. This protein is 64% identical to BT4123, which is an exo-alpha-D-galacturonidase (PMC:PMC5784806). BT4187 is expected to be secreted, but no specific signal for protein export was identified by PSORT-b. exo-poly-alpha-D-galacturonosidase precursor (NCBI ptt file) MNTMTRRLLWMVVCCLPFVSGCKQSECAISENAIDDTIYQNLPFEMPKVQQPVFPAYEVNISKFGAKGDGMTLNTKAINDAIKEVNQRGGGKVIIPEGTWLTGPIELLSNVNLYTERNALILFTGDFEAYPIIPTSFEGLETRRCQSPISARNAENIAITGYGIFDGNGDCWRPVKKEKLTASQWNKLVKSGGVLDEQERIWYPTAGSLKGAMACKDFNVPEGINTDEEWNEIRAWLRPVLLNFVKSKRILLEGVTFKNSPSWCLHPLSCEDFTVNNIQVINPWYSQNGDALDLESCKNALILNSVFDAGDDAICIKSGKDENGRRRGEPCQNVIVKNNTVLHGHGGFVVGSEMSGGVKNIYVEDCTFLGTDVGLRFKSTRGRGGVVENIYINNINMINIPNEPLLFDLFYGGKGAGEESEEDLLSRMKTAIPPVTEETPAFRDIHISNVICRGSGRAMFFNGLPEMPIRNVTVKNVVMTEATDGVVISQVDGVTLENIYVESTKGKNILNVKSAKNLKVDGETYEEIDAKGQILNFK Bacteroides thetaiotaomicron VPI-5482 Btheta 353937 BT4411 predicted hyaluronic acid binding protein (DUF4627) Specifically important in carbon source Hyaluronic acid sodium salt from Streptococcus equi. The adjacent polysaccharide lyase BT4410 has similar phenotypes. Both proteins are periplasmic and this protein belongs to DUF4627, which is related to a family of carbohydrate binding proteins (PF02018). hypothetical protein (NCBI ptt file) MKKVLLVSLLAIAGVSISAQNLIKNEKFATEVTNKVTNPSKATAGEWFIMNNEADGVTTIAWEQTGDAKYPNAMKIDNSGAEKNTSWYKAFLGQRITDGLEKGIYVLTFYAKAKEAGTPVSVYIKQTNEEKNDNGKLNTTFFMRRDYDADAQPNASGAQYNFKIKDADKWTKVVVYYDMGQVVNAISSKKSNPALEVSDTDDDAAILKDCYVAILGQNKGGVVEISDVTLKKK Caulobacter crescentus NA1000 Caulo CCNA_01698 CCNA_01698 predicted periplasmic 3-ketoglycoside hydrolase (DUF1080) Specifically important in carbon source D-Raffinose pentahydrate. Raffinose utilization which appears to proceed via the 3-ketoglycoside pathway. This protein is in a conserved cluster with the 3-ketoglycoside pathway starting with lacABC. DUF1080 (PF06439) has structural similarity to endo-glucanases. This protein has a signal peptide so is probably periplasmic. Note that another DUF1080 protein (CCNA_01705) is also involved. endo-1,3-1,4-beta glucanase-related protein MTIKAITGLASFAVGMALLSATASAQTRPEDTEVWKPVPAVVTPASAPGGAPSDAIILFDGRNLDQWVTAADKSPAGWTVADGVITVDKARGNIETKRAFRDYQLHLEWRIPADIAGSGQGRGNSGVFLASTGSRDQGYEVQILDSYQSATYVNGQAGAVYKQHPPLANANRKPGEWQTYDIIWRAPVFGSDGALTTPASVTVLHNGVLVQDNAVLAGETVYIGKPGYKAHGPSPIKLQAHGDPSIPISFRNIWVRELAPR Caulobacter crescentus NA1000 Caulo CCNA_01700 CCNA_01700 predicted 3-ketohexose transporter Important for utilization of raffinose, lactose, and salicin. In a conserved cluster with the 3-ketoglycoside pathway starting with lacABC. The 3-ketoglycoside is probably cleaved in the periplasm by DUF1080 (CCNA_01698) so this is probably a 3-ketohexose transporter. nucleoside permease MGTSFRLFVMMVLQLAIWGAWAPKIFPYMGMLGFAPWQQSLVGSAWGVAALVGIFFSNQFADRNFSAERFLAVSHLIGGVALLGTAFSTEFWPFFACYLVFSLVYVPTLSVTNSIAFANLRDPAAGFGGVRMGGTVGWVLVSWPFVFLLGAQATVEQVRWIFLVAAIVSFVFAGYALTLPHTPPRKADDAVDKLAWRRAFKLLGAPFVFVLFVVTFIDSVIHNGYFVMADAFLTNRVGIAGNLSMVVLSLGQVAEIITMLLLGRVLAKLGWKVTMIVGVLGHAARFAVFAYFADSVPVIVAVQLLHGVCYAFFFATVYIFVDAVFPKDVRSSAQGLFNLLILGVGNVAASFIFPALIGRLTTDGSVDYTTLFLVPTAMALAAVCLLALFFRPPTRGPVSEADSASSAASSAQA Caulobacter crescentus NA1000 Caulo CCNA_01701 CCNA_01701 predicted sugar epimerase in the 3-ketoglycoside pathway Important for the utilization of lactose, salicin, and raffinose. In a conserved cluster with the 3-ketoglycoside pathway starting with lacABC. The 3-ketoglycoside is probably cleaved in the periplasm by DUF1080 (CCNA_01698) and this is probably involved in breaking down the resulting 3-ketohexose. Note that another epimerase (CCNA_01703) is also involved. xylose isomerase family protein MSGKVIPMRMTAFDNQSQGLSRRGLLAAGAAALGAGVAGAAGASALPFFQRRNQPVGIQLYSLGPDLAKELDAQLATVAKIGFRTVELAGYLGRTPAELRALFDRHGLVCPSAHISPKGPNGFSGDLVKLADELHVIGAKSAIMPIFYIPERMGAADLRQAGVQMTADEWKWNADFLNEKAAILKKAGILAGYHNHNFEFAPLKDAKGRETTGMDILLKGTDPSLVTFELDAGWVTAAGQDPFALLKAYPGRFTQMHVKDVKPSTKPNFELRQDPTEVGSGMIDWKRLLPAAYDAGIRGFYYEQEPPFAYTRLESARISFDYLAKVVA Caulobacter crescentus NA1000 Caulo CCNA_01702 CCNA_01702 predicted 3-ketohexose reductase Important for the utilization of lactose, salicin, and raffinose. In a conserved cluster with the 3-ketoglycoside pathawy starting with lacABC. This is a putative sugar dehydrogenase and is probably involved in consuming the 3-ketohexose. NAD-dependent oxidoreductase MALRMAMVGGGPGSFIGPVHRMAAELDGRIRLVAGVFSRDPAKSAQAAVAWGVAPDRVYPDHHTMFAAERARADGVQLVSVVTPNHLHFDVSAAALKAGLHVISDKPATLNLAEAQALAKVVAASGKQYGLTYTYTGYPMVREAREIVARGDLGAVRKVVVEYSQGWLSTPLERDSANKQASWRADPKQSGVGGCIGDIGVHAFNIAEFITGRRVERLCADVATVVPGRDLDDDCNVLLRFEGGARGVLIASQISAGARNGLTISVYGEKGGLTWSHEDPNILTLDWLDGPSHVLHAGSGYLGPAARAVTRLPTGHPEGFIEAFATIYRDFADAIEGRAGGLVPDIAEGLRGMTFVERAVAASRDDAGWVSLQGEG Caulobacter crescentus NA1000 Caulo CCNA_01703 CCNA_01703 predicted sugar epimerase in the 3-ketoglycoside pathway Important for the utilization of lactose, salicin, and raffinose. In a conserved cluster with the 3-ketoglycoside pathway starting with lacABC. The 3-ketoglycoside is probably cleaved in the periplasm by DUF1080 (CCNA_01698) and this is probably involved in breaking down the resulting 3-ketohexose. Note that another epimerase (CCNA_01701) is also involved. IolE-related protein MKTLKGPAIFLAQFIGDTPPFDKLETMAAWVSSLGYAGVQMPTGGADSFFDLALAAESQTYCDDIAGLLAEYGLEITELSTHLQGQLVAVHPAYDELFDGFAPPELRGKPKERQAWAVEQVKAAAVASRRLGLKAHATFSGSLAWPYLYPWPQRPAGLIEEAFAELGRRWKPILDVFDENGVDAAYEIHPGEDLHDGATFERFLDEVGGHPRANILYDPSHFVLQQLDYLAYIDRYHERIKAFHVKDAEFRPSARSGVYGGYQGWVDRPGRFRSLGDGQVDFKAIFSKLAQYDYDGWAVLEWECALKHPEQGAAEGAPFIRDHIIRVTDKAFDDFASAGSEAGRNRRLLGL Caulobacter crescentus NA1000 Caulo CCNA_01704 CCNA_01704 lacB: cytochrome c2 component of periplasmic glucoside 3-dehydrogenase (EC 1.1.99.13) Specifically important in carbon source Beta-Lactose, and also important for carbon sources salicin and raffinose. Previously proposed to be a component of lactose 3-dehydrogenase (PMCID:PMC2863468) cytochrome c MMKVRLTLAAVFAALASGAVAAPSGQQLFEQRCGMCHSLQQAPGKMGPPLAGVVGRKAASFPGYTYSAALKGSGITWTADKLDAYSKAPTKVVPGTKMLLGAPNDAERAAVIAYLASVKK Caulobacter crescentus NA1000 Caulo CCNA_01706 CCNA_01706 lacA: subunit of periplasmic glucoside 3-dehydrogenase (EC 1.1.99.13) Specifically important in carbon source D-Raffinose pentahydrate; carbon source Beta-Lactose; carbon source. Previously shown to be required for and induced by growth on lactose and to be a component of lactose 3-dehydrogenase (PMCID:PMC2863468) BetA-family choline dehydrogenase MANLNGRARRKNTYDAIVVGSGITGGIAAKELTEKGLKVLVLERGPMVRHLEDYPTAMLDPWQSKYPQGKLPEAELNAHYKVQRRTGYTMTEQTQHFFVRDDEHPYTEENRFDWIRGYHVGGRSLTWGRQSYRHSPIDFEANAREGIAVDWPIRYEDLAPWYEHVERFIGVSGQAEGLPHFPDGHYQPPMELNCVEKAFKARSEARFPERRVTIGRTAHLTDPTEEQLALGRTKCQYRNLCIRGCPFGAYYSSNSGGLIAAERTGNLVIRPNSIVTELIYDERAGRASGVRILDAETRKDEEFHADVIFLCASALNSAWIMMNSTSSRFPNGFGNASDQLGRNVMDHHLGAGATGQAPEFADMYFSGRRPNGIYVPRFRNLGDAASKRSDYLRGFGYQGGAGRATWERDRGQGGRGFGAARKAALSQPGPWTMGLSGFGEMLPYADNRVTLNRDVEDKFGLPTLTMNVTMRDNEMAMRRDMQAAAAEMLEAAGFQNVRAHDNGFAPGLGIHEMGTARMGRDPKTSVLNAHNQVHECKNVYVTDGAAMASASCVNPSLTYMALTARAADHAVRARKRGEL Caulobacter crescentus NA1000 Caulo CCNA_01707 CCNA_01707 lacC: subunit of periplasmic glucoside 3-dehydrogenase (EC 1.1.99.13) Important for the utilization of lactose, salicin, and raffinose. Previously proposed to be a component of lactose 3-dehydrogenase (PMCID:PMC2863468) gluconate 2-dehydrogenase subunit 3-family protein MLNRRDALRGLALTVGAAATGWAGTAAATTALSWTPTALTPEQAQILDVVAELIIPATDTPGARAAGVPQFIDRAIANYCEKWQVDQLVGGFARMDADAKAAHGKLFVALAPEQQVAILNVYDRETAVSTSGHFFPLLEDFVTVGYFTSEPGATLALKYDPVPGAYNGCVPLAEIGRGWATR Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1841 Echvi_1841 predicted cytochrome c component of periplasmic glucoside 3-dehydrogenase (EC 1.1.99.13) Important for utilizing various glucosides (salicin, trehalose, cellobiose, and perhaps lactose). In a conserved cluster with the 3-ketoglycoside pathway starting with lacAC. This is probably the cytochrome c subunit, replacing lacB. Cytochrome c551/c552 MNLSKLASAGAIALAGMAYACGGGSDTKSEETTSAAESAAPKKEMSFDEMYKDNPDYVEGLALVKESDCPSCHMVERKIVGPAYKDVAEKYESTDENIETLAKRVVDGNNGVWGQVPMPAHPGLSEDDAKKMVKYILMLKK Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1842 Echvi_1842 predicted sugar epimerase in the 3-ketoglycoside pathway Important for utilizing various glucosides (salicin, trehalose, cellobiose, and lactose). In a conserved cluster with the 3-ketoglycoside pathawy starting with lacAC. This is probably involved in consuming the 3-ketohexose. Another epimerase (Echvi_1846) also seems to be involved. Sugar phosphate isomerases/epimerases MKTIKGPALFLAQFADDQAPFNSLKSICEWAASIGYKAVQIPSWDGRFMDLKKAAEEPEYANEIKQTVADAGLEISELSTHLQGQLVAVNPAYNELFDAFAPEELKGDLEGKTKWATQQLMYAAKASKNLGLTKHGTFSGALMWHTVYPWPQRPAGLVEAGFEELAKRWLPILDEFDKNGVDLCYELHPGEDLHDGVTFEMFLEKVNQHPRANILYDPSHFVLQCLDYVQFIDFYKDRIKMFHVKDAEFNPTGKQGVYGGYQGWIDRAGRFRSLGDGQVDFNAIFSKLSQYGFDGWAVLEWECAIKHPEAGAIEGAKFISEKIIRVTEKTFDDFASAGTDDALNKKVLGI Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1844 Echvi_1844 predicted 3-ketohexose reductase Specifically important for utilization of salicin and cellobiose. In a conserved cluster with the 3-ketoglycoside pathawy starting with lacAC. This is a putative sugar dehydrogenase and is probably involved in consuming the 3-ketohexose. Echvi_3375 (not in the cluster) may also have this role during salicing catabolism. Predicted dehydrogenases and related proteins MTNHRKLRMGMIGGGPGAFIGAVHRIAANIDGQIALVAGAFSSRPEKSAQAGKDLFLDPKRVYQSYDEMFEKEKQLPEGERIDFVSIVTPNHAHFDPTIKALQNGFHVVLDKPMTLTLDEAKQLDKVIQETGMLFCLTHTYTGYPMVKEAKQLIANGTLGKIRKVYVEYPQGWLWKDFSDEGNKQAAWRTDPKKSGVAGCMGDIGTHAMNLAEYVSGLKLDKLCADLNTVVPGRTLDDDGIVLLKFDNGASGVLMASQVATGAENNLKIRVYGDKAGLEWQQEDANSLIVRHPEQPDQIYRAGANVPYLSSYALANTRTPAGHPEGYLEAFANHYHNFARTLLAKLNNQTPEKEWLDFPGTEDGVRGMAFIEQVVKSGQSEQKWTKFEI Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1845 Echvi_1845 predicted 3-ketohexose transporter Specifically important in carbon source D-Salicin; carbon source D-Trehalose dihydrate. In a conserved cluster with the 3-ketoglycoside pathway starting with lacAC. The 3-ketoglycoside is probably cleaved in the periplasm by DUF1080 (Echvi_2921 or Echvi_1840) so this is probably a 3-ketohexose transporter. Nucleoside H+ symporter. MSFNTKFKLSFMMFLEFFIWGGWFVTLGLFLGNNLGTNGAQDAAVFSTQSLGAIIAPFIIGLIADKYFNAERILGILHLIGAVLMYLMYTATDFESFYPYVFAYMVAYMPTLALVNSVSFNQMSNPEKEFGVIRVWGTIGWIVAGLVISLVFAWDSTENAAAGMLKYTFLMTCIASLVLGVYSFMLPKTPPKIAKGEKKSISEILGLDAFTLLKDRNYLVFFLSSVLICIPLAFYYQNASKFFGEIGMTNLTSKMALGQGSEVLFMLLLPIFFGKFGVKKTLLVGMLAWVVRYALFAFGNVGELSFMLLTGIALHGICYDFFFVSGQIYTDSKAGEKFKSAAQGMITLATYGVGMLIGFWVAGWAYDTYEMSDKVHDWKTIWLIPSGIAVLVALIFAVAFKQKKTTPVEA Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1846 Echvi_1846 predicted sugar epimerase in the 3-ketoglycoside pathway Specifically important in carbon source D-Salicin. In a conserved cluster with the 3-ketoglycoside pathawy starting with lacAC. This is probably involved in consuming the 3-ketohexose. Another epimerase (Echvi_1842) also seems to be involved. Hydroxypyruvate isomerase MMVGSAVLSGLPYLNLKAKNKEMLKGNINHSVCRWTYGHLSLDELCVLIKDIGFNAIDLLGPDDWPTAQKYGVYSSMCNGAEISLEEGFSHSEYHDTLIKNYTEMIPLVAKNGYKNLICFSGNRNGMDDETGLQNSVKGLQKLLPLAEKHGVTLTMELLNSKVDHPDYMCDKSVWGVELCKRLDSEHFNLLYDIYHMQIDEGDVIRTIGENHQYYGHYHTAGNPGRNEIDDTQELNYPAIIKAIAKTGFKGYIAQEFIPKADDKAASLREAIALCDI Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1847 Echvi_1847 periplasmic glucoside 3-dehydrogenase (lacA subunit) (EC 1.1.99.13) Important for utilization of various glucosides (trehalose, salicin, cellobiose, and perhaps lactose). Related to lacA of Caulobacter crescentus which is a component of lactose 3-dehydrogenase. Choline dehydrogenase and related flavoproteins MANQEYDAIVVGSGISGGWAAKELTEKGLKVLLLERGQNVEHVKDYKNATLPPWEIPHRGRRTTEMVENHPNLKRDYVLNELVLDWWAHEDTSPYVEEKPFTWFRGYQVGGRSLLWGRQSYRWSDLDFEANLKEGIAVDWPIRYKDIAPWYDYVEKFAGIAGNRDGLDVLPDGEFMPPFAMNCVEKDVKERIAKHFEGKRHLINSRVANITEPLPGRPGCQARNKCWLGCPFGGYFSTQASTLPAAMATGNLTLRPYSIVHRVLYDKDTKKATGVEIVDAETMETIEYKSKIVFLCASALNSAHVLMRSATDIWPEGLGSSSGELGHNVMDHHFRLGASGTVEGYDDKYYFGRRPGGIYIPRYRNVGDDKRDYVRGFGYQGGASRSGWGRDVAEMNIGGPMKEALTEPGPWSMGMMAFGEILPYHENTIKISKDVKDKWGMYALVMNAEIKDNEQKMRKDMMNDAAEMLEAAGVKNIHTYDSGYTFGQGIHEMGTARMGRDPKTSVLNENNQVWDAKNVFVTDGAAMTSAAAVNPSLTYMALTARAADFAVKELKKGNL Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1848 Echvi_1848 periplasmic glucoside 3-dehydrogenase (lacC subunit) (EC 1.1.99.13) Important for utilization of various glucosides (trehalose, salicin, cellobiose, and perhaps lactose). Related to lacC of Caulobacter crescentus which is a component of lactose 3-dehydrogenase. hypothetical protein MAMNRRDALKSFALMMGGTMVGANALLTGCTPDKQIEGLDFSPEEIDFLDEIGDTIIPTTDTPGAKAVGIGSFMVMMVKDTYWEEEQKQFIDGLNSLRKGFKEEVGKDFMDASQEERTAYLNKLNAAAREENGPKYFNMLKDLTVLGYFTSEIGATQALNYVEVPGKWEPCIDYKKGDKAHAI Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_2921 Echvi_2921 predicted 3-ketoglycoside hydrolase (DUF1080) Specifically important in carbon source D-Trehalose dihydrate, which appears to be catabolized via the 3-ketoglycoside pathway. This protein may be partially redundant with another DUF1080 protein (Echvi_1840). The other DUF1080 protein is in a conserved cluster with the 3-ketoglycoside pathway starting with lacABC. DUF1080 (PF06439) has structural similarity to endo-glucanases. Echvi_2921 has a potential signal peptide or N-terminal hydrophobic patch; its localization is uncertain. Domain of Unknown Function (DUF1080). MKLNLLFPVLAGSMLAVPVMAQHDPIQLPPQATEVWEPVPPVVTPGEENHMPPSDAIVLFDGSDLSAWKSVKTGGEAEWTVHDGIFTVKPGTGEIATKEKFGDVQVHIEWKAPDVVKGEGQGRGNSGLFFCERYEVQILDSYQNRTYSNGQAASLYKEGIPLANAMRSPQEWNTYDVFFTAPRFNKDGMVISPAYVTVIHNGVLVQNHYEVKGSTAYIGVHKYEAHETELPIKLQDHGNLVNFRNIWVRKL Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_3375 Echvi_3375 predicted 3-ketohexose reductase Specifically important in carbon source D-Salicin, which appears to be catabolized via the 3-ketoglycoside pathway. Related proteins are found in the 3-ketoglycoside pathway cluster. This is a sugar dehydrogenase and is probably a 3-ketohexose reductase. Predicted dehydrogenases and related proteins MTKTIKAAIVGTGFIGPAHLEALRRIPNIEVIALCEVNQELAEEKAKLLGIPQAFTFEEMLKQPEIEVVHICTPNFLHYNQSKAALEAGKHVVCEKPLATKIDEAEALVALAKEKGLVNAVHFNLRYYPMVRQMKTMRENGELGDIYSIMGSYLQDWLYLNTDYNWRLEPDKSGDSRAIADIGSHLLDLTEYVTGLKITEVMADFSTVHKTRLKPLKPIETYSGKMLQESDYEEVPINTEDHATVLLRFDNGNKGSVTVSQVNAGRKNRLNIEIAGSKSNFEWCSERPNEMWIGKRESPNQQLMKDPALFTPEAAGLISFPGGHNEGFPDTSKQMFKEVYAAVAAGKQPENPSFPTFKDGYRELLICERIIESNQKQAWVKI Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS15340 CA265_RS15340 periplasmic glucoside 3-dehydrogenase (lacC subunit) (EC 1.1.99.13) Specifically important in carbon source D-Salicin; carbon source D-Trehalose dihydrate; carbon source D-Cellobiose; carbon source Beta-Lactose (all are glucosides). Related to lacC of Caulobacter crescentus which is a component of lactose 3-dehydrogenase. twin-arginine translocation pathway signal protein MHRREALKNVAFLLGGAISASTMGVLFESFTLPENEKNFVLYSLEDEKIFAEFADIIVPTTKSSAGAKAAGLGKFIPMMMKDCYPAAMQTSFAQGFKDLQAKSKKDFGKNYITLTPAERKKLMIDLRAIALAQKESKSEENKDLAYFFITARDLTLLGYYSSEIGCTKAREYVLIPGRYDGNAPLKPGQKSWAT Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS15345 CA265_RS15345 periplasmic glucoside 3-dehydrogenase (lacA subunit) (EC 1.1.99.13) Specifically important in carbon source D-Trehalose dihydrate; carbon source D-Salicin; carbon source Beta-Lactose; carbon source D-Cellobiose (all are glucosides). Related to lacA of Caulobacter crescentus which is a component of lactose 3-dehydrogenase. GMC family oxidoreductase MMNLNTNLKAENTYDAIVIGSGISGGWAAKELTEKGLRVLMLERGMNIEHITGYETAMKNPWDFKHAGKLTEEQKRTHPVQKRDYPYQEANEKWWVNDLECPYTEDKRFDWYRGFHVGGKSLMWGRQSYRLSDHNFEDNARDGHGSDWPVRYAELSPWYDYAERFAGISGSKENWPTCPDGQFLPPMDLNIVEKSVKARIEEHYKRERIMMIGRVANLTVPHKGRGNCQYRNLCSRGCPFGAYFSTQSSTLPAAMATKRLTLRPYSIVNHIIYDKDTKKAKGVMVIDAETNKTMEFYAKIVFVNGSTLGSTFVLLNSTSEAHPNGLGNGSGQLGHNLMDHHFRCGASGEAEGFDDKYTYGRRANGIYIPRYQNIGNDKRDYLRGFGYQGGASRANWQGDVAELSFGADLKQKMTTPGKWSMGLGGFGEMLPYYENKVYIDKTKKDKWGQPVLAIDCEYKENEKKMRVDMMNDAAEMLEKAGMKNIKTFDNGCYPGMAIHEMGTARMGNDPKTSVLNKWNQMHEVNNVFVTDGSCMPSIACQNPSLTFMALTARACDYAVKELKKKNI Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS15350 CA265_RS15350 predicted 3-ketohexose reductase Important for utilization of various glucosides (trehalose, salicin, lactose, and cellobiose). In a conserved cluster with the 3-ketoglycoside pathawy starting with lacAC. This is a putative sugar dehydrogenase and is probably involved in consuming the 3-ketohexose. oxidoreductase MKRKLRMGMIGGGKDAFIGAVHRLAANMDGLIELSAGALSVNPEIGYESGKLLFLPDNRIYTNYEEMLTKESELPADERIDFVTIVTPNFAHFAPAMMALDKGFNVVIEKPMTLTLEEAKQLQAKVEETGLTLCLTHTYSGYPMVKQAKQMVSEGALGAIRKIMVEYPQGWLSTLSEREGNAQAAWRTDPSKTGKSGSMGDIGTHAAHLAEYITGLKITKICADLNIVVPGRAIDDDGNVLLKFDNGANGVLVASQIAAGEENALKIKVYGEKGGMEWHQMEPNTLIVKWLNAPAQIYRTGNGYMGSFAQHNTRTPGGHPEGYLEAFANIYRNFALTVDAKLNNEQPTAAMLDFPGTEDGIRGMAFIENVVASSQSDQKWLDYKL Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS15355 CA265_RS15355 predicted sugar epimerase in the 3-ketoglycoside pathway Specifically important in carbon source D-Salicin; carbon source D-Trehalose dihydrate; carbon source D-Cellobiose; carbon source Beta-Lactose. In a conserved cluster with the 3-ketoglycoside pathway starting with lacAC. This is probably involved in consuming the 3-ketohexose. AP endonuclease MTTIKGPAVFLAQFISDEAPFNSLDSICEWAAGLGFKGIQMPTLDARFIDLQKAAESKTYADELKGKIASYGLEITELSTHLQGQLVAVHPAYDDLFDAFAPKEVHKNPKARTEWAVQQMKYAAKASQNLGLNAHATFSGSLLWQYFHPWPQRPAGLVEEGFAELAKRWTPILNEFDQCGVDICYEIHPGEDLFDGETYEMFLAAVNNHPRACLLYDPSHFVLQQLDYIQYIDFYHERIKAFHVKDAEFNPTGKQGTFGGYQSWANRAGRYRSPGDGQVDFKTIFSKLAQYDFKGWAVMEWECCIKNQQDGAREGAAFIKNNIINVTDKAFDDFAASGSDSAFNKRILGL Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS15360 CA265_RS15360 predicted cytochrome c component of periplasmic glucoside 3-dehydrogenase (EC 1.1.99.13) Although we do not have fitness data for this gene, a similar protein (Echvi_1841) is also part of a cluster with glucoside 3-dehydrogenase (lacAC) and has similar phenotypes. This is probably the cytochrome c subunit, replacing lacB. cytochrome C552 MKKTFLILGAVVIFMASFSKADLSREKTVVATATMTKHAAFQSNPGEKLINKSDCLGCHNKTNKIIGPAYVEIAKKYPATEKNINMLADKIIKGGTGVWGNMPMTAHATLKKDDAKLMVKYILSLKK Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS15375 CA265_RS15375 predicted 3-ketohexose transporter Specifically important in carbon source D-Salicin; carbon source D-Trehalose dihydrate; carbon source Beta-Lactose; carbon source D-Cellobiose (all glucosides). In a conserved cluster with the 3-ketoglycoside pathway starting with lacAC. The 3-ketoglycoside is probably cleaved in the periplasm by DUF1080 (CA265_RS22975 or CA265_RS15370) so this is probably a 3-ketohexose transporter. MFS transporter MNNTTRFKLSAMMFLEFFIWGAWFVTMGTYLGKNLLANDVQIGSAYSTQSLGAIIAPFIIGLIADKFFSAQKVLGVLHLVGGALLWVAGTSLNFDSFFPFILGYMIAYMPTLALVNSISFKQMKDPGKEFPSIRVFGTIGWIIAGLVIGWLNWEQSGNLVFTFKMASVASIILGLLSFFLPNTPPVKKGEKTTFGEIIGLDAIGLLKNKSYLLFFLASVAICIPLAFYYNFTNPFLNEVGMKGAAGVQSLGQVSETLFMLLMPLFFARLGVKKMLAIGMIAWVVRYLFFAFGNADSNYWMLIGGIVLHGICYDFFFVTGQIYTDRLAGEKFKSAAQGFITLATYGVGMLIGSIISGMVVNKYVVEGGHIWQSIWIIPAGIAGLVALLFLLFFSDKNKPVTEANTI Bacteroides thetaiotaomicron VPI-5482 Btheta 353287 BT3761 N-succinylglutamate synthase This gene is in an operon with and conserved cofit with other arginine synthesis genes. The traditional synthase (argA) was not found in the genome. This protein is 59% identical to Cabys_1732 which is reported to form N-acetylglutamate (PMID:28265262). However, Bacteroides are believed to use succinylated intermediates for arginine synthesis, as they have N-succinylornithine carbamoyltransferase (PMID:16704984) and N-succinylglutamate kinase (PhD thesis of Juan Manuel Cabrera Luque, 2010). The prior studies were of Bacteroides fragilis, but Bacteroides thetaiotaomicron has close homologs (the carbamoyltransferase is BT3717; the kinase is BT3395; mutants of all of these genes from B. thetaiotaomicron appear to be arginine auxotrophs) hypothetical protein (NCBI ptt file) MDTQQIDVMVADASHEVYVDTILETIRNAAAVRGTGIAERTHEYVATKMKEGKAIIALCGDTFAGFTYIESWGNKQYVATSGLIVHPDFRGLGLAKRIKQASFQLARLRWPKAKIFSLTSGAAVMKMNTELGYVPVTFNELTDDEAFWKGCEGCTNHDILAAKNRKFCICTAMLYDPTDPRNIKKEQERNNI Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_3845 Echvi_3845 N-succinylglutamate synthase This gene is in an operon with and conserved cofit with other arginine synthesis genes. The traditional synthase (argA) is not present. This protein is 63% identical to Cabys_1732 which is reported to be a N-acetylglutamate synthase (PMID:28265262). However, Bacteroidetes are thought to use succinylated intermediates for arginine synthesis (see PMID:32576650) N-acetylglutamate synthase and related acetyltransferases MTKSQFIIQTAGVQHCKYAETIVDEMALSAKARGTGIAKRSPDYIIQKMMEGKAVIALSKEGEWAGFCYIEAWGHGKFVANSGLIVSPNFRKSGLAREIKKAVFKLSRSKFPHAKIFGLTTGAAVMKINSELGYVPVSYSDLTDDEEFWKGCQSCVNYEILKSKNRQNCLCTAMLYVPKDQKKKEVAMKKDFGKNLNLFERLVRMKRAVFTGIKKKTIKTFELI Bacteroides thetaiotaomicron VPI-5482 Btheta 353392 BT3866 ammonium-dependent carbamoyl phosphate synthetase CarB2 (EC 6.3.4.16) Important for fitness when ammonia is added, and it seems to function without any glutaminase partner. BT0557 is a glutaminase component, but the fitness data suggests that BT0557 functions solely with BT0556 glutamine-dependent carbamyl phosphate synthetase (NCBI ptt file) MEKEIKKVLVLGSGALKIGQAGEFDYSGSQALKALKEEGISSVLVNPNIATIQTSEGIADKVYFLPVTTYFVEEIIKKERPDGILLAFGGQTALNCGAELYTQGILDKYGVKVLGTSVEAIMYTEDRDLFVKKLDEINMKTPVSQAVESMEDAIAAARKIGYPVMVRSAYALGGLGSGICANEEEFLKLAESSFAFSKQILVEESLKGWKEIEFEVIRDANDHCFTVASMENFDPLGIHTGESIVVAPTCSLDDKELKLLQELSAKCIRHLGIVGECNIQYAFNSDTDDYRVIEVNARLSRSSALASKATGYPLAFVAAKIALGYSLDQIGEMGTPNSAYLAPQLDYYICKIPRWDLTKFAGVSREIGSSMKSVGEIMSIGRSFEEIIQKGLRMIGQGMHGFVGNDDVHFDDLDKELSRPTDLRIFSIAQAMEEGYSIDRIHELTKIDPWFLGKLKNIVDYKAKLSTYNKVEDIPADVMREAKILGFSDFQIARFVLNPTGNMEKENLAVRAHRKALGILPAVKRINTVASEHPELTNYLYMTYAVEGYDVNYYKNEKSVVVLGSGAYRIGSSVEFDWCSVNAVQTARKLGYKSIMINYNPETVSTDYDMCDRLYFDELSFERVLDVIDLEQPRGVIVSVGGQIPNNLAMKLYRQSVPVLGTSPVSIDRAENRNKFSAMLDQLGIDQPAWMELTSLEEVKGFVEKVGYPVLVRPSYVLSGAAMNVCYDDEELENFLKMAAEVSKEYPVVVSQFLENTKEIEFDAVAQNGEVVEYAISEHVEFAGVHSGDATLVFPAQKIYFATARRIKKISRQIAKELNISGPFNIQFLARNNEVKVIECNLRASRSFPFVSKVLKRNFIETATRIMLDAPYSQPDKTAFDIDWIGVKASQFSFSRLHKADPVLGVDMSSTGEVGCIGDDFSEALLNAMIATGFKIPEKAVMFSSGAMKSKVDLLDASRMLFAKGYQIYATAGTAAFLNAHGVETTPVYWPDEKPGAENNVMKMIADHKFDLIVNIPKNHSKRELTNGYRIRRGAIDHNIPLITNARLASAFIEAFCELKLSDIQIKSWQEYK Bacteroides thetaiotaomicron VPI-5482 Btheta 351685 BT2157 periplasmic 3-ketoglycoside hydrolase Important for the utilization of palatinose, D-trehalose, D-leucrose, and possibly raffinose. This gene is in a conserved cluster for disaccharide catabolism via the 3-ketoglycoside pathway. A biochemical assay confirmed that it cleaves 3-ketotrehalose. According to the PFam curators, this family (DUF1080 or PF06439) has structural similarity to endo-glucanases. conserved hypothetical protein (NCBI ptt file) MKKVFYPLACCLAAGVLVSCSGQKKAGSAQEEQSANEVAVSYSKSLKAAEMDSLQLPVDADGYITIFDGKTFNGWRGYGKDRVPSKWTIEDGCIKFNGSGGGEAQDGDGGDLIFAHKFKNFELEMEWKVSKGGNSGIFYLAQEVTSKDKDGNDVLEPIYISAPEYQVLDNDNHPDAKLGKDNNRQSASLYDMIPAVPQNAKPFGEWNKAKIMVYKGTVVHGQNDENVLEYHLWTKQWTDLLQASKFSQDKWPLAFELLNNCGGENHEGFIGMQDHGDDVWFRNIRVKVLD Bacteroides thetaiotaomicron VPI-5482 Btheta 351686 BT2158 predicted periplasmic glycoside 3-dehydrogenase (EC 1.1.99.13) It was difficult to map insertions in this gene because of a paralog, but reexamination of the data suggests that this gene has a similar fitness pattern as the surrounding genes and is important for growth on trehalose, leucrose, palatinose, and raffinose. And a clean deletion mutant failed to grow on trehalose. It is probably involved in the 3-ketoglycoside pathway. It is a putative sugar dehydrogenase and has a TAT (twin arginine transport) signal. It is probably exported together with its NAD(P) cofactor, as with the glucose:fructose oxidoreductase Gfo. It's unclear what the electron acceptor could be. putative dehydrogenases and related proteins (NCBI ptt file) MSDFSRRKFLKTGAAALAGITIAPSSILGMSHGHVSPTDKLNLAAVGIGGMGHANINNVKGTENIVALCDVDWKYAKGVFDEFPNAKKYWDYRKMYDEMGKSIDGVIIATADHTHAIITADAMTMGKHVYCQKPLTHSVYESRLLTKLAASTGVVTQMGNQGASGEGTDLVCEWIWNGEIGEVTKVECATDRPIWPQGLNAPEKADRIPNTLNWDLFTGPAKLNPYNNVYHPWNWRGWWDYGTGALGDMACHILHQPFRALKLGYPTKVEGSSTLLLSACAPQAQHVKMIFPARDNMPKVALPEVEVHWYDGGMMPERPKGFPEGKQLMGPGGGLTIFHGTKDTLICGCYGEQPFLLSGRVPNAPKVCRRVTCSHEMDWVRACKEDKSNRVMPKADFSESGPMNEMVVMGVLAIRLQGLNKTLEWDGANMCFTNIGDNETLRTCIKDGFTIHDGHPSFNKTWTDPINAKQFAAELVKHNYREGWKLPDMPR Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_2929 Ga0059261_2929 oxygen-dependent methionine synthase, methyltransferase component MesD # Required for methionine synthesis in the absence of cobalamin. Contains the C-terminal domain of MetE (catalytic and homocysteine-binding) but not the N-terminal (folate-binding) domain. Requires MesX (Ga0059261_2928, DUF1852) and oxygen, but not 5-methyltetrahydrofolate. See https://doi.org/10.1101/2020.04.21.054031 methionine synthase (B12-independent) (EC 2.1.1.14) MNIVLPTSTAGSLPKPAWLAQPETLWSPWKLEGEELVAGKQDALRLAVEDQRQAGISIVGDGEQTRQHFVTTFIEHLSGVDFEKRETVRIRNRYDASVPTVVGAVSRPNPVFVDDAKFLRAQTDQSIKWTLPGPMTMIDTLYDAHYRSREKLAWEFARILNQEARELEAAGVDIIQFDEPAFNVFFDEANDWGIATLEKAAEGLTCETAVHICYGYGIKANTDWKKTLGSEWRQYEQTFPNLQKSKIDIVSLECHHSHVPMDLIELIRGKKVMVGAIDVASDTVETPEEVADTLRRALAFVDADKLYPSTNCGMAPLSRSVARGKLNALGAGAAIVRRELSA Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_2928 Ga0059261_2928 oxygen-dependent methionine synthase, putative oxygenase component MesX # Required for methionine synthesis in the absence of cobalamin, along with MesD (Ga0059261_2929). This system requires oxygen, but not 5-methyltetrahydrofolate. See https://doi.org/10.1101/2020.04.21.054031 Domain of unknown function (DUF1852) MSKSAFTFSIKSIAFDEDYRPADNTRITTNFANLARGESRQENLRNTLRMIDNRFNSLAHWDNPRGDRYSVELKIITAEMRIDSDGDGDVFPLIEILQTTIIDKKTGERIDGMVGNNFSSYVRDYDFSVVLPDYMKNHPNSGAPRDFGNLHGNLFKHFLNSSAYRDNFSKPPVICLSVSSSKTYHRTTNEHPVLGVEYRNDEFSATDEYFAKMGMKVRYFMPPNSVAPYAFYHIGDLLGDYTSLELVSTISVMETFQKIYRPEIYNANSAAAEHYQPSLKYQDYSLTRIVYDREERSRLAVEQGKFAEERFIKPYQAVLEQWSASFAA Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_2983 2-methylbutanoyl-CoA dehydrogenase (EC 1.3.8.5) Specifically important for utilizing L-Isoleucine, which is oxidized via 2-methylbutanoyl-CoA Butyryl-CoA dehydrogenase (EC 1.3.99.2) MIPNDDQQQIRDMARDFAQERLKPFAAEWDREHRFPKEAIGEMAGLGFFGMLVPEQWGGCDTGYLAYAMALEEIAAGDGACSTIMSVHNSVGCVPILNYGTDEQKERFLKPLASGAMLGAFALTEPQAGSDASGLKTRARLEGDHYVLNGCKQFITSGQNAGVVIVFAVTDPSAGKRGISAFIVPTDSPGYKVARVEDKLGQHASDTCQILFEDVKVPLANRLGEEGEGYRIALANLEGGRVGIASQSVGMARAAFEAARDYARERESFGKPIIEHQAVAFRLADMATQIAVARQMVHYAAALRDSGKPALVEASMAKLFASEMAEKVCSSALQTLGGYGYLNDFPVERIYRDVRVCQIYEGTSDIQRMVISRNL Pseudomonas stutzeri RCH2 psRCH2 GFF2392 Psest_2440 isobutyryl-CoA dehydrogenase (EC 1.3.8.5) Important for valine utilization as N source, and isobutyryl-CoA is an intermediate in valine catabolism. SEED annotated it as butyryl-CoA dehydrogenase, which is also expected to perform this reaction Acyl-CoA dehydrogenases MHDLELSEDQRMIRDMARDFARREIAPHAQAWEKAGWIDDTLVAQMGELGLLGMVVPEEWGGSYIDYVAYALAVEEISAGDGATGALMSIHNSVGCGPVLNYGSQAQKDEWLTELASGRAIGCFALTEPQAGSEAHNLRTRAELVDGHWVLNGSKQFCSNAKRSKLAIVFAVTDPELGKKGLSAFLVPTDTPGFAVERSEHKMGIRASDTCGVSLSDCRIPEANLLGERGKGLAIALSNLEGGRIGIGAQALGIARAAFEAALLYARERVQFGKPIAEHQSIANMLADMQTQLNAARLLILHAARLKSAGLPCLSEASQAKLFASEMAEKVCSQAVQIHGGYGYLEDYPVERYYRDARITQIYEGSSEIQRLLIARELANYAL Phaeobacter inhibens BS107 Phaeo GFF1616 PGA1_c16380 citrulline utilization hydrolase Specifically important for: L-Citrulline. This enzyme is distantly related to characterized arginine deiminases (see PF02274) and has conserved catalytic residues. It might be a citrullinase. Uncharacterized protein conserved in bacteria containing a pentein-type domain MSQLQAPGAVVMIRPHHFCSNPETRDDNAFQTLADDTADVTSAQAQAEFDGAVTALRGAGVSVHVFDDTGTETPDSVFPNNWFSTHAGGHVAVYPMYAANRRKERRWDVIELLKRDYRVQDVIDYSGLEQDGLALEGTGAMVLDHIGRIAYTVKSNRADPVLLERFCTHFNFEPMVFEARDAQGRDVYHTNVLMGIGTDYALICLDMITDPTRRAEVAARLEETGRRVIDLTPEQIAGFAGNALELTGHSRLLALSSRAAEVLRADQITIIERSATLLPLSIPTIETAGGSVRCMLAAIHLSPRERTQS Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_25635 AO353_25635 citrulline utilization hydrolase Specifically important for: L-Citrulline. This enzyme is distantly related to characterized arginine deiminases (see PF02274) and has conserved catalytic residues. It might be a citrullinase. amidinotransferase MQTTNTVLMIRPTRFSFNQDTAANNRFQRPAAAAEDVQLKALQEFDGYVAALREHGVEVMVHNDSEAPHTPDSIFPNNWWSSHPDGTLVLYPMQGHNRRLERDKGVLDWLRDAYRIEQLLDLSDLEQQEVFLEGTGSMVLDREQRICYAGYSTRTHAKALDQVVEHLGYELCAFNAVDRHGVPIYHTNVMMSVGRQLAVVCLESVSDLDERNALRSRLECSGKQVLTLSFDQLESFAGNMLEVHNAAGEPLLVMSRTAWRSLHADQRRMVEAYAKPLPVNIDTIERIGGGSARCMLAEVYLPKRVSPQEQH Pseudomonas simiae WCS417 WCS417 GFF3434 PS417_17580 citrulline utilization hydrolase Important on citrulline. This enzyme is distantly related to characterized arginine deiminases (see PF02274) and has conserved catalytic residues. It might be a citrullinase. amidinotransferase MQTTNTVLMIRPARFAFNPDTAINNRFQRQPLDPLGAQQKALEEFDGYVDTLRRHGVEVLVVQDTPAPHTPDSIFPNNWWSSHADGSLVLYPMEGQNRRLERNKGVLQVLEQRFAINSTIDLSHLEQQNIFLEGTGSMVLDRQHRISYACHSGRTHQDALRQFAERLDYQLCVFHAVDRHHAPIYHSNVMMSVGRDLSVVCLQALPDASERQGLERSLRDTGKDILALDFDQLEGFAGNMLEIHDRDGQPLLVMSASAWGALQPAQRQHVERHTRPVVVNIDNIERIGGGSARCMLAEVHLPARATVQ Caulobacter crescentus NA1000 Caulo CCNA_00857 CCNA_00857 D-xylose transporter Specifically important for D-xylose utilization. Also see PMC2168598 and PMC344409. May also be important for lactose utilization, which is not explained. glucose/fructose transport protein MASVSNAGPSAGMSADGGKVNMTFVAAIVAVATIGGFMFGYDSGVINGTQEGLESAFNLSKLGTGLNVGAILIGCAIGAFAAGRLADVWGRRTVMIISALLFVISAIGTGAAESSIVFIIFRLIGGLGVGAASVLCPVYISEVTPANIRGRLSSVQQIMIITGLTGAFVANYALAHTAGSSTAEFWLGLPAWRWMFWMQIIPAGVFFLCLLGIPESPRYLVAKGKDAQAEAILSRLFGAGQGAKKVEEIRASLSADHKPTFSDLLDPTTKKLRVILWAGLVLAVFQQLVGINIVFYYGSVLWQSVGFTEDDSLKINILSGTLSILACLLAIGLIDKIGRKPLLLIGSAGMAVTLGVLTWCFSTATTVNGALTLGDQIGLTALIAANLYVIFFNLSWGPVMWVMLGEMFPNQMRGSALAVCGFAQWIANFAISVSFPALAAASLPMTYGFYALSAVVSFFLVQKLVHETRGKELEAMQG Bacteroides thetaiotaomicron VPI-5482 Btheta 350320 BT0792 xylulokinase (EC 2.7.1.17) Specifically important for D-xylose utilization. xylulose kinase (xylulokinase) (NCBI ptt file) MFLLGYDIGSSSVKASLVNAETGKCVSSAFFPKTEAKIIAVNPGWAEQDPESWWENLKLSTQAIMAESGVSAAEIKAIGISYQMHGLVCVDKNQQVLRPAIIWCDSRAVPFGQQAFETIGEERCLSHLLNSPGNFTASKLAWIKQNEPAVYEQIYKIMLPGDYIAMKLSGDICTTVSGLSEGMFWDFKNNRVADFLMDYYGFDSSLIADIKPTFAEQGRVNAVAANELGLKEGTPITYRAGDQPNNALSLNVFNPGEIASTAGTSGVVYGVNGEVNYDPQSRVNTFAHVNHTMEQTRLGVLLCINGTGILNSWVKRNIAPEGISYNEMNVLASKAPIGSAGISILPFGNGAERMLNNKEIGCSIRGVDFNAHGKHHIIRAAQEGIVFSFKYGIDIMEQMGIPVKKIHAGHANMFLSSIFRDTLAGVTGATIELYDTDGSVGAAKGAGIGAGIYKDNNEAFATLDKLDVIEPNIAKRQEYADAYARWKYNINNDIITF Dinoroseobacter shibae DFL-12 Dino 3608248 Dshi_1652 glucose/maltose/trehalose/sucrose ABC transporter, substrate-binding component Related to alpha-glucoside transporter component aglE. Specifically important for utilization of D-glucose, D-maltose, D-trehalose, and sucrose. extracellular solute-binding protein family 1 (RefSeq) MRHTLHASAAALALSAGMAGAGGHLAFTPGEGEFNWDSYQAFAEATDLSGQDLSIFGPWLAGEADAFSNLVAFFNEATGANATYVGSDSLEQQIVIDAEAGSAPDLTVFPQPGLATTMAARGFLTPLPDGTDDWLRENYAAGQSWIDLGTYADGSGNDQLYGFFFNVNVKSLVWYIPENFEDFDYEVPETMEEFKALMDQMVEDGQTPLCVGLGSGGATGWPATDWVEDLMLRTQPPEVYDAWVSNEMPFDDPRVVAAIEEYGSFTRNDDYVVGNANDTASVDFRESPLGLFASPPACMMHRQASFIPAYFPEGTELGEDADFFYFPAFEEKDLGRPVLGAGTLFAITNENPAASAFIEFLKTPFAHEIMMAQDGFLTPFKGANPAAYASDTLRGQGEILTNATTFRFDGSDLMPGGVGAGTFWTGMVDYSSGAKSAADVASEIQASWESLK Dinoroseobacter shibae DFL-12 Dino 3608247 Dshi_1651 glucose/maltose/trehalose/sucrose ABC transporter, permease component 1 Related to alpha-glucoside transporter component aglF. Specifically important for utilization of D-glucose, D-maltose, D-trehalose, and sucrose. binding-protein-dependent transport systems inner membrane component (RefSeq) MHPAFQGLITIIIGVGGCVGYFYFANQFLDKVLYPAKGPKAGRNINRANQIRPWIFLFPALFVLLLYLGYPVVETLRLSLLERVPGGGYQWVGLDNYAQMASEPKFWEAMRNNMFWLIVVPALSTAFGLLAAQLTDRIKWGNVAKSIIFMPMAISFVGASVIWKLVYDGRPIEQEQIGILNAIIVGLGGDPVTFLTIPFWNNFFLMIVLVWVQTGFAMVILSAALRGIPEETIEAAIIDGASPLQIFFKIKVPQIMPTVVVVWTTITLVVLKVFDIVFAMTNGQWETQVLANYMFDKLFRANDWGVGSASAMVIMLLVTPILIWNIHSARKEMR Dinoroseobacter shibae DFL-12 Dino 3608246 Dshi_1650 glucose/maltose/trehalose/sucrose ABC transporter, permease component 2 Related to alpha-glucoside transporter component aglG. Specifically important for utilization of D-glucose, D-maltose, D-trehalose, and sucrose. binding-protein-dependent transport systems inner membrane component (RefSeq) MDNIAGSKSSLTWAVQLSVVGLVVLWLLPTFGLFVSSFRTVEQISSSGWWKAMFPSEQNLTLRAADPDDFRMPQGDLFVVKGNLFEDEGISEAEISVWGTSSRDVAAYTAGETADLGDGETITVQSNGAYVWSGTDDQISGRGQRVFVTATTPPEFTFANYENMLLDPNNSEGMARAFFNTLTVTIPATIIPILVAAFAAYALAWMEFPGRALLIALIVGLLVVPLQLALIPLLTLHNAIGIGKGYLGTWLAHTGFGMPLAIYLLRNYMVGLPRDIIENAKVDGATDFQIFTKIVLPLSFPALASFAIFQFLWTWNDLLVAKVFLIDATGQTTVMTNQIVELLGTRGGNWEILATAAFVSIAVPLLVFFSMQRFLVRGLLAGSVK Dinoroseobacter shibae DFL-12 Dino 3608244 Dshi_1648 glucose/maltose/trehalose/sucrose ABC transporter, ATPase component Related to alpha-glucoside transporter component aglK. Specifically important for utilization of D-glucose, D-maltose, D-trehalose, and sucrose. ABC transporter related (RefSeq) MADLKLTGVEKAYGDVKVLSNINLDIQQGELIVFVGPSGCGKSTLLRMIAGLEKITGGTLEIDGTVVNDVPPAQRGIAMVFQSYALYPHMTVRENMSFALKIAKKSQAEIDAAVEAAAEKLQLGQYLDRLPKALSGGQRQRVAIGRSIVRDPKVYLFDEPLSNLDAALRVATRLEIAQLKEAMPESTMVYVTHDQVEAMTLATRIVVLAGGGIAQVGSPLELYEKPENEFVAQFIGSPKMNLLPGKIIGTGAQTTVEMTDGGRAVSDYPSDDSLMGAAVNVGVRPEDMVEAAPGGDYVFEGKVAITEALGEVTLLYFEAPSGEDPTIGKLQGIHKDLKGQVTRLTAEPAKVHVFKDGVSLHYPHGKHVTFAPH Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_0566 Echvi_0566 TonB-dependent receptor for glucose (SusC-like) Specifically important for utilization of D-glucose. TonB-linked outer membrane protein, SusC/RagA family MAKLLSNFKLGVALLCLMASTLIPLSFAFGQSIQVTGKVTDADNGESIPGASISQKGTTKGTITDLDGNYSIEVSEGATLVFSFIGYSTQEVPVSGQSTIDVSMKTDIKGLEEVVVVGYGTQKKQDLTGAVSVVKMEEMTQQPSPQLTSQLQGRVSGVTITGSGQPGQAPEIKIRGVNTFGNNTPLFIVDGVPTPNINDINPNDVETMQVLKDAGAASIYGSRAANGVIIVTTKKGRGDVKVNYNMYIGSQQVQGGNPWDILSSQEMADLKFMALRNTNPGGTINDDQYGSGPDPVLPNYIAPVGAQTVDESLYNVNPYYTDPQALDNFYRIVEANKTGTNWFQEIFSPARIQSHNLSVNGGSDRANYFFSMSYFDQQGTLNNTYLKRYTIRSNTSYNVTDNIRIGENLTYSISENPTIDNLTEGSAIGMAFRQQPIIPVYDIMGNFAGSFGSGLGNAKNPVAIQERTKNNRGVASRLFGNVFAEVDFLEHFTARTSFGGQYYSNTYNRFQFPEYENSENLNVNQYTEGSNFNFNYTWTNTLTYKREFNEQHDLTVLLGTEAYRNNGRNMEAFTQGYFSFDPDYVTLTNGSGTQQHSSSVYKDALFSLFGRVDYTYNDKYILSATVRRDGSSRFLNEQYGVFPAVSAGWRISEESFMPENGWIDDLKLRGGYGQMGNQLNVAPGNAYSTYEGNRNASYYPIDGSNSTIQEGFQEQRIGNPDAKWERNINSNIGIDASFWQGKVQLTLDYYNKTVDDLLYNPEVIGTQGAAEPPYINIAKMTNKGFDMDASTYFILAPDLTFTTTLSFTTYSNEIVKIADGVPYFDQEGRRFNGSNIIRNQVGHPVSEFFGYQVVGFWNSEQEISDANASAAEATGDAEAVYQDGIGLGRFKYQDTNGDGVITPDDRTPLGNPNPKFTYGINLGLEYRNWDFSMFLYGVSGNDIWNNVKWWTDFYSSFQGAKSHTALYDSWTPENMNATAPIQETTGSFSTAGVPNSYFVENGSYLRARQTQIGYTFNQSFLDRYHIGGLRLYAQAANLFTITNYSGLDPEISGGTTSFGIDEGQYPNQRQFIFGLNLTF Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_0567 Echvi_0567 outer membrane binding protein for glucose (SusD-like) Specifically important for utilization of D-glucose. SusD family. MKYATIKYFILGMLLIGTLPSCSDEFLDQPALGALGDDVLATRDGVNKLLIGAYAALDGQGEGGTDALGGGNGWEAAPENWIYGTVAGGEASKGSFAGDQPAIDPIVNFYSSPSNGFFNTKWKATFEGIKRTNNVLKLLPNVPELTDSERQDIAGQARFLRGHFYFELKKMFNMVPWIDETTEDPNQPNDQDIWPMIEADFQFAYENLPPTQPEFARANKWAAAAYLGKTYLYQKKYQEANTIFKEVIASGVNPAGTKYALLDNFSDNFDAAKENNAETVFDIQMVANSGTGTISNSNSGNMLNFPYNSPFRCCGFYQPTQDLVNSFKTDPATGLPYLENYNQNPVKSDMGITSAQAFDPYTGSLDPRLDWTVGRRGVPYHDWGHHPGQSWVRDQTYGGPYAPKKTIYWQATQNLYADQSSWAPGTAINVHIIRFADIILMCAETEAHLGNLMEAMNLVNQIRERAMNPDGYLKTYIDESAPMDGFTNTPAANYTIELYTAAQFGSQEDALKAIYFERKLELAMEGHRFFDLVRWEIAEQELNAYFDYQGSITQDVKDGSFSAPKNNYYPIPQRQIDLSVKDGEPMLKQNPGYN Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS19360 HSERO_RS19360 2-keto-3-deoxyxylonate dehydratase (EC 4.2.1.141) Nearly identical to C785_RS13680 = WP_039786859.1, which was reported to be D-2-keto-3-deoxypentoate dehydratase by PMC6336799 (this is the same reaction). HSERO_RS19360 is also 55% identical to xylX from Caulobacter crescentus, which is also required for xylose utilization (PMC1855722) and is believed to have this activity as well. fumarylacetoacetate hydrolase MAHTFSLQAHLPEDHAQATLIGRIWQPGVGPVLVRIDADGAYDLTLIAATSSELLELDNPAAAVRSATNMTRIATLQELLDNADAAGRDTSRPWLLAPIDLQAVKASGVTFVASMLERVIEEQARGDAGKAESVRKAITAVIGDNLSSVVPGSPEAARLKEVLLDQGVWSQYLEVGIGPDAEIFTKAQPMSSVGLGDEVGIHPKSAWNNPEPEIVLAINSRGKVVGATLGNDVNLRDFEGRSALLLGKAKDNNASCAVGPFIRLFDANFSIDDVRRAELTMRVDGTEGFTLKGSSSMSMISRDPLQLVEHAIGPNHQYPDGLVLFLGTMFAPTQDRFGPGQGFTHQVADIVTISTPKLGALVNTVNFSDQTAPWTFGLTALFKNLADRKLI Pseudomonas simiae WCS417 WCS417 GFF4321 PS417_22130 glucose/xylose ABC transporter, ATPase component Specifically important for utilization of D-glucose 6-phosphate and D-xylose. Glucokinase (PS417_22685) is important for glucose-6-phosphate utilization, which implies that it is hydrolyzed to glucose before uptake. sugar ABC transporter ATPase MATLELRNVNKTYGAGLPDTLKNIELSIKEGEFLILVGPSGCGKSTLMNCIAGLETITGGAIMIGDQDVSGMSPKDRDIAMVFQSYALYPTMSVRENIEFGLKIRKMPQADIDAEVARVAKLLQIEHLLNRKPGQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPKEIYNNPANQFVASFIGSPPMNFVPLRLQRKDGRLVALLDSGQARCELALNTTEAGLEDRDVILGLRPEQIMLAAGEGDSASSIRAEVQVTEPTGPDTLVFVQLNDTKVCCRLAPDVAPQVGETLTLQFDPSKVLLFDANTGERLGTASSLPAQGHADNVAQFKGR Pseudomonas simiae WCS417 WCS417 GFF4322 PS417_22135 glucose/xylose ABC transporter, permease component 1 Specifically important for utilization of D-glucose 6-phosphate and D-xylose. Glucokinase (PS417_22685) is important for glucose-6-phosphate utilization, which implies that it is hydrolyzed to glucose before uptake. sugar ABC transporter permease MTSLASKPAISLSRIAIYAVLILAVLLYLVPLVVMLLTSFKTPEDISSGNLLSWPTVVTGIGWVKAWATVDGYFWNSIKITVPAVLISTAIGALNGYVLSFWRFKGSQLFFGLLLFGCFLPFQTVLLPASFTLGKMGLASTTTGLVFVHVVYGLAFTTLFFRNYYVSIPDALIKAARLDGAGFFTIFRQIILPMSTPIIMVCLIWQFTQIWNDFLFGVVFSSGDSQPITVALNNLVNTSTGAKEYNVDMAAAMIAGLPTLLVYVIAGKYFVRGLTAGAVKG Pseudomonas simiae WCS417 WCS417 GFF4323 PS417_22140 glucose/xylose ABC transporter, permease component 2 Specifically important for utilization of D-glucose 6-phosphate and D-xylose. Glucokinase (PS417_22685) is important for glucose-6-phosphate utilization, which implies that it is hydrolyzed to glucose before uptake. sugar ABC transporter permease MSSVAVFSKASPFDALQRWLPKLVLAPSMFIVLVGFYGYILWTFVLSFTNSTFLPTYKWAGLAQYARLFDNDRWWVASKNLAVFGGMFIGITLVIGVTLAIFLDQKIRREGFIRTIYLYPMALSMIVTGTAWKWLLNPGMGLDKLLRDWGWEGFRLDWLIDPDRVVYCLVIAAVWQASGFIMAMFLAGLRGVDQSIVRAAQIDGASMPRIYWSVVLPSLRPVFFSAVMILAHIAIKSFDLVAAMTAGGPGYSSDLPAMFMYSFTFSRGQMGMGSASAILMLGAILAIIVPYLYSELRTKRND Pseudomonas simiae WCS417 WCS417 GFF4324 PS417_22145 glucose/xylose ABC transporter, periplasmic substrate-binding component Specifically important for utilization of D-glucose 6-phosphate and D-xylose. Glucokinase (PS417_22685) is important for glucose-6-phosphate utilization, which implies that it is hydrolyzed to glucose before uptake. PS417_22145 is 88% identical to GtsA from P. putida, which is well known as a glucose transporter, but is also involved in xylose uptake in strain S12 (PMC3340264). sugar ABC transporter substrate-binding protein MNAINRLAVAISIASLFPLSAFAADSKGTVEVVHWWTSGGEKAAVDVLKAQVEKDGFVWKDGAVAGGGGATAMTVLKSRAVAGNPPGVAQIKGPDIQEWASTGLLDTDVLKDVAKEEKWDSLLDKKVSDTVKYEGDYVAVPVNIHRVNWLWINPEVFKKAGITKNPTTLQEFYAAGDKLKAAGFIPLAHGGQPWQDSTVFEAVVLSVMGADGYKKALVDLDNGALTGPEMVKALTELKKVATYMDVDGKGQDWNLEAGKVINGKAGMQIMGDWAKSEWTAAKKVAGKDYECVAFPGTDKAFTYNIDSLAVFKQKDKGTAAGQQDIAKVVLGENFQKVFSINKGSIPVRNDMLNKMDSYGFDSCAQTAAKDFLADAKTGGLQPSMAHNMATTLAVQGAFFDVVTNYINDPKADPADTAKKLGAAIKSAK Pseudomonas simiae WCS417 WCS417 GFF1743 PS417_08865 large component of pyruvate transporter (actP-like) Specifically important for pyruvate utilization. acetate permease MIRRLLAILGASIFAPAVWAADALTGEVHKQPLNVSAIVMFVVFVGATLCITYWASKRNKSAADYYAAGGKITGFQNGLAIAGDYMSAASFLGISALVYTSGYDGLIYSIGFLVGWPIILFLIAERLRNLGKYTFADVASYRLGQTQIRSLSACGSLVVVAFYLIAQMVGAGKLIQLLFGLDYHVAVILVGILMVLYVLFGGMLATTWVQIIKAVLLLSGASFMALMVMKHVNFDFNALFSEAIKVHPKGEAIMSPGGLVKDPISAFSLGLALMFGTAGLPHILMRFFTVSDAKEARKSVFYATGFIGYFYILTFIIGFGAILLVSTNPAFKDAAGALMGGNNMAAVHLANAVGGSIFLGFISAVAFATILAVVAGLTLAGASAVSHDLYASVIKKGKANDKDEIRVSKITTIALGVLAIGLGILFESQNIAFMVGLAFSIAASCNFPVLLLSMYWKNLTTRGAMIGGWLGLVSAVGLMVLGPTIWVSILHHEKAIFPYEYPALFSMIIAFVGIWFFSITDKSSAAEKERALYFPQFVRSQTGLGSSGAVSH Pseudomonas simiae WCS417 WCS417 GFF1742 PS417_08860 small component of pyruvate transporter (yjcH-like) Specifically important for pyruvate utilization. 59% identical to E. coli yjcH. membrane protein MNDSIYLSIQNSPRFKELVRKRERFAWILSAIMLGLYSAFILLIAYGPQLLGAKISPGSSITWGIPLGVGLIVSAFVLTGIYVRRANGEFDDLNNAILKEAAQ Azospirillum brasilense Sp245 azobra AZOBR_RS02940 AZOBR_RS02940 large component of pyruvate transporter (actP-like) Specifically important for pyruvate utilization. actetate permease MRSLVNRVGVAAVAAGALIPASVHAAAVEGAVQKQATNFSAIVMFLVFVLATLGITYWAARRTKSAKDFYAAGGGITGFQNGLAIAGDYMSAASFLGIAGLVYTSGFDGLIFSVGWLVGWPIILFLVAERLRNLGKYTFADVASYRFQQTPMRTMAACGSLATVTFYLIAQMVGAGKLIQLLFGMDYLWAVVIVGVLMIAYVTFGGMLATTWVQIIKAVLLLSGASFMAFAVLAKFGFSPEAMFSTAVQVHPKATGIMAPGALITDPVSAISLGMALMFGTAGLPHILMRFFTVSDAKEARKSVFYATGFIGYFYILTFIIGFGAIVLLLAPDATGAYPFLDAAKLAAAGGKPNPSMIIGGSNMAAIHTAHAVGGDLFFGFISAVAFATILAVVAGLTLAGASAVSHDLYASVIAKGRASEHDEIRVSKITTVIIGIVSIFLGIAFENQNVAFMVGLAFVIAASANFPVLLMSMFWSRMTTRGAVLGGWIGLVSSVSLLIMGPTVWKSVLGNPAALFPYDNPGVFTIPLSFLAIWFFSITDNSKAAQDEREAYKAQYIRSQTGLGAEGASAH Azospirillum brasilense Sp245 azobra AZOBR_RS02935 AZOBR_RS02935 small component of pyruvate transporter (yjcH-like) Specifically important for pyruvate utilization. 54% identical to E. coli yjcH. membrane protein MKENAQRILANPKFQELVQKRSAFAWTLSIAMLVIYFGFILLVAFGKGFLGTPIGSGVTTWGIPVGLFTIISAFILTGIYVHRANGEFDELNRQIMEESK Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_3673 large component of pyruvate transporter (actP-like) Specifically important for pyruvate utilization. Acetate permease ActP (cation/acetate symporter) MIRRLMALLSIAAFAPGVWAAEALTGAVQKQPLNVSAILMFVAFVGATLCITYWASKRNNSAADYYAAGGKITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSIGFLVGWPIILFLIAERLRNLGKYTFADVASYRLGQTQIRSLSACGSLVVVAFYLIAQMVGAGKLIQLLFGLDYHVAVILVGILMCMYVLFGGMLATTWVQIIKAVLLLSGASFMALMVMKHVNFDFNALFSEAIKVHPKGEAIMSPGGLVKDPISAFSLGLALMFGTAGLPHILMRFFTVSDAKEARKSVLYATGFIGYFYILTFIIGFGAILLVSTNPAFKDAAGALMGGNNMAAVHLANAVGGSVFLGFISAVAFATILAVVAGLTLAGASAVSHDLYASVIKKGKANEKDEIRVSKITTIALAVLAIGLGILFEKQNIAFMVGLAFSIAASCNFPVLLLSMYWKKLTTRGAMVGGWLGLVSAVGLMVLGPTIWVQILGHEKAIFPYEYPALFSMAIAFVGIWFFSVTDKSAEGVNERALFFPQFVRSQTGLGASGAVSH Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_3672 small component of pyruvate transporter (yjcH-like) Specifically important for pyruvate utilization. 62% identical to E. coli yjcH. Putative membrane protein, clustering with ActP MNDSIYLSIQNSPRFKELVSKRERFAWILSAIMLGLYSGFILLIAYGPHILGAKISPESSITWGIPIGVGLIVSAFVLTGIYVRRANGEFDDLNNAILKEAQQ Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5849 large component of pyruvate transporter (actP-like) Important for pyruvate utilization. Acetate permease ActP (cation/acetate symporter) MIRRLLALLSIAAFAPGAWAAEALTGAVQKQPLNVAAILMFVAFVGATLYITYWASKKNNSAADYYAAGGKITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSIGFLVGWPIILFLIAERLRNLGKYTFADVASYRLGQTQIRSLSASGSLVVVAFYLIAQMVGAGKLIQLLFGLDYHVAVILVGILMCLYVLFGGMLATTWVQIIKAVLLLSGASFMALMVMKHVNFDFNMLFAEAVKVHPKGEAIMSPGGLVKDPISAFSLGLALMFGTAGLPHILMRFFTVSDAKEARKSVLYATGFIGYFYILTFIIGFGAILLVSTNPAFKDAAGALLGGNNMAAVHLANAVGGSIFLGFISAVAFATILAVVAGLTLAGASAVSHDLYASVIRKGRVNEKDEIRVSKITTIALAVLAITLGILFEKQNIAFMVGLAFSIAASCNFPVLLLSMYWKKLTTRGAMIGGWLGLVSAVGLMILGPTIWVQIMGHEKAIFPYEYPALFSMAIAFVGIWFFSITDKSAEGANERALFFPQFVRSQTGLGASGAVNH Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5848 small component of pyruvate transporter (yjcH-like) Important for pyruvate utilization. 58% identical to E. coli yjcH. Putative membrane protein, clustering with ActP MNDSIYLSIQNSPRFKELVRKREKFAWILSAIMLGLYSGFILLIAYGPHILGAKITPESTMTWGIPIGVGLILSAFVLTAIYVRRANGEFDDLNNAILKEAQQ Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS20515 RR42_RS20515 large component of pyruvate transporter (cstA-like) Specifically important for pyruvate utilization. 70% identical to E. coli cstA, which is involved in pyruvate transport (PMID:29358499) carbon starvation protein A MNRIGQHLVWLAVAILGAFAFATVALSRGEAVSALWIVVAAICIYLIAYRYYSKFIAEKVMQLDPKRMTPAWRHNDGLDYVPTNKAVLFGHHFAAIAGAGPLVGPVLAAQMGYMPGMLWILAGVVFAGAVQDFMVLFISTRRDGRSLGDLIKSEMGTVPGMIALFGCFMIMIIILAVLALIVVKALAGSPWGTFTVGVTIPIALFMGIYTRYIRPGRIGEVSVIGFVLLMLAIIGGQYVHESAVLAPLFTYDGKALTWMLIIYGFIAAVLPVWLLLAPRDYLSTFLKIGTIIALAIGILIVAPELKMPAFTQFAKGGGPVWSGNLFPFLFITIACGAVSGFHALISSGTTPKLLESEAHMRFIGYGAMLAESFVAIMALVAASVIEPGVYFAMNSPAAVIGTSPESVAQVVSGWGFVITPDVLIQTAKDVGENSIISRAGGAPTLAVGIAHILHQVVGGQAMMAFWYHFAILFEALFILTAVDAGTRAGRFMLQDLLGSFVPSFRRTDSLPANLIATALTVSFWGYFLYQGVVDPLGGINTLWPLFGISNQMLAAVALVLGTCVLVKMKRGQYAWVTLVPTIWLLICTLTAGWQKLFDADPKVSFLTHAAKFSDAIAQGKVLAPAKSMEQMHRIVFNDYLDAGLCALFMFVVLSIVFYGFKTAMKARAENRPTDRETPFEPMPASASAQH Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS20510 RR42_RS20510 small component of pyruvate transporter (ybdD-like) Specifically important for pyruvate utilization. 58% identical to E. coli ybdD, which is involved in pyruvate transport (PMID:29358499) hypothetical protein MLEQLGTMGRYLGQSLRLMVGLPDYQTYVAHMEATHPEREPMTYEAFFRERQEARYGGGQGKCC Marinobacter adhaerens HP15 Marino GFF1281 HP15_1251 large component of pyruvate transporter (actP-like) Important for pyruvate utilization. Distantly related to E. coli actP. sodium: solute symporter family protein MSQFAINIIFVGGSFLLYIAIAIWAKAGSTSDFYVAGGGVHPITNGAAIGADWMSAASFISMAGLIAAGGYANSTFLMGWTGGYVLLAMLLAPYLRKFGKFTVPEFIGDRFYSKNARLVAVICLIVASVTYVIGQMAGAGVAFSRFLEVDSTVGLMIAAVVVFVYAVMGGMKGITYTQVAQYCVLIVAYTIPAVFISLQLTGNPIPGLGLFSTHVDSGMPILSKLNQVITDLGFNEYTADIDNKLNMVLFTLSLMIGTAGLPHVIIRFFTVPKVADARWSAGWALVFIALLYLTAPAVASMARLNLMTTIYPDGTSAEPIQYDERPNWIKEWEITGLIQFTDKNEDGRIQLYNDSEAFAPTAEARGWNGNELVVNRDILVLANPEIANLPGWVIGLIAAGGLAAALSTAAGLLLAISSAVSHDLIKGSINPAISEKGELLAARISMAVAIVVATYLGANPPGFAAQVVALAFGIAAASLFPALMMGIFSKRVNNTGAIAGMLSGLTFTLVYIFVYKGWLFIPGTNNLPDTPDNWVLGISPLSIGAIGAIVNFAVAFIVSNATEEPPVEIQELVESVRYPRGAGQAQDH Marinobacter adhaerens HP15 Marino GFF1282 HP15_1252 small component of pyruvate transporter (TIGR03647) The data for HP15_1252 is noisy, but it is important for pyruvate utilization, and is 74% identical to Psest_0346, which is also important for pyruvate utilization. HP15_1252 belongs to TIGR03647, which was predicted to be the small subunit of a transporter. membrane protein containing probable solute: sodium symporter, small subunit domain MSAGHSYDAEAYWKANLRLIFGSLIVWALVSYGFAILLRPMLAGIPIGGTDLGFWFAQQGSILTFIALIFHYAWRMNKIDEKFGVHEE Pseudomonas stutzeri RCH2 psRCH2 GFF345 Psest_0346 small component of pyruvate/D-alanine transporter (TIGR03647) Important for utilization of D-alanine and pyruvate, along with Psest_0347. Belongs to TIGR03647, which was predicted to be the small subunit of a transporter. putative solute:sodium symporter small subunit MADNDKENAAAYWKANVRLITWSLVVWALVSYGFGILLRPLVAGIPVGGTDLGFWFAQQGSIITFIAIIFHYAWRLNKLDKEFGVEE Pseudomonas stutzeri RCH2 psRCH2 GFF346 Psest_0347 large component of pyruvate/D-alanine transporter (actP-like) Important for utilization of D-alanine and pyruvate, along with Psest_0346. probable sodium:solute symporter, VC_2705 subfamily MSQYWINMLFVGASFLLYIGIAVWARAGSTKEFYVAGGGVHPVTNGMATAADWMSAASFISMAGLIASGGYATSVYLMGWTGGYVLLAMLLAPYLRKFGKFTVPDFIGDRFYSRGARLTAVVCLILISVTYVIGQMAGAGVAFSRFLEVSNSAGIWIAAAIVFAYAVFGGMKGITYTQVAQYIVLIIAYTIPAVFIAMQLTGNPIPMFGMFGTHVDSGVPLLDKLDQVVTDLGFAAYTADVDNKLNMFLFTLSLMIGTAGLPHVIIRFFTVPKVADARWSAGWTLVFIALLYLTAPAVASMARLNLVNTIYPEGPQAEAIRYEDRPEWVQTWERTGLIKWEDKNADGRVQMYNDANAKFTPTATERGWNGNELTVNNDIIVLANPEIANLPGWVIGLIAAGAIAAALSTAAGLLLAISSAISHDLIKTLINPKISEKNEMLAARLSMTAAILLATWLGLNPPGFAAQVVALAFGLAAASLFPALMMGIFSKRVNSKGAVAGMLVGVISTAVYIFLYLGWFFIPGTASIPNTPDQWWMGISPQAFGAVGAMLNFAVAYAVSMATEAPPQEIQDLVESVRTPKGAGVALDH Pseudomonas stutzeri RCH2 psRCH2 GFF3020 Psest_3078 L-proline:Na+ symporter Specifically important for proline utilization. 76% identical to PutP (Q9I5F5) from P. aeruginosa. sodium/proline symporter MSISTPTLITFLIYIAAMILIGFVAYRATKNFDDYILGGRSLGSFVTALSAGASDMSGWLLMGLPGAIFVAGLSESWIAIGLIVGAWLNWLFVAGRLRVHTEHNHNALTLPDYFSHRFEDESRMLRIFSALVILVFFTIYCASGVVAGARLFESSFGVPYEYALWIGAAATILYVFIGGFLAVSWTDTVQATLMIFALLITPVFVILALGDMGAAMDTIATQNPAAFDMFSGLSFVAIISLLAWGLGYFGQPHILVRFMAADSIKTIPNARRIGMAWMILTLAGAVAVGFFGIAYFAGHPEQAGAVSQNGERVFMELVKILFNPWVAGIILSGVLAAVMSTLSAQLLVSSSALTQDFYKAMLRKSASQTELVWVGRGMVLLIALIAIGIASNPESKVLGLVSYAWAGFGAAFGPVVLISLLWKRMTRNGALAGMLVGAVTVVVWKEFIGLGLYEIIPGFILASIAIFVVSKMGAEPAPSIIKRFEEADADYHAG Sinorhizobium meliloti 1021 Smeli SMc03061 SMc03061 ABC transporter for D-maltose/D-trehalose/sucrose, substrate-binding component (AglE) Specific phenotype on D-Maltose monohydrate; D-Trehalose dihydrate. Also mildly important for D-cellobiose utilization, which has its own ABC transporter, so the cause is unclear. Also reported to transport sucrose (PMID:10400573, PMID:12003938) alpha-glucoside ABC transporter periplasmic-binding protein MKRSLLIGVAAFALLAGTAGLAGTAGAADLKFKPGEDSRFNWASLEEFKKGHDLKGQTLTIFGPWRGEDEALFKSVYAYFVEATGVELKYSSSENYEQQIVIDTQAGSPPDVAILPQPGLIADLAAKGLLTPLGDETKQWLLDNYAAGQSWVDLSTYNGKDGTSALYAFPYKIDVKSLVWYVPENFEDAGYEVPKTMEELKALTEKIAEDGEKPWCIGLGSGGATGWPATDWVEDLMLRTQPAETYDKWVKNEIPFTDAAVTGALEEFGWFARNDAFVDGGAAAVASTDFRDSPKGLFSSPPKCYLHHQASFIPSFFPEGKVVGEDADFFYMPPYESKKELGNPVLGAGTLAMITKDTPAARAFIEFLKTPIAHEVWMAQTSFLTPYKSVNVDVYGNPPLKKQGEILLNATTFRFDGSDLMPGKIGAGAFWTGMVDFVGGKSSADVAAGVQKAWDSIK Sinorhizobium meliloti 1021 Smeli SMc03062 SMc03062 ABC transporter for D-maltose/D-trehalose/sucrose, permease component 1 (AglF) Specific phenotype on D-Maltose monohydrate; D-Trehalose dihydrate. Also mildly important for D-cellobiose utilization, which has its own ABC transporter, so the cause is unclear. Also reported to transport sucrose (PMID:10400573, PMID:12003938) alpha-glucoside ABC transporter permease MEQLIAAILTMVAGVLVCAAYFWSTNLVLDWIFPSKGKFGAVASRNLRIANSIRPWLFLAPALLALTLYLVYPVVQSVWLSLHGRGGQNFVGLSNYSWMINDGEFRQSIFNNFLWLLVVPALSTFFGLIIAALTDRIWWGNIAKTLIFMPMAISFVGAAVIWKFIYDYRAAGSEQIGLLNAIVVALGGEPQAWITLPFWNNFFLMVILIWIQTGFAMVILSAALRGIPEETIEAAVIDGANGWQIFFKIMVPQIWGTIAVVWTTITILVLKVFDIVLAMTNGQWQSQVLANLMFDWMFRGGGDFGRGAAIAVVIMILVVPIMIWNIRNATRESGGH Sinorhizobium meliloti 1021 Smeli SMc03063 SMc03063 ABC transporter for D-maltose/D-trehalose/sucrose, permease component 2 (AglG) Specific phenotype on D-Maltose monohydrate; D-Trehalose dihydrate. Also mildly important for D-cellobiose utilization, which has its own ABC transporter, so the cause is unclear. Also reported to transport sucrose (PMID:10400573, PMID:12003938) alpha-glucoside ABC transporter permease MNPSRRSPLTWAVHLSVLLLVLLWTLPTAGLLISSLRDKDQLAVSGWWTALSSSSRNAVVRAPSAEDQVERDGKFVISGNLLEGRGEVSAFGFSSREPTKFKPGETAELNDGERLTVQSDGSFEIVSDQRMEGSRGQRIFFTATTPPRFTLDNYAEVLSAAGIGRSFLNSLTVAVPSTVIPILIAAFAAYALAWMPFPGRAVLLAVVVGLLVVPLQMSLIPLLQLYNGVGAFFGVSAKTYMGIWLAHTGFGLPLAIYLLRNYMAGLPREIMESARVDGASDFDIFVKIILPLSFPALASFAIFQFLWTWNDLLVAIVFLGAGDDKLVLTGRLVNLLGSRGGNWEILTASAFITIVVPLIVFFALQRYLVRGLLAGSVKGG Sinorhizobium meliloti 1021 Smeli SMc03065 SMc03065 ABC transporter for D-maltose/D-trehalose/sucrose, ATPase component (AglK) Specific phenotype on D-Maltose monohydrate; D-Trehalose dihydrate. Also mildly important for D-cellobiose utilization, which has its own ABC transporter, so the cause is unclear. Also reported to transport sucrose (PMID:10400573, PMID:12003938) alpha-glucoside ABC transporter ATP-binding protein MTGLLLKDIRKSYGAVDVIHGIDLDIKEGEFVVFVGPSGCGKSTLLRMIAGLEEITGGDMFIDGERVNDVPPSKRGIAMVFQSYALYPHMTVYDNMAFGMRIARESKEEIDRRVRGAADMLQLTPYLDRLPKALSGGQRQRVAIGRAICRNPKVFLFDEPLSNLDAALRVATRIEIAKLSERMSDTTMIYVTHDQVEAMTLADRIVVLSAGHIEQVGAPLELYERPANLFVARFIGSPAMNVIPATITATGQQTAVSLAGGKSVTLDVPTNASENGKTASFGVRPEDLRVTEADDFLFEGTVSIVEALGEVTLLYIEGLVENEPIIAKMPGIARVGRGDKVRFTADKAKLHLFDTNGQSYRA Sinorhizobium meliloti 1021 Smeli SM_b20325 SM_b20325 ABC transporter for D-trehalose/D-maltose/sucrose, substrate-binding component (ThuE) Specific phenotype on trehalose, but also reported to transport maltose and sucrose (PMID:12003938; also PMC1635973) trehalosemaltose-binding protein MNVKPFVRTLISCAAIAGAIDLAAAAELSMAANSTGKNLSFLRDQIARFEKETGHKVNLVTMPASSSEQFSQYRLWLAAGNKDVDVYQTDVIWAPQLAEQFVDLTEATKDVVGEHFPSIIQSQTVNGKLVALPFYTDAPALYYRKDLLDKYGKTPPKTWDELAATAKEVQDKERAAGSADIWGFVFQGNAYEGLTCNALEWIKSSGGGQIIEPDGTISVNNEKAAAAVEKVKEWIGTIAPKGVLAYQEEESRGVWQTGNAVFMRNWPYAYALGNGDDSAVKGKFEVAPLPAATDGDQPSSTLGGWNLAVSKYSDEQEAAIAFVKFLGSAETQKVRAIELSNLPTIAALYDDPEVAAAQPFMPHWKPIFQSAVPRPSAVAKVKYNEVSSKFWSAVHNTLSGNGTAAENLELLEVELTELKGDAW Sinorhizobium meliloti 1021 Smeli SM_b20326 SM_b20326 ABC transporter for D-trehalose/D-maltose/sucrose, permease component 1 (ThuF) Specific phenotype on trehalose, but also reported to transport maltose and sucrose (PMID:12003938; also PMC1635973) trehalosemaltose transporter permease MTDLSLADRPAALAHGGRIGSDLQAQRVRSAWLFLAPTFLVLALVAGWPLIRTIYFSFTNASLTNLSGAEFVGFANYLSWITLKSGRTIYRGLLADPAWWNAVWNTLKFTVLSVSIETALGLIVALVLNAQFPGRGLVRAAILIPWAIPTIVSAKMWAWMLNDQFGILNDMLIGLGLIGEKIAWTASPDTAMIAELIVDVWKTTPFMALLILAGLQMVPGDIYEAAKIDGVHPVRVFWRVTLPLIRPALMVAVIFRMLDALRIFDLIYVLTPNNAQTKTMSVMARENLFDFDKFAYGAAASTMLFLIIATITILYMWLGRLNLSGGER Sinorhizobium meliloti 1021 Smeli SM_b20327 SM_b20327 ABC transporter for D-trehalose/D-maltose/sucrose, permease component 2 (ThuG) Specific phenotype on trehalose, but also reported to transport maltose and sucrose (PMID:12003938; also PMC1635973) trehalosemaltose transporter permease MVVAIAKRTAFYALVAVIILVAVFPFYYAILTSLKSGTALFRIDYWPTDISLANYAGIFSHGTFVRNLGNSLLVATLVVAISLLLAVTAAYALARVRFRGRGLLLLTILSVSMFPQIAVLAGLFELIRFVGIFNTPLALIFSYMIFTLPFTVWVLTTFMRDLPIEIEEAAIVDGASPWVVITRVFMPLMWPALVTTGLLAFIAAWNEFLFALTFTSSNTQRTVPVAIALLSGGSQFEIPWGNIMAASVIVTVPLVVLVLIFQRRIISGLTAGGVKG Sinorhizobium meliloti 1021 Smeli SM_b20328 SM_b20328 ABC transporter for D-trehalose/D-maltose/sucrose, ATPase component (ThuK) Specific phenotype on trehalose, but also reported to transport maltose and sucrose (PMID:12003938; also PMC1635973) trehalosemaltose transporter ATP-binding protein MAELQLRDIRKSFGAFDVIKGVSMEIKPGEFMVFVGPSGCGKSTLLRLIAGLEEITSGTLAFDGQIVNQLTPSRRGIAMVFQSYALYPHMTVYENMAFGMQLAGKDKQQCRKRVEAAAEMLQLTPYLERLPRQLSGGQRQRVAIGRAIVRDPKVFLFDEPLSNLDAALRVATRLEIAKLHRSMHKTTMIYVTHDQVEAMTLADRICVLRDGLVEQIGTPLELYETPNSVFVAGFIGSPKMNFLSGAFAEPYKADTIGIRAEHLEIDEQGGEWSGTVIHSEMLGSDSYIYLDIGTGEPVIVRESGIAKHQPGQTIRISPAAGQVHRFDAGGRALGRMQMRGAA Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_28590 AO356_28590 sucrose alpha-glucosidase (EC 3.2.1.48) Specifically important for sucrose utilization; sucrose is probably taken up by thuEFGK-like AO356_28570:AO356_28585 glycosyl hydrolase family 32 MTLSLNSLSNPMPASLEHAQQALRDGLSRLIHDYRPDYHLAPPTGWMNDPNGVVFFRGEYHVFYQHHPFDAKWGPMYWGHAKSADLVHWQHLPIALAPGDDFDRDGCFSGSAVVCGDTLALIYTGHTWLGEVGDERLIRQVQCLATSVDGVRFVKHGAVIEDAPQAAIMHFRDPKVWQEDGYWYLIAGARLGDTPLLPLYRSTDLRAWEFLDYVSRGTDGDGYMWECPDLFRLDGRDVLLYSPQGMQPAGYERLNKYQTGYRIGHLDSEWHFSGGPFIELDNGHDFYAAQTLVAADGRRLVWAWLDMWESPMPSQAHHWCGMLGLPRELELQGDRLGVFPARELVALRQAPLPSIAPWGESGSRWVPQVSGDRLEIHVHLDLLDCTEGHLGIALRCSADEQEQTLLYYDASLRRLVLDRSRSGAQVSGQRSVPIEPAQTQLHLRVFLDRSSIEVFEQSGRFSLSSRLYPRPDSLGVKLLASGTGGHVAISNAWPLASGWL Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_5112 sucrose ABC transporter, substrate-binding component Specific phenotype on sucrose Maltose/maltodextrin ABC transporter, substrate binding periplasmic protein MalE VGAELQLCKEAVQAWSKQTGNNVEVVSTPNSATERLSFYQQILSAQSSDIDIIQIDMVWPGMLAKHLLDLREVLPANATQGYFQAQVDNATVNGRLVTMPWFTDSGLLYYRKDLLEKYNQQVPRTWEEMTATARNIQQAERTAGNPNAWGYIFQGRAYEGLTCNALEWISSQPEGGLVNSRGDIVVNSQASRTALTLAKSWVGDISPRGVLNYTEEEGRGVFQSGNALFMRNWPYVWALVQGQDSAVKDKVGVAPLPRGGETGTHASTLGGWGLAVSRYSAHPKLAAELVSYLTSAQEQKHRALIGAYNPVIESLYQDPELLAAMPYYAQLHSILNDGVMRPASITADRYPRVSNAFFDRVHGVLAGELPVDQALAELESELTRIKRRNW Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_5113 sucrose ABC transporter, permease component 1 Specific phenotype on sucrose Maltose/maltodextrin ABC transporter, permease protein MalF VRAAWLFLTPMLLCLALVAAWPLLRTFWFSLTDANLADTGGGTFIGFGNYLFHNGSSWSGILVDPQWWNAVRNTLYFTVVSVGLEVVLGLLVALLLNIKFTGRALVRALILIPWAIPTIVSAKIWSWMLNDQFGIINHLMLSLGLIDAPLAWTADADLSMWAVIIVDVWKTVPFVTLLMLAALQMLPSDCYEAARVDGIHPLKVFWRVTLPLLMPALLVAAIFRILDSLRVFDVIYVLTSNSSSTMSMSVYARQHLVEFQDVGYGSAASTLLFLVVAVIALLYLYLGRRQLEVRS Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_5114 sucrose ABC transporter, permease component 2 Specific phenotype on sucrose Maltose/maltodextrin ABC transporter, permease protein MalG MNLRLLKKALLRLGFWCLIGVLLLYAVFPFYYAIVTSLKPSSALFEVSYWIENPDFSNYAAVLNQASFLRAIGNSLVVALCVVTLALFLSLTAAYALGRVKFRGRGTVLMMVLGVSMFPQVAVLSGLFEVIRALGLYNTSWALILSYTIFTLPFTVWVLTTFMGQLPHELEEAAIMDGASPWVTLTRVLLPLLWPALVTTGLLAFIAAWNEFLFALTFTLTDTQRTVPVAIALISGGSPHELPWGLLMAASVVVTVPLVILVLIFQRRIVSGLTAGALKG Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_5115 sucrose ABC transporter, ATPase component Specific phenotype on sucrose Maltose/maltodextrin transport ATP-binding protein MalK (EC 3.6.3.19) VIKLKLDNVNKQLGGMRILRDVSLEIAAGEFVVFVGPSGCGKSTLLRLIAGLDSICGGDLLIDGRRVNDLEPRERGVGMVFQSYALYPHMSVYDNISFGLKLAKTDKTSLRERVLKTAQILQLDKLLQRKPKELSGGQRQRVAMGRAMAREPDILLFDEPLSNLDASLRVQMRNEIARLHDRLGSTMIYVTHDQVEAMTLADKIVVLNGGRVEQVGSPRELYERPASRFVAGFLGSPRMNFLSARLQTPGETSLVDTLVWGITSLPFDSSNLAAGTPLSLGIRPEHVSLKAADGTAGVVVTAVEYLGSETYVHLETGQDEPLICRCEVSAGWQAGDRVELLLDLDNLHLFDADGVALSRHPHAIETLPAGVPLRSARASAL Azospirillum brasilense Sp245 azobra AZOBR_RS32335 AZOBR_RS32335 fructose-specific PTS system (fructose 1-phosphate forming), EII-B'BC components (FruA) Specific phenotype on fructose. PTS fructose transporter subunit IIBC MANMLAVIAAGDLSTQAVLAAEALRKAAAALGHTIQVEVRSSLGVRNTLPTGAAQGAQGVILVGSGDLGEERFAGLKRSAAALDAVLRDARAVLEQALATAPAQAPAQTGTKKIVAITSCPTGIAHTFMAAEGIQQAAQALGHAVRVETQGSVGARDTLTEQEIREADVVLIAADTQVDLARFAGKRVFKSGTKPAINDGRALVERALAEAQPHGTAPALADGVAAGKAAKAEHAAAQRSGPYKHLMTGVSFMLPFVVTGGLLIAIAFALGGIYVFEDSQQGTLGNALFQIGAKGAFALMVPALAGYIAFSIADRPGITPGMVGGILAANLGAGFLGGIVAGFIAGYATSFLNRNIRLHKNLEGLKPVLILPLLGSLVTGLAMIYVVGAPVAEALATLSAWLKGMQGSSAILLGLLIGAMMAFDMGGPVNKAAYAFSTGLIASQVYTPMAAAMAAGMVPPLGLALATKLFADRFTREEREAGNAAGILGIAFITEGAIPFAARDPLRVIPALVLGAALTGAISMGIGAELKVPHGGIFVLPIPNAVTHLAGYVVALVAGTVTTAVALRFLKRPVSSVVTA Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS03360 RR42_RS03360 fructose ABC transporter, ATPase component (FrcA) Specific phenotype on fructose sugar ABC transporter ATP-binding protein MSDTSTKAPLLALRNICKTFPGVRALRKVELTAYAGEVHALMGENGAGKSTLMKILSGAYTADPGGECHIDGQRVQIDGPQSARDLGVAVIYQELSLAPNLSVAENIYLGRALQRRGLVARGDMVRACAPTLARLGADFSPAANVASLSIAQRQLVEIARAVHFEARILVMDEPTTPLSTHETDRLFALIRQLRGEGMAILYISHRMAEIDELADRVTVLRDGCFVGTLDRAHLSQAALVKMMVGRDLSGFYTKTHGQAVEREVMLSVRDVADGRRVKGCSFDLRAGEVLGLAGLVGAGRTELARLVFGADARTRGEVRIANPAGSGGLVTLPAGGPRQAIDAGIAYLTEDRKLQGLFLDQSVHENINLIVAARDALGLGRLNRTAARRRTTEAIDTLGIRVAHAQVNVGALSGGNQQKVMLSRLLEIQPRVLILDEPTRGVDIGAKSEIYRLINALAQSGVAILMISSELPEVVGLCDRVLVMREGTLAGEVRPAGSAAETQERIIALATGAAAAAPAWVDVPLPGAGNATGITLH Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS03365 RR42_RS03365 fructose ABC transporter, permease component (FrcC) Specific phenotype on fructose ribose ABC transporter permease MTRPAASTGAPLPAGTLGRLTTQERLRALGMLPVLVLLCIGFSVLTENFAGWQNLSIIAQQASINMVLAAGMTFVILTGGIDLSVGSILSISAVVAMLVSLMPQLGMLSVPAALLCGLLFGIVNGALVAFMKLPPFIVTLGTLTAVRGLARLVGNDSTIYNPDIGFAFIGNGEVLGVPWLVIIAFAVVAVSWFVLRRTVLGLQIYAVGGNAEAARLSGIKVWVVLLFVYAVSGLLAGLGGVMSSARLYAANGLQLGQSYELDAIAAVILGGTSFVGGTGSIVGTLVGALIIAVLSNGLVLLGVSDIWQYIIKGLVIIGAVALDSYRRKGSART Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS03370 RR42_RS03370 fructose ABC transporter, substrate-binding component (FrcB) Specific phenotype on fructose ABC transporter MFKQYLAALATAALSLLCTGAAAQSAPDAAPASAAAQRPLKKVGVTLGSLGNPYFVALAHGAEAAAKKINPDAKVTVLSADYDLNKQFSHIDSFIVSKVDLILINAADARAIEPAVRKARKAGIVVVAVDVAAAGADATVQTDNTRAGELACAFLAGRLGGRGNLIIQNGPPVSAVLDRVKGCKMVLGKHPGIHVLSDDQDGKGSREGGLNVMQLYLTRFPKIDAVFTINDPQAVGADLAARQLNRGGILIASVDGAPDIEAALKANTLVQASASQDPWAIARTAVEIGVGLMHGQAPANRTVLLPPTLVTRANVNEYKGWAAPR Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS03635 HSERO_RS03635 D-mannose ABC transporter, substrate-binding component Specific phenotype on D-mannose sugar ABC transporter periplasmic protein MIKNTIAIACSTLLLAAAAQPAMAADKPLKSVGVTVGDLANPFFVAIAKGAESGAHKINPDAKVTVVSSKYDLNTQVGQIENFIANKVDLIVLNAADSKGVGPAVKKAQKAGIVVVAVDVAAAGADVTVMSDNTMAGAESCKFLAEKLQGKGNVVIVNGPPVSAVMDRVTGCKAEFKKSPGIKILSDNQNAGGSRDGGMTTMSNLLAAQPKIDAVFAINDPTAIGAELAIRQAKRSDIKWISGVDGAPDAERALKDSKSLFAASPAQDPYGMAAESVAIGYAVMNGRAPQQKVKLLPVKLITRDNVADYQGWVPAK Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS03640 HSERO_RS03640 D-mannose ABC transporter, ATPase component Specific phenotype on D-mannose D-ribose transporter ATP-binding protein IPVDMTQTPLLQMRGIRKSFGATLALSDMHLTIRPGEIHALMGENGAGKSTLMKVLSGVHAPDQGEILLDGRPVALRDPGASRAAGINLIYQELAVAPNISVAANVFMGSELRTRLGLIDHAAMRSRTDAVLRQLGAGFGASDLAGRLSIAEQQQVEIARALVHRSRIVIMDEPTAALSERETEQLFNVVRRLRDEGLAIIYISHRMAEVYALADRVTVLRDGSFVGELVRDEIDSERIVQMMVGRSLSEFYQHQRIAPADAAQLPTVMQVRALAGGKIRPASFDVRAGEVLGFAGLVGAGRTELARLLFGADPRSGGDILLEGRPVHIDQPRAAMRAGIAYVPEDRKGQGLFLQMAVAANATMNVASRHTRLGLVRSRSLGGVARAAIQRLNVKVAHPETPVGKLSGGNQQKVLLARWLEIAPKVLILDEPTRGVDIYAKSEIYQLVHRLASQGVAVVVISSELPEVIGICDRVLVMREGMITGELAGAAITQENIMRLAT Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS03645 HSERO_RS03645 D-mannose ABC transporter, permease component Specific phenotype on D-mannose ribose ABC transporter permease MTHTHDAVPPGARRSSSTTAQWLLHRLGMLPVLVVLYLLFYGLTLYLSGDGTSNFASAENTMNILRQVAINLVLAAGMTFVILTAGIDLSVGSVLAVSAVLGMQVSLGAAPGWAIPMFIFSGLVMGMVNGAMVALLNINAFVVTLGTMTAFRGAAYLLADGTTVLNNDIPSFEWIGNGDFLHVPWLIWVAVAVVLLSWVILRKTVLGMHIYAIGGNLQAARLTGIRVGLVLLFVYSISGLFSGLAGAMSASRLYGANGNWGSGYELDAIAAVVLGGTSLMGGVGSIWGTVVGALIIGVMNNGLTILGLSSFWQYVAKGAVIVLAVILDKWRQKDAAQSA Caulobacter crescentus NA1000 Caulo CCNA_00435 CCNA_00435 L-proline transporter Mildly important for growth with proline as the carbon or nitrogen source, and detrimental in most other conditions. amino acid transporter MVGGTPKVSFWTRRKAIDTITAGHADSHQLKKTLSWPHLVALGVGAIVGTGIYTLTGVGAGLAGPGVILSFLIAGAVCACAALCYAELSTMIPASGSAYTYSYAAMGEPVAWFVGWSLILEYTLVCAAVAVGWSAHAHGLFKMIGFPDALLAGPHQGGLINMPAVFISMAVAGLLALGTRESATVNMVLVFVKIIALIVFVVLCLPAFNLAHFTPFMPNGFQAHVPEGAAADAAKVGVMAAASLIFFAFYGFDAVSTAAEETKNPKRDLTIGIVGSMAVCTAIYMIVAAVSIGASRTEVFSKSEAPLVFILESLNHGKIAQLVALAAVIALPTVILAFMYGQSRIFFVMARDGLLPRALSKVNAKTGTPVMMTLLTGVLAAVISGLLSLKDIAELANAGTLWAFIAVGASVILLRLREPNRPRVFSTPLWPIVAPAGILGCLYLFLSLPGKTQLYFLYAHLIGAVVYLAYGMRKSVLAQQERA Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_2924 N515DRAFT_2924 L-proline transporter Mildly important for growth with proline as the carbon source, but not in other conditions amino acid/polyamine/organocation transporter, APC superfamily (TC 2.A.3) MLKNLFATTQISPASADLPGGGAHGEATLKRALTARHLVLLGIGAIIGAGIFVITGQAAAEHAGPAIVLSFVFAGIACALAALCYAEFAAMLPVSGSAYSYSYATLGEYVAWFVGWSLVLEYLFTVATVAAGWSGYFNKLLALISGWIGHDVSLPQTLAAAPFTVVDGHIQATGMFINLPAVAIIAAITGLCYVGITQSAFVNSIIVAIKVTVILLFIAFATKYINPDNWHPFIPASEGASKYGWAGVGRAAAIVFFSYIGFDAVSTAAGEAKNPQRDMPIGIIGSLILCTILYIIVAGILTGIADFRLLGTPEPVSTALDNYPSLHWLQIIVVIGAVTGLSSVMLVMLMGQPRIFYSMARDGLIPAVFGRIHQKFRTPHVGTVVVGVLAAALGGLFNIGVLGEMVAMGTLLAFATVCIGVLVLRYTRPELPRAFRVPVPWIVCPLGALACMALFLQSFLEHWRWMLAWIAIGQAIYFLYGYSHSKLRKPAA Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS00870 HSERO_RS00870 L-proline ABC transporter, substrate-binding component Specifically important for utilizing proline as a carbon or nitrogen source ABC transporter substrate-binding protein MFKRVSGLNIIAASLALIPAFAMAQETQVVKIGFSSPLTGPQASAGKDNQGGLMMAIERLNAQPITVGGKKIKFDVIAEDDQADPKSGVAVAQKLADQGVKAIVGPYNSGVTIPASRVYNDAGIVVATVASNPKITQQGFATLFRVAASDSQLGGKMALYAAKELKFKRVAVIDDRTAYGQGLAQEFIKVAKANGIDVVSTDFTNDKATDFTAILTSIKGKKPDAVFLGGYAPQGGPIKRQMKQLGVDVPLMGGDGICSPEMGRLGGDAIGESVYCTQGGTMLDKAKEGKVFSDEYQKKYNRPAETYAVSFYDGMMLIAQAMKQANSVDPKQFGPALAKISYKGVAGQYDFDANHDLKQSPVTVYRFKDGLPVPLTSY Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS00885 HSERO_RS00885 L-proline ABC transporter, permease component 1 No data for this gene, but fitness data for surrounding genes implies this is part of a proline transporter ABC transporter permease MDIFIQQIINGLVLGSMYALIALGYTMVYGVLNLINFAHGDILMVGAMVGLSLLKVVQQVAPGLPGIVQLVIAIVGAIPVCIVVSLLIERIAYRPLRNAPRLAPLITAIGVSILLQTLAMMIWGRSPLPFPQVMPSDPVHIAGALISPTQIMLLALAVLAMVGLVLIVEKTKMGRAMRATAENPRIAGLMGVDANKVIVVTFAIGAGLAAIAGVMWAANYSTAQFAMGFVPGLKAFSAAVLGGIGNIYGAMLGGILLGLIESLGAGYIGDLTGNFLGSNYQDIFAFIVLIIVLTLRPSGIMGERVADRA Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS00890 HSERO_RS00890 L-proline ABC transporter, permease component 2 Specifically important for utilizing proline as a carbon or nitrogen source ABC transporter ATP-binding protein MALLTFDMKRNPQQARISLLLLLALMIVFPFVAQQFGNSWVRIMDVALLYIMLALGLNVVVGFAGLLDLGYIAFYAIGAYSAGLLASPQFAAVIESFVNTYPSVGNFLVWLCGPEIVQNGIHLSLWLIVPISAFLAALFGALLGAPTLKLRGDYLAIVTLGFGEIIRIFMNNLNAPVNITNGPQGINLIDPIKVFGVSLAGEPGSGSMVKVFGMSMPSVNAYYFLFLLLCIGVIFFSVRLQDSRLGRAWVAIREDEIAAKAMGINTRNVKLLAFAMGASFGGVAGAMFGAFQGFVSPESFSLTESIAVLAMVVLGGIGHIPGVVLGGVILAALPEVLRHVVEPVQMAIFGKVWIDAEVLRQLLYGLAMVVIMLTRPAGLWPSPRHEDRPEADHTQVGTTGEVKA Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS00895 HSERO_RS00895 L-proline ABC transporter, ATPase component 1 Specifically important for utilizing proline as a carbon or nitrogen source ABC transporter MSQTLLKIRDVSKRFGGLQALNGVGITIERGQIYGLIGPNGAGKTTFFNVITGLYQPDTGTFELDGKPYSPSAPHEVAKAGIARTFQNIRLFGEMTVLENVMVGCHVRTRQNVFGAVFRHKAAREEEAAIREKSQKLLDFVGIGQFAKRTARHLSYGDQRRLEIARALATDPQLLALDEPAAGMNATEKLGLRELLVKIQAEGKTILLIEHDVKLMMGLCNRITVLDYGKPIAEGVPADVQKNPAVIEAYLGAGH Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS00900 HSERO_RS00900 L-proline ABC transporter, ATPase component 2 Specifically important for utilizing proline as a carbon or nitrogen source amino acid ABC transporter ATPase MTTNILKVQQLSVAYGGIQAVKGIDLEVNEGELVTLIGANGAGKTTTLKAITGTLPASRVEGHIEYLGQPLKGKKSFELVKDKLAMVPEGRGVFTRMSIQENLLMGAYTSDDKGQIAADIDKWFAVFPRLKERAAQMAGTLSGGEQQMLAMARALMSHPKLLLLDEPSMGLSPIMVEKIFEVIRNVSAQGITILLVEQNAKLALEAAHRGYVMESGLITMQGQAQQMLDDPRVKAAYLGEG Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_1695 ABC transporter for glutamine/isoleucine/leucine/phenylalanine/proline/serine/tyrosine, permease component 1 Important for utilization of glutamine/isoleucine/leucine/phenylalanine/proline/serine/tyrosine High-affinity branched-chain amino acid transport system permease protein LivH (TC 3.A.1.4.1) MDILLQQIINGLVLGSMYALIALGYTMVYGIIQLINFAHGEVLMIGALTSWSCIGMMQGAMPGAPGWVILLLATIIACVVAATLNFVIEKVAYRPLRSSPRLAPLITAIGMSILLQTLAMIIWKPNYKPYPTMLPSSPFEIGGAFITPTQILILGVTAVALASLVYLVNHTNLGRAMRATAENPRVASLMGVKPDMVISATFIIGAVLAAIAGIMYASNYGTAQHTMGFLPGLKAFTAAVFGGIGNLAGAVVGGILLGLIEAIGSGYIGTLTGGLLGSHYTDIFAFIVLIIILTLRPSGLLGERVADRA Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_1694 ABC transporter for glutamine/isoleucine/leucine/phenylalanine/proline/serine/tyrosine, permease component 2 Important for utilization of glutamine/isoleucine/leucine/phenylalanine/proline/serine/tyrosine Branched-chain amino acid transport system permease protein LivM (TC 3.A.1.4.1) MKNTKTNWIIGAVALLVLPLILQSFGNAWVRIADLALLYVLLALGLNIVVGYAGLLDLGYVAFYAVGAYLFALMASPHLADNFAAFAAMFPNGLHTSLWIVIPVAALLAAFFGAMLGAPTLKLRGDYLAIVTLGFGEIIRIFLNNLDHPVNLTNGPKGLGQIDSVKVFGLDLGKRLEVFGFDINSVTLYYYLFLVLVVVSVIICYRLQDSRIGRAWMAIREDEIAAKAMGINTRNMKLLAFGMGASFGGVSGAMFGAFQGFVSPESFSLMESVMIVAMVVLGGIGHIPGVILGAVLLSALPEVLRYVAGPLQAMTDGRLDSAILRQLLIALAMIIIMLLRPRGLWPSPEHGKSLTQKT Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_1693 ABC transporter for glutamine/isoleucine/leucine/phenylalanine/proline/serine/tyrosine, ATPase component 1 Important for utilization of glutamine/isoleucine/leucine/phenylalanine/proline/serine/tyrosine Branched-chain amino acid transport ATP-binding protein LivG (TC 3.A.1.4.1) MTEKSNEVVLKVAGISKRFGGLQALSDVGITIKRGQVYGLIGPNGAGKTTFFNVITGLYTPDAGTFELAGKPYEPTAVHEVAKAGIARTFQNIRLFAEMTALENVMVGRHIRTGSGLFGAVFRTKGFKAEEAAIAKRAQELLDYVGIGKFADYKARTLSYGDQRRLEIARALATDPQLIALDEPAAGMNATEKVQLRELIDRIRNDNRTILLIEHDVKLVMGLCDRVTVLDYGKQIAEGNPAEVQKNEKVIEAYLGTGGH Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_1692 ABC transporter for glutamine/isoleucine/leucine/phenylalanine/proline/serine/tyrosine, ATPase component 2 Important for utilization of glutamine/isoleucine/leucine/phenylalanine/proline/serine/tyrosine Branched-chain amino acid transport ATP-binding protein LivF (TC 3.A.1.4.1) MAEKSNKVLLQVKGLKVAYGGIQAVKGVDFEVREGELVSLIGSNGAGKTTTMKAITGTLSMNDGNIEYLGKSIKGKGAWDLVKEGLVMVPEGRGVFARMTITENLQMGAYIRKDKAGILADIEKMFTIFPRLRERKDQLAGTMSGGEQQMLAMGRALMSQPKVLLLDEPSMGLSPIMVDKIFEVVRDVYALGVTIVLVEQNASRALAIADRGYVMESGLITMTGPGQQLLNDPKVRAAYLGE Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2396 ABC transporter for glutamine/isoleucine/leucine/phenylalanine/proline/serine/tyrosine, substrate-binding component Important for utilization of glutamine/isoleucine/leucine/phenylalanine/proline/serine/tyrosine Extracellular ligand-binding receptor precursor MQLKLKLTVVAAIAAAAGVASAQEQVVKIGHVAPVSGAQAHYGKDNENGARMAIEELNAQGVTIGGKKIKFELVAEDDAADPKQGTAAAQKLCDAKVAGVVGHLNSGTTIPASKVYNDCGIPHVTGAATNPNLTKPGYKTTFRIIANDNALGAGLAFYAVDTLKLKTVAIIDDRTAYGQGVADVFKKTATAKGMKVVDEQFTTDKATDFMAILTAIKAKNPDAIFYGGMDPQGGPMLRQMEQLGMGNVKYFGGDGICTSEIAKLAAGAKTLGNVICAEGGSSLAKMPGGTAWKAKYDAKYPNQFQVYSPYTYDATFLIVDAMKRANSVDPKVYTPELAKSSFKGVTSTIAFEPNGEMKNPAITLYVYKDGKKTPL Sinorhizobium meliloti 1021 Smeli SMc02520 SMc02520 glycerol-3-phosphate dehydrogenase (EC 1.1.5.3) Specifically important for glycerol utilization. Expression is induced by glycerol or glycerol-3-phosphate (PMC1635973). glycerol-3-phosphate dehydrogenase MSEQTIFDVFVIGGGINGCGIARDAAGRGYSVALAEMSDFASGTSSGSTKLIHGGLRYLEHYEFRLVREALMEREVLWAMAPHVIWPMRFVLPFHKGGPRPAWLIRLGLFLYDHIGGRKLLPATKTLDMTRDPAGAPLKGLFTKAFEYSDGWVDDARLVVLNARDAADRGARIMARTRVVSARREGGRWAIEIESTETGARETMRARMLVNAAGPWVDRVLSEAVGNNDVRNVRLVQGSHIVVKKKFDDPRAYFFQNPDGRIMFAIPYQDEFTLIGTTDRDFTGNPADVRISDAEIDYLCRAASEYFSDPVGREDIVWTYSAVRPLFDDGASKAQEATRDYVLRVENGDAPLLNVFGGKLTTYRRLAESALEKIGETIGEKGRKWTAVSHLPGGDFPAAGYDDEVAKLRTRYPFLTASHARRLVRLYGTRAAQLLGNAASEADLGKHFGADLYAAEVDWLIVQEWALRAEDVLWRRTKLGLKFSRAQTAELEEYMRGAVNAAA Phaeobacter inhibens BS107 Phaeo GFF775 PGA1_c07890 cytoplasmic trehalase (AlgA) Specifically important for trehalose utilization and part of an operon with an algEFGK-type transporter for trehalose and cellobiose. Also important for cellobiose utilization, but this may be a polar effect (the cellobiase is PGA1_c07840) putative alpha-glucosidase AglA MNAQAQLDPAQVLAADPDWWRGAVIYQIYPRSYQDSNGDGIGDLRGITQRLPHIASLGVDAIWISPFFTSPMKDFGYDVSDYCDVDPMFGSLSNFDQLVAAAHRLGLRVMIDLVLSHTSDQHAWFGESRQSRDNARADWYVWADPQPDGTPPNNWLSIFGGSAWQWDPRREQYYLHNFLVSQPDLNFHSPAVQDALLDVTRFWLERGVDGFRLDTINFYYHDAELRSNPALPPEQRNATIAPSVNPYNHQEHLYSKNQPENLAFLGRFRALLDEYPAKAAVGEVGDAQRGLEIMGSYTAANTGVHMCYAFELLAKDVLTASRLAEVFAEVDRVAANGWACWAFSNHDVIRHSSRWGLNPAAQRLFTTMMMCLRGTTCIYQGEELGLPEADIAFEDLQDPYGIEFWPEFKGRDGCRTPMVWEPSNGSGGFSAGKPWLPVSPEHLNLSVASQEADPDAMLHHYRRAIALRKAHPALAVGTHDQLRAEGNVAFFTRQDRDEVIFCAFNLGDIPAEITLPEGTWRKPDTDIALADLPQSGARVVLAPWQACLAVRV Phaeobacter inhibens BS107 Phaeo GFF530 PGA1_c05420 glucokinase (EC 2.7.1.2) Important for the utilization of glucose, trehalose, and cellobiose; trehalose and cellobiose are cleaved to glucose glucokinase Glk MGSDMTVLVGDVGGSNTRLALAGPEIGVTALQSFANDSFSSLDDVLAAYCAQPDLPPLAGACIAVAGPVYGNEYQLTNRNWQGSAADLAQQLQLGAGARVDVINDLAALGHSLLALIPGQLSSLRAGHQRGTQALVAGIGTGFNVSLSVDGHTAEAEMGHTSLSAPVTRGLTDLLGDRAGEFATNEDLFSGRGLVRYHQALHGIAAEGGAQIVADYLADGDSPAAKTVTSWARLLGDFARELVPTYMPGQGIFFAGSVARGILGTAACEVFLNSFLQPATGVQSRCETTPLWLITDDAAGVSGAARFALERAGRKS Klebsiella michiganensis M5al Koxy BWI76_RS01840 BWI76_RS01840 maltose ABC transporter, ATPase component (MalK) Specifically important for maltose utilization ABC transporter ATP-binding protein MASVQLRNVTKAWGDVVVSKDINLEIQDGEFVVFVGPSGCGKSTLLRMIAGLETVTSGDLLIGDTRMNDVPPAERGIGMVFQSYALYPHLSVAENMSFGLKLAGAKKELINQRVTQVAEVLQLAHLLERKPKALSGGQRQRVAIGRTLVAEPRVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIEQVQVELPNRQQVWLPVDSARVQVGANMSLGIRPEHLLPSDIADVTLEGEVQVVEQLGHETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGV Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_0695 Echvi_0695 UDP-glucose--hexose-1-phosphate uridylyltransferase (EC 2.7.7.12) Specifically important for utilizing D-Galactose; this is part of the Leloir pathway galactose-1-phosphate uridylyltransferase, family 1 MTDFNFEDHSHRRYNPFTGDWLQVSPHRGKRPWQGQEEDTAEAQKPAYDEKCYLCPGNTRINGEKNPDYTGAYVFQNDFGALTSDIPQGEMSEGEFFRAKSERGICKVICFSPRHDLTIPELDVQAITKVVELWKKEYQELGGKDFINHVQIFENKGSVMGCSNPHPHGQIWAQESIPVEPAKKQVKFGEYYQKYGRSMVLDYVYEELKKGERILFENDYFVGLVPFWAVWPFEAMIAPKTHIASLSEMDAAQMEALADAYRQLAIMYDNVFKVSFPYSAGIHQAPTDGQNHPEWDLHMVFYPPLLRSATVKKFMVGYEMLANPQRDITAESAVKILKSQPKEHYKV Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS06120 CA265_RS06120 UDP-glucose--hexose-1-phosphate uridylyltransferase (EC 2.7.7.12) Specifically important for utilizing D-Galactose; this is part of the Leloir pathway galactose-1-phosphate uridylyltransferase MNQTFELDSNPHTRLNILTGEWVLVSPHRTKRPWQGKVEDVTPDNRPEYDPKCYLCPGNSRADGDSNPEYTESFVFNNDFAALLEDTPAGNMNEHDLLVASNQRGLCKVISFSPKHHLTLPEMSVKAITAVVNVWQNEFNSLAENNWIKYIQIFENKGEIMGCSNPHPHGQIWSQGDIPLEIAKETERQKSYYAIHKRSLLSDYLKLEQKKKERIIFENDHFAVLVPFWAVWPYETMIISKRHVNSIRLFTEAEKESLAEAIKVLTTKYDNLFETSFPYSAGMHQAPVNNGYYPEWHWHMHFYPPLLRSASVKKFMVGYEMLANPQRDITPEFAANRLKEMSATHYKISKV Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1472 Echvi_1472 UDP-glucose 4-epimerase (EC 5.1.3.2) Important for utilizing D-Galactose; this is part of the Leloir pathway UDP-glucose-4-epimerase MQQILITGGAGYIGSHTAVALVNAGYEPIIVDNFSNSNKEVLNGLEKILGAPVKYHEGDCNDRKFMQAVFEENDLQGVIHFAASKAVGESTKIPLTYYSNNINSLIILLETMKQFGVKDIVFSSSCTVYGQPDKLPVKETTPRKDAESPYGNTKKICEDILTDHVKSGAPARVVALRYFNPIGAHPSSLIGELPLGVPANLIPFVTQTGAGIREKITVFGDDYNTPDGTCIRDYIHVMDLADAHVKSIQYLADQPENFIDLFNVGTGNGNTVMEVIKAFEKVSEKPLNYEIGPRRSGDIEKVWANTDKVSKVLGWTPQFGLEEALRDAWNWQLSLKK Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1871 Echvi_1871 transporter for D-glucose/D-galactose/D-xylose/methyl-beta-D-galactopyranoside Important for utilizing glucose, galactose, xylose, and methyl-b-D-galactopyranoside, but not in most other carbon source experiments transporter, SSS family MTFNTLDLVVFVAYCLLIITMGIVVSREKKGHVKDSKDYFLASKALPWWAVGASLIASNISAEQFIGMSGSGFALGLAISTYEWMAAATLLVVAIFFLPIYLKEGIYTMPQFLNRRYDGRVRTVMAIFWLLIYVFVNLTSVLYLGALSLETIMGVPLTYGIIGLALFAMVYSIYGGLKAVAWTDVVQVVFLVAGGLATTYLALSLVGDGDVWEGIGILRKAAPSHFSMIIEKGEMMIPDGSGGSRDAYLDLPGLSVLIGGMWIVNLNYWGCNQYITQRALAAKSLGEAQTGMVFAGFLKLLMPLIVVIPGIAAYVIVQKGADASFIESMTDPVTGLAKSDRAYPTLLHLLPPGLKGLAFAALTAAIVSSLASMANSTSTIFTIDIYKEFFNKNVSEGKQVTIGRITAVVAFIIAAIVAPQLRQLDQAFQYIQEYTGFVSPGVFAIFIFGFFWKKTTSNAALTAAVLTIPLSAAFKVITPNLPFIDRMGVVFLVLSVLIIAISLYEGKGKDSKKAIEVDAELFSTSTKFKVGAVLICGILVALYSVFW Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS06130 CA265_RS06130 D-galactose transporter Specifically important for D-galactose utilization sodium transporter MKNNLLDTKDYIVFAIYFVIVAAYGLYIYNKKKSESTGSKDYFLAEGSLTWWAIGASLIASNISAEQFIGMSGSGFKMGLAIATYEWMGAATLVVVAVFFIPVYLKNKIATMPQFLHQRYNGTVAMIMAVFWLLLYVVVNLTSILYLGALAVSSISGFDLSFCMYAIAGFAIIITLGGMKVIGYTDVIQVFFLILGGLATTYLALNLVSTHYGTTGIFEGYSLMTSKASEHFHMILKPENENYIDLPGLSVLVGGMWIVNLNYWGCNQYITQRALGANLETARGGILFAAFLKLLMPIIVVLPGIAAYVLFKDGAFQSEMLQDGAVNPDRAYPVLLNLLPAGLKGLSFAALTAAVVASLAGKANSIATIFTLDIYKKVLRTDATEKNLVTTGKISIIVAMILGVLIAPHLGIDKKGGFQYIQEYTGFVSPGIFAMFILGFFWKRTTSTAALFATIGGFGLSILLKFLPNLTDLSWLSGMGFSVKNAAGVYEIPFLDRMGFVFVFCIIGMYIISMLSNKAEAEAKGLAIDAKMFKTSTSFAVGALIIIGLLVALYSVYW Burkholderia phytofirmans PsJN BFirm BPHYT_RS16950 BPHYT_RS16950 2-dehydro-3-deoxygalactonokinase DgoK (EC 2.7.1.58) specifically important for D-galactose utilization 2-dehydro-3-deoxygalactonokinase MKRAGSPTQAAGHAAAVAVDASHEHAALIALDWGTTSLRAYLYDASGNVLATRASTAGIMNLPRSAEQGGFDAAFDDTCGAWLAHAPAAPVIAAGMVGSAQGWLEAPYVDTPASADALVAGIVRVKAACGVTLHIVPGVLQRGELPNVMRGEETQIFGALGEETNTADSGKRSLIGLPGTHAKWAVVQADRIERFHTFMTGEVFAALREHTILGRTMLTPDSPDTSAFLHGVNIAREKGQAGVLATVFSSRTLGLTGQLSREQQPDYLSGLLIGHELAGLDAVLAQQQSALAGQSLRLIGNEALCERYRLALAQFGCTQAELVKHATERGLWRVASQAGLVKPAAKTARA Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_615 L-arabinolactonase/D-galactonolactonase (EC 3.1.1.15; EC 3.1.1.25) Specifically important for utilizing L-arabinose or D-galactose; the EC numbers given are for the 1,4-lactonase reactions, but this is not certain. The dehydrogenase (Ac3H11_614) could form 1,5-lactones instead. L-arabinolactonase (EC 3.1.1.15) MRPFLDTPFSPPEGAAFSAPVTGAVRCVIALGNALGEGVLWSVREQAVYWVDILGRELHRWDPATGAHQRWTFDEEISAIAERAHAPGFIVTLRRGFALFDPATDMAPRYLHQPEPDRAGNRFNDGKCDAQGRFWAGSMDFACEAPTGALYRYDSDGSCTRHDDGFAVTNGPTWSGTGQGAAMFFNATIEGNTYRYDSDLATGTVSNKTLWKHWLPEDGLPDGMTTDAQGRLWIAHWGGWCVTCHDPVTAAELGRVRLPVSQVTTCAFGGADLRTLFISSARVGLTPEQLAAEPLAGALFAVDTDSLGLPAHPFGG Burkholderia phytofirmans PsJN BFirm BPHYT_RS16935 BPHYT_RS16935 D-galactose ABC transporter, substrate-binding component Specifically important for D-galactose utilization arabinose ABC transporter substrate-binding protein MKRRIFLTLAAAATGVLFNAPVAQAADPVKIGFLVKQPEEPWFQDEWKFAEIAAKEKGFTLVKIGAPSGEKVMSAIDNLSAQKAQGFVICTPDVKLGPGIVAKAKADGLKMMTVDDRLVDGAGKPIASVPHMGISAYNIGKQVGDGLAAEIKKRGWDMKDVGAIDVTYEQLPTAHDRTSGATDALIAAGFPKANIVMAPQAKTDTENAFNAANIALTKNPQFKHWVAYALNDEGVLGAVRAAEGRGFKADNMIGIGIGGSDSALNEFKKPSPTGFYGTVIISPKRHGEETSTLMYDWITQGKAPPPLTLTTGMLATRDNVADVRQKMGLAAN Burkholderia phytofirmans PsJN BFirm BPHYT_RS16930 BPHYT_RS16930 D-galactose ABC transporter, ATPase component Specifically important for D-galactose utilization arabinose ABC transporter ATP-binding protein MSATLRFDNIGKVFPGVRALDGVSFDVNVGQVHGLMGENGAGKSTLLKILGGEYQPDSGRVMIDGNEVRFTSAASSIAAGIAVIHQELQYVPDLTVAENLLLGQLPNSLGWVNKREAKRFVRERLEAMGVALDPNAKLRKLSIAQRQMVEICKALLRNARVIALDEPTSSLSHRETEVLFKLVRDLRADNRAMIYISHRMDEIYELCDACTIFRDGRKIASHPTLEGVTRDTIVSEMVGREISDIYNYSARPLGEVRFAAKGIEGHALAQPASFEVRRGEIVGFFGLVGAGRSELMHLVYGADHKKGGELLLDGKPIKVRSAGEAIRHGIVLCPEDRKEEGIVAMATVSENINISCRRHYLRVGMFLDRKKEAETADRFIKLLKIKTPSRRQKIRFLSGGNQQKAILSRWLAEPDLKVVILDEPTRGIDVGAKHEIYNVIYQLAERGCAIVMISSELPEVLGVSDRIVVMRQGRISGELTRKDATEQSVLSLALPQSSTALPGTQAAAQQAA Burkholderia phytofirmans PsJN BFirm BPHYT_RS16925 BPHYT_RS16925 D-galactose ABC transporter, permease component Specifically important for D-galactose utilization arabinose ABC transporter permease MQARENLAQQAAKGAAEALIPQSNDKAKWWQQITEYSLIVIFVVMFATMSLTVDHFFSIENMLGLALSISQIGMVSCTMMFCLASRDFDLSVGSTVAFAGVLCAMVLNATGNTFIAIVAAVAAGGVIGFVNGAVIAYLRINALITTLATMEIVRGLGFIVSHGQAVGVSSDTFIALGGLSFFGVSLPIWVTLLCFIVFGVMLNQTVYGRNTLAIGGNPEASRLAGINVERTRVYIFLIQGAVTALAGVILASRITSGQPNAAQGFELNVISACVLGGVSLLGGRATISGVVIGVLIMGTVENVMNLMNIDAFYQYLVRGAILLAAVLLDQLKNRGSRD Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5968 ABC transporter for D-galactose/L-arabinose, substrate-binding component Specifically important for utilizing D-galactose and L-arabinose L-arabinose-binding periplasmic protein precursor AraF (TC 3.A.1.2.2) MKHRRGIRSLCRAALAVTAVSLSSHLLAADAVKIGFLVKQAEEPWFQTEWAFAEKAAKDKGFQLIKIAVPDGEKTLSAIDSLAANGAKGFVICPPDVSLGPAIVAKAKLNDMKVIAVDDRFVGSDGKFMEDVPYLGMAAFEVGQKQGGAMAAEAKKRGWDWKDTYAVINTYNELDTGKKRTDGSVDALKKAGMPADHILYSALKTLDVPGSMDSTNSALVKLPSAAKNLIIGGMNDNTVLGGVRATEAAGFKAANVIGIGINGTDAIGELKKPDSGFFGSMLPSPHIEGYKTAEMMYEWITTGKEPPKYTAMDEVTLITRENFKQELEKIGLWN Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5969 ABC transporter for D-galactose/L-arabinose, ATPase component Specifically important for utilizing D-galactose and L-arabinose L-arabinose transport ATP-binding protein AraG (TC 3.A.1.2.2) MQAQTATRQHNIGGSLRFNGIGKSFPGVQALANISFVAHPGQVHALMGENGAGKSTLLKILGGAYIPSSGDLQIGEQTMAFKGTADSIASGVAVIHQELHLVPEMTVAENLFLGHLPARFGLVNRGVLRQQALTLLKGLADEIDPQEKVGRLSLGQRQLVEIAKALSRGAHVIAFDEPTSSLSAREIDRLMAIIGRLRDEGKVVLYVSHRMEEVFRICNAVTVFKDGRYVRTFENMSELTHDQLVTCMVGRDIQDIYDYRPRERGDVALQVKGLLGPGLHEPVSFQVHKGEILGLFGLVGAGRTELLRLLSGLERQREGSLVLHDKELKLRSPRDAIAAGVLLCPEDRKKEGIIPLGSVGENINISARPSHSTLGCLLRGDWERGNADKQIKSLKVKTPTAGQKIMYLSGGNQQKAILGRWLSMPMKVLLLDEPTRGIDIGAKAEIYQIIHNLAADGIAVIVVSSDLMEVMGISDRILVLCEGAMRGELSRDQANESNLLQLALPRQRVADAAN Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_5970 ABC transporter for D-galactose/L-arabinose, permease component Specifically important for utilizing D-galactose and L-arabinose L-arabinose transport system permease protein (TC 3.A.1.2.2) MTIQNNALPTARKPLDLRRFLDDWVMLLAAIGIFVLCTLMIDNFLSPLNMRGLGLAISTTGIAACTMLYCLASGHFDLSVGSVIACAGVVAAVVMRDTNSVFLGISAALVMGLIVGLINGIVIAKLRVNALITTLATMQIVRGLAYIFANGKAVGVSQESFFVFGNGQMFGVPVPILITIVCFLFFGWLLNYTTYGRNTMAIGGNQEAALLAGVNVDRTKIIIFAVHGVIGALAGVILASRMTSGQPMIGQGFELTVISACVLGGVSLSGGIGMIRHVIAGVLILAIIENAMNLKNIDTFYQYVIRGSILLLAVVIDRLKQR Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_411 ABC transporter for D-galactose/L-arabinose, substrate-binding component Specifically important for utilizing D-galactose and L-arabinose L-arabinose-binding periplasmic protein precursor AraF (TC 3.A.1.2.2) MKRRRGIRSLCCAALAVTAVSLSSTLLAAEEVKIGFLVKQAEEPWFQTEWAFAEKAGKDKGFTLIKIAVPDGEKTLSAIDSLAANGAKGFVICPPDVSLGPAIMAKAKLNGLKVIAVDDRFVDAGGKFMEDVPYLGMAAFEVGQKQGAAMATEAKKRGWEWKDTYAVINTYNELDTGKKRTDGSVKALEDAGMPKDHILFSALKTLDVPGSMDATNSALVKLPGAAKNLIIGGMNDNTVLGGVRATESAGFAAANVIGIGINGTDAIGELKKPNSGFFGSMLPSPHIEGYNTASMMYEWVTTGKEPPKYTAMDDVTLITRDNFKQELEKIGLWN Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_410 ABC transporter for D-galactose/L-arabinose, ATPase component Specifically important for utilizing D-galactose and L-arabinose L-arabinose transport ATP-binding protein AraG (TC 3.A.1.2.2) MHAHVQTQEQRIGGSLRFNGIGKTFPGVKALDGISFVAHPGQVHALMGENGAGKSTLLKILGGAYTPSSGDLQIGEQKRIFKSTADSIGSGVAVIHQELHLVPEMTVAENLFLGHLPASFGLINRGVLRQQALACLKGLADEIDPQEKVGRLSLGQRQLVEIAKALSRGAHVIAFDEPTSSLSAREIDRLMAIIGRLRDEGKVVLYVSHRMEEVFRICNAVTVFKDGRFVRTFEDMSALTHDQLVTCMVGRDIQDIYDYRSRPRGAVALKVDGLLGPGLREPVSFEAHKGEILGLFGLVGAGRTELFRMLSGLTRNTAGRLELRGRELKLHSPRDAIAAGILLCPEDRKKEGILPLASVAENINISARGAHSTFGCLLRGLWEKDNADKQIKALKVKTPNAAQKIMYLSGGNQQKAILGRWLSMPMKVLLLDEPTRGIDIGAKAEIYQIIHNLAASGIAVIVVSSDLMEVMGISDRILVLCEGAMRGELTREQANESNLLQLALPRQRVADVAN Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_409 ABC transporter for D-galactose/L-arabinose, permease component Specifically important for utilizing D-galactose and L-arabinose L-arabinose transport system permease protein (TC 3.A.1.2.2) MTVQNKALPTPRKPLDLRRFLDDWVMLLAAVGIFVLCTLLIDNFLSPLNMRGLGLAISTTGIAACTMLYCLASGHFDLSVGSVIACAGVVAAVVMRDTDSVFLGVSAALVMGLIVGLINGIVIAKLRVNALITTLATMQIVRGLAYIFANGKAVGVSQEQFFVFGNGQLFGVPVPILITIVCFLFFGWLLNYTTYGRNTMAIGGNQEAALLAGVNVDRTKTLIFAVHGVIGALAGVILASRMTSGQPMIGQGFELTVISACVLGGVSLSGGIGMIRHVIAGVLILAIIENAMNLKNIDTFYQYVIRGSILLLAVVIDRLKQR Sinorhizobium meliloti 1021 Smeli SM_b21217 SM_b21217 glucosamine kinase (EC 2.7.1.8) Specifically important for utilizing glucosamine sugar kinase MRPLAAIGNVNVDLILGPAEPWPKPGTEVIVDHDELRVGGCAGNNALAWDSLGVDYVIAANVGNDQFGTWLKEAFGERSRNWPVEAVGTTLSVGITHPDGERTFFTTRGHLPLFSFPEVHSMLDGNRLRGGYALLSGSFLTDALTLAYDALFDWADAHEIAVALDTGWPLDGWTETNRLRTLGWLKRCHCALFNEVETTTLTGLSDPAEAALSLKGEMPAEAIVVVKRGPHGALAIDRDGGTFSVPAPQVQVVDTIGAGDVFNAGFLAALAAEMPLEACLKTGVTIASEAISTLPRRYGKPLSAFLEESRR Sinorhizobium meliloti 1021 Smeli SM_b21218 SM_b21218 glucosamine-6-phosphate deaminase, isomerizing (EC 3.5.99.6) Specifically important for utilizing D-glucosamine sugar-processing protein MSISKDRPAGLIAIDREMARQHADAIASYEGATATAQRIAASLKSTGRLLLLGMGGSHAVGRAVEPLYRALGIEAVAVPLSEQLGEPLSIEGKTILVTSQSGESAEVLRWFRETDGGTSETFGLTLEEDAFLAKAVPSLVGSGGTERAFAATRSLTVTFALHLAVLAALGADPADALRALRDPEAPVIDGALAALADVGAIVTSGRKLQGLAEAIALGLTELSRLPCFSLEGGQLRHGPMEMLGASVGVVLFRAADPTAKLVGAMATSAAEAGSPVIVFDASDESPAAGATTIRFKPAAGLAAILAMLPVAQSLMIAFADARVENAGTPVRSTKVTRSE Bacteroides thetaiotaomicron VPI-5482 Btheta 351286 BT1758 fructose transporter Specifically important for utilizing fructose. Also important for utilizing fructooligosaccharides. Part of a PUL for utilizing levan (PMC3225772). glucose/galactose transporter (NCBI ptt file) MENTKNASLSKLVPVMLCFFAMGFVDLVGIASNYVKADLGLTDSQANIFPSLVFFWFLIFSVPTGMLMSRIGQKKTVLLSLIVTFASLLLPVFGDSYALMLISFSLLGIGNALMQTSLNPLLSNIVRGDRLASSLTFGQFVKAIASFLAPYIAMWGATQAIPSFDLGWRVLFPIYMVIAILAILLLNATQIEEEKEEGKPSTFGQCLALLGKPFILLCFIGIMCHVGIDVGTNTTAPKILMERIGMTLDDAAFATSLYFIFRTAGCFLGSFILRQMSPKSFFGISVVMMLAAMVGLFIFHDKAVIYACIALIGFGNSNVFSVIFSQALLYLPGKKNEVSGLMIMGLFGGTVFPLAMGVASDTSMGQNGAIAVMTVGVLYLLFYTFRIKK Bacteroides thetaiotaomicron VPI-5482 Btheta 353094 BT3567 periplasmic beta-1,2-glucosidase / beta-1,3-glucosidase Specifically important in carbon source Laminaribiose (beta-D-glucose-(1->3)-D-glucose). Cleaves beta,1-2 and beta,1-3 linkages and has little activity on cellobiose (PMID:28343388). periplasmic beta-glucosidase precursor (NCBI ptt file) MINKKIFFSLLLLAAGFLSAAAQKSPQDMDRFIDALMKKMTVEEKIGQLNLPVTGEITTGQAKSSDIAAKIKRGEVGGLFNLKGVEKIRDVQKQAVEQSRLGIPLLFGMDVIHGYETMFPIPLGLSCTWDMTAIEESARIAAIEASADGISWTFSPMVDISRDPRWGRVSEGSGEDPFLGAMIAEAMVLGYQGKDMQRNDEIMACVKHFALYGAGEGGRDYNTVDMSRQRMFNEYMLPYEAAVEAGVGSVMASFNEVDGVPATANKWLMTDVLRGQWGFNGFVVTDYTGISEMIDHGIGDLQTVSARAINAGVDMDMVSEGFVSTLKKSIQEGKVSMETLNTACRRILEAKYKLGLFDNPYKYCDLKRPARDIFTKAHRDAARRIAAESFVLLKNDNVTLRPGTPAEPLLPFNPKGNIAVIGPLADSRTNMPGTWSVAAVLDRCPSLVEGLKEMTAGKANILYAKGSNLISDASYEERATMFGRSLNRDNRTDEQLLNEALTVANQSDIIIAALGESSEMSGESSSRTDLNIPDVQQNLLKELLKTGKPVVLVLFTGRPLTLTWEQEHVPAILNVWFGGSEAAYAIGDALFGYVNPGGKLTMSFPKNVGQIPLYYAHKNTGRPLAQGKWFEKFRSNYLDVDNEPLYPFGYGLSYTTFSYGDIDLSRSTIDMTGELTAAVMVTNTGTWPGSEVVQLYIRDLVGSTTRPVKELKGFQKIFLEPGQSEIVRFKIAPEMLRYYNYDLQLVAEPGEFEVMIGTNSRDVKSARFTLK Dechlorosoma suillum PS PS Dsui_0518 Dsui_0518 methylmalonyl-CoA-mutase-associated GTPase MeaB Strongly cofit with methylmalonyl-CoA mutase (Dsui_0519). MeaB is required for the mutase's activity and is involved in loading vitamin B12 (see PMC4631608). LAO/AO transport system ATPase MQMSEASTVGQHSLAGADQALVDGVLARQRRALAKAITLIESSRADHQVRAQQVLASLLPHTGKAIRIGISGVPGAGKSTFIEALGIHLIERGHRLAVLAVDPSSSVSGGSILGDKTRMETLCQREEAFIRPSPSAGSLGGVAEKTREAMLLCEAAGFDVIIVETVGVGQSETTVAGMVDMFCLLQLPNAGDDLQAIKKGIVEIADMVVINKADIDPRAAQVVRAQWNNALHMLRHASPNWAPPVITLSALHKEGIGDFWAQVEKYRQALTPTGEFEARRQRQSIDWMWSLIDSGLRQYFRNHPAVRRDLPGLTQAVTQGRTTPAAAAYKLLGDLRTDSPSE Shewanella sp. ANA-3 ANA3 7025754 Shewana3_2904 propionate/L-lactate/D-lactate transporter Specifically important for propionate utilization. Shewana3_2904 and its orthologs in other Shewanellas also have mild phenotypes during L-lactate or D,L-lactate utilization. 95% identical to SO1522 (lctP1), which is involved in utilization of both L- and D-lactate (PMC5603553) L-lactate permease (RefSeq) MTILQLLASLTPVISVMIFLVLLRMPASKAMPISMIITALAAVFIWQMDTTLLAASVLEGLLSAITPLTIIFGAVFLLNTLKYSGAMDTIRAGFTNISADARVQVIIICWLFGAFIEGSAGFGTPAAIGAPLLVLLGVPPVAAAVVALIADSACVSFGAIGLPVLFGMEQGLTQGGVSLAAEQFAAHGGSYVGYARFIVMHMITIDLITGTLIPLVMVTILTGFFGRNKSFKEGLAIWKFAIFAGLAFTVPAWIINYLAGPEFPSVIGSLVGMALVIPVARKGYLLPKTPWNDFAENDSQEGAKIETTAKFSQIAAWTPYIIMAALLVLSRTVAPLKAWLSSFNISWTGLMGTELKASFATLYAPGAFFVAVCILGFFLFKMKSPAIKQSIGVSCKSMLPTIISLGASVPMVKIFLNSGVNGAGLASMPVALADMLGQSMGAVWAWMAPIVGIFGAFLSGSATFSNMMFSSLQYSVADNIGMNHTLVLALQGIGANAGNMMCVMNVVAAATVVGMAGRESEIIRKTMPVAIGYALLAGTIATLWGGF Shewanella oneidensis MR-1 MR1 200013 SO0827 lldP propionate/L-lactate/D-lactate transporter Specifically important for propionate utilization. Another study named it lctP2 and found that it was involved in utilization of both L- and D-lactate (PMC5603553) L-lactate permease (NCBI ptt file) MTWTQTYTPLGSLWLTAIVALLPIVFFFLALTVLKLKGHIAGALTLLIALAVAIITYKMPVSIALASAIYGFSYGLWPIAWIIITAVFLYKITVKTGQFEIIRSSVISVTEDQRLQMLLVGFSFGAFLEGAAGFGAPVAITAALLVGLGFNPLYAAGLCLIANTAPVAFGAMGIPIIVAGQVSSLDPFHIGQLAGRQLPILSIIVPFWLIAMMDGIRGIRQTWPATLVAGVSFAVTQFLTSNFIGPELPDITSALVSLICLTLFLKVWQPKEIFTFSGMKQRAVTPKSTFSNGQIFKAWSPFIILTAIVTLWSIKDVQLALSFATISIEVPYLHNLVIKTAPIVAKETPYAAIYKLNLLGAVGTAILIAAMISIVVLKMSISNALTSFKDTLIELRFPILSIGLVLAFAFVANYSGLSSTLALVLAGTGVAFPFFSPFLGWLGVFLTGSDTSSNALFGALQANTANQIGVTPELLVAANTTGGVTGKMISPQSIAVACAATGLAGKESDLFRFTLKHSLFFCTFIGVLTVLQAYIVPWTLVFFTK Azospirillum brasilense Sp245 azobra AZOBR_RS15925 AZOBR_RS15925 gluconate TRAP transporter, small permease component Specifically important for gluconate utiliation. This region was originally annotated as a pseudogene, but there is a reading frame of 179 a.a.; for its sequence, see AZOBR_p130075 or G8AR26. The large compoennt is AZOBR_RS15915. C4-dicarboxylate ABC transporter permease Azospirillum brasilense Sp245 azobra AZOBR_RS15915 AZOBR_RS15915 gluconate TRAP transporter, periplasmic solute-binding component Specifically important for gluconate utilization. The small component is AZOBR_RS15925 (misannotated as a pseudogene). ABC transporter substrate-binding protein MKLLRSVLLATGLAAAILAPVAASAQDIKPRLIRFGYGLSESSNQGRAVKFFVEDMAKRSGGKLKVKGFADASLGSDIQMQNALIGGAQEMMVGSTATLVGIVKDFAVFDLPFLFNNEQEADAVFDGPFGQKLAAKLNDKGLVGLVYWENGFRNLTNSKRPVEKVEDLKGIKLRVMQNPVYIDMFNGFGANAVPLSFSELFTAMETGTVDGQENPVTTIQSSKFYEVQKYLTISKHVYSPWIVLASKRWYDGLSADERKIINEAAVASRDFERKDSREASKQSIAYLKDKGMQINELSDAELGRMREMVKPAMDKFAADGGADLLNELQGEISKVRK Pseudomonas stutzeri RCH2 psRCH2 GFF2080 Psest_2123 fusion of gluconokinase (EC 2.7.1.12) and the small permease component of the D-gluconate TRAP transporter This protein has pleiotropic phenotypes which are not explained, but it is most important for fitness with D-gluconate as the carbon source, consistent with its putative roles as part of the tripartite gluconate transport system and as gluconate kinase. Also, the N-terminal part is 49% identical to PP3416 or gnuK from P. putida, which is the catabolic gluconate kinase (PMC1951859). The SEED and KEGG annotations ignore the dctQ-like C-terminal portion. carbohydrate kinase, thermoresistant glucokinase family MPSVHTSKASALPVLVVMGVSGSGKTETSHAVADALGLPHIEADNFHPAENVARMRAGTPLSDADRMEWLHALIAEMQRTLAAGSGFVLACSALKRSYRELLRSAVPELRFAHLAIDYETAVQRVGGRAGHFMPISLVDSQFATLESPEGEPGVLTVDASQPREGVLRQIVEWMQGSGLDELIETRVDLSSRPFDSATTAPPLTNEPIYSGRVAQHFDRLTDWLMAALMAFMVIVVFSSVVLRYAFGTGWTGAEELSRLAFVWLVFVGVASSMRRGELMSFSMLRDRFPRLFRRVVDSLSWLLVAAASCLAAWGGWNQMQFGWTINSPVVGYPLGLAMLPVAASMVALAVLALLQLVNVWRRDQPSATAAANVTAD Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_3228 gluconate TRAP transporter, small permease component Specifically important for gluconate utilization Tripartite ATP-independent periplasmic transporter, DctQ component MSSPAQDAVPQSRFARVSQVLMASCLGVMAVAVFINVVLRYGFGSGVAASEELSRLLFVWMVFIGAAAAYPAGEHMAFTSLAGLLAKRPVAFAALTAVIRLLVMAACAMLAWGAWQQVVVGMGSRSVVMAYPAALLPLPAFLCAVAIGVMATIELIQRKPLDLGHGAEVE Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_3227 gluconate TRAP transporter, large permease component Specifically important for gluconate utilization TRAP-type C4-dicarboxylate transport system, large permease component VMLGLTPEAMAFVVFSLGMLVLMGTGMNMGLALVLTGAGMAWVLDFWDAQLLAQNLVAGVDSFPLLAVPFFILAGELMNSGGISRRIIDMAQAWVGHIRGGLGYVAIGAAVLMASMSGSALADTAALATILLPMMRQQGYPMNTSAGLIASGGIIAPIIPPSMPFVIYGVTTNTSISALFVSGIVPGLMMGVGLIFAWRWVLRDLDLPQGEPLPVKDRLRATARAFWAMLMPLIIIGGMKTGVFTPTEAAVVAAFYALVVALFIHREMKLADIYGVLVRAAKTTSIVMFLCAGAQVASYMITLADLPNVLTSWLGPLVENPRLLMAVMMIVLVLIGTALDLTPTILIFAPVMLPIAVKAGIDPVYFGLMFVLNGAIGLITPPVGTVLNVVAGVGRISMHSVIKGVNPFLFTYVLILALLVVFPQIVTAPVVWLR Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_3226 gluconate TRAP transporter, periplasmic solute-binding component Specifically important for gluconate utilization TRAP-type transport system, periplasmic component, predicted N-acetylneuraminate-binding protein MKTFRRTLLAALSVAAITCSFQAAAQDFKPRIIRFGYGLNEVSNQGRATKLFAEEVEKASGGKMKVRAIGAAALGSDVQMQQALIGGAQEMMVGSTATLVGITKEMAIWDTPFLFNNAKEADVVLDGPVGQKVMDKLQEKGLVGLVYWENGFRNLTNSKRPVNKLEDMDGIKLRVMQNNVFLDSFKTLGANAVPLPFSELFTALETKTVDGQENPYNTILSSKFYEVQKYLTVTNHVYSPWIVLVSKKYWDGLSKAEQKVLLDAAKKSRDFERQDTRAEADKALADLKGKGMQVNELPAAEANRMREKLSAVNASIAANVGESLWKDVQGAVAQARAAK Caulobacter crescentus NA1000 Caulo CCNA_00096 CCNA_00096 asparaginase (EC 3.5.1.1) Specifically important for utilization of asparagine as a nitrogen source L-asparaginase MSNKRFSLALHGGAGAKRGHDYGVEIAHMRGLVEAARDRLAAGAGALDVAVETVVGLEASGLYIAGKGASPNADGEYELDASLMDGATLRAGSVAALQGFKSPILAARAVMEHTPHVMLAGQGAIAFAREQGLETVEDPDAWFTRAGAFEDNHPPDALPTGTVGCVVRDGEGRLAAATSTAGVFGKRPGRVGDSPIIGAGAWADGHAAVSCTGQGEYFIRAAVAAQIAHRVRFGGEALDAAAQAAIDSVAALGGHGGLIAVDRDGNIAMPFVSSGLKRAALMPDGTIVSAAF Burkholderia phytofirmans PsJN BFirm BPHYT_RS17540 BPHYT_RS17540 L-aspartate/L-glutamate/L-glutamine:H+ symporter Specifically important for utilization of glutamine, glutamate, or asparagine. amino acid:proton symporter MKSSIQRNIGPFALMLTGLGSIIGSGWLFGAWKAAKIAGPAAVCAWVIGAVVILAIALTYAELGAMFPESGGMVRYARYSHGALVGFISAWANWIAIVSVIPIEAEASIQYMSTWPYPWAHALFVDGSLTTNGLLLSAALVIIYFMLNYWGVKLFARANSAITIFKFLIPGATILGLMFAGFHKENFGEASTFAPYGWSAVLTAVSTSGIVFAFNGFQSPINLAGEARNPAKSVPFAVIGSILLALVIYVLLQIAYIGAVNPSDVMKGWSHFNFASPFAELAIALNLNWLAILLYVDAFVSPSGTGTTYMATTSRMIYAMERNNTMPKMFGNVHPFYGVPRQAMWFNLLVSFIFLFFFRGWSSLAAVISVATVISYLTGPISLMALRRAATDLERPLHIPGMKIIAPFAFVCASLILYWAKWPLTGEIILLMVVALPVYFYFQAKSGFAGWGRDLKAAWWLVAYLPVMAILSLIGSKQFGGHDLIPYGWDMVVVIAFSLVFYYWGVTSGYRSEYLDERSEHDEVLEGMGAH Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_01905 AO356_01905 L-aspartate transporter Specifically important for aspartate utilization amino acid:proton symporter VKKNKLPRRIAMGIALGVLVGWACHHFAGSEQSAKEIASYFSMVTDIFLRMIKMIIAPLVFATLVGGIASMGNSRSVGRIGARAMAWFVTASVVSLLIGMGLVNLFQPGAGLNMDVAQHATAAVPVNTGDFSLKAFIGHVFPRSIAEAMANNEILQIVVFSLFFGFALAGVKRAGYTRITDSIEELAKVMFKITDYVMAFAPIGVFAAIASAITTQGLGLLVDYGKLIAEFYLGILILWALLFGAGYLFLGRSVFHLGKLIREPILLAFSTASSESAYPKTIEALEKFGAPKRVSSFVLPLGYSFNLDGSMMYQAFAILFIAQAYNIDLSFTQQLLILLTLMITSKGMAGVARASVVVVAATLPMFNLPEAGLLLIIGIDQFLDMARTATNVVGNSIATAVVAKSESHEEADEEEGEHAPARSRSEPVPVA Shewanella sp. ANA-3 ANA3 7024899 Shewana3_2073 L-arabinose ABC transporter, substrate-binding component AraU Specifically important for L-arabinose utilization; the gene name is from PMC2996990 periplasmic binding protein/LacI transcriptional regulator (RefSeq) MKHNKIITALGLWAVSATCAYATTVGFSQVGSESGWRTSFSEAVKAEAKQRGIDLKFADAQQKQENQIKAVRSFIAQGVDAIIIAPVVETGWKPVLKEAKRAKIPVVIVDRNIKVDDDSLFLTRIASDFSEEGRKIGQWLMDKTQGNCDIAELQGTVGATAAIDRAAGFNQVIANYPNAKIVRSQTGEFTRAKGKEVMEGFLKAQNGQPLCAVWSHNDEMALGAVQAIKEAGLKPGKDILIVSVDGVPDYFKAMADGDVNATVELSPYLGGPAFDAIDAYLKGNKDQAKLISTTGDVFTQETAAAEYEKRRQQ Shewanella sp. ANA-3 ANA3 7024900 Shewana3_2074 L-arabinose ABC transporter, ATPase component AraV Specifically important for L-arabinose utilization; the gene name is from PMC2996990 ABC transporter related (RefSeq) MSLILELKQISKHYPGVKALEDVSLRLFAGEVHALLGENGAGKSTLVKVMTGAQSKDMGDILFLGEPQHFNTPMDAQKAGISTVYQEVNLVPNLTVAQNLFLGYEPRRLGLIHFKKMYADARAVLTQFKLDIDVSAPLSDYSIAVQQLIAIARGVAMSAKVLVLDEPTASLDAKEVQVLFGILNQLKAKGVAIVFITHFLDQVYQISDRITVLRNGQFIGEYLTAELPQPKLIEAMLGRSLQEQLVDKQEKERTVTRAEAVLLSLEDVSVKGSIQSMNLTVPKGQAVGLAGLLGSGRSEVCNAVFGLDLVDSGSIHLAGQKLNLSQPVDAISAGIALCPEDRKIDGIIGPLSIRENIILALQARIGWWRYLSNTRQQEIAQFFIDKLQIATPDADKPIEQLSGGNQQKVILARWLAIEPILLVLDEPTRGIDIGAHAEIVKLIRTLCDEGMSLLVASSELDELVAFSNKVVVLRDRYAVRELSGAELTSQHVMQAIAEG Shewanella sp. ANA-3 ANA3 7024901 Shewana3_2075 L-arabinose ABC transporter, permease component 1 AraW Specifically important for L-arabinose utilization; the gene name is from PMC2996990 inner-membrane translocator (RefSeq) MKSSAETLSSTRMSADLISPQMNASEAHSSERQPRMQESHKTMVQEKNARYQAGKSTSMGRYLWPLLALSILLLANLFIDSSFFNISYQDDRLYGSLIDILNRSAPVALLSIGMSLVIATGGIDLSVGAVMAIAGAVCANLLLVPDISLVTVIAAGLIVGLLAGCINGGLVSFLGIQPIVATLLLMVAGRGVAQLINQGQIITFQHPGFAAIGVGQFLGLPMPVWIVIGMLTFSQLLLRKTALGLFIEAVGCNAKASRYLGINDKSIKLFAYGIAGLCAALAGMISTADIQGSDANNAGLWLELDAVLAVVIGGAALTGGRFSLILSVVGALIIQTLATTIIVSGLPAKFNLLIKAIVILTVLLLQSAKFRRQLSALFKSKRHADAKPAEKATSAKASAATGEKL Shewanella sp. ANA-3 ANA3 7024902 Shewana3_2076 L-arabinose ABC transporter, permease component 2 AraZ Specifically important for L-arabinose utilization; the gene name is from PMC2996990 inner membrane ABC transporter permease protein YjfF (RefSeq) MIARRFIPLWITASLLLTMFLVGTFQFDGFASGRVVTNLLRDNAFLLITALGMTLVIISGGIDLSVGAVIALSGVVTSLLITEYQWHPLLAFVVILPLGTLFGALMGTIIHVYKLQPFIVTLAGMFLARGLATTLSEESIAIDHPFYDAVAEMSIALPGNGALDLSSLIFILFFVIIAVVMHYTRFGTNVYAIGGNQHSAELMGISIAKTTISIYAISSFLATLAGIVFTFYTFSGYALGAIGVELDAIAAVVIGGTLLTGGSGFVLGTVLGVILMGVIQTYITFDGSLSSWWTKIVIGLLLFFFILLQKLLNGRKTQHG Bacteroides thetaiotaomicron VPI-5482 Btheta 349883 BT0355 L-arabinose/L-arabinobiose symporter Specifically important for L-arabinose utilization and also required for arabinobiose utilization (see PMC5061871). PMC5061871 proposed that it takes up arabinobiose, but because the arabinobiose hydrolase was not identified, it is not certain if arabinobiose is transported. Also important for D-arabinose utilization, but this seems to be a polar effect. Na+/glucose cotransporter (NCBI ptt file) MEALDWLVIGVFFLALIGIIVWVVRQKQNDSADYFLGGRDATWLAIGASIFASNIGSEHLIGLAGAGASSGMAMAHWEIQGWMILILGWVFVPFYSRSMVYTMPEFLERRYNPQSRTILSVISLVSYVLTKVAVTVYAGGLVFQQVFGIKELWGIDFFWIAAIGLVVLTALYTIFGGMKSVLYTSVLQTPILLLGSLIILVLGFKELGGWDEMMRVCGAVTVNDYGDTMTNLIRSNDDANFPWLGALIGSAIIGFWYWCTDQFIVQRVLSGKNEKEARRGTIFGAYLKLLPVFLFLIPGMIAFALHQKYIGAGGEGFLPMLANGTANADAAFPTLVAKLLPAGVKGLVVCGILAALMSSLASLFNSSAMLFTIDFYKRFRPETPEKKLVGIGQIATVVIVILGILWIPIMRSVGDVLYTYLQDVQSVLAPGIAAAFLLGICWKRTSAQGGMWGLIAGMIIGLTRLGAKVYYSNAGEVADSTFKYLFYDMNWLFFCGWMFLFCIIVVIVVSLATEAPTAEKIQGLVFGTATKEQKAATRASWDHWDIIHTVIILAITGAFYWYFW Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1880 Echvi_1880 L-arabinose symporter Specifically important for L-arabinose utilization. transporter, SSS family MSAGFSTLDYVIFIVYALAIVSVGLWVSRTKKGLEKTAQEYFLADKSLTWWAVGASLLAANISAEHFIGTSGSGFAIGLGISAYEWIAAIALIIVAKYFLPIFLKHGVYTMPQFLSERFNKGVSTAFAVFWLLVYVFVNLTSVSYLGALALDKIMGIPLQYGIIGLLIFSGIYSIYGGLEAVAWTDVVQVIILVAGGLITTFLALDAVGMGDGIFAGMSNLYNDAKDHFVMIMPQGRVMVPDGLGGSRDAFQDLPGLAVILGGMWLTNLGYWGFNQYIIQKGLAAKSIEEAKKGLLFAGYLKLLMPIIVVIPGIAAYVLINDYSPEQLAAILNMPVEHIGTIQKSDEAYPWLLRNFIPNGIRGLAFAALAAAIVSSLASMINSTSTIFTMDIYKVYFKPNANNHQLVRTGRIVAVVALAIAMIVAPQLASLDQVFQYIQEYTGYIYPGVVVVFGMGLIWRQATASAALWTAIATIPAGIVFKIFYPEMPFLLRMGYVFIILCFIASLISFAEKKKFANPDYKTNKQAAKTVASSYFFIILGIICAVLGFALFNSYEHVGIESIFMIAALFLMLGTILYTNVKMETADPKSFNTDPVLFNTTSSFNLGAAGIILIVGLLYYFFWM Bacteroides thetaiotaomicron VPI-5482 Btheta 349878 BT0350 ribulokinase (EC 2.7.1.16) Specifically important for L-arabinose utilization, along with the arabinose isomerase BT0351, which forms ribulose, and the ribulose-5-phosphate epimerase BT0353. Also important for D-arabinose utilization, which is not explained. xylulose kinase (xylulokinase) (NCBI ptt file) MKLDAKSTIETGKAILGIELGSTRIKAVLIDQENKPIAQGSHTWENQLVNGLWTYSIDAIWSGLQDCYADLRSNVKKLYDTEIETLAAIGVSAMMHGYMPFNEKEEILVPFRTWRNTNTGRAAAELSELFVYNIPLRWSISHLYQAILDNEAHVKDIKFLTTLAGYVHWQITGEKVLGIGDASGMLPIDPTTNNYSAEMVAKFNNLIASKEYSWKLEDILPKVLSAGENAGVLTPEGCKKLDASGHLKAGIPVCPPEGDAGTGMVATNAVKQRTGNVSAGTSSFSMIVLEKELSKPYEMIDMVTTPDGSLVAMVHCNNCTSDLNAWVNLFKEYQELLGIPVDMDELYGKLYNIALTGDTDCGGLLSYNYISGEPVTGLAEGRPLFVRSANDKFNLANFMRAHLYASVGVLKIGNDILFNEEKIKVDRITGHGGLFRTKGVGQRVLAAAINSPISVMETAGEGGAWGIALLGSYLVNNKKGQSLADFLDESVFVSDAGVEVSPTPEDVAGFNTYIESYKAGLPIEEAAVKFK Sinorhizobium meliloti 1021 Smeli SMc00883 SMc00883 L-arabinolactonase/D-galactonolactonase (EC 3.1.1.15; EC 3.1.1.25) Specifically important for L-arabinose utilization. Also has a mild phenotype on galactose. PMC3430339 reports that a mutant can grow on galactose, but might not have detected a subtle defect. hypothetical protein MTDLVPFSGRTLSEAASELGEGPTFDPGTGTAWWFNITGRELHELHLESGRKAIHPLPFLGSVLAVIDPLRQLIASDQGLFVRDTESSKLGHFATLEEKPGNRSNDGRIHPCGALWIGTMGRSAEKHAGAIYHVAGSRVTKLYSNITIPNAICFSPDGATAYFTDTDVNQLMRVDIDPATALPTGDPVLLSDESTSPGGVDGAVCDADGLIWNARWGASAVEVYKPDGQKVARYAVPATQPSCPAFVGAKAERLLVTSAWQGMDDAARAADPHAGKTFELGIEVKGRFEPAFRL Marinobacter adhaerens HP15 Marino GFF2715 HP15_2659 Citrate uptake transporter, large transmembrane component TctA Specifically important for citrate utilization. tricarboxylic transport TctA METLGFLMDGFAVALTPYNLMFALFGAFVGTLIGCLPGLGPANGVAILIPLAFTLGLPPETAMILLTAVYAGAMYGGRISSILLNIPGDEPAMMTCLDGYPMAQKGRAADALAVSAIASFAGGLIGTIGLIMLAPVLAKFALTFGPAEYFALFLLAFATLGGITGKNPVKTVVAATLGIMISTVGIDISTGTQRYTFGVLELYEGIDFILAIVGLFAISELLFFVESRMGRGRDKMNVGKLTLTMKELVMTIPTQLRGGVLGFISGVLPGAGASLGSFISYTLEKQVVGKKGKFGEGDIRGVVAPEAGNNGASSGALVPMLTLGVPGSGTTAVLLAMLISLNITPGPLMFTQNADIVWGVIAALLIGNVLLLVLNIPLVGFFVKLLSVPPMYLLPIVTMVAFVGIYSISHSTFDLYFMVAFGVAGYFLRKLEIPLVPIILGLLLGPEMEKNLGHALVLSDGEWSVLWASPLAMGLWIVAGLGLILPYLVGPLLRRRMNAAMKESPVSD Marinobacter adhaerens HP15 Marino GFF2716 HP15_2660 Citrate uptake transporter, small transmembrane component TctB Specifically important for citrate utilization. tricarboxylic transport membrane protein MTGLGDRILGLGLLVLAVAYGWAAQQWPEPFGGAETVGPETFPTMLAVVLVAGSLYLMIKPDPDAQWPVGKSAAELGISLVVLVVYTLLLEPLGFVIATTLAVGTLSWRMGAAPRPAFLTGLLSAVVVFVLFNYGLSLSLPAGLLEVH Marinobacter adhaerens HP15 Marino GFF2717 HP15_2661 Citrate uptake transporter, substrate-binding component TctC Specifically important for citrate utilization. tricarboxylic transport TctC MTTMIIKRTLSFVAAAAVSMSAMAWQPSGKVECLAPADPGGGWDFTCRSVGNVLQDLGLVDGSVQTVNMAGAGGGVAYAHTVSKRAEDNKLLVAASTATTTRLAQKQFPGMNADMVTWVGALGADYGIIAVGKNSEYQNLSELMAAVKANPKSVKFAGGSARGGWDHLKVLIAAKAAGADKLPSIPYLSYNNGGEAMSQVVGGQVDAFTGDISEATGFLESGDLRVVAVLAEERLPGKFSDLPTAKEQGIDAVGPNWRGFYMPKGASEEAKSYWVEAVDTLYASEEWKKVMKSNGLIPFHPPASQFDEFVRNQVQDIENLSREIGLLK Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS12130 HSERO_RS12130 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase IolD (EC 3.7.1.22) Specifically important for utilizing m-Inositol. 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase MNAQVNVRPTLRLTMAQALVRYLDALRIQTPQGVLPLFGGVFSIFGHGNVAGMGEALYQYRATLPTYRAHNEQAMAHSAIAYAKAHLRQRMMAVTTSIGPGATNLLTAAALAHVNRLPVLLLPGDVFVSRRPDPVLQQLEDFNDPGLSVNDAFRPLSRMFDRICYPEQLLTALPRAIQVLTDPAQCGPVTLALPQDVQTMAYDYPLDFFSPRVIVPRAQAPAAQELEDAVALLRQARQPLLIAGGGVLYGNACEHLRRFAEQHGVPVAETQAGKSALPWSHALQMGAIGVTGSPAANALAQEADVVIAVGTRLQDFTTGSHTLFAQARLLNLNVNAMDAHKWRGLALQADAGLGLEALSHALEGWRSAPEWHARAHTLAQDWRERVAQITGQTDTGGRLPYDGEVIGAIQRSVADSPSQDIVVCAAGTLPAELHKLWRAGRPGAYHVEYGYSCMGYEVAGGLGVKLAQPQREVIVIVGDGSYLMMNSELATSVMLGAKLIVVVLDNRGYGCINRLQQACGGAPFNNMLADCLQAGPGAPAIDFAAHARSLGALGENVKTITELEAALQRARAADRSYLVCIDTDASRTTDDGGCWWEVAVPEVSPRSQVQQARSQYEQARQAQSV Klebsiella michiganensis M5al Koxy BWI76_RS03090 BWI76_RS03090 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase IolD (EC 3.7.1.22) Specifically important for utilizing m-Inositol. 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase MGKLRLTMAQALVKFLDNQYLEVDGEEHKFVKGIFAIFGHGNVLGMGQALEQDSGEMRVYQGRNEQGMAHVATGFARQSLRRQIIACTSSIGPGAANMITAAATATANRIPLLLLPGDVFATRQPDPVLQQIEQSHDLSITTNDAFRAVSKYWDRITRPEQLMSACINAMRVLTDPAETGAVTLCLPQDVQGEAWDYPESFFTRRVHRLDRRPASAAQLADAVAAIKASRKPLIVCGGGVKYSGAGEALTRFAERYGVPFAETQAGKGSVVSSHPYNVGGVGETGCLAANLLAKEADLVIGLGTRFSDFTTSSKWIFQHPGVRFLNINVSNFDAWKLDGIPMLADAREALTALDGALSGESWQAGWGEQIESVQSRQLKETQRVYQAVWQETAFVPEIDDHLDRESVYREFRQITDSTLTQSSVLGVLNETLPADAVIVAAAGSLPGDLQRVWRNRAANTYHVEYGYSCMGYEVSAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINIVLLDNMANGCINNLQMEHGMDSFGTEFRFRCAESGQLQGGLVPVDFATVAAGYGCKTWRVTTLEELRHALDAARRETVSTLIDIKVLPKTMVHKYGSWWNVGVAQSALSERIRKVAQMINEKRAQARDY Phaeobacter inhibens BS107 Phaeo GFF710 PGA1_c07250 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase IolD (EC 3.7.1.22) Specifically important for utilizing m-Inositol. 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase IolD MTTPPKTVKLTTAQAIIRWLSNQFIEVDGEELRLCGGGFGIFGHGNVTCLGEALYEARDALPLYRGQNEQSMGFAAAGYAKQWLRQRFMFCTASAGPGTSNLLTSAALAHANRLPMLMLCGDTFLTRLPDPVLQQMENFNDPTFGVNDAFKPVSRYWDRITHPAQIIQSLPAAIATMLDPGDCGPAFLGLPQDVQGWTYDYPEVFFEKKIHRIRRVTPDASEIAEAAAALRGAKRPMIIAGGGVQYSRAVAELTAFAETHQIPVVETIAGRANLRDTHPLNIGPIGVTGSDSANAIAAEADVILAVGTRLQDFTTGSWTAFAQDAQFISINAARHDAGKHRSLPVVGDAQRALRDLGAACEGYSTPQDWVARAQEERHSWVAYVADNVSYGDNRPNSYAQAIGVVNALCNPKDRVVAAAGGLPAEVTANWRTLEPGTVDVEFGFSCMGYEIAGAWGARIAQAEREPDRDTIVFVGDGSYMMLNSDIYSSVLSQKKLIILVLDNGGFAVINKLQNNTGNTSFNNLLEDCPTIPEAFGVDFASHAASMGALTETVANPAELGEAFKRAQASDRTTVIVMKVDAYEGWTTEGHAWWEVGTPHITNDPKVQEAHVDWESSRSRQRRGV Sinorhizobium meliloti 1021 Smeli SMc01166 SMc01166 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase IolD (EC 3.7.1.22) Specifically important for utilizing m-Inositol. malonic semialdehyde oxidative decarboxylase MSQKTVRLTMAQAVARFLTRQMTIIDGERVPIFGGVFAIFGHGNVAGVGEALYGVRETLPTYRAQNEQGMANAAIAFAKASFRRRFMACTTSIGPGALNMVTSAALAHVNRLPVLLLPGDVFANRRPDPVLQQVESFGDGTISANDCFKPVSRYFDRITRPEQIIPALRRAMQVLTDPADCGPVTLSLCQDVQAEAYDYPESFFDEKVWVPRRIEPDLDELASAIEALRSAKKPIIIAGGGVLYSEASAELAAFAEKHGIPVVETQAGKSALPHSHPLNMGSVGVTGTSASNALAEEADVVLAVGSRLQDFTTGSWALFKNEALKIIGLNVQAFDAGKHEGQPLISDARAGLNRISGGLGSYKADSAWTERAKAGKAEWLAAAERATATTNAALPSDAQVIGAVQRARGGRKTTLVCAAGGLPGELHKLWQAEEPGGYHMEYGFSTMGYEVAGGLGVKLAKPDSDVIVMVGDGSYMMLNSEIASSIMLGAKFTVVLLDNAGYGCINRLQMGTGGANFNNLLKDTHHVELPQIDFAAHAAAMGAVTRKVGSIPELEAALAETADEVRTTVIVIDTDPLITTEAGGHWWDVAVPEVSDRDQVKAAREGYEKALQAQRFG Pseudomonas simiae WCS417 WCS417 GFF2328 PS417_11870 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase IolD (EC 3.7.1.22) Specifically important for utilizing m-Inositol. 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase MTTTRLTMAQALVKFLDNQYIEVDGVQSKFVAGVFTIFGHGNVLGLGQALEQDAGDLVVHQGRNEQGMAHAAIGFAKQHLRRKIYACTASVGPGAANMLTAAATATANRIPLLLLPGDVYASRQPDPVLQQIEQFHDLSISTNDAFRSVSKYWDRINRPEQLMTAAIHAMRVLTDPAETGAVTLALPQDVQGEAWDYPDYFLQKRVHRIDRRPATAAMIGDALAAFRGKRKPLIICGGGVKYSGANATLQAFAERFDIPFAETQAGKSAVVSSHPLNVGGIGETGCLAANLLAPEADLIIGIGTRYTDFTTSSKSLFKHAEVKFLNLNISPCDALKLDGVQVLADAHVALEALADALGDYRSGWGGQIAEAKAQLEAEVDRVHQVEYAGDGFVPEVDDHLDRTVLREFIELTGSCLTQSRVLGVLNEALADDAIIVAAAGSLPGDLQRAWRSKGVNTYHVEYGYSCMGYEINAALGVKLAEPTKEVYALVGDGSYMMLHSELATSIQERRKINVVLLDNMAFGCINNLQIGNGMDSFGTEFRYRNPESGKLDGGLVPVDFAMSAAAYGCKTYKVSSVEQLEAALADARKQTVSTLIDIKVLPKTMIHGYLSWWRVGVAQVSTSERTNAAAKKLNEHLAKARQY Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_4279 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase IolD (EC 3.7.1.22) Specifically important for utilizing m-Inositol. Epi-inositol hydrolase (EC 3.7.1.-) MTTTRLTMAQALVKFLDNQYIEVDGVQSKFVAGIFTIFGHGNVLGLGQALEQDSGDLIVHQGRNEQGMAHAAIGFAKQHLRRKIYACSSSVGPGAANMLTAAATATANRIPLLLLPGDVYACRQPDPVLQQIEQFHDLSISTNDAFKAVSKYWDRINRPEQLMTAAIHAMRVLTDPAETGAVTLALPQDVQAEAYDYPDYFLQKRVHRIERRPATEAMLGDAVALFKGKHKPLIICGGGVKYSGANAALQAFAERFDIPFAETQAGKSAVVSSHPLNVGGIGETGCLAANLLAKDADLIIGVGTRYSDFTTASKSLFKHPDVQFLNLNISPCDALKLDGVQLLADAKTGLQALAEVLGDYRSSWGDQPRQAKTQLDEEVDRIYQVEYQAKDFVPEINDHLDPAVLREFIELTGSCLTQSRVLGVLNETLADDAVIVAAAGSLPGDLQRSWRSKGVNTYHVEYGYSCMGYEVNAALGVKLAEPEREVYALVGDGSYMMLHSELATSIQERRKINVVLLDNMTFGCINNLQMEHGMDSFGTEFRFRNPETGKLDGGFVPVDFAMSAAAYGCKTYKVNTVEQLQDALADARLQTVSTLIDIKVLPKTMIHKYLSWWRVGVAQVSTSARTDAVAKTLNERLAKARQY Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_21360 AO353_21360 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase IolD (EC 3.7.1.22) Specifically important for utilizing m-Inositol. 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (decyclizing) MSTTRLTMAQALVKFLDNQYVEVDGVQSKFVAGIFTIFGHGNVLGLGQALEQDSGDLIVHQGRNEQGMAHAAIGFAKQNLRRKIYACSSSVGPGAANMLTAAATATANRIPLLLLPGDVYASRQPDPVLQQIEQFHDLSISTNDAFKAVSKYWDRINRPEQLMSAAIHAMRVLTDPAETGAVTLALPQDVQAEAYDYPDYFLQKRVHRIDRRPATEAMLGDAVALLKGKRKPLIICGGGVKYSGANTALQAFAERFDIPFAETQAGKSAVVSSHPLNVGGIGETGCLAANLLAKEADLIIGIGTRYSDFTTSSKWLFQHPEVKFLNLNISPCDALKLDGVQLLADARSGLQALSEALTDYRSSWGDQPHQAKAQLDEEVDRVYQVEYQTQDFIPEINDHMEPAVLREFIELTGSCLTQSRVLGVLNQTLADDAVIVAAAGSLPGDLQRSWRSKGVNTYHVEYGYSCMGYEVNAALGVKLAEPTREVYALVGDGSYMMLHSELATSIQERRKINVILLDNMTFGCINNLQMEHGMDSFGTEFRFRNPSTCKLDGGFVPVDFAMSAAAYGCKTYKVNTVEQLQAALADARLQTVSTLIDIKVLPKTMIHKYLSWWRVGVAQVSTSARTDAVAKTLNERLAKARQY Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_23185 AO356_23185 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase IolD (EC 3.7.1.22) Specifically important for utilizing m-Inositol. 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (decyclizing) MTTTRLTMAQALVKFLDNQYVEVDGVQSKFVAGVFTIFGHGNVLGLGQALEQDSGDLVVHQGRNEQGMAHAAIGFAKQHLRRKIYACSSSVGPGAANMLTAAATATANRIPLLLLPGDVYASRQPDPVLQQIEQFHDLSISTNDAFKAVSKYWDRINRPEQLMTAAIQAMRVLTDPAETGAVTLALPQDVQAEAYDYPDYFLQKRVHRIDRRPATEAMLGDARALLKGKRRPLIICGGGVRYSGANAALQAFAERFDIPFAETQAGKSAVVSSHPLNVGGVGETGCLAANLLAKKADLIIGIGTRYSDFTTGSKWLFQHPDVQFLNLNISPCDALKLDGVQLLADARSGLESLSAALGDYRAEWGGQIADAKAQLDAEVDRIYQADYQAEEFLPEIDDHMDPAVFREFIELTGSCLTQSRVLGTLNETLADDAIIVAAAGSLPGDLQRAWRSKGVNTYHVEYGYSCMGYEVNAALGVKLAEPDKEVYALVGDGSYMMLHSELATSIQERRKINVVLLDNMAFGCINNLQMGNGMDSFGTEFRFRNPDTGKLDGDFVPVDFAMSAAAYGCKTYKATTLEELRAALADARRQTVSTLIDIKVLPKTMIHSYLSWWRVGVAQVSTSARTDAVAKTLNERLAKARQY Burkholderia phytofirmans PsJN BFirm BPHYT_RS13925 BPHYT_RS13925 5-deoxy-D-glucuronate isomerase (EC 5.3.1.30) Specifically important for utilizing m-Inositol. 5-deoxyglucuronate isomerase MSLLVKAQREGQTIARVTPESACWRYVGFAAYRLGENEVVHVFEPSRETCIVVLTGAVDIETADTKWSSLGSRDSVFEDAAPYAVYLPPNVRITVRACRDAEIGVASAPAKGELPARLIEPGSMKRSTRGKGLNTRYVCDILPQTEPAESLLVVEVRTPGGHASSYPPHKHDTDNVPHESSLEETYYHRLDPPQGFAFQRVYTDMRDIDESMAVENHDVVMVPRGYHPVIVPYGYDSYYLNVMAGGQRVWHFRNDPAHEWIINKDA Klebsiella michiganensis M5al Koxy BWI76_RS03075 BWI76_RS03075 5-deoxy-D-glucuronate isomerase (EC 5.3.1.30) Specifically important for utilizing m-Inositol. 5-deoxy-glucuronate isomerase MSLLAKAKKEGQIQHITPQSAGWKYIGFDVWMLKKGQTVTLESGDRELCLVLVAGLASVKTTRADFPNLGQRMSPFERTPPWSVYVPPQDKVEVTADSDLELAVCSAPGKGTLPARVISPQDVGVEHRGKGRNQRLVHNILPDSAQADCLLVVEVYTEEGATSSWPSHKHDTALPGQETQLEETYYHRFDPPQGFAFQRVYTDDRSLDACMAPYNHDVVMVPRGYHPVAAIAGYDSYYLNVMAGPDRKWMFTWEEDHAWINSPDYPRHD Phaeobacter inhibens BS107 Phaeo GFF708 PGA1_c07230 5-deoxy-D-glucuronate isomerase (EC 5.3.1.30) Specifically important for utilizing m-Inositol. putative myo-inositol catabolism protein MHIAPHDNQNKAIVEAENDLVPLNYFNIVKLTKGQTFEYQVPGYETCIVPATGTVDIEVEGLSYAGVGKRTVDVWDGEPEGVYIPVGAKVTITCTTDATETFIAGAKYDKVLEPFDVRAGGIDKVQYGSDDTKTHRKIKHILGQKQHDKVGRLLVSELFTVGQGGWSGFPAHKHDTDRKDADGNIIETRHDETYNFRFRPNHGSGVQILQREEGKPGDAYQLMDGSTIMIDKGYHPCAVMPGYEMYYFTILGGLSQRSLIQYFQPTHAYQVETIPGIKDMVAKFK Sinorhizobium meliloti 1021 Smeli SMc00432 SMc00432 5-deoxy-D-glucuronate isomerase (EC 5.3.1.30) Specifically important for utilizing m-Inositol. myo-inositol catabolism protein MSRLLVKPKAQAGLMQEITPESAGWTYVGFALHRLQPGETAGGETGEKELCLVLVSGKAKISVDGEDFGELGERMTPFEGRPYAVYVPKGSSWQAEAATALDLAVCSAPGGEGFKAKVIRPGTHPQMTRGKGTNTRYVTNIMPEDDGSAQSLLVVEVITPGGHTSSYPPHKHDEDNLPAESYLEETYYHRLNPPQGFAMQRVYTDDRSLDETMAVEDGDVTLVPKGYHPVAAIHGYDSYYLNVMAGPKRIWKFHNAREHEWLFTGV Pseudomonas simiae WCS417 WCS417 GFF2326 PS417_11860 5-deoxy-D-glucuronate isomerase (EC 5.3.1.30) Specifically important for utilizing m-Inositol. 5-deoxyglucuronate isomerase MSLLVKSSKRGQTMVALEAGRLEYVGFCAYRLSLGETLPVSAGDKELCLVLLSGRVNIEGEGFNWQNLGDRQSVFEDKSPFAAYLPPGTDALVTALSDVQIAVCAAPGTVGYEPRLIRPENCKRSVRGKGANTRYVCDILPDSEPAHSLLVVEVRTPSGHSSSYPPHKHDTDDLPHQSFLEETYYHQINPPQGFVFQRVYTDDRSIDQAMAVENSDLVVVPKGYHPVSVPYGYESYYLNVMAGPKRAWHFHNDPQHSWLLDL Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_21345 AO353_21345 5-deoxy-D-glucuronate isomerase (EC 5.3.1.30) Specifically important for utilizing m-Inositol. 5-deoxy-glucuronate isomerase MSLLVKSSAKGRTLVEVPAGALEYVGFSAYRLSLGETLPVSAGDKELCLVLLSGRVDVSGEAPGQGAFNWDNIGDRQSVFEDKSPFAAYLPPGSQAQVVALSDVQIAVCAAPGSASAGLAPRLITPDSMKRSVRGKDANTRYVCDILPDTESAHSLLVVEVRTPSGHSSSYPPHKHDTDDLPHQSFLEETYYHQVNPPQGFVFQRVYTDDRSIDQAMAVENSDLVVVPKGYHPVSVPYGYESYYLNVMAGPKRVWQFHNDPQHSWLLDL Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_23170 AO356_23170 5-deoxy-D-glucuronate isomerase (EC 5.3.1.30) Specifically important for utilizing m-Inositol. 5-deoxy-glucuronate isomerase MSLLIKSHSSGRTMVQLPAGELEYVGFAAYRLSLGETLPVAAGDQELCLVLLSGRISLKGEAPGQGAFDWDNLGDRQSVFEDKSPYAAYLPPGSQAQVTALSDVQVAVCAAPGSARNEYGPRLIRPESMKRSVRGKGANTRYVCDILPDSEPAHSLLVVEVRTPSGHSSSYPPHKHDTDDLPHQSFLEETYYHQVNPSQGFVFQRVYTDDRSIDQAMAVENSDLVVVPKGYHPVSVPYGYESYYLNVMAGPKRVWQFHNDPQHSWLLDL Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_514 5-deoxy-D-glucuronate isomerase (EC 5.3.1.30) Specifically important for utilizing m-Inositol. 5-deoxy-glucuronate isomerase (EC 5.3.1.-) MSLLIKSHSSGRTMVQLPAGELEYVGFAAYRLSLGETLPVAADDKELCLVLLSGRISLKGEAPGQGAFDWDNLGDRQSVFEDKSPYAAYLPPGSQAQVTALSDVQIAVCAAPGSAQNSYGPRLIRPDSMKRSVRGKGANTRYVCDILPDSEPAHSLLVVEVRTPSGHSSSYPPHKHDTDDLPHQSFLEETYYHQVNPSQGFVFQRVYTDDRSIDQAMAVENSDLVVVPKGYHPVSVPYGYESYYLNVMAGPKRVWQFHNDPQHSWLLDL Sinorhizobium meliloti 1021 Smeli SMc03201 SMc03201 branched-chain alpha-ketoacid dehydrogenase, E1 component alpha subunit (EC 1.2.4.4) Specifically important for utilizing L-Leucine. 2-oxoisovalerate dehydrogenase subunit alpha MDEFSRLSLHVPEPAVRPGDLPDFSNVKIPKAGSVPRPDVDVDPEEIRDLAYSIIRVLNREGEAVGPWAGFLSDEELLTGLRHMMLLRAFDARMLMAQRQGKTSFYMQHLGEEAVSCAFRKALRKGDMNFPTYRQAGLLIADDYPMVEMMNQIFSNELDPCHGRQLPVMYTSKEHGFFTISGNLATQYVQAVGWAMASAIKNDTRIAAGWIGDGSTAESDFHSALVFASTYKAPVILNIVNNQWAISTFQGIARGGSGTFAARGLGFGIPALRVDGNDYLAVYAVARWAAERARLNLGPTLIEYVTYRVGAHSTSDDPSAYRPKTESEAWPLGDPVLRLKKHLILRGAWSEERHAQAEAEIMDEVIQAQKEAERHGTLHAGGRPSVRDIFEGVYAEMPPHIRRQRQKAGY Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_3540 branched-chain alpha-ketoacid dehydrogenase, E1 component alpha subunit (EC 1.2.4.4) Specifically important for utilizing L-Isoleucine. Branched-chain alpha-keto acid dehydrogenase, E1 component, alpha subunit (EC 1.2.4.4) MTQAYEPLRLHVPEPSGRPGCKTDFSYLHLTDAGTVRKPPIDVEPADTADLARGLIRVLDDQGNALGPWAENVPVEILRKGMRAMLKTRIYDNRMVVAQRQKKMSFYMQSLGEEAIGSAQALALNIDDMCFPTYRQQSILMARDVPLVDLICQLLSNERDPLKGRQLPIMYSVKDSGFFTISGNLATQFVQAVGWGMASAIKGDTKIASAWIGDGATAESDFHTALTFAHVYRAPVILNVVNNQWAISTFQAIAGGEATTFAGRGVGCGIASLRVDGNDFYAVYAASAWAAERARRNLGPTMIEWVTYRAGPHSTSDDPSKYRPADDWSHFPLGDPIARLKQHLIKIGQWSEEEHAAVSAELEAQVIAAQKEAEQYGTLAGGQIPSAATMFEDVYKEMPEHLKRQRQELGI Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_26635 AO353_26635 branched-chain alpha-ketoacid dehydrogenase, E1 component alpha subunit (EC 1.2.4.4) Specifically important for utilizing L-Isoleucine; L-Leucine. 2-oxoisovalerate dehydrogenase MNQAYEPLRLHVPEPSGRPGCKTDFSYLRLTDAGTVRKPPIDVEPADTADLAKGLIRVLDDQGNALGPWAEGVPVEILRKGMRAMLKTRIFDNRMVVAQRQKKMSFYMQSLGEEAIGSAQALALNIDDMCFPTYRQQSILMAREVPLVDLICQLLSNERDPLKGRQLPIMYSVKDAGFFTISGNLATQFVQGVGWGMASAIKGDTKIASAWIGDGATAESDFHTALTFAHVYRAPVILNVVNNQWAISTFQAIAGGEATTFAGRGVGCGIASLRVDGNDFVAVYAASAWAAERARRNLGPTMIEWVTYRAGPHSTSDDPSKYRPADDWSHFPLGDPIARLKQHLVKIGQWSEEEHVALSAELEAEIIAAQKEAEQYGTLAGGQIPSAATMFEDVYKEMPEHLKRQRQELGI Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_22990 AO356_22990 branched-chain alpha-ketoacid dehydrogenase, E1 component alpha subunit (EC 1.2.4.4) Specifically important for utilizing L-Isoleucine. 2-oxoisovalerate dehydrogenase MNPAYEPLRLHVPEPSGRPGCKTDFSYLHLSDAGTVRKPPIDVEPADTADLARSLIRVLDDQGNALGDWAADIPVEILRKGMRAMLKTRIYDNRMVVAQRQKKMSFYMQSLGEEAIGSAQALALNIDDMCFPTYRQQSILMAREVPLVDLICQLLSNERDPLKGRQLPIMYSVKDAGFFTISGNLATQFIQGVGWGMASAIKGDTKIASAWIGDGATAESDFHTALTFAHVYRAPVILNVVNNQWAISTFQAIAGGEATTFAGRGVGCGIASLRVDGNDFMAVYAASRWAAERARRNLGPALIEWVTYRAGPHSTSDDPSKYRPADDWSHFPLGDPIARLKQHMVKIGQWSEEEHAAVSAELEAEVIAAQKEAEQYGTLAGGQIPSAATMFEDVYKEMPEHLKRQRQQLGI Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_481 branched-chain alpha-ketoacid dehydrogenase, E1 component alpha subunit (EC 1.2.4.4) Specifically important for utilizing L-Isoleucine. Branched-chain alpha-keto acid dehydrogenase, E1 component, alpha subunit (EC 1.2.4.4) MNPAYEPLRLHVPEPSGRPGCKTDFSYLHLSDAGTVRKPSIDVEPADTADLARSLIRVLDDQGNAHGPWAEDVPLDILRKGMRAMLKTRIYDNRMVVAQRQKKMSFYMQSLGEEAIGSGQALALNIDDMCFPTYRQQSILMAREVPLVGMICQLLSNERDPLKGRQLPIMYSVKDAGFFTISGNLATQFIQGVGWGMASAIKGDTKIASAWIGDGATAESDFHTALTFAHVYRAPVILNVVNNQWAISTFQAIAGGEATTFAGRGVGCGIASLRVDGNDFMAVYAASRWAAERARRNLGPALIEWVTYRAGPHSTSDDPSKYRPADDWSHFPLGDPIARLKQHMVKIGQWSEEEHAAVTAELEAEVIAAQKEAEQYGTLAGGQIPSAATMFEDVYKEMPEHLKRQRQQLGI Sinorhizobium meliloti 1021 Smeli SMc03202 SMc03202 branched-chain alpha-ketoacid dehydrogenase, E1 component beta subunit (EC 1.2.4.4) Specifically important for utilizing L-Leucine. 2-oxoisovalerate dehydrogenase subunit beta MARMTMIEAVRSAMDVSMARDDNVVVFGEDVGYFGGVFRCTQGLQAKYGKTRCFDTPISESGIVGTAIGMAAYGLKPCVEIQFADYMYPAYDQLTQEAARIRYRSNGDFTCPIVVRMPTGGGIFGGQTHSQSPEALFTHVCGLKVVVPSNPYDAKGLLISAIEDPDPVMFLEPKRLYNGPFDGHHERPVTAWSKHELGDVPDGHYTIPIGKAEIRRKGSGVTVIAYGTMVHVALAAAEETGIDAEVIDLRSLLPLDLETIVQSAKKTGRCVVVHEATLTSGFGAELAALVQEHCFYHLESPVVRLTGWDTPYPHAQEWDYFPGPARVGRALAEAMEG Pseudomonas simiae WCS417 WCS417 GFF3430 PS417_17550 branched-chain alpha-ketoacid dehydrogenase, E1 component beta subunit (EC 1.2.4.4) Specifically important for utilizing L-Isoleucine; L-Leucine. 2-oxoisovalerate dehydrogenase MNDHNNSIEVETAMTTTTMTMIQALRSAMDVMLERDDNVVVFGQDVGYFGGVFRCTEGLQTKYGSSRVFDAPISESGIVGVAVGMGAYGLRPVAEIQFADYVYPATDQIISEAARLRYRSAGQFTAPLTMRMPCGGGIYGGQTHSQSIEAVFTQVCGLRTVMPSNPYDAKGLLIASIENDDPVIFLEPKRLYNGPFDGHHDRPVTPWSKHPQAQVPDGYYTVPLDVAAIVRPGSAVTVLTYGTTVYVSQVAAEETGIDAEVIDLRSLWPLDLETIVKSVKKTGRCVVVHEATRTCGFGAELVSLVQEHCFHHLEAPIERVTGWDTPYPHAQEWAYFPGPSRVGAALKRVMEV Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_3541 branched-chain alpha-ketoacid dehydrogenase, E1 component beta subunit (EC 1.2.4.4) Specifically important for utilizing L-Isoleucine. Branched-chain alpha-keto acid dehydrogenase, E1 component, beta subunit (EC 1.2.4.4) MNDHNNNIELETAMTTTTMTMIQALRSAMDVMLERDDNVVVFGQDVGYFGGVFRCTEGLQAKYGTSRVFDAPISESGIVGTAVGMGAYGLRPVVEIQFADYVYPAYDQIISEAARLRYRSAGEFTAPMTLRMPCGGGIYGGQTHSQSIEALFTQVCGLRTVMPSNPYDAKGLLIASIENDDPVIFLEPKRLYNGPFDGHHERPVTPWSKHPAAQVPDGYYTVPLDVAAIARPGKDVTVLTYGTTVYVSQVAAEESGVDAEVIDLRSLWPLDLETITKSVKKTGRCVIVHEATRTCGFGAELTALVQEHCFHYLEAPIERVTGWDTPYPHAQEWAYFPGPSRVGAALKRVMEV Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_22985 AO356_22985 branched-chain alpha-ketoacid dehydrogenase, E1 component beta subunit (EC 1.2.4.4) Specifically important for utilizing L-Isoleucine. 2-oxoisovalerate dehydrogenase MNDHNNNIALDTAMTTTTMTMIQALRSAMDVMLERDDNVVVFGQDVGYFGGVFRCTEGLQNKYGTSRVFDAPISESGIVGVAVGMGAYGLRPVAEIQFADYVYPASDQIISEAARLRYRSAGEFTAPMTLRMPCGGGIYGGQTHSQSIEAMFTQVCGLRTVMPSNPYDAKGLLIASIENDDPVIFLEPKRLYNGPFDGHHDRPVTPWSKHPSAQVPDGYYTVPLDVAAITRPGKDVTILTYGTTVYVSQVAAEETGIDAEVIDLRSLWPLDLETIVKSVKKTGRCVVVHEATRTCGFGAELVSLVQEHCFHHLEAPIERVTGWDTPYPHAQEWAYFPGPSRVGAALKRVMEV Shewanella amazonensis SB2B SB2B 6937189 Sama_1359 3-methylcrotonyl-CoA carboxylase, alpha (biotin-containing) subunit (EC 6.4.1.4) Specifically important for utilizing L-Leucine. 3-methylcrotonyl-CoA carboxylase alpha subunit (RefSeq) MFNKLLIANRGEIACRVIRTARDMGIKTVAVYSDADRDARHVALADESFYLGESAPASSYLRGELIIDIAKKCGAEAIHPGYGFLSENAAFARACEASGIAFVGPGSDAIDAMGSKSAAKLIMEKAGVPLVPGYHGDDQSDATLLAEAKKIGYPLLIKAAYGGGGKGMRIVESESELKAAIDSARREAASSFGNDKLLMERYLRQPRHVEVQVFADSQGNCVYLSDRDCSIQRRHQKVVEEAPAPGLPDSLRKQMGEAAVAAAKAIDYRGAGTVEFLLDVDMSFFFMEMNTRLQVEHPVTEMVTGQDLVKWQLLVAAGAQLPLEQHEIQIHGHAFEVRIYAEDPNNEFLPASGKLTFLREPEPSRHVRIDSGVRENDVISNYYDPMIAKLIVWDESRPRALARLTRALGDYRVGGLKHNIEFLSNIAEHPAFAQANFSTDFIGRYGDALIGDSRDEADTAFVLAVLTQLRLREAVSQDVAGHDPFSPWSSLKGFRLSSPRRHSVTLLDDAHQSRSAELTESNGRYQLCLNDKLIELSGSIEDSELKCEINGHKMKVTVSLEDGGLTVFLSSGSYHFREVLGQVLEETASSEDKLKAPMNGTVVTHLVAAGDKVSAGQGLLVMEAMKMEYTIEAPFDGVVSEFFFAPGELVSDGTLLLALEMADAAADSKETEA Sinorhizobium meliloti 1021 Smeli SM_b21124 SM_b21124 3-methylcrotonyl-CoA carboxylase, alpha (biotin-containing) subunit (EC 6.4.1.4) Specifically important for utilizing L-Leucine. methylcrotonoyl-CoA carboxylase biotinylated subunit MFSKLLIANRGEIACRIIRTARRLGIRTVAVYSDADGDALHVALADEAIRIGGAPAAESYLASAPIVQAARSVGAQAIHPGYGFLSENADFAEAVAEAGMIFVGPPPAAIRAMGLKDAAKALMERSGVPVVPGYHGEEQDASFLADRAREIGYPVLIKARAGGGGKGMRRVERQEDFGPALEAARREAESAFGDGSVLLERYLTKPRHIEMQVFGDRHGNIVHLFERDCSLQRRHQKVIEEAPAPGMTAEVRRAMGDAAVRAAQAIGYVGAGTVEFIADVTNGLWPDHFYFMEMNTRLQVEHPVTEAITGIDLVEWQLRVASGEPLPKKQADISMNGWAFEARLYAEDPARGFLPATGRLTELSFPEGTSRVDSGVRQGDTITPYYDPLIAKLIVHGQNRSAALGRLQDALKECRIGGTVTNRDFLIRLTEEHDFRSGHPDTGLIDREIERLTAPVAPGDEALALAAIFSTGALDPNRSTDPWSSLGSWQIWGDAHRMVVIEHADVRATVTLASRGRDQFAVRAGASTLPVLVLDRFEGGARLEVAGQKRLIRFSRDREALTLFHGGRNLVFHVPDGLTGGQSSEIADDELVAPMPGLVKLVRVGAGDAVTKGQALVVMEAMKMELTLSASREGTIANVHVAEGAQVSEGTVLVTLMEEAAQ Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_3984 3-methylcrotonyl-CoA carboxylase, alpha (biotin-containing) subunit (EC 6.4.1.4) Specifically important for utilizing L-Leucine. Methylcrotonyl-CoA carboxylase biotin-containing subunit (EC 6.4.1.4) MSAPVLTTLLVANRGEIACRVMRTAKALGLTTVAVHSATDRDARHSREADIRVDLGGSKAADSYLQIDKLIAAAKASGAQAIHPGYGFLSENAGFARAIEAAGLIFLGPPASAIDAMGSKSAAKALMETAGVPLVPGYHGEAQDLETFRDACERIGYPVLLKATAGGGGKGMKVVEDVSQLAEALASAQREALSSFGDSRMLVEKYLLKPRHVEIQVFADQHGNCLYLNERDCSIQRRHQKVVEEAPAPGLSPELRRAMGEAAVRSAQAIGYVGAGTVEFLLDARGEFFFMEMNTRLQVEHPVTEAITGLDLVAWQIRVARGEALPMTQDQVPLIGHAIEVRLYAEDPGNDFLPATGRLALYRESAAGPGRRVDSGVEEGDEISPFYDPMLGKLIAWGEDREQARLRLLSMLDEFAIGGLKTNINFLRRIIGHPAFAAAELDTGFIPRYQEQLLPAPSDLSDEFWQAAAQAFAQSQSSTTRADDLSSPWGIGNGFRAGLPTEITLHLSCEEQDRALTLGDADAHTAQLKGEYLLTEHNGLRRQHRAIRRGDTLYLQWDGELRRIESYDPISAVEASHSHQGGLTAPMNGSIVRVLVEAGQTVEAGAQLVVLEAMKMEHSIRAPHAGIIKALYCQEGEMVSEGSALVELEHA Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_01595 AO356_01595 3-methylcrotonyl-CoA carboxylase, alpha (biotin-containing) subunit (EC 6.4.1.4) Specifically important for utilizing L-Leucine. 3-methylcrotonyl-CoA carboxylase MSAPALTTLLVANRGEIACRVMRTARAMGLTTVAVHSATDRDARHSREADIRVDLGGSKAADSYLQIDKLIAAAKASGAQAIHPGYGFLSENAGFARAIENAGLIFLGPPASAIDAMGSKSAAKTLMETAGVPLVPGYHGEAQDLETFRDAAERIGYPVLLKATAGGGGKGMKVVEDVSQLAEALASAQREAQSSFGDSRMLVEKYLLKPRHVEIQVFADQHGNCLYLNERDCSIQRRHQKVVEEAPAPGLTPQLRRAMGEAAVRAAQAIGYVGAGTVEFLLDARGEFFFMEMNTRLQVEHPVTEAITGLDLVAWQIRVAQGEPLPITQAQVPLLGHAIEVRLYAEDPGNDFLPATGRLALYRESAEGPGRRVDSGVEEGDEISPFYDPMLGKLIAWGEDREQARLRLLSMLDEFVIGGLKTNIGFLRRIVAHPAFAAAELDTGFIPRYQAQLLPEPSELDDAFWFAAAQGVALSLAPHVRGDDAGSPWASTTGMRLGLPRETTLHLSCEGQDRALTLDVTAHCAELEGERLTIEHHGVRRSHRAIRQVDSLYLQWEGDLHRIDLYDPLAAAEASHSHQGGLVAPMNGSIVRVLVGVGQTVEAGAQLVVLEAMKMEHSIRAPKAGVIKALYCQEGEMVSEGSALVAFEE Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2194 3-methylcrotonyl-CoA carboxylase, alpha (biotin-containing) subunit (EC 6.4.1.4) Specifically important for utilizing L-Leucine. Methylcrotonyl-CoA carboxylase biotin-containing subunit (EC 6.4.1.4) MSAPALTTLLVANRGEIACRVMRTAKAMGLTTVAVHSATDRDARHSREADIRVDLGGSKAADSYLQIDKLIAAAKASGAQAIHPGYGFLSENAGFARAIENAGLIFLGPPASAIDAMGSKSAAKALMETAGVPLVPGYHGEAQDLETFRDAAERIGYPVLLKATAGGGGKGMKVVEDVSQLAEALASAQREAQSSFGDSRMLVEKYLLKPRHVEIQVFADQHGNCLYLNERDCSIQRRHQKVVEEAPAPGLTAQLRQAMGEAAVRAAQAIGYVGAGTVEFLLDARGEFFFMEMNTRLQVEHPVTEAITGLDLVAWQIRVAQGEPLPITQAQVPLLGHAIEVRLYAEDPVNDFLPATGRLALYRESAKGPGRRVDSGVEEGDEISPFYDPMLGKLIAWGENREQARLRLLSMLDEFAIGGLKTNIGFLRRIVAHPAFAAAELDTGFIPRYQAQLLPEPGELDDAFWLAAAQGFALSLAPHIRGDDAGSPWASTTGMRLGLSRETTLHLSCEGQDRALTLDVTAHCAELKGERLTIEHHGVRRSHRAIRQGDSLYLHWAGDLHRIDLYDPLAAAEASHSHQGGLAAPMNGSIVRVLVSVGQPVDAGAQLVVLEAMKMEHSIRAPKAGVIKALYCQEGEMVSEGSALVAFEE Shewanella amazonensis SB2B SB2B 6937191 Sama_1361 3-methylcrotonyl-CoA carboxylase, beta subunit (EC 6.4.1.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (6.4.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. propionyl-CoA carboxylase (RefSeq) MTQLTSRVNPRSDEFKQKHDAMAALVADLKDKLAHIEQGGGLVAMERHLSRGKLAPRARVEKLLDPGSPFLELSQFAAFEVYDEDVPAAGIIAGIGRVSGVECMIIANDATVKGGTYYPITVKKHLRAQAIAERCHLPCIYLVDSGGANLPRQDEVFPDRDHFGRIFFNQARMSAKGIPQIAVVMGLCTAGGAYVPAMADESIIVREQGTIFLAGPPLVKAATGEEVSAEELGGGDVHTKISGVADHLAQNDEHALELARKAVSRLNHQKQVELQLSKVKPPKYDINELYGIVGTDLKKPFDVKEVIARIVDDSDFDEFKANYGTTLVCGFARIHGYPVGIVANNGILFSESAQKGAHFIELCCQRKIPLVFLQNITGFMVGKKYEHEGIAKHGAKMVTAVSCATVPKFTVLIGGSYGAGNYGMCGRAFEPTLMWMWPNARISVMGGEQAAGVLATVRKDGLARKGETMSAEEEAKFKAPIIAQYDKEGHPYHASARLWDDGIIDPAQTRDVLGLAISAALNAPIEETRFGVFRM Sinorhizobium meliloti 1021 Smeli SM_b21122 SM_b21122 3-methylcrotonyl-CoA carboxylase, beta subunit (EC 6.4.1.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (6.4.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. methylcrotonoyl-CoA carboxylase non-biotinylated subunit protein MTVLRSHISPSSEEFKANRAAMTEAIATIEDAVRLAAAGGGETARERHVSRGKLLPRDRLATLIDPGTPFLEVGATAAYGMYNDDAPGAGLITGIGRISARECMIVCNDPTVKGGTYYPLTVKKHLRAQEIAAENRLPCVYLVDSGGANLPNQDEVFPDRDHFGRIFYNQANMSAAGIPQIAVVMGSCTAGGAYVPAMSDEAIIVEKQGTIFLAGPPLVRAATGEVVSAEDLGGADVHTRLSGVADHLARDDAHALALARRAVSALNREKPWTVERIEPEPPLYDPEEIAGIVPADLKTPYEIREVIARLVDGSRFDEFKARFGTTLVCGFAHVHGIPVGIVANNGVLFSESAVKGAHFVELCAQRRIPLVFLQNITGFMVGRKYETEGIAKHGAKLVTAVATVKVPKITMLVGGSFGAGNYGMCGRAFSPRFLWTWPNSRISVMGGEQAAGVLSSVRGEALKRSGKPWSEEEEARFRQPVLDLFERQSHPLYASARLWDDGVIDPRKSRDVLALSLSAALNAPIEETRFGLFRM Pseudomonas stutzeri RCH2 psRCH2 GFF1050 Psest_1083 3-methylcrotonyl-CoA carboxylase, beta subunit (EC 6.4.1.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (METHYLCROTONYL-COA-CARBOXYLASE-RXN) was linked to the condition via a MetaCyc pathway. This annotation was also checked manually. Acetyl-CoA carboxylase, carboxyltransferase component (subunits alpha and beta) MAILHTQINIRSPEFAANSAAMLEQVNDLRALLGRVSEGGGATAQQRHVSRGKLLVRERIDTLLDAGSAFLELAPLAAHEVYGEDVAAAGVVAGIGRVEGIECMIIANDATVKGGTYYPLTVKKHLRAQTVARENRLPCIYLVDSGGANLPRQDEVFPDREHFGRIFFNQANMSAMGIPQIAVVMGSCTAGGAYVPAMADETIMVRNQATIFLAGPPLVKAATGEVVTAEELGGADVHCKTSGVADHYAENDEHALSIARRCVANLNWRKLGQLQTREPRAPLYAADELYGVIPAQAKQPYDVREVIARLVDGSEFDEFKALFGTTLVCGFAHLHGYPIAILANNGILFAEAAQKGAHFIELACQRGIPLLFLQNITGFMVGQKYEAGGIAKHGAKLVTAVACAQVPKFTVLIGGSFGAGNYGMCGRAYDPRFLWMWPNARIAVMGGEQAAGVLAQVKQEQSERAGKSLGDDEVAAIKQPILEQYERQGHPYYSSARLWDDGVIDPAQTREVLGLALSAALNAPIEPTRFGVFRM Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_01585 AO356_01585 3-methylcrotonyl-CoA carboxylase, beta subunit (EC 6.4.1.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (6.4.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. methylcrotonoyl-CoA carboxylase MATLHTQLNPRSPEFIANREAMLGHVEALRTLLAQIRQGGGLKAQERHTSRGKLLPRERINRLLDPGSPFLEISPLAAHDVYGEDVPAAGVIAGIGRVEGVECMIVANDATVKGGSYYPLTVKKHLRAQTIAQQNRLPCIYLVDSGGANLPRQDEVFPDREHFGRIFFNQANMSAQGIPQIAVVMGSCTAGGAYVPAMADEAIMVRQQATIFLAGPPLVKAATGEVVSAEDLGGADVHCKISGVADHYADSDEHALALARRSVANLNWRKLGELQQRQPIAPLYSSDELYGVVSADAKQPFDVREVIARLVDGSVFNEFKALFGTTLVCGFAHLHGYPVAILANNGILFAEAAQKGAHFIELACQRGIPLLFLQNITGFMVGQKYEAGGIAKHGAKLVTAVACAKVPKFTVIIGGSFGAGNYGMCGRAYDPRFLWMWPNARIGVMGAEQAAGVLVQVKREQAERSGHPFSAEQEAEIKQPILDQYEEQGHPYYSSARLWDDGVIDPAQTRDVLGLALSASLNAPIEPSRFGVFRM Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2192 3-methylcrotonyl-CoA carboxylase, beta subunit (EC 6.4.1.4) Specifically important for utilizing L-Leucine. Automated validation from mutant phenotype: the predicted function (6.4.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Methylcrotonyl-CoA carboxylase carboxyl transferase subunit (EC 6.4.1.4) MATLHTQLNPRSPEFIANRDAMLGHVEALRTLLAQIRQGGGPKAQERHTSRGKLLPRERINRLLDPGSPFLEISPLAAHEVYGEDVPAAGVIAGIGRVEGVECMIVANDATVKGGSYYPLTVKKHLRAQTIAQQNRLPCIYLVDSGGANLPRQDEVFPDREHFGRIFFNQANMSAQGIPQIAVVMGSCTAGGAYVPAMADEAIMVRQQATIFLAGPPLVKAATGEVVSAEDLGGADVHCKISGVADHYADSDEHALALARRSVANLNWRKQGELQHRLPIAPLYSGEELYGVVSADAKQPFDVREVIARLVDGSVFDEFKALFGTTLVCGFAHLHGYPIAILANNGILFAEAAQKGAHFIELACQRGIPLLFLQNITGFMVGQKYEAGGIAKHGAKLVTAVACAKVPKFTVIIGGSFGAGNYGMCGRAYDPRFLWMWPNARIGVMGAEQAAGVLVQVKREQAERSGHPFSAEQEAEIKQPILDQYEEQGHPYYSSARLWDDGVIDPAQTRDVLGLALSASLNAPIEPSRFGVFRM Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS06555 RR42_RS06555 3-oxoacid CoA-transferase (EC 2.8.3.5), subunit A Specifically important for utilizing L-Leucine. The B subunit is probably RR42_RS06560, but that gene lacks fitness data. succinyl-CoA:3-ketoacid-CoA transferase MNKVYASAAEALAGVVRDGQTIAVGGFGLCGIPEALIAALRDSGAKQLTCISNNAGVDGFGLGLLLATRQIKKMISSYVGENKEFERQYLAGELELEFTPQGTLAEKLRAGGSGIPAFFTKTGVGTIVADGKEIREFDGQQYVMERALTADVALVKAYKADRAGNLVFRRTARNFNPMCAMAGKVTIVEVEHLVDTGTLDPDEVHTPGIFVQRIVLNANPEKRIEQRTVRAAG Shewanella amazonensis SB2B SB2B 6937187 Sama_1357 3-oxoacid CoA-transferase (EC 2.8.3.5), subunit A Specifically important for utilizing L-Leucine. The B subunit is Sama_1356. 3-oxoacid CoA-transferase (RefSeq) MAGLYKVVDSYDQALAGLTDNMTIMVGGFGLCGIPEGLINQMVKLGTKGLTAISNNAGVDDFGLGLLLQNKQISTMIASYVGENATFERQMLSGELNVILTPQGTLAEKIRAGGAGIPAFFTATGYGTPVAEGKETREIKGRHYVLEESLTADFALIRAWKADTMGNLVFRKTAANFNPMMATAGKITVVEVEEIVEPGELDPDHIHTPGIYVDRIIKGSFEKRIEQRTVKKA Shewanella amazonensis SB2B SB2B 6937186 Sama_1356 3-oxoacid CoA-transferase (EC 2.8.3.5), subunit B Specifically important for utilizing L-Leucine. The A subunit is Sama_1357. 3-oxoacid CoA-transferase (RefSeq) MALSREQLAQRVAKELKDGYYVNLGIGIPTLVANYIPDGMQVMLQSENGLLGMGEFPTEETIDPDLINAGKQTVTAVKGASFFSSAESFAMIRGGHVDLTVLGAFEVDVEGSIASWMIPGKLVKGMGGAMDLVAGADNIIVTMMHADKYGNSKLLPKCELPLTGFGCIKRVLTDLAFIEIKDGAFHLLERAPGVTVEEIVEKTAGKLIVPEHVPEMQF Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS34245 RR42_RS34245 branched-chain alpha-ketoacid:ferredoxin oxidoreductase, fused Specifically important for utilizing L-Leucine as a carbon or nitrogen source. indolepyruvate ferredoxin oxidoreductase MNAPLSSAQQDALASVSLDDKYTLEKGRVYLSGTQALVRLPMLQKARDLAAGLNTAGFISGYRGSPLGGVDQALWKAKKHLAASDVVFQPGVNEDLAATAVWGTQQVNLFPDATRDGVFSMWYGKGPGVDRSIDVLKHANSAGSAKHGGVLLLAGDDHAAKSSSVAHQSEHVLLASGIPVLYPSNVQEYLDYGLHGWAMSRYSGLWVSMKCVTDVVESTASVEVDPDRVRIVLPEDFAMPEGGLNIRWPDPPLAQEARLLDHKWYAALAYIRANKLNRVVLDSPNARFGIMTAGKAYLDVRQALSDLGLDDDTCRRIGIRVFKVGCVWPLDAHDAREFATGLEEILVVEEKRQILEYALKEELYNWRDDVRPKVYGKFDERGNHGGEWSLPRGNWLLPAHYELSPALIAKAIATRLEKSDLPTDVRERIAARVALIEAKEREAARPRISVERKPWFCSGCPHNTSTRVPEGSRALAGIGCHYMAMWMDRNTDTFSQMGGEGVAWTGQMHFTGEKHVFVNLGDGTYFHSGLLAVRASIAAKANITYKILFNDAVAMTGGQPVDGVLTVPQIAHQVLAEGASKIVVVTDEPEKYGDGGMLPASVTVHHRDQLDEIQVQLRDTAGVTILIYDQTCATEKRRRRKRGTMADPAKRAFINDAVCEGCGDCSVKSNCLSVEPLETPLGTKRKINQSSCNKDFSCVNGFCPSFVTAEGAQVRKPAAAGGKGALADFSALPQPALPTLERPYGVLVTGVGGTGVVTIGGLLGMAAHLEQKGVTVLDMAGLAQKGGAVISHVQIAPTPAALHATRIATGEARLVIGCDAIVSASPEVLSKTRIDVTAAAINSADTPTADFIKNPNWKFPGASAEQDLRASVGDACAFIDANAWAVKLLADSIYSNPLLLGFAWQKGWVPLRRESLVRAIELNGVAVEKNLLAFDWGRYLAHHGEAALAAQLQITPRAQVVAMPETLDSVIRQREALLTAYQNPAYAARYRAAVESVRAAEKRVGANPRLPLAEAVARNLAKLMAYKDEYEVARLYADPAFLDKLRAQFEGEPGRDYQLSFHLAPPLLAKRDSHGHLVKRRFGPAMLTAFRLLARAKGLRGTAFDVFGKTAERRAERKLIEDYIAMAEEFGATLNADRLDTAVALASLPDDIRGFGHVKEANMEKAAARRVALLAQYRGAAARVAA Sinorhizobium meliloti 1021 Smeli SM_b21126 SM_b21126 3-methylglutaconyl-CoA hydratase (EC 4.2.1.18) Specifically important for utilizing L-Leucine as a carbon or nitrogen source. enoyl-CoA hydratase MTFDTIRCAIDQRGVARVTLARSEKHNALSATMIGELTAVVGRLATDASIRAVILDAEGKSFCAGGDLDWMRQQFSADRPTRIAEATRLAMMLKALNDLPKPLIARVHGNAFGGGVGLISVCDTVIAASGAQFGLTETRLGLIPATISPYVIARTGEARARPLFMSARVFGAEEAKVAGFVTTVVDGTMLDGAVEAAVTAYLVAAPGAAGRAKRLARSLGLPITDAVIAATIEQLADTWETDEAREGVSAFFERRNPSWRQ Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS11480 HSERO_RS11480 D-ribose ABC transporter, substrate-binding component RbsB Specifically important for utilizing D-Ribose. LacI family transcriptional regulator MNKFTRRHFAIAALACAVLPGAAMAQTPAKPKVALVMKSLANEFFLNMENGAREYQKANASKFDLIANGIKDEQDTANQIKIVEQMIVSKVNALVIAPADSKALVPVVKKAIDAGIIVVNIDNKLDDAALKEKGITVPFVGPDNRKGAKLAGDYLGKQLQKGDKVAIIEGVSTTFNAQQRTLGFQDAMKDVGANVVTVQSGQWEIDQGNKVAASILNAHPDIKAILAGNDNMALGAVAAIRAAGKTGKVQLVGYDNINAIKPMLKDGRVLATVDQFAQQQAVFGIETALKALSEKKPQSALGGVVETKVSLVTK Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS11485 HSERO_RS11485 D-ribose ABC transporter, ATPase component RbsA Specifically important for utilizing D-Ribose. ribose ABC transporter ATPase MQPNDSLSQGSPLLTLSGIGKRYAAPVLDGIDLDLRPGQVLALTGENGAGKSTLSKIICGLVDASAGGMMLDGQPYAPASRTQAEGLGIRMVMQELNLIPTLSIAENLFLEKLPRRFGWIDRKKLAEAARAQMEVVGLGELDPWTPVGDLGLGHQQMVEIARNLIGSCRCLILDEPTAMLTNREVELLFSRIERLRAEGVAIIYISHRLEELKRIADRIVVLRDGKLVCNDDIGRYSTEQLVQLMAGELTKVDLDAEHRRIGAPVLRIRGLGRAPVVHPASLALHAGEVLGIAGLIGSGRTELLRLIFGADRAEQGEIFIGDSQEPARIRSPKDAVKAGIAMVTEDRKGQGLLLPQAISVNTSLANLGSVSRGGMLDHAAESSVAQDYVKKLRIRSGSVAQAAGELSGGNQQKVVIARWLYRDCPIMLFDEPTRGIDIGAKSDIYRLFAELAAQGKGLLVVSSDLRELMQICDRIAVMSAGRIADTFSRDDWSQERILAAAFSGYVGRQEAAAAAHVAGNTA Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS11490 HSERO_RS11490 D-ribose ABC transporter, permease component RbsC Specifically important for utilizing D-Ribose. ABC transporter permease MQTSSSTPAASRQAAYLAGFKNYLGLMAALLAMCVMFAFLSENFLSAATFITLSNDIPPLVVMSVGMTFILIIGGIDLSVGSVMALAASMLSMAMVRWGWPLYAAAPLGVVVAALCGTLTGMVSVHWRIPSFIVSLGVLEIARGLAYQVTNSRTEYIGSAVDVISSPILFGMSPAFLSAIAIVIIAQLVLTRTVLGRYWIGIGTNEEAVRLSGVNPNPSKILAFALMGALAGIAALFQVSRLEAADPNGGVGMELQVIAAVVIGGTSLMGGRGSIVSTFIGVLIISVLEAGLAQVGVSEPMKRIITGAVIVVAVILDTYRRRGQRHAR Pseudomonas simiae WCS417 WCS417 GFF3595 PS417_18405 D-ribose ABC transporter, substrate-binding component RbsB No fitness data for this gene, but data for PS417_18400:18395 confirm this is the ABC transporter for ribose. LacI family transcriptional regulator MKLPFAGRLLAVAVLAAASAALPLSSAFADDAAKPKVGLVMKSLANEFFVTMQDGAKTYQKEHAADFDMITNGIKNETDTSAQIDIVNQMILAKVNAIVIAPADSKALVTVLKKASDAGIKVVNIDNRLDPDVLKSKNLDIPFVGPDNRKGSKLVGDYLAKQLASGDKVGIIEGVPTTTNAQQRTAGYKDAMDAAGMKIVSTQSGNWEIDQGQKVASAMLSEYPDLKALLAGNDNMALGAVSAVRAAGKAGKVLVVGYDNIEAIKPMLQDGRVLATADQAAAQQAVFGIQNALKLVKGEKVDSKDGVIETPVELVLKK Pseudomonas simiae WCS417 WCS417 GFF3594 PS417_18400 D-ribose ABC transporter, ATPase component RbsA Specifically important for utilizing D-Ribose. sugar ABC transporter ATPase MSSSAPNAVLSVSGIGKTYAQPVLSDITLTLNRGEVLALTGENGAGKSTLSKIIGGLVTPTTGHMQFNGQDFRPGSRTQAEELGVRMVMQELNLLPTLTVAENLFLDNLPSHCGWISRKQLRKAAIEAMAQVGLDAIDPDTLVGSLGIGHQQMVEIARNLIGDCHVLILDEPTAMLTAREVEMLFEQITRLQARGVAIIYISHRLEELARVAQRIAVLRDGKLVCVEPMANYNSEQLVTLMVGRELGEHIDLGPRTIGGPALTVKGLTRSDKVRDVSFEVRAGEIYGISGLIGAGRTELLRLIFGADLADSGTVALGSPAQVVSIRSPVDAVGHGIALITEDRKGEGLLLTQSISANIALGNMPEISGGGVVNSRDETALAKRQIDAMRIRSSSPAQLVSELSGGNQQKVVIGRWLERDCSVMLFDEPTRGIDVGAKFDIYALLGELTRQGKALVVVSSDLRELMLICDRIGVLSAGRLIETFERDSWTQDELLAAAFAGYQKRDALLNDAVLRDTP Pseudomonas simiae WCS417 WCS417 GFF3593 PS417_18395 D-ribose ABC transporter, permease component RbsC Specifically important for utilizing D-Ribose. ABC transporter permease MKTTTSPGKTGGNFYGLGTYLGLAGALLAMIALFSVLSDHFLSYDTFSTLANQIPDLMVLAVGMTFILIIGGIDLSVGSVLALAASAVSVAILGWGWSVLPAAVLGMGCAALAGTITGSITVAWRIPSFIVSLGVLEMARGVAYQMTGSRTAYIGDSFAWLSNPIAFGISPSFIIALLVIIAAQLVLTRTVFGRYLIGIGTNEEAVRLAGINPKPYKILVFSLMGLLAGVAALFQISRLEAADPNAGSGLELQVIAAVVIGGTSLMGGRGSVISTFFGVLIISVLAAGLAQIGATEPTKRIITGAVIVIAVVLDTYRSQRASRRG Marinobacter adhaerens HP15 Marino GFF3099 HP15_3042 acetylornithine aminotransferase (EC 2.6.1.11); succinylornithine aminotransferase (EC 2.6.1.81) Important for fitness in many minimal media experiments, and mostly rescued by addition of arginine, which suggests a role as acetylornithine aminotransferase. Important for utilization of arginine as a nitrogen source, which suggests a role as succinylornithine aminotransferase in the AST pathway. 65% identical to O30508 (AruC) from P. aeruginosa, which is reported to have these two activities. bifunctional N-succinyldiaminopimelate-aminotransferase/acetylornithine transaminase protein MNKEPVSRELFDEVMVPNYAPGSIIPVRGEGSRIWDQEGREFIDLQGGIAVTCLGHSHPGLVGALHDQAEKIWHLSNVMTNEPALRLAKTLCDLTFAERVFFANSGAEANEAAFKLARRYAWEHHGKEKNEIISFKNSFHGRTLFTVSVGGQPKYLEGFEPAPGGIHHAEFNDLESVKKLISKEKTCAIVVEPIQGEGGVMPGDQAFLQGLRDLCDENDALLVFDEVQSGVGRSGHFYAYQMYGVVPDILSSAKGLGGGFPVAAMLTTAKVAASLGVGTHGSTYGGNALACAVAQRVVDTVSQPEILKGVKARSDKLRKGMMDIGERYGVFTEVRGAGLLLGCVLTEKWQGKAKDFLNAGLEEGVMVLVAGANVIRLAPSLIIPEPDIELALERFEAAVKKLTA Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_805 gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (EC 1.2.1.99); 4-guanidinobutyraldehyde dehydrogenase (EC 1.2.1.54) Specifically important for utilization of putrescine as part of the gamma-glutamyl-putrescine pathway. 87% identical to 4-guanidinobutyraldehyde dehydrogenase (kauB = PP_5278 = Q88CA3) from P. putida, which is involved in arginine degradation, and 93% identical to AO356_12580, which is mildly important on arginine. So PfGW456L13_805 probably acts on both substrates. Aldehyde dehydrogenase (EC 1.2.1.3) MTTLTRADWEQRARDLKIEGRAYINGEYTDAVSGETFECISPVDGRLLGKIASCDAADAQRAVENARATFNSGVWSRLAPTKRKSTMIRFAGLLKQHAEELALLETLDMGKPISDSLYIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAELAVEAGIPKGVLNVLPGYGHTVGKALALHNDVDTLVFTGSTKIAKQLLIYSGESNMKRVWLEAGGKSPNIVFADAPNLQDAAEAAAGAIAFNQGEVCTAGSRLLVERSIKDKFLPLVIEALKAWKPGNPLDPATNVGALVDTQQMNTVLSYIESGHADGARLVAGGKRTLQETGGTYVEPTIFDGVSNAMKIAQEEIFGPVLSVIEFDSAEEAIAIANDTPYGLAAAVWTADISKAHLTARALRAGSVWVNQYDGGDMTAPFGGFKQSGNGRDKSLHAFDKYTELKATWIKL Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_12580 AO356_12580 gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (EC 1.2.1.99); 4-guanidinobutyraldehyde dehydrogenase (EC 1.2.1.54) Specifically important for utilization of putrescine (as part of the gamma-glutamyl-putrescine pathway) and L-arginine. Similar to kauB = PP_5278 = Q88CA3, a 4-guanidinobutyraldehyde dehydrogenase from P. putida that is involved in arginine degradation. aldehyde dehydrogenase MTTLTRTDWEQRARDLKIEGRAFINGEYTDAVSGETFDCLSPVDGRLLGKIASCDVADAQRAVENARATFNSGVWSRLAPSKRKTTMIRFAGLLKQHAEELALLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKLYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVVLKPSEKSPLTAIRIAALAIEAGIPKGVLNVLPGYGHTVGKALALHMDVDTLVFTGSTKIAKQLMIYSGESNMKRIWLEAGGKSPNIVFADAPDLQAAAESAASAIAFNQGEVCTAGSRLLVERSIKDTFLPLVIEALKGWKPGNPLDPATNVGALVDTQQMNTVLSYIEAGHSDGAKLVAGGKRILEETGGTYVEPTIFDGVSNAMKIAQEEIFGPVLSVIAFDTAEQAIEIANDTPYGLAAAVWTKDISKAHLTAKALRAGSVWVNQYDGGDMTAPFGGFKQSGNGRDKSLHAFDKYTELKSTWIKL Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_4383 gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (EC 1.2.1.99); 4-guanidinobutyraldehyde dehydrogenase (EC 1.2.1.54) Important on putrescine; this is the dehydrogenase reaction in the gamma-glutamyl-putrescine pathway. Similar to the 4-guanidinobutyraldehyde dehydrogenase kauB from P. putida, which is involved in arginine catabolism, and 99% id. to AO356_12580, which has a phenotype on arginine. So Pf6N2E2_4383 probably has both activities. Aldehyde dehydrogenase (EC 1.2.1.3) MTTLTRADWEQRARDLKIEGRAFINGEYTDAVSGETFDCLSPVDGRLLGKIASCDVADAQRAVENARATFSSGVWSRLAPSKRKATMIRFAGLLKQHAEELALLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKLYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVVLKPSEKSPLTALRIAALAIEAGIPKGVLNVLPGYGHTVGKALALHMDVDTLVFTGSTKIAKQLMIYSGESNMKRIWLEAGGKSPNIVFADAPDLQAAAESAASAIAFNQGEVCTAGSRLLVERSIKDTFLPLVIEALKGWKPGNPLDPATNVGALVDTQQMNTVLSYIEAGHSDGAKLVAGGKRILEETGGTYVEPTIFDGVSNAMKIAQEEIFGPVLSVIAFDTAEQAIEIANDTPYGLAAAVWTKDISKAHLTAKALRAGSVWVNQYDGGDMTAPFGGFKQSGNGRDKSLHAFDKYTELKSTWIKL Pseudomonas simiae WCS417 WCS417 GFF5420 PS417_27745 gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (EC 1.2.1.99); 4-guanidinobutyraldehyde dehydrogenase (EC 1.2.1.54) Specifically important for putrescine utilization as part of the gamma-glutamylputrescine pathway. Similar to the 4-guanidinobutyraldehyde dehydrogenase from P. putida (kauB), which is involved in arginine catabolism, and 92% identical to AO356_12580, which is also involved in arginine catabolism. Mutants in PS417_27745 seem to have a very subtle defect in arginine catabolism; it probably has both activities. aldehyde dehydrogenase MTTLTRADWEQRAKDLKIEGRAYINGEYTAAVSGDTFECISPVDGRLLATVASCDAADAQRAVENARATFNSGVWSRLAPAKRKSAMLRFAALLKANAEELALLETLDMGKPISDSLNIDVPGAANALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALALHMDVDTLVFTGSTKIAKQLLIRSGESNMKRVWLEAGGKSPNIVFADAPDLQAAAESAAGAIAFNQGEVCTAGSRLLVERSIKDKFLPLVIEALKGWKPGNPLDPATNVGALVDTQQMNTVLSYIEAGHADGAKLVAGGKRTLEETGGTYVEPTIFDGVTNAMKIAKEEIFGPVLSVITFDSAEEAVAIANDTIYGLAAAVWTADISKAHLTAKALRAGSVWVNQYDGGDMTAPFGGFKQSGNGRDKSLHAFDKYTELKATWIKL Burkholderia phytofirmans PsJN BFirm BPHYT_RS17345 BPHYT_RS17345 bifunctional thiolase PaaJ: 3-oxo-5,6-didehydrosuberyl-CoA thiolase (EC 2.3.1.223); 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) Specifically important for utilization of phenylacetate and phenylalanine. This is probably the bifunctional thiolase in the aerobic phenylacetyl-CoA degradation pathway (also known as PaaJ). acetyl-CoA acetyltransferase MNDAFICDAIRTPIGRYGGALKDVRADDLGAVPIKALIERNPGVDWRTVDDVIYGCANQAGEDNRNVARMSALLAGLPVEAPGSTINRLCGSGMDAVGTAARAIKAGEARLMIAGGVESMTRAPFVMGKATSAFARQADIYDTTIGWRFINPLMKRQYGVDSMPETAENVAAEFSVSRADQDAFALASQQKAARAQQDGTLAQEIVGVEIAQKKGDPVRALLDEHPRETSLESLGKLKGVVRPDGSVTAGNASGVNDGACALLLANQQAADQYGLRRRARVVGMATAGVEPRIMGIGPAPATQKLLKQLGMTLEQLDVIELNEAFASQGLAVLRTLGLRDDDPRVNPNGGAIALGHPLGASGARLITTALYQLERTNGRFALCTMCIGVGQGIALVIERL Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_05723 H281DRAFT_05723 bifunctional thiolase PaaJ: 3-oxo-5,6-didehydrosuberyl-CoA thiolase (EC 2.3.1.223); 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) Specifically important for utilization of phenylacetate. This is probably the bifunctional thiolase in the aerobic phenylacetyl-CoA degradation pathway (also known as PaaJ). acetyl-CoA acyltransferase MNDAYICDAIRTPIGRYGGALKDVRADDLGAVPIKALIERNPGVDWRAVDDVIYGCANQAGEDNRNVARMSALLAGLPADAPGATINRLCGSGMDAVGTAARAIKAGEAQLMIAGGVESMTRAPFVMGKAASAFARQAEIHDTTIGWRFVNPLMKRQYGVDSMPETAENVAEQFGISRADQDAFALVSQQKAARAQRDGTLAQEIVGVEIAQKKGDAIRVTLDEHPRETSLESLAKLKGVVRPDGTVTAGNASGVNDGACALLIASQQAADQYGLRRRARVVGMATAGVEPRIMGIGPAPATQKLLRQLGMTLDQLDVIELNEAFASQGLAVLRMLGLRDDDPRVNPNGGAIALGHPLGASGARLVTTALHQLERSNGRFALCTMCIGVGQGIALVIERL Burkholderia phytofirmans PsJN BFirm BPHYT_RS17340 BPHYT_RS17340 3-oxo-5,6-didehydrosuberyl-CoA semialdehyde dehydrogenase PaaZ (EC:1.2.1.91) Specifically important for utilization of phenylalanine and phenylacetate. This dehydrogenase (also known as PaaZ) is part of the aerobic phenylacetyl-CoA degradation pathway. 86% identical to BCAL0408 from B. cenocepacia, which is also involved in phenylacetate degradation and was proposed to be PaaZ (PMC2580687). aldehyde dehydrogenase MTHPLFTKHEDTLQKALTAVETRGYWSPFVEMPSPKVYGETANADGEAAFKAHLNATFQLDQPSTGETVGAEVSPFGFPLGVRYPKAEPAALIAAAAAAQRDWRAAGPQAWIGVCLEILARVNRASFEIGYSVMHTTGQAFMMAFQAGGPHAQDRALEAVVYAWDQLRRIPGDTHWEKPQGKNPPLAMHKRYTVVPRGTGLVLGCCTFPTWNGYPGLFADLATGNTVIVKPHPGAILPLALTVRIARDVLREAGFDPNVVTLLATEPNDGALVQDLALRPEIKLIDFTGSTQNGTWLERNAHQAQVYTEKAGVNQIVIDSVDDIKAAARNVAFSLALYSGQMCTAPQNIYVPRGGIRTAEGTLSFDEVAQAIAGAVQKLVADPARAVELLGAIQNEGVTQRIDEAAKLGRVLVESLTLEHPAFAGARVRTPLVLQLDAATDHAQFTKEWFGPISFVIATDSTAQSLDLAGAIASEHGALTLSVYSTDEAVLDDAHEASIRGGVALSINLTGGVFVNQSAAFSDFHGTGANPAANAALADAAFVANRFRVVQSRVHVEPKAAPAVAG Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_05724 H281DRAFT_05724 3-oxo-5,6-didehydrosuberyl-CoA semialdehyde dehydrogenase PaaZ (EC:1.2.1.91) Specifically important for utilization of phenylacetate. This dehydrogenase (also known as PaaZ) is part of the aerobic phenylacetyl-CoA degradation pathway. 86% identical to BCAL0408 from B. cenocepacia, which is also involved in phenylacetate degradation and was proposed to be PaaZ (PMC2580687). phenylacetic acid degradation protein paaN MTHPLFTKHEDTLQKALAAVETRGYWSPFVEMPSPKVYGETANADGEAAFKAHLNATFELDQPSTGETVGTEVSPFGFPLGIRYPKSDPDALLAAAAEAQRDWRAAGPQAWIGVSLEILARLNRASFEIGYSVMHTTGQAFMMAFQAGGPHAQDRALEAVVYAWDQLRRIPADAHWEKPQGKNPPLAMQKRYTIVPRGTALVLGCCTFPTWNGYPGLFADLATGNAVIVKPHPGAILPLAVTVRIARDVLREAGFDPNVVTLLATEPNDGAIVQSLAVRPEIKLIDFTGSTQNGTWLERNAHQAQVYTEKAGVNQIVIDSADDIKAVARNIAFSLALYSGQMCTAPQNIYVPRDGIQTADGTLSFDEVAQAIAGAVQKLVADPARAVELLGAIQNEGVAQRVDEAATLGRVLVESQALEHPAFAGARVRTPLVLQLDAATDGEQFTKEWFGPISFVIATDSTAHSLDLAGTIAAEHGALTLSVYSTDEAVLDQAHEASIRGGVALSINLTGGVFVNQSAAFSDFHGTGANPAANAALADAAFVANRFRVIQSRVHVEPKAAPAVAG Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_04042 H281DRAFT_04042 phenylacetate transporter Specifically important for phenylacetate utilization. aromatic amino acid:proton symporter, AAT family VPVRCKKSAGWYQYLGNIGRGKIFGSAGADHKSGRAIEIHTLGRNLDNALQQDGLKRGLKNRHIQLIALGGAIGTGLFLGSASVLQAAGPSMILGYAIGGVIAFMIMRQLGEMVAQEPVAGSFSHFAYKYWGDFPGFLSGWNYWVLYVLVSMAELTAVGTYVHYWWPGVPTWVSALVCFAGINAINLANVKAYGETEFWFAIIKVVAVIGMILFGGYLLVSGHGGPQASISNLWSHGGFFPHGFHGLFTMLAVIMFSFGGLELIGITAAEADEPQKSIPKAVNQVIYRILIFYICSLAVLLSLYPWNEVAAGGSPFVMIFSQIGSTLTANVLNVVVLTAALSVYNSGVYANSRMLYGLAEQGNAPRALMKVDRRGVPYMAIGLSALATFTCVIVNYLIPAEALGLLMALVVAALVLNWALISLTHLKSRRAMVAAGETLVFKSFWFPVSNWICLAFMALILVILAMTPGLSVSVLLVPVWLVVMWAGYAFKRRRAAAHVAARVVGR Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_05725 H281DRAFT_05725 2,3-dehydroadipyl-CoA hydratase / enoyl-CoA hydratase (EC 4.2.1.17) Specifically important for phenylacetate utilization. 51% identical to the characterized enzyme (paaF = Q845K2) from Pseudomonas sp. Y2, which is part of the aerobic phenylacetyl-CoA pathway. Also, 84% identical to enoyl-CoA hydratase Crt2 = H16_A3307 from Ralstonia eutropha (PMID:30243533). short chain enoyl-CoA hydratase MVYENILVETRGRVGLVTLNRPKALNALNDALMDELGAALREFDADDAIGAIVLTGSEKAFAAGADIGMMSTYSYMDVYKGDYITRNWETVRSIRKPIIAAVAGFALGGGCELAMMCDMIFAADTAKFGQPEIKLGIMPGAGGTQRLPRAVSKAKAMDLCLTARFMDAAEAERAGLVSRVIPAASLIDEAIAAAATIAEFPLPAVMMVKESVNRAYETTLAEGVHFERRLFHSLFATEDQKEGMAAFVEKRKPVFKHR Burkholderia phytofirmans PsJN BFirm BPHYT_RS17335 BPHYT_RS17335 2,3-dehydroadipyl-CoA hydratase / enoyl-CoA hydratase (EC 4.2.1.17) Specifically important for utilization of phenylacetate and phenylalanine. 51% identical to the characterized enzyme (paaF = Q845K2) from Pseudomonas sp. Y2, which is part of the aerobic phenylacetyl-CoA pathway. Also, 83% identical to enoyl-CoA hydratase Crt2 = H16_A3307 from Ralstonia eutropha (PMID:30243533). enoyl-CoA hydratase MAYENILVETRGRVGLVTLNRPKALNALNDALMDELGAALREFDADDAIGAIVVTGSEKAFAAGADIGMMSTYTYMDVYKGDYITRNWETVRSIRKPIIAAVAGFALGGGCELAMMCDIIFAADTAKFGQPEIKLGIMPGAGGTQRLPRAVSKAKAMDLCLTARFMDAAEAERAGLVSRVIPAASLVDEAIAAAATIAEFPSPAVMMVKESVNRAYETTLAEGVHFERRLFHSLFATEDQKEGMAAFVEKRKPVFKHR Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS20660 HSERO_RS20660 bifunctional thiolase PaaJ: 3-oxo-5,6-dehydrosuberyl-CoA thiolase (EC 2.3.1.223); 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) Specifically important for phenylacetate utilization. This is part of the aerobic phenylacetyl-CoA pathway. acetyl-CoA acetyltransferase MEALICDAIRTPFGRYGGALGAVRADDLAAAPIRSLMERNPGVDWSRVEDILYGCANQAGEDNRNVARMAGLLAGLPIAVPGSTVNRLCGSSLDAVGMAARAIKSGEVQLMIAGGVESMTRAPFVMGKAESAFARSAAIFDTTIGWRFVNPLMKAQYGIDSMPETAENVATDFQINRADQDAFALRSQQRWAAAQAAGFFAGEIAPLTIPQKKGDPLVVTTDEHPRPDTTLATLAKLKGVVRPDGTVTAGNASGVNDGACALLLASPKAADLYRLKPRARVLGMATAGVAPRIMGFGPAPAVRKVLAQVGLTLAQMDVIELNEAFAAQGLAVMRDLGLPDDAAHVNPNGGAIAIGHPLGASGARLVTTAINQLERSGGRYALCTMCIGVGQGIALVIERVA Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_05722 H281DRAFT_05722 1,2-epoxyphenylacetyl-CoA isomerase (EC 5.3.3.18) Specifically important for phenylacetate utilization. This is part of the aerobic phenylacetyl-CoA pathway. short chain enoyl-CoA hydratase /Enoyl-CoA hydratase MAYEAIGLDIDAASRVATITLNRPDKLNSFTRAMHQELNAALNEVETSGARALVLTGAGRGFCAGQDLADLDFTPGAMTDLGELIDLHFNPLIRRLQALPLPVIAAVNGTAAGAGANLALACDIVLAARSASFIQAFVKIGLVPDSGGTWFLPQRVGMARALGLAITGDKLSAEKAESWGLIWQTVDDQELAATAAKLAAQLAQQPTRAIAAIKQAMRAGATQTLDQQLDLERDLQRELGASHDYAEGVQAFVEKRAPRFEGR Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2921 ABC transporter for L-leucine/L-phenylalanine/D-alanine, substrate-binding component LivK Important for utilization of leucine, phenylanine, or D-alanine. Slightly important for utilization of isoleucine as a carbon source and detrimental when isoleucine is the nitrogen source. High-affinity leucine-specific transport system, periplasmic binding protein LivK (TC 3.A.1.4.1) MTKATKQISKLFAAMVLAGVASHSFAADTIKIGIAGPKTGPVAQYGDMQFSGSKMAIEQINAKGGVNGKQLVAVEYDDACDPKQAVAVANKVVNDGIKFVVGHLCSSSTQPASDIYEDEGVVMITPAATSPDITARGYKMIFRTIGLDSAQGPAAGNYIADHVKPKIVAVLHDKQQYGEGIASAVKKTLEDKGVKVAVFEGVNAGDKDFSSMIAKLKQANVDFVYYGGYHPELGLILRQSQEKGLKAKFMGPEGVGNDSISQIAKESSEGLLVTLPKSFDQDPANIALADAFKAKKEDPSGPFVFPSYSAVTVIADAIKAAKSEDAGKVAEAIHAGTFKTPTGDLSFDKNGDLKDFKFVVYEWHFGKPKTEASPQ Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2923 ABC transporter for L-leucine/L-phenylalanine/D-alanine, permease component 1 LivH Important for utilization of leucine, phenylanine, or D-alanine. Slightly important for utilization of isoleucine as a carbon source and detrimental when isoleucine is the nitrogen source. High-affinity branched-chain amino acid transport system permease protein LivH (TC 3.A.1.4.1) MPDIYHFFQQLVNGLTVGSTYALIAIGYTMVYGIIGMINFAHGEVYMIGSYVAFIAIAGLAMMGLDSVPLLMTAAFIASIVVTSSYGYSIERIAYRPLRGSNRLIPLISAIGMSIFLQNTVLLSQDSKDKSIPNLIPGNFAIGPGGAHEVLISYMQIVVFVVTLVAMLGLTLFISRSRLGRACRACAEDIKMANLLGINTNNIIALTFVIGAALAAIAAVLLSMQYGVINPNAGFLVGLKAFTAAVLGGIGSIPGAMLGGLVLGVAEAFGADIFGDQYKDVVAFGLLVLVLLFRPTGILGRPEVEKV Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2924 ABC transporter for L-leucine/L-isoleucine/L-phenylalanine/D-alanine, permease component 2 LivM Important for utilization of leucine, phenylanine, or D-alanine. Slightly important for utilization of isoleucine as a carbon source and detrimental when isoleucine is the nitrogen source. Branched-chain amino acid transport system permease protein LivM (TC 3.A.1.4.1) MTRHLKSALFSALLVWAVAYPVLGLKLTIVGINLEVHGTSPAILATIAVCSLLMFLRVLFSTQISAMWKSSPGLPVIPAKASNFLTLPTTQRWIVLALIVGALVWPFFGSRGAVDIATLILIYVMLGLGLNIVVGLAGLLDLGYVGFYAVGAYSYALLSHYFGLSFWICLPIAGMMAATFGFLLGFPVLRLRGDYLAIVTLGFGEIIRLFLRNLTDITGGPNGISNIEKPTFFGLTFERKAAEGLQTFHEYFGLEYNSINKVIFLYLVALLLALAALFVINRLLRMPIGRAWEALREDEIACRALGLNPTVIKLSAFTLGAAFAGFAGSFFAARQGLVTPESFTFIESAIILAIVVLGGMGSQLGVILAAIVMILLPEMMREFSEYRMLMFGALMVLMMIWRPQGLLPMQRPHMELRK Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2925 ABC transporter for L-leucine/L-isoleucine/L-phenylalanine/D-alanine, ATPase component 1 LivG Important for utilization of leucine, phenylanine, or D-alanine. Slightly important for utilization of isoleucine as a carbon source and detrimental when isoleucine is the nitrogen source. Branched-chain amino acid transport ATP-binding protein LivG (TC 3.A.1.4.1) MSREILKVENLSMRFGGLLAVNGVALTVKEKQVVALIGPNGAGKTTVFNCLTGFYQPTGGTILLDGEPIQGLPGHHIARKGVVRTFQNVRLFKDMTAVENLLIAQHRHLNTNFFAGLFKTPAFRKSEREAMEYAEYWLDKVNLTEFANRPAGTLAYGQQRRLEIARCMMTRPRILMLDEPAAGLNPKETEDLKALIGVLREEHNVTVLLIEHDMKLVMSISDHIVVINQGTPLADGTPEQIRDNPEVIKAYLGEA Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_2926 ABC transporter for L-leucine/L-isoleucine/L-phenylalanine/D-alanine, ATPase component 2 LivF Important for utilization of leucine, phenylanine, or D-alanine. Slightly important for utilization of isoleucine as a carbon source and detrimental when isoleucine is the nitrogen source. Branched-chain amino acid transport ATP-binding protein LivF (TC 3.A.1.4.1) MLQFENVSTFYGKIQALHSVNVEVRQGEIVTLIGANGAGKSTLLMTLCGSPQAHSGSIRYMGEELVGQDSSHIMRKSIAVVPEGRRVFARLTVEENLAMGGFFTDKGDYQEQMDKVLHLFPRLKERFTQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFDIIEQLRKDGVTVFLVEQNANQALKIADRAYVLENGRVVMQGTGEALLTDPKVREAYLGG Burkholderia phytofirmans PsJN BFirm BPHYT_RS34250 BPHYT_RS34250 ABC transporter for L-rhamnose/L-fucose/xylitol, substrate-binding component Specifically important for utilizing L-rhamnose, L-fucose, and xylitol. ABC transporter substrate-binding protein MSFAKGPLMARRLFRTSLSVTAAAACFAGLAVSGAAQAADSGKIGLGLPLLTSPFWQSYNNYLPKYAKESGLDILAPVNSNGDPVQQITDMNNLLNLGAKGIVVGPLDSAAISRALDAAAAKNVPVVAVDVAPTQGKVAMVVRADNHAYGEKACKYIGEHVKSGKVVQIMGDLASVNGRDRSEAFRSCLKGYPGLTLLEIPASWKGDVAATALDSLLTANPDVKAIYMQAGGVYLSPTLQTLRRKQMLFPAGDAKHVVIVSNDGIPQEFDAIRRGDIDATVSQPADSYAKYGLFYIKAALAGQTFKPGPTDHGSNIIQLAPGILEDQLPAPLVTKSNVDDKALWGNTVK Burkholderia phytofirmans PsJN BFirm BPHYT_RS34245 BPHYT_RS34245 ABC transporter for L-rhamnose/L-fucose/xylitol, ATPase component Specifically important for utilizing L-rhamnose, L-fucose, and xylitol. multidrug ABC transporter ATP-binding protein MNGQMSELTSSVPVVEALEVTKRFGSTAALNDVSIRVMPGESHALVGRNGAGKSTLVSILTGLRKPDTGEVRFSGAAAPSIADRDAWRERVACVYQHSTIIRDLSVAENLFINRQPLRGGVIDWQAMRRDARALLDHWKIDVREDARAGDLSVEARQLVEIARALSYGARFIILDEPTAQLDGDEIKRLFRRISELQREGVTFLFISHHLQEVYEICQAVTVLRDARHIVSAPVSALPREQLIEAMTGERGGLAVADAAARGALPADTAVALELKELTGADYEGVSFTVKRGEVVGLTGATSSGRTSVAEAIAGLRAAKRGTISVDGAILPPGDVPASLAHGIGCVPKDRHHEGLVLTQSVAENASMTIARVLGKFGIAAPAKKNAFGQKMIDALGIVAQGPEHVVSGLSGGNQQKVVMARALATNPNVLVLIDPTAGVDVKSKEALLSVVDRVREEGKAVLVVSGELDDLRTCDRVLVMFRGRVAAEFPAGWQDHDLIASVEGVSLHEE Burkholderia phytofirmans PsJN BFirm BPHYT_RS34240 BPHYT_RS34240 ABC transporter for L-rhamnose/L-fucose/xylitol, permease component Specifically important for utilizing L-rhamnose, L-fucose, and xylitol. ATPase MKNSVPSPAFGAAQAGAQSQLALPASRGKRARSELARLRELALLPALALLIVIGAFISPSFLTKANLISVLGASAALALVVLAESLIVLTGKFDLSLESTVGIAPAVGAMLVMPAASAGFGMQWPAAAGLLAIVVVGAVIGFINGFLVVRLRLNAFIVTLAMLIVLRGMLVGATKGGTLFDMPTSFFALATTIVLGLPLSVWLAAAAFAIAAFMLRYHRLGRALYAIGGNPEAARAAGIRVERITWGVFVLGSILASVGGLIVTGYVGAINANQGNGMIFTVFAAAVIGGISLDGGKGTMFGALTGVLLLGVVQNLLTLAQVPSFWIQAIYGAIILGSLMVARLASGEGQN Bacteroides thetaiotaomicron VPI-5482 Btheta 353291 BT3765 L-rhamnose:H+ symporter Specifically important for utilizing L-rhamnose. L-rhamnose/H+ symporter (NCBI ptt file) MDILIGLLIIAIGSFCQSSSYVPIKKVKEWSWESFWLVQGVFAWLVFPFLGSLLGIPAGGSLFDLWGAGGAGMSIFYGVLWGIGGLTFGLSMRYLGVALGQSIALGTCAGFGTLFPAIFAGTNLFEGNGLILLLGVCITLAGIAIIGYAGGLRAQNMSEEEKRAAVKDFALTKGLLVALLAGVMSACFALGLDAGTPIKEAALAGGVDGLYAGLPVIFLVTLGGFMTNAAYCLQQNIANKSVGDYAKGKVWGNNLVFCALAGVLWYMQFFGLEMGKSFLTESPVLLAFSWCILMALNVTFSNVWGIILKEWKGVSAKTITVLICGLVVLIFSLVFPNLF Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1617 Echvi_1617 L-rhamnose transporter Specifically important for utilizing L-rhamnose. Predicted to have 11 transmembrane helices and belongs to the Solute carrier families 5 and 6-like superfamily (CDD cl00456). hypothetical protein MSDKKNLVQKLESVNEYEREAIPQNKLKSWKSFVGTYAGEHTAGTEFVLGPLFVAHGASAVDLVSGLLVGNILAVLSWAFFTGKAATKTRHTLYFQLEKIAGSRFTMIYNLVNAVAFCFLAGAMITVAATAVGIPFDLAMPALDDTLPTSLGFVLTVFVVGAITTVIAMFGFNQVVKFANIAAPWMIMIFVAAAVAVLPRLGINSIGDFWPVAKETIWSGVPLEGKTKFTFWHIMFFAWFCNMAMHIGMADMSILRYAKKWTAGFATSTGVFLGHYVAWIASGILYSLFLLESDGSLVFAPGPIAYEAVGIAGAICVIIAGWTTANPTLYRAGLAIQSINPNWKTWKVTLFVGLITTIAACFPALMMQLLDFVALYGLVLMPLGAVIFIDIFLFPKMGMQSNFAALTHRNFNPAVGITWLITLIFCLGLNLFAGVEIFFLGLPGWFVAVLVYIASSKIVQKNTSIPHTAKPNAKSEVPAS Bacteroides thetaiotaomicron VPI-5482 Btheta 353292 BT3766 rhamnulose 1-phosphate aldolase RhaD (EC 4.1.2.19) Specifically important for utilizing L-rhamnose and rhamnogalacturonan from potato. rhamnulose-1-phosphate aldolase (NCBI ptt file) MKSILENRPALAKEVNKVAEVAGYLWQKGWAERNGGNITVNITEFVDDEIRRMEPISEVKSIGVTLPYLKGCYFYCKGTNKRMRDLARWPMENGSVIRILDDCASYVIIADEAVAPTSELPSHLSVHNDLLSKNSPYKASVHTHPIELIAMTHCEKFLQKDVATNLLWSMIPETKAFCPRGLGIIPYKLPSSVELAEATIKELQDYDVVMWEKHGVFAVDCDAMQAFDQIDVLNKSALIYIAAKNMGFEPDGMSQEQMKEMSVAFNLPK Bacteroides thetaiotaomicron VPI-5482 Btheta 353293 BT3767 L-lactaldehyde reductase FucO (EC 1.1.1.77) Specifically important for utilizing L-rhamnose. lactaldehyde reductase (NCBI ptt file) MNRIILNETSYFGAGCRSVIAVEAARRGFKKAFFVTDKDLIKFGVAAEIIKVFDDNHIPYELYSDVKANPTIANVQNGVAAYKASGADFIVALGGGSSIDTAKGIGIVVNNPDFADVKSLEGVADTKHKAVPTFALPTTAGTAAEVTINYVIIDEDARKKMVCVDPNDIPAVAIVDPELMYSMPKGLTAATGMDALTHAIESYITPGAWAMSDMFELKAIEMIAQNLKAAVDNGKDTVAREAMSQAQYIAGMGFSNVGLGIVHSMAHPLGAFYDTPHGVANALLLPYVMEYNAESPAAPKYIHIAKAMGVNTDGMTETEGVKAAIEAVKALSLSIGIPQKLHEINVKEEDIPALAVAAFNDVCTGGNPRPTSVAEIEVLYRKAF Bacteroides thetaiotaomicron VPI-5482 Btheta 350805 BT1277 L-fucose/D-arabinose symporter FucP Specifically important for utilizing L-fucose and D-arabinose. The transporter BT0355 also has negative fitness during D-arabinose utilization, but the effect is strand-dependent, which suggests that it is a polar effect. BT1277 is probably the main D-arabinose transporter. L-fucose permease (NCBI ptt file) MKHTKQSIISKDGVSYLIPFILITSCFALWGFANDITNPMVKAFSKIFRMSATDGALVQVAFYGGYFAMAFPAAMFIRKFSYKAGVLLGLGLYAFGAFLFFPAKMTGEYYPFLIAYFILTCGLSFLETSCNPYILSMGTEETATRRLNLAQSFNPMGSLLGMYVAMQFIQAKLHPMGTDERALLNDSEFQAIKESDLAVLIAPYLIIGLVILAMLLLIRFVKMPKNGDQNHKIDFFPTLKRIFTQTRYREGVIAQFFYVGVQIMCWTFIIQYGTRLFMSPEYGMDEKSAEVLSQQYNIVAMVIFCISRFICTFILRYLNAGKLLMILAIFGGIFTLGTIFLQNIFGLYCLVAVSACMSLMFPTIYGIALKGMGDDAKFGAAGLIMAILGGSVLPPLQASIIDMKEIASMPAVNVSFILPLTCFLVIIGYGYRTVKRNW Bacteroides thetaiotaomicron VPI-5482 Btheta 351703 BT2175 L-fuculose kinase FucK (EC 2.7.1.51); D-ribulose 1-kinase Specifically important for utilizing L-fucose and D-arabinose, which are catabolized via L-fucolose-1-phosphate or D-ribulose-1-phosphate. hypothetical protein (NCBI ptt file) MSNLNSYIYSRQINVRYMRRLKLYYLFFHSTLKINVPLSILGALIVSKADWSLFWEAFPYLLGGWGIVASLLYKEFLEKEAYFFYYNSGILKRNLIVFVFAVYWSVLWIVKLCITCLK Bacteroides thetaiotaomicron VPI-5482 Btheta 350802 BT1274 L-fuculose-1-phosphate aldolase FucA (4.1.2.17); D-ribulose-1-phosphate aldolase Specifically important for utilizing L-fucose and D-arabinose, which are catabolized via L-fucolose-1-phosphate or D-ribulose-1-phosphate. L-fuculose-1-phosphate aldolase (NCBI ptt file) MITDEHIELFLAQAHRYGDAKLMLCSSGNLSWRIGEEALISGTGSWVPTLAKEKVSICNIASGTPTNGVKPSMESTFHLGVLRERPDVNVVLHFQSEYATAISCMKNKPTNFNVTAEIPCHVGSEIPVIPYYRPGSPELAKAVVEAMLKHNSVLLTNHGQVVCGKDFDQVYERATFFEMACRIIVQSGGDYSVLTPEEIEDLEIYVLGKKTK Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS05265 HSERO_RS05265 L-fucono-1,5-lactonase Important for utilizing L-fucose. amidohydrolase MKPPRIDAHQHFWFYQPQAYPWIGAGMELLACDRTPGQLQPLLDAEGLGQSIAVQARAGREETGFLLELARGNRRIAGVVGWEDLASPHLAANVERWGRDKLVGFRHQLQDEADVGGCVDAPAFNAGVAWLQRQGMVYDVLVYARQMAEVQAFCARHDRHWLVLDHLGKPALTEFGRGDTAFEGWQRQLRALAALPHVACKLSGLVTEADWQRGLRQKDFDNISLCLDTALEAFGPQRLMFGSDWPVCLLAASYAKVAGVVREWAATRLSAAEQELLWGATAARCYGLA Burkholderia phytofirmans PsJN BFirm BPHYT_RS34220 BPHYT_RS34220 L-fucono-1,5-lactonase Specifically important for utilizing L-fucose. amidohydrolase MHIDAHQHYWDPARGDYEWLTPELKILYRTFGPEDLKPLRERAGIERTVVVQAAPTIDETRYLLDLARHEPSIAGVVGWVPLLLPTAPQVIEALAHEPKFKGVRPMLQDLPDDTWIANPDLTPAIEALIAHDLAFDALIYARHVEPFETFATRFPALRIVVDHGAKPPIRYGRAGYQSWADAITRLAQLPHVHCKLSGLVTEASPGWTEETLHPYVEHLLKSFGPARLMWGSDWPVLDLNGDYLLWHSVANTLLTSLSDAERDAVFGGNAAAFYRL Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS19365 HSERO_RS19365 2-keto-3-deoxy-L-fuconate 4-dehydrogenase FucDH Specifically important for L-fucose utilization; this is part of the oxidative pathway. oxidoreductase MSASTGRLAGKTVLITAAAQGIGRASTELFAREGARVIATDISKPHLDELAGIAGVETHLLDVTDDAAIKALVAKIGTIDVLFNCAGYVAAGNILECDDKAWDFSFNLNAKAMFHTIRAVLPGMLAKKAGSIVNIASAASSVKGVANRFAYGASKAAVVGLTKSVAADFVAQGIRCNAICPGTIESPSLNQRISTQAKETGKSEEEVRAAFVGRQPMGRIGKAEEVAALALYLASDESNFTTGSIHMIDGGWSN Burkholderia phytofirmans PsJN BFirm BPHYT_RS34215 BPHYT_RS34215 2-keto-3-deoxy-L-fuconate 4-dehydrogenase FucDH Specifically important for L-fucose utilization; this is part of the oxidative pathway. oxidoreductase MTQRLAGKTALITAAGQGIGLATAELFAREGARVIATDIRIDGLAGKPVEARKLDVRDDAAIKALAAEIGAVDVLFNCAGFVHAGNILECSEEDWDFAFDLNVKAMYRMIRAFLPAMLDKGGGSIINMSSAASSVKGVPNRFAYSASKAAVIGLTKSVAADFITRGVRCNAICPGTVASPSLEQRIVAQAQAQGATLDAVQAAFVARQPMGRIGKPEEIAALALYLGSDESSFTTGHAHVIDGGWSN Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS06355 HSERO_RS06355 2,4-diketo-3-deoxy-L-fuconate hydrolase (EC 3.7.1.26) Specifically important for utilization of L-fucose, L-rhamnose, D-ribose, and D-xylose. The substrate is also known as 2,4-didehydro-3-deoxy-L-rhamnonate. This reaction is part of fucose or rhamonase oxidation. The phenotypes on ribose or xylose are not explained. ureidoglycolate lyase MKLLRYGPVGQEKPGILDQAGKIRDLSAHIKDVNGAVLDDASLEKIRKLDLNTLPVVEGNPRIGACVGNIGKFICIGLNYADHAAESNLPIPAEPVVFNKWTSAVVGPNDNVKIPRGSKKTDWEVELGVIIGKGGSYIDEKDAMSHVAGYCVVNDVSEREYQIERGGTWDKGKGCDTFGPIGPWLVTRDEVADPQKLGMWLEVDGKRYQNGNTSTMIFNVAHIVSYLSRFMSLQPGDVISTGTPPGVGMGVKPEAVYLRAGQTIRLGIDGLGEQEQKTIDA Bacteroides thetaiotaomicron VPI-5482 Btheta 350804 BT1276 L-fucose mutarotase FucU (EC 5.1.3.29) Specifically important for utilization of L-fucose and D-arabinose. The phenotype on D-arabinose is strand-dependent and may be a polar effect on the downstream permease. conserved hypothetical protein (NCBI ptt file) METPQTGYQVKTYNVPVKRYCQTLDLRDSPELIAEYRKRHSQAEVWPEILAGIREVGILEMEIYILGTRLFMIVETPVDFDWDTAMARLNTLPRQQEWEEYMSILQQAAPGMSSAEKWIPMERMFHLYNT Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS05250 HSERO_RS05250 ABC transporter for L-fucose, ATPase component Specifically important for L-fucose utilization. D-ribose transporter ATP binding protein MQEDKETSTTGVAASSSSSVPVIALRNVCKRFPGVLALDNCQFELAAGEVHALMGENGAGKSTLMKILSGVYQRDSGDILLDGKPVEITEPRQAQALGIGIIHQELNLMNHLSAAQNIFIGREPRKAMGLFIDEDELNRQAAAIFARMRLDMDPSTPVGELTVARQQMVEIAKALSFDSRVLIMDEPTAALNNAEIAELFRIIRDLQAQGVGIVYISHKMDELRQIADRVSVMRDGKYIATVPMQETSMDTIISMMVGRALDGEQRIPPDTSRNDVVLEVRGLNRGRAIRDVSFTLRKGEILGFAGLMGAGRTEVARAIFGADPLEAGEIIIHGGKAVIKSPADAVAHGIGYLSEDRKHFGLAVGMDVQANIALSSMGRFTRVGFMDQRAIREAAQMYVRQLAIKTPSVEQQARLLSGGNQQKIVIAKWLLRDCDILFFDEPTRGIDVGAKSEIYKLLDALAEQGKAIVMISSELPEVLRMSHRVLVMCEGRITGELARADATQEKIMQLATQRESAVAS Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS05255 HSERO_RS05255 ABC transporter for L-fucose, permease component Specifically important for L-fucose utilization. ribose ABC transporter permease MANNIHSATSASTTMANTASAQGLRARLFNPAARQKLLAFASLLLMILFFSFASPNFMEVDNLVSILQSTAVNGVLAIACTYVIITSGIDLSVGTMMTFCAVMAGVVLTNWGMPLPLGIAAAIFFGALSGWISGMVIAKLKVPPFIATLGMMMLLKGLSLVISGTRPIYFNDTEGFSAIAQDSLIGDLIPSLPIPNAVLILFLVAIGASIILNKTVFGRYTFALGSNEEALRLSGVKVDFWKVAVYTFSGAICGIAGLIIASRLNSAQPALGQGYELDAIAAVVIGGTSLSGGTGTILGTIIGAFIMSVLVNGLRIMSVAQEWQTVVTGVIIILAVYLDILRRRRRA Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS05260 HSERO_RS05260 ABC transporter for L-fucose, substrate-binding component Specifically important for L-fucose utilization. LacI family transcriptional regulator VFKNKLLGAALGLAFAMGASAAQAQEAYIPLISKGFQHQFWQAVKAGADQAGKDYKVKVTFEGPETEAMVDKQIDMLSAALAKKPQAIGFAALDSKAAIPLLKKAQAAKIPVVAFDSGVDSDIPVTTATTDNRAAAALAADKMAELVGKEGEVAVVAHDQTSRTGVDRRDGFLERIKSAYPKIKVVSVQYGAGDQLKSTEVTKSILQAYPKIKGIFGTNEGSAIGVVNGVKEMKRKIIIIGYDSGKQQKDAIREGIMAGAITQNPVGIGYKTVEAAVKAIKGEKLPKVIDTGFYWYDKSNIDDAKIAAVLYD Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_05930 AO353_05930 L-tryptophan transporter Specifically important for utilization of tryptophan as a nitrogen source. amino acid permease MTDTLGFETISNREHGLRRQLTSGQMSMIAIGGAIGTGLFMGSAYAIGYAGPSVLLSYAIGAVITLLLMGCLAEMTVAHSTSGSFGAYAEFYISPLAGFLVRYAYWAAIVLAVGTEVTAVAMYMKYWFANVPEWIWIVSFSSILIVLNAISVKTFGTFEYWFSTIKIGAIVGFIILAVYVVFGSGNPEYGVHHYTSHGGFFPNGLQGMWVAVIVSIFSYLSVEMIAVAAGEAEDPERAVKKAFRATIVRLVVFYLLTLALMLAIVPWVQAGHAQSPFVTVMQTIGIPGATGVMNFVILIAALSAMNSQLYITTRMMFSLSRGGYAPKAMGALSKSGIPLNALLLSSSGIALATLLNVMYPESSFTLMMAISMFGAIFTWFMIFLTHYCFRRYHQRHGERKLSFRMRLFPYTTLLGLVLMGAVMITTYFTEAFKMTLVFGVPFLLILSLVYGVFFRKTRALAGTLDNAPAP Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4291 L-tryptophan transporter Specifically important for utilization of tryptophan as a carbon source. Aromatic amino acid transport protein AroP MADEILRQGELKRGLKNRHIQLIALGGAIGTGLFLGSAGVLKSAGPSMILGYAIAGFIAFLIMRQLGEMIVEEPVAGSFSHFAHKYWGGYAGFLSGWNYWVLYVLVGMAELTAVGKYVQFWWPEVPSWVSAAVFFVLVNLINMMNVKVFGEMEFWFAIIKVVAIIGMIALGCYMLFSGTGGPQASVSNLWDHGGFFPNGYSGLLMAMAFIMFSFGGLELVGITAAEASEPGKVIPKAINQVVYRVLIFYVGALTVLLSLYPWDQLLQTLGASGDAYGGSPFVQIFSLIGSDTAAHILNFVVLTAALSVYNSGVYCNSRMLYGLAEQGDAPKALMKLNKQGVPLLALGVSALITLLSVLVNYLAPHEALELLFALVVASLMINWAMISLTHLKFRKIMSQQGIVPGFKSFWFPFSNYLCLAFMVMIVCVMLMIPGIRASVFAIPVWVLIIFGFYRMRMAKDRALPVVQ Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS17000 HSERO_RS17000 ABC transporter for D-sorbitol/xylitol, substrate-binding component Specifically important for utilization of D-sorbitol and xylitol. sugar ABC transporter substrate-binding protein VNKICLGAACAVLGAALPLVASAQSCNVPVLKVLAQKSLGLTVMEKSLADYQKRSGTRIEISYFGENDRRAKSRLDAATKAGSYQVYYVDEANVAEFASAGWIVPLLKYFPKDADYDDFLPGRRAVASYKDVAYFAPLIGGSDFLFYRRDLLEKAGLPVPRTLDELVADIKKLHSPPSVYGWVARGQRGSGMNVWRWAPFMLAQGGQWTDKNNQPAFNSPAAVKATQLYADLFKYAPPGAATYDWSNALEAFRSGKVAFMIESTPFADWMEDSSKSSVADKVGYARPPAPLPSAAYGHGLAISAVGAKDECTRQAAGKFIAFATGKEQEQARLREKVFSDYNRSSTIQSDYFQKNVKPQILAGLKDTTPVSKLTIWPSPQWPDIGDNLGVALEEVFTGTQKDITRALDEAAQYAQDAMEHARK Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS17005 HSERO_RS17005 ABC transporter for D-sorbitol/xylitol, permease component 1 Specifically important for utilization of D-sorbitol and xylitol. sugar ABC transporter permease MFNRGKTSLPYLFLGPSLLVMLVLGLVPTVAAINLALKNRVLRYPDSDYVWLRNLERLMSDRRFLNAIEVSAVWEVVTVLGAVIVGIAIAVYLFENVHGKWRQAMCVLLITPVLLPRVSAAFIWKFMYSPLTGILGWLLGLVGIHDTAFLSDPALALYAVALVDIWQWGLFFAVIVLKLLETLPPEPLEAARLDYARTWQVYAYIALPMLKGPLISLVFIKMVESLRSFDLIYVMTKGGPGVATETLDMYAYAQGIGLSGKVSYASTMAVLMMIATTLIFTLIWKRVSKWED Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS17010 HSERO_RS17010 ABC transporter for D-sorbitol/xylitol, permease component 2 Specifically important for utilization of D-sorbitol and xylitol. sugar ABC transporter permease MGRLITRCAVWGVGIVLVLVAVFPLLWALLNSVKTLLDIVTPTPRFLFTPTLENYRQVIGSPEVLVGLTNSAVIVGSAVLLGTFMGVPAAYVIARYHVPGKRDIQFFLLSLRFLPPVAVAIPLIAIWVDLGLYDTRFSMIVTYLLTTLSTITWLSIPVFQRMPREIEEAATLDGYGPYAVFWKIALPNCATTLLGGIIFSFVLVWNELMIALALTSSNSATLPVVASAFTSMGQEVPWGVINASTVLLALPPLIFVGVLSRLLNSMLKGK Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS17020 HSERO_RS17020 ABC transporter for D-sorbitol/xylitol, ATPase component Specifically important for utilization of D-sorbitol and xylitol. sugar ABC transporter ATP-binding protein MADIHCQALAKHYAGGPPVLHPLDLHIGDGEFVVLLGPSGCGKSTMLRMIAGLEDISGGTLRIGGTVVNDLPARERNVAMVFQNYALYPHMSVYDNIAFGLRRLKRPAAEIDRRVREVAALLNLEALLERKPRAMSGGQQQRAAIARAIIKTPSVFLFDEPLSNLDAKLRAQLRGDIKRLHQRLRTTTVYVTHDQLEAMTLADRVILMQDGRIVQAGSPAELYRYPRNLFAAGFIGTPAMNFLSGTVQRQDGQLFIETAHQRWALTGERFSRLRHAMAVKLAVRPDHVRIAGEREPAASLTCPVSVELVEILGADALLTTRCGDQTLTALVPADRLPQPGATLTLALDQHELHVFDVESGENLSLPDAALTAPGSDDGPHGKETKHESGSGAGPYPPGPIVQGLGA Pseudomonas simiae WCS417 WCS417 GFF2366 PS417_12065 xylitol ABC transporter, ATPase component Specifically important for utilizing xylitol. D-ribose transporter ATP-binding protein MARPLLLQAEHVAKAYAGVPALRDGRLSLRAGSVHALCGGNGAGKSTFLSILMGITQRDAGSILLNGAPVQFNRPSEALAAGIAMITQELEPIPYMTVAENIWLGREPRRAGCIVDNKALNRRTRELLDSLEFDVDATSPMHRLSVAQIQLVEIAKAFSHDCQVMIMDEPTSAIGEHEAQTLFKAIRRLTAQGAGIVYVSHRLSELAQIADDYSIFRDGAFVESGRMADIDRDHLVRGIVGQELTRIDHKVGRECAANTCLQVDNLSRAGEFHDISLQLRQGEILGIYGLMGSGRSEFLNCIYGLTVADSGSVTLQGKPMPIGLPKATINAGMSLVTEDRKDSGLVLTGSILSNIALSAYKRLSSWSLINARKETQLAEDMVKRLQIKTTSLELPVASMSGGNQQKVVLAKCLSTEPVCLLCDEPTRGIDEGAKQEIYHLLDQFVRGGGAAIVVSSEAPELLHLSDRIAVFKGGRLVTISTDTALSQEALLRLAS Pseudomonas simiae WCS417 WCS417 GFF2365 PS417_12060 xylitol ABC transporter, permease component Specifically important for utilizing xylitol. sugar ABC transporter permease MNAKTITAPVTAAPRNRLRLSLDRFGLPLVFILLCVVMAFSSEYFMTWRNWMDILRQTSINGILAVGMTYVILTKGIDLSVGSILAFAGLCSAMVATQGYGLLAAVSAGMFAGAMLGVVNGFMVANLSIPPFVATLGMLSIARGMTFILNDGSPITDLPDAYLALGIGKIGPIGVPIIIFAVVALIFWMVLRYTTYGRYVYAVGGNEKSARTSGIGVRKVMFSVYVVSGLLAGLAGVVLSARTTSALPQAGVSYELDAIAAVVIGGTSLSGGTGSIVGTLFGALLIGVINNGLNLLGVSSYYQQVAKGLIIVFAVLIDVWRKKKR Pseudomonas simiae WCS417 WCS417 GFF2364 PS417_12055 xylitol ABC transporter, substrate-binding component Specifically important for utilizing xylitol. sugar ABC transporter substrate-binding protein MKLGTTLAATAALSLLACSIAMAADGKTYKVGAAVYGLKGQFMQNWVRELKEHPAVKDGTVQLTVFDGNYDALTQNNQIENMVTQRYDAILFVPIDTKAGVGTVKAAMSNDVVVIASNTKVADASVPYVGNDDVEGGRLQAQAMVDKLNGKGNVVIIQGPIGQSAQIDREKGELEVLGKHPDIKIIEKKTANWDRAQALALTEDWLNAHPKGINGVIAQNDDMALGAVQALKSHGLTSKDVPVTSIDGMPDAIQAAKKDEVTTFLQDAQAQSQGALDVALRALAGKDYKPQSVIWERYAKEVKWGDGTAKNYILPWVPVTNANADALYKQVSGGK Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS28305 RR42_RS28305 L-threonine:H+ symporter Specifically important for utilizing threonine as a carbon source proline-specific permease MTDVRKLLNEERVHEEKDLHRGLKDRHIQMIAIGGAIGVGLFLGAGRAIAIAGPGLMLSYAIGGVAIFFIMRALGELLLYRPVSGSFATYAEEFVGPFAGFATGWSYWFMWVVTGMAEITAVAVYVHYWFPDVPQWIPALATLAVLYLVNCVAVAVFGELEFWFALIKVVTIVAMIVIGLAIIFFGVTPLGPTASFSNLWTHGGFMPFGTLGVVLTLQIVMFAYQGVELIGVTAGEAQNPEKVLPHATNGVVWRILIFYVGALIIMMALVPWNELKPGVSPFVYVFERIGVPGAAAIVNLVVITAAASSCNSGIFSTGRMLYTLAQFGQAPRAFGRVSSKHVPSIAITFSAALMGIGVLLNYIVPEQVFVWVTSISLVGSLWTWSIIMIAHLGYRKAIAAGRVKAVAFRMPGAPYANWLVVAFMIAVAVLLSLDPGTRVALYVAPVWFALLGIGYRFTKSRALLEGHVQKSA Shewanella oneidensis MR-1 MR1 200693 SO1522 D,L-lactate/pyruvate symporter LctP2 Important for utilization of L-lactate, D,L-lactate, or pyruvate. Has phenotypes in many nitrogen source experiments with D,L-lactate as the carbon source. Also see PMID:28285200 for evidence that LctP2 transports D-lactate. L-lactate permease, putative (NCBI ptt file) MTILQLFASLTPVLSVMIFLVLLRMPASKAMPISMVVTAIAAVFIWQMDTTLLAASVVEGLLSAITPLTIIFGAVFLLNTLKYSGAMDTIRAGFTNISADARVQVIIICWLFGAFIEGSAGFGTPAAIGAPLLVLLGVPPVAAAVVALIADSACVSFGAIGLPVLFGMEQGLIQGGVSMAAEQFAAHGGTYAGYARYIVMHMITIDLITGTLIPLVMVTMLTGFFGRNKSFKEGLAIWKFAIFSGLAFTVPAWIINYLAGPEFPSVIGALIGMAMVIPVARKGYLLPKTPWNDFAENDNQDGVKLETTAKFSQIAAWTPYIIMAALLVLSRTVAPLKAWLSGFNINWTGLLGTELKASFATLYAPGAFFVAVCILGFFLFKMKSPAIKQSIGVSCKSMLPTIISLGASVPMVKIFLNSGANGAGLASMPVALADMLASSMGAVWAWMAPIVGIFGAFLSGSATFSNMMFSSLQYSVADNIGMNHTLVLALQGIGANAGNMMCVMNVVAAATVVGMAGRESEIIRKTMPVAIGYALLAGTIATLWGGF Pseudomonas stutzeri RCH2 psRCH2 GFF926 Psest_0955 D,L-lactate:H+ symporter Important for utilization of L,-lactate, D-lactate, D,L-lactate. Also important in many nitrogen source experiments with D,L-lactate as the carbn source. L-lactate transport MSNGLLALFAFTPILLAAIMLIGLRWPASRAMPLVFLFTAAIGLFVWDMSVNRIIASTLQGLVITLGLLWIIFGAILLLNTLKHSGGITAIRAGFTTISPDRRIQAIIIAWLFGCFIEGASGFGTPAAIAAPLLVAVGFPAMAAVLLGMLVQSTPVSFGAVGTPIVVGINSGLDTATIGAQLVAQGSSWNAYLQQITSSVAITHAIVGTVMPLVMVLMLTRFFGKEKSWKAGFEVLPFAIFAGLAFTLPYAATGIFLGPEFPSLLGGLVGLAIVTTAARFKFLTPKTTWDFADAKEWPAEWLGTIEMKLDEMAARPMSAFRAWLPYVLVGAILVISRVFPQVTAALKSVSIAFANILGETGINAGIEPLYLPGGILVMVVLITFFLHGMRVSELKAAVKESSGVLLSAGFVLLFTVPMVRILINSGVNGAELASMPIVMARYVADSVGSIYPLLAPAVGALGAFLAGSNTVSNMMFSQFQFGVAQSLGISGAMVVATQAVGAAAGNMVAIHNVVAASATVGLLGREGSTLRKTIWPTLYYVLFTGVIGLIAIYVLGVTDPLVGV Pseudomonas putida KT2440 Putida PP_4493 PP_4493 D-2-hydroxyglutarate dehydrogenase (EC 1.1.99.39) Specifically important in carbon source D-Lysine; carbon source L-Lysine; carbon source DL-2-Aminoadipic acid. This is part of the pathway from D-lysine to 2-oxoglutarate. For detailed rationale, see PMC6509195. putative oxidoreductase MIAQLSTVAPSANYPEFLEALRNSGFRGQISADYATRTVLATDNSIYQRLPQAAVFPLDADDVARVATLMGEPRFQQVKLTPRGGGTGTNGQSLTDGIVVDLSRHMNNILEINVEERWVRVQAGTVKDQLNAALKPHGLFFAPELSTSNRATVGGMINTDASGQGSCTYGKTRDHVLELHSVLLGGERLHSLPIDDAALEQACAAPGRVGEVYRMAREIQETQAELIETTFPKLNRCLTGYDLAHLRDEQGRFNLNSVLCGAEGSLGYVVEAKLNVLPIPKYAVLVNVRYTSFMDALRDANALMAHKPLSIETVDSKVLMLAMKDIVWHSVAEYFPADPERPTLGINLVEFCGDEPAEVNAKVQAFIQHLQSDTSVERLGHTLAEGAEAVTRVYTMRKRSVGLLGNVEGEVRPQPFVEDTAVPPEQLADYIADFRALLDGYGLAYGMFGHVDAGVLHVRPALDMKDPVQAALVKPISDAVAALTKRYGGLLWGEHGKGLRSEYVPEYFGELYPALQRLKGAFDPHNQLNPGKICTPLGSAEGLTPVDGVTLRGDLDRTIDERVWQDFPSAVHCNGNGACYNYDPNDAMCPSWKATRERQHSPKGRASLMREWLRLQGEANIDVLAAARNKVSWLKGLPARLRNNRARNQGQEDFSHEVYDAMAGCLACKSCAGQCPIKVNVPDFRSRFLELYHGRYQRPLRDYLIGSLEFTIPYLAHAPGLYNAVMGSKWVSQLLADKVGMVDSPLISRFNFQATLTRCRVGMATVPALRELTPAQRERSIVLVQDAFTRYFETPLLSAFIDLAHRLGHRVFLAPYSANGKPLHVQGFLGAFAKAAIRNATQLKALADCGVPLVGLDPAMTLVYRQEYQKVPGLEGCPKVLLPQEWLMDVLPEQAPAAPGSFRLMAHCTEKTNVPASTRQWEQVFARLGLKLVTEATGCCGMSGTYGHEARNQETSRTIFEQSWATKLDKDGEPLATGYSCRSQVKRMTERKMRHPLEVVLQYAQR Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS17300 RR42_RS17300 D-lactate dehydrogenase, FAD-linked subunit GlcD (EC 1.1.99.6) Specifically important for: Sodium D-Lactate. glycolate oxidase MNAPHEVSLVADDARRSALLAGLAKILPDAALLWKPEDTVPYECDGLAAYRQVPMAVALPDNEDQVCAILRLCHSLQVPVVPRGAGTSLSGGAMPIATGLVLSLAKFKRIVSVDVRSRTAVVQPGVRNLAISEAAAQYNLYYAPDPSSQIACTIGGNVSENSGGVHCLKYGLTVHNVLRVRAVTMEGDVVEFGSEAPDAPGLDLLAAVIGSEGMLAVVTEVSVKLIPKPQLAQVIMASFDDVAKGGNAVADVIGAGIIPAGLEMMDKPATAAVEEFVRAGYDLDAAAILLCESDGTPEEVAEEVERMSEVLRASGASRIQVSQSEPERLRFWSGRKNAFPAAGRISPDYYCMDGTIPRKHIGTLLKRIEEMERKYGLRCMNVFHAGDGNMHPLILFDGADQDEWHRAELFGSDILESCVELGGTVTGEHGVGVEKLNSMCVQFSAQERDLFFGVKAAFDPARLLNPDKAIPTLARCAEYGRMHVKRGLLPHPDLPRF Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS17310 RR42_RS17310 D-lactate dehydrogenase, FAD binding subunit GlcE (EC 1.1.99.6) Important on D-lactate glycolate oxidase MPATPADQQATLTAFRDAIRHATGTRTPLRLRGGGSKDFYGQHPQGTLLDTRAYSGIVDYDPPELVITARCGTPLAQIEAALAERRQMLAFEPPHFSTGADGSDVATIGGAVAAGLSGPRRQAVGALRDFVLGTRVMDGRGDVLSFGGQVMKNVAGYDVSRLMSGSLGTLGLILEVSLKVLPVPFDDATLRFALDEAAALDRLNDWGGQPLPIAASAWHDGVLHLRLSGAAAALRAARARLGGEAVDAAQADALWRALREHSHAFFAPVQAGRALWRIAVPTTAAPLALPGGQLIEWGGGQRWWLGGSDSAADSAIVRAAAKAAGGHATLFRNGDKAVGVFTPLSAPVAAIHQRLKATFDPAGIFNPQRMYAGL Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS17315 RR42_RS17315 D-lactate dehydrogenase, iron-sulfur subunit GlcF (EC 1.1.99.6) Important on D-lactate glycolate oxidase MQTTLAEFLRDTPDGEEAKSIVGKCVHCGFCTATCPTYQLLGDELDGPRGRIYLMKQVLEGQPVTQSTRLHLDRCLTCRNCESTCPSGVKYGRLVDIGRKVVDDRLEAQGIQRPARERFARWALRETMTRPALFGTAMRMGQRVRPLLPQALRNKVPQAVDAGAWPRTTHARKMLLLDGCVQPSMSPNINAATARVFDRLGVQLVMAREAGCCGAVRYHTGDHDGGLDNMRRNIDAWWPAVQAGAEAIVMTASGCGVMVKEYGHLLRNDAHYADRARQISALTKDLSELLPNFADALQDAAAEAGSSKGTNGTDGQRVAYHPPCTLQHGQQIRGKVEALLTGLGVDVKLCADSHLCCGSAGTYSVLQPALSYRLRDEKLANLQALKPEAIVSANIGCITHLQSGTGTPVMHWIELVDRMLG Phaeobacter inhibens BS107 Phaeo GFF2923 PGA1_c29700 D-lactate dehydrogenase, iron-sulfur subunit GlcF (EC 1.1.99.6) Specifically important for: Sodium D,L-Lactate; Sodium D-Lactate. glycolate oxidase iron-sulfur subunit MQTTFSEKQLRDPGTQRANEILRSCVHCGFCTATCPTYQVLGDELDSPRGRIYLIKDMLENERVPDAKTVKHIDRCLSCLACMTTCPSGVHYMHLVDHARAYIDKHYNRPWSDRALRWLLARILPYPGRFRLALIGAKLAQPFKRLVPDARLRAMLDMAPRHIPPVSRNDDPQSFAAKAPRRKRVALMTGCAQKALNTDINDATIRLLTRLGCEVVVAAGAGCCGALTHHMGREEESHATAAKNIRAWTDEIDGQGLDAIVINTSGCGTTVKDYGHMFRNDALAEDAARVSAIAMDISELLMQLDLPEGEDKETTVAYHAACSLQHGQQIKTHPKTLLKRAGFTVVEPADSHLCCGSAGTYNLLQPEISAELKARKVTSLEARQPDLIAAGNIGCMMQIGSATDIPILHTVELLDWATGGPKPRALVAGGPGADPRAGEIPILR Phaeobacter inhibens BS107 Phaeo GFF2924 PGA1_c29710 D-lactate dehydrogenase, FAD binding subunit GlcE (EC 1.1.99.6) Specifically important for: Sodium D-Lactate; Sodium D,L-Lactate. glycolate oxidase subunit GlcE MTPQSEAELAQIIVGATAPLAVSGGGTRGLSTGGETLSVAGLNGVTLYEPGALTLVVQAGTSVEEVQALLAGENQRLAFEPMDHRGLLGTKGTPTIGGVFAANVSGPRRIQCGAARDFLLGVRFVDGRGDVLSNGGRVMKNVTGYDLVKLMAGSHGTLGVLSEVSLKVLPCSEACATVTVHVADLTSAVAAMSTALGSPYDVTGAAYDPEAGAVYIRVEGFEASVTYRAEALKMALGKFGEVSLALGAGDALWEGIRNVAAFHDRPGDVWRISVKPSDAVALAPALEAEGLLFDWGGGLIWALVPAGRDLRFRLTVPGHATLVRASAQTRAELGQFQPQPGPLAAISGGLRRQFDPRGILNPGLMG Phaeobacter inhibens BS107 Phaeo GFF2925 PGA1_c29720 D-lactate dehydrogenase, FAD-linked subunit GlcD (EC 1.1.99.6) Specifically important for: Sodium D,L-Lactate; Sodium D-Lactate. glycolate oxidase subunit GlcD MEMPIPDQTVLSQKTELALRLAAVLPDDALVQDPAETRAYECDALTAYKCPPMLVVLPRTTKEVSDVLRICHAAGVPVVPRGAGTSLAGGALPTADCVILGVARMNAVLETDYDNRIIRVQTGRTNLSVSGAVEEEEFFYAPDPSSQLACAIAGNIAMNSGGAHCLKYGVTTNNLMGVTMVMMDGTVVEIGGAHLDAGGLDLLGVICGSEGQLGVVTEATLRILRKPEGARPVLIGYDSNEVAGACVSDIIKAGVLPVAIEFMDRPCIEACEAFAKAGYPMCEALLIVEVEGSDAEIDHQLRLITEIARSHNPVELREARDSDEAARIWLGRKSAFGAMGQINDYMCLDGTIPVTSLPHVLRRIGEMSKEFGLDVANVFHAGDGNMHPLILFDANKPGDLETCEAFGAEILKLCVEVGGCLTGEHGVGIEKRDLMLDQYGVADIEAQLRVKDVFDPKWLLNPAKVFPLSTTQSRRTPAVTPL Pseudomonas stutzeri RCH2 psRCH2 GFF3770 Psest_3839 D-lactate/glycolate dehydrogenase, iron-sulfur subunit GlcF (EC 1.1.99.6; EC 1.1.99.14) Specifically important for: Glycolic Acid; Sodium D-Lactate. This is the first step in both D-lactate and glycolate oxidation. Fe-S oxidoreductase MQTNLSEAAKKLPRAEEAESILRSCVHCGFCNATCPTYQLLGDELDGPRGRIYLMKQMFEGGEVTESTQLHLDRCLTCRNCETTCPSGVKYHNLLDIGRDFIEQQVQRPLGERVVRGGLRTVIPRPGLFKALLGAGNALKPLMPASLKDHLPREIRPAKPRPQVMHSRRVLILEGCVQPSLSPSTNAAAARVLDRLGISVSPAREAGCCGAVDYHLNAQDAGLDRARRNIDAWWPAIEAGAEAIVQTASGCGAFVKEYGHLLKDDPAYAAKAARVSELAKDLVEVLRSAELEKLNVRADKRMAFHCPCTLQHAQKLGGAVEDVLTRLGYQLTAVPDAHLCCGSAGSYSITQPEISHQLRDNKLNALESGKPEVIVTANIGCQTHLDGAGRTPVKHWIEVVEESMQ Pseudomonas stutzeri RCH2 psRCH2 GFF3771 Psest_3840 D-lactate/glycolate dehydrogenase, FAD binding subunit GlcE (EC 1.1.99.6; EC 1.1.99.14) Specifically important for: Sodium D-Lactate; Glycolic Acid. FAD/FMN-containing dehydrogenases MSVIANDASAQLLDQVNQALAANTPLRIQGSGSKSFLGLQADGVLLDTREHRGIVSYDPTELVVTVRAGTPLTELETALDEAGQMLPCEPPHFGEGATVGGMIAAGLSGPRRPWSGSVRDFVLGSRVITGQGKHLRFGGEVMKNVAGYDLSRLMAGSFGCLGVLTEVSLKVLPKPRLCTSLRLEIDLERALLKLAEWGQQPIPISAASHDGQALHLRLEGGEGSVGAARERIGGEDLDPGYWNDLREQRLAFFADPRPLWRLSLPNNTPALGLPGDQLVDWAGAQRWLKSDADAVTIRGIAIEVGGHATCFTAGATTNPFQPLAAPLLRYHRQLKAALDPQGIFNPGRMYSEV Pseudomonas stutzeri RCH2 psRCH2 GFF3772 Psest_3841 D-lactate/glycolate dehydrogenase, FAD-linked subunit GlcD (EC 1.1.99.6; EC 1.1.99.14) Specifically important for: Sodium D-Lactate; Glycolic Acid. This is the first step in both D-lactate and glycolate oxidation. glycolate oxidase, subunit GlcD MNILYDERVDGALPKVDKAALLAELQAQLPDLDILHRSEDLKPYECDGLSAYRTTPLLVVLPERIEQVETLLKLCHQRGVPVVARGAGTGLSGGALPLEQGILLVMARFNKILEVDPAGRFARVQPGVRNLAISQAAAPYELYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKVDILTVEGERMTLGSDALDSPGFDLLALFTGSEGMLGIVTEVTVKLLPKPQVAKVLLAAFDSVEKAGRAVGDIIAAGIIPGGLEMMDNLSIRAAEDFIHAGYPVDAEAILLCELDGVEADVHDDCARVSEVLKLAGATEVRLAKDEAERVRFWAGRKNAFPAVGRISPDYYCMDGTIPRRELPGVLKGISDLSEQFGLRVANVFHAGDGNMHPLILFDANQPGELERAEDLGGKILELCVKVGGSITGEHGVGREKINQMCSQFNADELTLFHAVKAAFDPSGLLNPGKNIPTLHRCAEFGRMHIHNGQLPFPELERF Sinorhizobium meliloti 1021 Smeli SMc00832 SMc00832 D-lactate dehydrogenase, FAD-linked subunit GlcD (EC 1.1.99.6) Specifically important for: Sodium D,L-Lactate. This is the first step in D-lactate oxidation. glycolate oxidase subunit protein MPETIGFLKPRQAVLDRRREIVADLADLLPEGGLISDERGLKPFETDAFIAYRRMPLAVVLPETTEHVAAVLKYCSRYGIPIVPRGAGTSLSGGAIPQEDAIVVGLSKMSRTLDIDLFNRTATVQAGVTNLNISDAVSADGFFYAPDPSSQLACTIGGNIGMNSGGAHCLKYGVTTNNLLGVKMVLFDGTVIELGGKALDAPGYDLLGLVCGSEGQLGIVTEATVRLIAKPEGARPVLFGFASSESAGSCVADIIGSGIIPVAIEFMDRPAIEICEAFAQAGYPLDVEALLIVEVEGSEAEMDATLAGIIEIARRHGVMTIRESQSALEAALIWKGRKSAFGATGRIADYICMDGTVPLSQLSHVLRRTGEIVAGYGLRVANVFHAGDGNMHPLILYNINDPEEAARAEAAGNDILKLCVEAGGCLTGEHGVGIEKRDLMLHQYSRADLGQQMAARAAFDPQWLMNPSKVFPLEGRPAA Sinorhizobium meliloti 1021 Smeli SMc00833 SMc00833 D-lactate dehydrogenase, FAD binding subunit GlcE (EC 1.1.99.6) Specifically important for: Sodium D,L-Lactate. This is the first step in D-lactate oxidation. glycolate oxidase subunit protein MIVHFEPASEEGIASVVRSAAAERVTLAVVGGGTRAGLGNPVRADRTLSTRRLSGIVTYDPAEMTMSALAGTPVAEVEAALHAKGQMLSFEPMDHRPIFATTGEPTIGGVFAANVSGPRRYVAGAARDSLLGVRFVNGRGEPIKAGGRVMKNVTGLDLVKLMAGSYGTLGILTEVTFKVLPLPPAAATVVVSGLNDAEAAAVMAEAMAQPVEVSGASHLPESVRSRFLDGALPDGAATVLRLEGLAASVAIRAEKLGEKLSRFGRISQLDEAQTRTLWAEIRDVKPYADGTRRPLWRISVAPSAGHQLVAALRLQTGVDAFYDWQGGLVWLRMEADPEAELLRRYIGAVGGGHAALLRAGEEARGRIPAFEPQPPAVARLSERIRAQFDPSGIFNPGRAAALVRN Sinorhizobium meliloti 1021 Smeli SMc00926 SMc00926 D-lactate dehydrogenase, iron-sulfur subunit GlcF (EC 1.1.99.6) Specifically important for: Sodium D,L-Lactate. This is the first step in D-lactate oxidation. glycolate oxidase iron-sulfur subunit protein MIQRPQGATWSTRLQTNFSPEQLADPHVAESETILRKCVHCGFCTATCPTYVVLGDELDSPRGRIYLIKDMLENGRAADSETVTHIDRCLSCLSCLTTCPSGVDYMHLVDHARAHIEKTYKRPFKDRLARSVIAATLPYPSRFRLALGAAGLARPLAGLLKRVPFLRTLGVMLDLAPSALPAARGAKPAVYAAKGTPRARVALLTGCAQPVLRPEINDATIRLLTGQGVEVVVSAGEGCCGALVHHMGRDEQALQAGRHNIDVWLKAAEEDGLDAIIITASGCGTTIKDYGHMLRLDPAYAEKAARVSALAKDVTEYLATLDLPEQGARNLTVAYHSACSMQHGQKITSAPKQLLKRAGFSVREPAEGHLCCGSAGTYNILQPEISAKLKARKVRNIEATKPEVIATGNIGCITQIASGTEIPILHTVELLDWAYGGPKPAGL Burkholderia phytofirmans PsJN BFirm BPHYT_RS26975 BPHYT_RS26975 L-lactate dehydrogenase, LldE subunit Specifically important for utilization of L-lactate and D,L-lactate as well as L-rhamnose and L-fucose, which are catabolized via L-lactate. Fe-S oxidoreductase MKVALFIPCFIDAFYPEVGIATLELLERFGIQVDYPQEQTCCGQPMANSGAHAEAAGTERVFARNFAGYDYIVGPSASCIHHVREHLTALEQTDEVKKVRANAYELVEFLHDVVGAREFPWAEFPHRVGLHNSCSALRHLKEASISEVAGAPFSKPRTLLEGVKGIEFVKPARPDECCGFGGTFSVTEEPVSVRMGQDKVRDHLNAGAEYIVSGDMSCLMHQQGCAERMKADARFIHIAQVLNGARA Burkholderia phytofirmans PsJN BFirm BPHYT_RS26970 BPHYT_RS26970 L-lactate dehydrogenase, LldF subunit Specifically important for utilization of L-lactate and D,L-lactate as well as L-rhamnose and L-fucose, which are catabolized via L-lactate 4Fe-4S ferredoxin MSNRIDHAKAAGAFIGKTEHVAFHDKRLWDLREKRDAQAHGIAEWETMRELASGIKEHTLSNLSQYLEQFAAAAEANGVTVHWAATAEEHNALVHQIMSERGMTTLVKSKSMLTDECKMREYLEPRGITVMETDLGERIQQLDHQDPSHMVVPAVHKLRADVAELFGRTIGTDPKNSDIHYLAESQRMNTRPYFVREKTAGMTGCNFAVAETGTVVVCTNEGNADLSANVPPLHIASIGIEKLIPKVSDLGVFIRMLSRSALGSPITQYTSHFRAPRPGTEMHFILVDHGRSERLAMEDFWYSLKCIRCGACMNTCPVYRRSGGLSYGGTYSGPIGAIINPTFDLKRYSALPFASTLNGSCTNVCPVKINIHEQIYKWRTVIAERHEVPFVKQEVLKMAGRLLASPTLYRATVSSMGSALRRLPNFVLYNPLNIWGKQRELPEAPKLTFHAWYKKNRGDGNGNA Burkholderia phytofirmans PsJN BFirm BPHYT_RS26965 BPHYT_RS26965 L-lactate dehydrogenase, LldG subunit Specifically important for utilization of L-lactate and D,L-lactate as well as L-rhamnose and L-fucose, which are catabolized via L-lactate. This gene has additional phenotypes which were not found for the other subunits and are not explained. hypothetical protein MATREAFLDKVRQAQPPSRPRPEVPLFDAPGGDLRVRFTAALQAMGGTCVQAVSATDVSGLIRERFGAEASVASATTEVPGTRALTADTEPASLQDIDVGVVRARFGVAETGSVWFSEREYVVNALGYIVQHLIVLLDPAQLIDGLQDVYRRDDFRDARYAALVTGPSATADIEGVLIRGAQGVRSLTVVWLAAQ Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS16820 HSERO_RS16820 2-oxoglutarate:H+ symporter Specifically important for the utilization of alpha-ketoglutarate alpha-ketoglutarate permease VRPTQEISMSDTTQASTPLSAAEYRKRIFAILGASSGNLVEWFDFYVYSFCAIYFAPAFFPKGDPTSQLLNTAGVFAAGFLMRPIGGWLFGRIADKHGRKTSMLISVLMMCGGSLAVAVMPTYATIGAWAPALLLLARLFQGLSVGGEYGTSATYMSEVAPNGRRGFFASFQYVTLIGGQLLAVLVLFGMQQWLTKAELMAWGWRVPFVLGAVGALVAMYLRSSLAETSSAGARKKKDAGTLKGLLQHKRAFLNVVGFTAGGSLMFYTFTTYMQKYLVNTAGMDPKVANGVMTGALFVYMILQPIFGAISDKIGRRNSMLCFAFFGMVGTFPILHFLKDVSSPGVAMALAILALTIVSFYTSISGLIKAEMFPPEVRALGVGLSYAVGNAIFGGSAEFVALSLKSAGIESAFYWYVSALCLVALIISLRMPDPQRDGHLKGDVAMNPDEHQGEADAAAGKLHKPA Dinoroseobacter shibae DFL-12 Dino 3607785 Dshi_1194 TRAP transporter for fumarate, succinate, L-malate, and 2-oxoglutarate, fused 4TM/12TM components Specifically important for utilization of fumarate, succinate, L-malate, and alpha-ketoglutarate. TRAP transporter, 4TM/12TM fusion protein (RefSeq) MTDQTKTADDHLIAEGVDEEPTESNRRLFEGRNFILISTFAALYAAFHMAALNGLSISEWTGIEVPFLPTFPMETWNFRIVHIAGALALGFLLFAARTDFPGPGKETPLLGYVAYGLMVPALFSLGMAASFSMEIASGVMWNGIDEGIKFNETWLFGLPLIVATAGGIVLSWFHKRARSGFSAPDLVLAICGVAVATYLITIYGTLMRNSTGTPFAPIGISIAAVAGTALIMELTRRVAGMALIVIAGIFLAYVFVGQYLPGFLNAPAVTWQRFFSQVYTDAGILGPTTAVSSTYIILFIIFAAFLQASKVGDYFVNFAFAAAGQSRGGPAKVAIFASGLMGMINGTSAGNVVATGSLTIPLMKKVGYHKKTAGAVEAAASTGGQIMPPIMGAGAFIMAEITGIPYTEIALAAIIPAILYFVSVYFMVDLEAAKLGMRGMSRDELPKFNKMVRQVYLFLPIIILIYALFMGYSVIRAGTLATVAAAVVSWFTPFRMGPRSIAKAFEIAGTMSVQIIAVCACAGIIVGVISLTGVGARFSAVLLGIADTSQLLALFFAMCIAILLGMGMPTTAAYAVAASVVAPGLVQLGIPLLTAHFFVFYFAVLSAITPPVALASYAAAGISGANPMETSVTSFKIGIAAFIVPFMFFYNSAILMDGTWFEVLRAGATAVVGVFFLSSGVQGWFMGGRAAWFLRVGLVFAALMLIEGGIMSDLIGVGTAVAIFLIQKLAAPKGGAIPVRGAD Dinoroseobacter shibae DFL-12 Dino 3607786 Dshi_1195 TRAP transporter for fumarate, succinate, L-malate, and 2-oxoglutarate, solute receptor component Specifically important for utilization of fumarate, succinate, L-malate, and alpha-ketoglutarate. TRAP transporter solute receptor, TAXI family (RefSeq) MKFTLMTGTAMAVALSATVVTTATAQDRDGWPDSFTVGTASQGGTYFAYGSGWANLVAEELGLSGGGEVTGGPMQNMALVHTGDAQFGMTTMGPAAESLAGTNPIAPGLQMDNACAMFPMYQTPFSVTALSSSGIASIADIPDGAKIGFGPAGSTSDTYFPRMMEALGVNFERRNGGWSDLGGQLQDGLLDVIAFAAGVPVPAVSQLEVQTDINIIEFTEEEQAKIMADFPVSEFSIGAGTYSTLEADARSVSMWNFAIANCDLPASFVKAATDVVMSDNARMVGIHKAARSTLPENWDKNKVLKWHPGAAEWFKENAGADIPDDMIHGM Marinobacter adhaerens HP15 Marino GFF744 HP15_723 TRAP transporter for fumarate, succinate, L-malate, and 2-oxoglutarate, fused 4TM/12TM components Important for utilization of fumarate, succinate, L-malate, and 2-oxoglutarate. Also important in many nitrogen source experiments with 2-oxoglutarate as the carbon source. TRAP transporter, 4TM/12TM fusion protein MTTEQDSKDLPDIEVGEDHVLAHNVDEEPVEANRRLFEGGLLKFVALLAIAYSAFHLYSLNIAPLETWSFRIVHIAGALVLGFVLFAGARFVSSEEGGARHRWTTWISAGAMLPALYVLYQTFSFWQMVQNGAMRIPVELEVWHFGWPLLAATGVGIVMSWFHQRERSVFSVPDLVLIVCSLAVAAYFLVVYNTSMRMSTGTSFAPVGISFAAIAGTALIMELTRRVAGMALVIIGLVFLAYVFAGPYLPGFLGYPGLSVQRFFSQVYTDAGILGPTTAVSSTYIILFIIFAAFLQSSKVGDYFVNFAFAAAGRSRGGPAKVSIFASGLMGMINGTSAGNVVSTGSLTIPLMKKVGYSKQSAGAVEAAASTGGQIMPPIMGAGAFIMAEITGIPYTEIAIAAIIPAILYFASVYFMVDFEAAKTGMRGMREDELPKLRTMMKQCYLFVPIIILIVALFMGYSVIRAGTLATVSAAVVSWLSPNKMGLRHILQALEIASYMAIQIIVVCAAAGVIVGVISLTGVGARFSVLLLDVAATSQLLALIFAMFISILLGMGMPTTAAYAVAASVVAPGLVQLGIEPLTAHFFVFYFAVVSAITPPVALASYAAAGISGANAMETSVASFRIGIAAFIVPFMFFYNGALLMEAGWFEIARALVTATFGVYMLSGGVLGWFASISASWITRLLLIAAALLMIEGGLWTDLTGIALAVLAFVIQKQRKTRLATAGAL Marinobacter adhaerens HP15 Marino GFF743 HP15_722 TRAP transporter for fumarate, succinate, L-malate, and 2-oxoglutarate, solute receptor component Important for utilization of fumarate, succinate, L-malate, and 2-oxoglutarate. Also important in many nitrogen source experiments with 2-oxoglutarate as the carbon source. immunogenic protein MKTQAVMAVAFASTFAVATPATAQDRSDWPSNFTVGTASQGGTYFAYGSGWANFVAENLGVSGGAEITGGPVQNMALVHTGDLKFGLTTMGPARESMDGNSPLAPGMKMDNVCAMFPMYETPFSVTALSSSGITSIADIPDGATIGFGPAGSTSDTYFPRMMETLGVNFERRNGSWSDLGGQLQDGLIDVVAFAAGIPIPAVSQLEVQTDVNIIGMNDAEAETIISNFPVSEFIIPASTYQSLDAPSRVVSMWNFAMVNCDVSESFVYEITKLTMENNDKMVSIHKAARNSVPENYTKNNVLPWHPGAARWFNENGYPIEDSQIK Phaeobacter inhibens BS107 Phaeo GFF2035 PGA1_c20680 TRAP transporter for fumarate, succinate, L-malate, and 2-oxogulatarate, substrate-binding component Specifically important for utilization of fumarate, succinate, L-malate, and alpha-ketoglutarate. Phenotypes on alpha-ketoglutarate are more mild, which might indicate some genetic redundancy. C4-dicarboxylate-binding periplasmic protein DctP MKFVTAAATAVALTMSAGTAMAACDDGEIVVKFSHVTNTDKHPKGIAASLLEKRINEEMNGTMCLEVYPNSTLYNDNKVLEAMLQGDVQLAAPSLSKFEKFTKQFRLFDLPFMFKNIDAVDAFQGSENGQAMLDSMQRRGLQGLSYWHNGMKQMSANKPLINPSDANGLKFRVQSSDVLVAQMEAIGGSPQKMAFSEVYGALQQGVVDGQENTWSNIYGKKFFEVQDGVTETNHGALDYLVVTSVDWLDSLDPAVREQFLTILGEVTATRNSESTKVNAEARQSIIDAGGVVRELTPEQRAAWVEAMKPVWEQFAGDVGQDMIDAAQAINAGM Phaeobacter inhibens BS107 Phaeo GFF2034 PGA1_c20670 TRAP transporter for fumarate, succinate, L-malate, and 2-oxogulatarate, small permease component Specifically important for utilization of fumarate, succinate, L-malate, and alpha-ketoglutarate. Phenotypes on alpha-ketoglutarate are more mild, which might indicate some genetic redundancy. TRAP transporter, subunit DctQ MAGAKPGPTGLINTLEETLIALLLGLMTLITFANVVARFVFNSNILWALELTVFLFAWLVLLGASYAVKVHAHLGVDAILNMVSPGARRVIGLISVGCCLVFSLLLLKGAYDYWAVFADLPPTSGRWFPTGFDMKARSQSFYEVQDVPMVAIFGFLEDLINYGDSYEKLPKVVPYVVLPLSMLLMLLRFAQAAMQILRGDVDRLVASHEVEDEIAEVQAQRGEHD Phaeobacter inhibens BS107 Phaeo GFF2033 PGA1_c20660 TRAP transporter for fumarate, succinate, L-malate, and 2-oxogulatarate, large permease component Specifically important for utilization of fumarate, succinate, L-malate, and alpha-ketoglutarate. Phenotypes on alpha-ketoglutarate are more mild, which might indicate some genetic redundancy. TRAP transporter, subunit DctM MDVVLLFSMVIGLLLIGVPIAVALGLSSTLFLLIYSDSSLASVAGTLFEAFEGHFTLLAIPFFILASSFMTTGGVARRIIRFSIACVGHLPGGLAIAGVFACMLFAALSGSSPATVVAIGSIVIAGMRQVGYSKEFAAGVICNAGTLGILIPPSIVMVVYAAAVEVSVGRMFLAGVIPGLMAGLMLMVTIYVMAKVKNLPKGEWLGWGEVAASAANASVGLLLIGIILGGIYGGIFTPTEAAAVASVYAFFVATFVYRDMGPLKSAPKPKDMGQFLTMLPKMLGQTVVYFIPSFFHADTRHALFEAGKLTVTLLFVIANALILKHVLTDEQVPQQIATAMLSAGFGPVMFLIVVNVILLIGGQFMEPSGLLVIVAPLVFPIAIELGIDPIHLGIIMVVNMEIGMITPPVGLNLFVTSGVAGMPMMAVVRAALPFLAVLFVFLIMITYIPWISTVLPNAVMGPEIITK Sinorhizobium meliloti 1021 Smeli SMc04385 SMc04385 L-2-aminoadipate semialdehyde dehydrogenase (EC 1.2.1.31) Specifically important for L-lysine utilization. This reaction is part of lysine catabolism via lysine 6-dehydrogenase (SMc02503), which forms (S)-2,3,4,5-tetrahydropyridine-2-carboxylate, which spontaenously interconverts with L-2-aminoadipate semialdehyde (also known as (S)-2-amino-6-oxohexanoate) in water. aldehyde dehydrogenase transmembrane protein MNIAAKKIDVASEAAALLDKMGVAKDLYTGGDMPSFSPVTGEKIASLKTVSAAEAAGKIEKADEAFRAWRLVPAPKRGELVRLLGEELRAFKADLGRLVSIEAGKIPSEGLGEVQEMIDICDFAVGLSRQLYGLTIATERPGHRMMETWHPLGVVGIISAFNFPVAVWSWNAALALVCGDAVVWKPSEKTPLTALACQAILERAIARFGDAPEGLSQVLIGDRAIGEVLVDHPKVPLVSATGSTRMGREVGPRLAKRFARAILELGGNNAGIVCPSADLDMALRAIAFGAMGTAGQRCTTLRRLFVHESVYDQLVPRLKKAYQSVSVGNPLESAALVGPLVDKAAFDGMQKAIAEAKNHGGAVTGGERVELGHENGYYVKPALVEMPKQEGPVLEETFAPILYVMKYSDFDAVLAEHNAVAAGLSSSIFTRDMQESERFLAADGSDCGIANVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKAYMRRATNTVNYSKALPLAQGVSFDIE Sinorhizobium meliloti 1021 Smeli SMc04384 SMc04384 (R)-2-hydroxyglutarate dehydrogenase (EC 1.1.99.39) Specifically important for L-lysine utilization. This is part of lysine catabolism via 2-aminoadipate and D-2-hydroxyglutarate synthase (also known as 2-oxoadipate dioxygenase/decarboxylase; SMc04383). oxidoreductase MIDEHHIDALTKLLGDKGVVTRREDMEAYEAGARYDRGRAAAVLRPVTTEEVSAAVGYCVRSGIALIPQSGNTGLVSGSTPDESGSEVVVSLDRLTRQFALDLDNRSVRVDAGFRLSELNRRLEEHGLFFPIDLGADPRIGGMIATNTGGSRFLKYGDVRRNTLGLKVVLADEAGTVLDLGSDLRKNNTGVDWKQIFIGTSGAFGIVTECVLNLERLPKQTATAFLVPASGAHVLPLLKAMEERLGAYLSAFEGMSRNAIAAAFAHVPALKNPFQGGKVPDYVILAEISRTSSPREGEQPLDAVLESVLAEIWEMEEVLLADALVGPPHEIWALRHALSEGVKHLGKLIAFDLSFRRGDIMAFCDHMKTEMPEKFPGVTVCDFGHIGDGGVHFNLVVAKDSPLLADATFEQRLREWVFAVAVEQYHGSFSAEHALGRRNQAFYDLYTPEKLKNMAAGLKTLTSPGKLGSVRFG Sinorhizobium meliloti 1021 Smeli SMc00140 SMc00140 L-lysine ABC transporter, substrate-binding component Specifically important for L-lysine utilization. The ATPase component is not encoded nearby and was not evident in the fitness data. amino-acid binding periplasmic protein MRISRRLAATASAAVFVLMAGVAMAEGEKVVIGTEGAYPPFNNLESDGTLTGFDIDIAKALCEEMKAECTFVTQDWDGIIPALIAKKFDAIVASMSITEERKQQVDFTNKYYNTPPAIVVPKDSPITEATAAALSGKALGAQGSTTHSNYAEAHMKESEVKLYPTADEYKLDLANGRIDAAIDDVVVLSEWLKTEDGACCKLLGTLPIDPVINGEGAGIAIRKGDDALREKLNKAIEAIRANGKYKQINEKYFPFDVYGS Sinorhizobium meliloti 1021 Smeli SMc00139 SMc00139 L-lysine ABC transporter, permease component 1 Specifically important for L-lysine utilization. The ATPase component is not encoded nearby and was not evident in the fitness data. amino acid ABC transporter permease MSGLFAALSAGLAWIGAIIDPLCGPAGIFRWFGSGTLLACGDAGWGDEIAYGFLVTASLAVATLPVGLVIGFFVALAKQSEEKSLRLAGNIYTTIFRGLPELLTLFIVYYGLQILVQQFLATVGYEGAVEINAFVAGMIALGVVFSAYCSEVLLSAFKAIPHGQYEAGDALGLHRGKTMRLIILPQLIRIALPGLGNLWMALLKDTALVSVIGLPDILRQTGIAARVTKHAFEFFGIACVLFLVLAMISSVVFSALERSTKRAEAGR Sinorhizobium meliloti 1021 Smeli SMc00138 SMc00138 L-lysine ABC transporter, permease component 2 Specifically important for L-lysine utilization. The ATPase component is not encoded nearby and was not evident in the fitness data. amino acid ABC transporter permease MSIAETMIPPQAPPPSPPKPYTFSRFFGSVALGIWLALGVGIFLTVVNGWDPEKFSRYGPSFLSGLGVTLTLVISSILMGAVLSLPVALGRMSKNRLWGWLAYAYVYFFRGTPLITQLFLIYYGLGSFRPQLETVGLWWFFRDAWNCALFTFTLNTAAYQAEILRGAIESVPRGQREGAAALGLPERVAFFKVILPQAMIVALRPYGNEIILMIKGSAIVAIVTVFDLMGETRRAFSRTFDYQMYIWAAILYLLMVELLRNIWGWLEARLTRHLKR Pseudomonas putida KT2440 Putida PP_3593 PP_3593 L-lysine and D-lysine ABC transporter, substrate-binding component Specifically important for utilization of L-lysine and D-lysine. Amino acid ABC transporter, periplasmic binding protein MNKSMALLGACALLLAGAASAETLRFATEGAYPPFNYVDADNKLHGFDVDITHALCEQMKVECTLVAQDWEGIIPALMARKYDAIVASMIDTEERRKKIAFTDHYYRTPLTVAVAKDSKIDSAQTDFVGYTVGAQSSSTQAIYAEDVYGKAGADVKLYPTMDEANADLAAGRLDGVIADKFPLHEWMNKNGGDCCKILGDVADTKADAAIAVRKDDEALRQRLNTALQQIVANGTYQKIASKYFAFDIYN Pseudomonas putida KT2440 Putida PP_3594 PP_3594 L-lysine and D-lysine ABC transporter, permease component 1 Specifically important for utilization of L-lysine and D-lysine. Amino acid ABC transporter, membrane protein MLDQLSLLSFASGGWGQALLAGALVTVSLALACLPIGLPLGLVVALAARSRKRLPRAWATTFSTVFRGLPELLTLLIIYYGCQIAAQKILAAMGYQGEFLINTFLAAMIAFSLVFAAFSSEIWLAAFKTLPKGQLEACSALGLSKRTGFFKVLLPQLTRIALPGLSNNWLSLLKDTSLVSTISLVDLMRQTNLAVSVTKEPMFFYGVACLGYLLFAALSGRVFAYIERRSNRHLQGARA Pseudomonas putida KT2440 Putida PP_3595 PP_3595 L-lysine and D-lysine ABC transporter, permease component 2 Specifically important for utilization of L-lysine and D-lysine. Amino acid ABC transporter, membrane protein MSFDQLLAMVLDPDLLERYGPRFIDGLLVTAKLVAISFSLGAVLGLLLALARLSRSLVLQRMAAGYVYFFRGSPLLAQLFLLYYGLGSLKGFWQDVGLWWFFRDAWFCTLLAFTLNTAAYQAEIFRGSLMAVAPGQHEAARALNLKRSTTFFKVILPQSLLVAIGPLGNELILMIKASAIASLVTIYDLMGVTKLAFSRSFDFQIYLWAAVLYLVIVELVRRLLKHLEARLGRHLN Pseudomonas putida KT2440 Putida PP_3597 PP_3597 L-lysine and D-lysine ABC transporter, ATPase component Specifically important for utilization of L-lysine and D-lysine. Amino-acid ABC transporter, ATP-binding protein MTAPLSLATLAPEPDPRPVLIRIEGLNKHYGAFHVLRDIDLQVREGERIVLCGPSGSGKSTLIRCINRLEVAQQGSIQVDGIDLAATTREAAQVRSDIGMVFQHFNLFPHMSVLDNCLLAPTSVRGLSRKDAEERARMYLSKVGIESQAHKYPSQLSGGQQQRVAIARALCMKPRIMLFDEPTSALDPEMVAEVLDVLVQLAGTGMTMLCVTHEMGFARQVAERVLFLEGGQIIEDSPPQVFFNQPRTERAKAFLAQILH Azospirillum brasilense Sp245 azobra AZOBR_RS00190 AZOBR_RS00190 L-glutamate dehydrogenase (NAD+) (EC 1.4.1.2) Very important for utilization of L-proline and L-glutamine, which are catabolized via glutamate. Also important for utilization of aspartate or leucine as nitrogen sources, which might indicate transamination to form glutamate. NAD-glutamate dehydrogenase MALRAEQLKDELTEEVVRQVRERLGRSRAAPAERFVRQFYDNVPPDDIIQAPAEQLYGAALAMWQWGQQREATDRAKVRVYNPRVEEHGWQSHRTVVEIVNDDMPFLVDSVTAELNRQGLTVHLVIHPVVRVKRDADGQLAELYEPAAAPTDAAPESFMHVEVGAVTGAAALDQAREGLERVLADVRAAVADWRAMRQQVRAAIVEADCARAAVPAIIPDDEVDEAKAFLSWADDDHFTFLGYREYRFESGADGADSSLGLVAGSGLGILRDDSVTVFDGLRNYATLPPDVRDFLRNPRVLMVTKGNRPSPVHRAVPMDAFLIKRFDAEGRIIGERLVAGLFTSVAYNRSPREIPYLRRKVAEVMELAGFDPQGHDGKALLHILETYPRDELFQIQVPELLDIAVGILHLQERQRLALFVRKDPFERFASCLVYVPRDRYDTTLRRRIQSILEAAYDGTCTGFTTQLTESVLARLHFIIRTEPGRVPTVDATDLEARLVQASRGWDDHLRDALVEAHGEEQGRTLFRRYADAFPTAYREEFNAEAAVFDIERIEKATAQGTLGINLYRPLEAEGDELHVKIYHEGRPVPLSDVLPMLEHMDLKVITEAPFEIAIAGHAAPVWIHDFTARSQNGLPIDCAMVKEKFQDAFAAVWDGRMEDDGFNRLVLRAGLTAREVTVLRAYAKYLRQARIPYGQDVVESTLAGHPAIARKLVALFHSRFDPARRSQNDPGLAAEIERALDGVKNLDEDRILRRFLNLLCNTLRTNAYQNGADGRPKTYLSFKIDSRNIDDLPLPRPMVEVFVYSPRMEGVHLRGGKVARGGIRWSDRREDFRTEILGLMKAQMVKNTVIVPVGSKGGFVVKRPPPPSAGREAQLAEGIECYKTLMRGLLDITDNLDAQGAVVPPPEVVRHDGDDPYLVVAADKGTATFSDIANSVSVDHGFWLGDAFASGGSAGYDHKKMGITARGAWESVKRHFRELGHDTQTQDFTVVGVGDMSGDVFGNGMLLSKHIRLLAAFDHRHIFIDPDPDAARSWEERQRLFDLPRSSWADYDASLLSAGGRVFDRSAKSLELTPEIRQRFGIAKDHVTPLELMQTLLKAEVDLLWFGGIGTYLKAAEETNAEVGDKANDALRIDGRDVRAKVIGEGANLGVTQRGRIEAAQHGVRLNTDAIDNSAGVDTSDHEVNIKILLNDVVVRGDMTLKQRDQLLAAMTDEVAGLVLADNYLQSQALTVARAQGPDALEAQARLIRSLEKAGRLNRAIEYLPDEEELSARMANREGLTRPELAVLLAYAKITLYDDLLASDLPDDPFMADDLTRYFPKPLRKAHAEAVGRHRLRREIIATSVTNSLVNRTGPTFVKEMMEKTGMGPADVARAYTIVRDAFGLRSLWTGIEDLDTVVPAALQTSMILETVRHMERAAAWFLASCQQPLDIARETEAFRPGIETLLAGLDNVLDAEETARLTARVASYQEQGVPAELARRMAALPVLAAAPDLVRIAGRTGRGVADVAAVYFMLGRRFGLEWLRDKAAAAKAENHWQKQAVAALVDDLFAHQTALTTRVLEAVDQLPAEAPVEAWIAHRRPVVERVEQLLSELRTQPNVDLSMLAVANRQLRGLTAG Shewanella amazonensis SB2B SB2B 6937149 Sama_1319 symporter for L-glutamate, L-glutamine, and L-aspartate Specifically important for utilization of L-glutamate or L-glutamine as carbon sources or L-aspartate as a nitrogen source. Glutamine is probably cleaved by a cytoplasmic glutaminase (Sama_2487), so glutamine is probably a substrate. sodium:dicarboxylate symporter (RefSeq) MAAAQSSKIGLTGKILIGMGAGILIGLLLRNFFGGSEWVQDYITEGFFHVIGTIFINSLKMLVVPLVFISLVCGTCSLSEPSKLGRLGGKTLAFYLFTTAIALVVAISAAVLVQPGNASLASESMQYSAKEAPSLADVLINIVPSNPMKALSEGNMLQIIIFAVIFGFAISHIGERGRRVAALFDDLNEVIMRVVTLIMQLAPYGVFALMGKLALTLGMETLESVIKYFMLVLVVLLFHGFVVYPTLLKLFSGLSPLMFIRKMRDVQLFAFSTASSNATLPVTMEASEHRLGADNKVASFTLPLGATINMDGTAIMQGVATVFIAQVFGIDLTITDYAMVVMTATLASIGTAGVPGVGLVMLAMVLNQVGLPVEGIALILGVDRMLDMVRTAVNVTGDTVATVVIAKSEGALNEAVFNDPKAGKTAGSFDAEVHRGE Pseudomonas stutzeri RCH2 psRCH2 GFF4002 Psest_4075 symporter for L-glutamate, L-glutamine, and L-proline Specifically important for utilization of L-glutamate, L-glutamine, or L-proline as carbon soruces. Glutamine is probably cleaved by a cytoplasmic glutaminaes (Psest_4081), so glutamine is probably a substrate. Mildly detrimental during tyrosine utilization, so tyrosine might also be a substrate. Na+/H+-dicarboxylate symporters MTQSTTLSAPLRLLVRLPLWQQILIGLALGVAAGMAFGADAQLLAPIGTLFLNAIKMLIVPLVFVSLVAGITSMQDSAKLGRISLKTIAIYLVTTAFAVSIGLLFGALFSPGEGMNMVASGNEQAKQAPSLVSILVGLVPANPVTAFAEGNILQIIVFAIALGVSINLIGERGAPAVRLFDALAETFYKLTDLVMRVAPIGVFALTAGVVGSHGAEVLLPLAGVIGVIYLASIAHVLLVYGGLLGLLARLNPLRFFQGIAPALAVAFSTSSSSGTLPVSIECARKNLGVSEGVAGFVLPVGATINMDGTAIYQGVLALFIAQAFGIDLSAGQYAMIILTATLASIGTAGIPGAGLIMLGLVLTAAGLPLEGVALIAGIDRILDMARTTVNVAGDLMTTTLVGRSEQELDRAIYDSSNKE Shewanella oneidensis MR-1 MR1 200848 SO1683 3-hydroxy-2-methylbutyryl-CoA dehydrogenase IvdG (EC:1.1.1.178) Important for utilization of L-isoleucine as a carbon or nitrogen source. SO1683 is expected to be the 3-hydroxy-2-methylbutyryl-CoA dehydrogenase for isoleucine degradation (PMC2612455), and this is confirmed by its mutants' phenotype. (Also see data from an independent set of transposon mutants in PMC3219624.) Mutants in SO1683 have many other phenotypes which are not explained. 3-oxoacyl-(acyl-carrier-protein) reductase, putative (NCBI ptt file) MDLKDKVVVITGGAGGLGLAMAHNFAQAGAKLALIDVDQDKLERACADLGSSTEVQGYALDITDEEDVVAGFAYILEDFGKINVLVNNAGILRDGMLVKAKDGKVTDRMSFDQFQSVINVNLTGTFLCGREAAAAMIESGQAGVIVNISSLAKAGNVGQSNYAASKAGVAAMSVGWAKELARYNIRSAAVAPGVIATEMTAAMKPEALERLEKLVPVGRLGHAEEIASTVRFIIENDYVNGRVFEVDGGIRL Azospirillum brasilense Sp245 azobra AZOBR_RS08240 AZOBR_RS08240 L-proline and D-alanine ABC transporter, permease component 2 Specifically important for utilization of L-proline and D-alanine. ABC transporter permease MTAISMSSPRAIAWPSILKEAAMTAFVALLLTIPLVGLRTVDRPTGLGLETRWNEVAAAVGLVFLGRLGLCLIREGHAVTVLVLAAAATAAGFFIAMPTEALRVILIAGGAVIAIRAVLAIRTGRSKLSQAERDKRMDHIAAQVQHASRWLGPIAVVVALAFPFTPLADRQLLDIGILLLTYIMLGWGLNIVVGLAGLLDLGYVAFYAVGAYSYALLAHYFGFSFWVCLPLAGFLAAMSGVLLGFPVLRLRGDYFAIVTLGFGEIIRIILINWYQFTGGPNGISGIPRPSFFGIADFTRTPAEGTAAFHEMFGLEFSPLHRIIFLYYLILVLALVVNLFTMRVRKLPLGRAWEALREDDIACASLGINRTNMKLAAFAIAAMFGGFAGSFFATRQGFISPESFTFIESAIILAIVVLGGMGSQIGVVVAAFLVIGLPEAFRELADYRMLAFGMGMVLIMLWRPRGLLAHRDPTILLHGRPKGGAGGPAAGSAAAGGQGIAGGSAK Azospirillum brasilense Sp245 azobra AZOBR_RS08245 AZOBR_RS08245 L-proline and D-alanine ABC transporter, ATPase component 1 Specifically important for utilization of L-proline and D-alanine. branched-chain amino acid ABC transporter ATP-binding protein MTTQSMTTTPLLTVEHLTMRFGGLVAVNDVSFSANNGEITAIIGPNGAGKTTLFNCITGFYTPTVGRLTLRHADGKEFLLERMPGYRISQKASVARTFQNIRLFGGMSVLENLIVAQHNKLIRASGFSIAGLLGLPSYTRTEREAVDLAKYWLDRVRLLEFADWEAGNLPYGAQRRLEIARAMCTEPVMLCLDEPAAGLNPRESGELADLLTYIRDEHKIGVLLIEHDMSVVMTISDHVVVLDYGRKISDGDPAFVKNDPAVIRAYLGEEEDEELPPEIKADLPEVAKRAEEGA Azospirillum brasilense Sp245 azobra AZOBR_RS08250 AZOBR_RS08250 L-proline and D-alanine ABC transporter, ATPase component 2 Specifically important for utilization of L-proline and D-alanine. amino acid ABC transporter ATPase MLKVSGVHTFYGAIEALKGVDIEIGAGEIVSLIGANGAGKSTLLMTICGSPRARMGRITFEGQDITQMPTYELVRLGIAQSPEGRRIFPRMSVLENLQMGSITAKPGSFANELERVLTLFPRLKERISQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPLVVKQIFQAVKDINREQKMTVFMVEQNAFHALKLAHRGYVMVNGKVTMSGTGAELLANEEVRSAYLEGGH Azospirillum brasilense Sp245 azobra AZOBR_RS08260 AZOBR_RS08260 L-proline and D-alanine ABC transporter, substrate-binding component Specifically important for utilization of L-proline and D-alanine. ABC transporter MNYKLSLLVAVAATAMTASVAKADIAVATAGPITGQYATFGEQMKKGIEQAVADINAAGGVLGQKLKLEVGDDACDPKQAVAVANQLAKAGVKFVAGHFCSGSSIPASQVYAEEGVLQISPASTNPKLTEQNLKNVFRVCGRDDQQGQIAGKYLLENYKGKNVAILHDKSAYGKGLADETQKALNAGGQKEKIYEAYTAGEKDYSALVSKLKQEAVDVVYVGGYHTEAGLLARQMKDQGLNAPIVSGDALVTNEYWAITGPAGENTMMTFGPDPREMPEAKEAVEKFRKAGYEPEGYTLYTYAALQIWAEAAKQANSTDSAKIADVLRKNSYNTVIGKIGFDAKGDVTSPAYVWYRWNNGQYAQVK Shewanella sp. ANA-3 ANA3 7023819 Shewana3_1039 nucleoside permease (cytidine, inosine, uridine, or thymidine) Specifically important for utilization of cytidine, inosine, uridine, and thymidine. Na+ dependent nucleoside transporter (RefSeq) MNILMSLVGVVVLLAIGFLLSNNKKAINLRTVGGALAIQAAFGGFVLYVPVGKDILKSVSDAVSSVIGYAQNGIGFLFGDLANFKLGFIFAVNVLPVIVFFSSLIAVLYYLGIMQWIIRIIGGGLQKALGTSRTESMSATANIFVGQTEAPLVVRPFIPTMTQSELFAIMVGGLASIAGSVLAGYAQMGVPIEYLVAASFMAAPGGLLMAKLMHPETEVAKNDMDELPEDPDKPANVLDAAAAGASSGMHLALNVGAMLLAFVGLIAMINGIIGGVGGWFGVEGLTLELILGYIFMPLAFLIGVPWNEALVAGSFIGQKIVVNEFVAYLNFAPYLKDIADGGMIVADTGLAMTDRTKAIISFALCGFANLSSIAILLGGLGAMAPNRRHDLAKLGIRAVIAGSLANLMSATIAGLFLAI Caulobacter crescentus NA1000 Caulo CCNA_01705 CCNA_01705 periplasmic 3'-ketolactose hydrolase Specifically important for the utilization of lactose, as part of the 3-ketoglycoside pathway. (3'-ketolactose is formed by LacABC, which are encoded on either side.) Belongs to the DUF1080 family, which includes the 3-ketotrehalose hydrolase BT2157. hypothetical protein MRGRRAMVWMKPSRGWASFGLVTGLALGLAGASHAEEVQAGPWRSLFDGKTLNGWTAKVARHPVGENYRQTFVADQGVIRVSYAGYDRFDNQFGHLFHKTPFSAYRLRFSYRFLTEGGLPDTPGWARANSGIMFHSQSAESMTVDQPFPVSIEFQLLGKDGDKPRPTGAVCTPGITITIDGAKVKEHCTPPANGPTIANGTWVQAELEVLPSGEITQKINGVVVHRYAGAALDPDDTVAGGAKPYILARGAQPVTGGYIALQSEGAPLEFKDIEIQELTPR Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS24655 CA265_RS24655 maltose phosphorylase (EC 2.4.1.8) Specifically important for utilizing D-maltose. family 65 glycosyl hydrolase MKNYIKADEWNIIEEGFDPHLNKISESIFSLGNGRMGQRANFEETYTGETLPGNYVAGVYYPDKTRVGWWKNGYPEYFAKVLNAANWIGIEVKLDGEILDLATAEVSDFKRVLNMHAGYLERTFTAKLKSGKTLKVKSTRFCSIADDEVGAIRYSITPLNFDGRLTLMPFIDGDVKNQDSNYDEKFWDKVADEISGTEAYIKLRTKKTEFEVCTGSNIELYKNAEKLAINPEAVRKEKFVGQTFSLEVKANEEISLVKIAANLSSENYPKESLLKETKSIIAKASAKGFDTLLKEQTEAWASKWEESDIIIEGDVSAQQAIRFNIFQLFQTYTGKDDRLNIGPKGFTGEKYGGSTYWDTEAYCVPFYLATAPQEVSKNLLVYRHKQLGKAIENAAKLGFKDGAALYPMVTMNGEECHNEWEITFEEIHRNGAIAFAIFNYIRYTGDESYLSDFGLEVLIGIARFWKQRVNWSNDKQQYVMLGVTGPNEYENNVNNNWYTNILATWCMKYATEAAEIVKTQQPEKYNSLLKSLNFDQKEFADWADIIEKMYYPQDEKLGIFLQQDGYLDKEQTLVKDLPASERPINQKWSWDRILRSCFIKQADVLQGLYFFEEDYDLDTLKRNFDFYEPRTVHESSLSPCVHSILAAKLNDEARAYEFYLRTARLDLDDYNNDTEDGLHITSMAGTWMSVVEGFAGMRVREGKLQFNPFLPGKWKSFSFTIGFRGATLKINITESGISIKNNAAVDLEIGIRNQLYKLAGNTEIEVNNAELV Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS22975 CA265_RS22975 periplasmic 3-ketotrehalose hydrolase (DUF1080) Specifically important in carbon source D-Trehalose dihydrate. Also important for utilization of maltitol, so it's probably active on other substrates as well. DUF1080 proteins are 3-ketoglycoside hydrolases, part of an oxidative pathway for utilization of disaccharides (see PMC8121099). This protein has a signal peptide so is probably periplasmic. hypothetical protein MNKYTLLFIPALFAGQAMAQDKKPDPAKDPKTTEVWEPVPKVVTPGKLPQDAPSDATILFGGRNLDAWHSVKDPSKPAEWTIDDGFFTVKKGTGNIETNKKFTDYQLHMEWKIPENISGEGQARGNSGVFLASTGGGDNGYEIQIMDAYNNKTYVNGQTGSVYKQAIPLANANKKPGEWQYYDIIWNAPRFNEDGTVQKPASVTVFLNGVLLQNGFVLKGETRYIGAPEYKKHGPSSIKLQDHGDPSPAISYRNIWVREL Pseudomonas putida KT2440 Putida PP_1170 PP_1170 D-glucaro-1,5-lactonase UxuL Specifically important for utilization of D-glucuronate. Glucuronate appears to be oxidized by an oxidative pathway via uronate dehydrogenase (PP_1171). PP_1170 is 72% identical to PSPTO_1052 or UxuL, which a glucaro-1,5-lactonase and a galactaro-1,5-lactonase (see PMC6304669). Gluconolactonase MNCELIVDARNGTGESPVWHPGEQALYWVDIPARQLHRWQAADGKHQCWQGDEMLACIARSGQGWVAGMESGIFQLQAKADGSLDSRLLSNVQHAQAGMRFNDGRCDRQGRFWAGTMLLDMQQGAHVGALYRHDGEGHLHLQQDGMIVPNGLAFSPDGKRMYLSDSHPNVQKVWAFDYDTDSGTPHGKHLFVDMRNYPGRPDGAAIDQDGCYWICGNDAGQIHRFTPEGRLDRSLSVPVKKPAMCAFGGASLDILYVTSIRPTGIDLSDQPLAGGVFALDPGTKGLEEPAYRG Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS32055 RR42_RS32055 3-carboxymuconate cycloisomerase PcaB (EC 5.5.1.2) Specifically important for 4-hydroxybenzoate utilization. 3-carboxy-cis,cis-muconate cycloisomerase MFGSAATLAAFSDTATVQRMLDFEAALARAEASCGVIPADAAEAIAATCRAGEIDFDALAAAAVAGGNLAIPLVRQLTARVAARDAQAARYVHWGATSQDAIDTGMVLQLREALQAVDADLKALGHACAALAAQHRDTPMVARTWLQHALPTTFGLKAAGWLDALRRDLRRLDAARAQAATLQFGGAAGTLASLGAAAPAVATALGSALSLAVAPTPWHAYRDRMVEVATTLGMLTGSLGKIARDVSLMMQTEVAEVAEPTGPGRGGSSTMPHKRNPVGCAAVLTAAVRVPPLVATMLAGMVQEHERALGGWQAEWDTLPQIVTLAAGALRQMLEVVGGLQVDAARMRANLGVTHGLILAEAAMLELGGKIGRLPAHHLVEGACRRAVAEGTTLRQALGATLAEDAAHAGLMDAAALDRVCDPANYAGQAAGFVDAVLAAWR Marinobacter adhaerens HP15 Marino GFF3088 HP15_3031 L-arginine ABC transporter, periplasmic substrate-binding component ArtJ/HisJ/ArtI/AotJ/ArgT Specifically important for utilization of arginine as a nitrogen source. extracellular solute-binding protein, family 3 MKKMIFAASCALALIAGGAQAQERDLRIAFDVPYEPFEYKDENGELTGFEVELAEAMCEEMNANCEFVIQAWDGMIPGLLARKFDLIMSSMSITPERAERVLFSEPYYNTPGGWFGPESFNTDVTDMSAMEGKTVGVQRGTTMDTYVTENMGGIVTIKRYTTADDMVLDLEGQRLDVVFVDYPVGEQTVLTKEGFKEVGEAVKLGEGVGVAMRQRDTDLAEEVNAALRTLKEDGTYDTIMQKYFAYDIKM Shewanella amazonensis SB2B SB2B 6938533 Sama_2636 gamma-aminobutyrate transaminase (EC 2.6.1.19) Specifically improtant for putrescine utilization 4-aminobutyrate aminotransferase (RefSeq) MSLTNDSLMVRRRAAVAGGVGQIHPVFTERAENATVWDVEGREYIDFAGGIAVLNTGHLHPKVKAAVAEQLEKFSHTCFMVLGYESYVAVCEKLNQLVPGDFAKKSALFTSGSEAVENAIKVARAYTKRAGVIAFTSGYHGRTMAALALTGKVAPYSKGMGLMQANVFRAEFPCALHGVSEDDAMASIERIFKNDAEPSDIAAIILEPVQGEGGFYAATPGFMKRLRELCDREGIMLIADEVQTGAGRTGTFFAMEQMGVAADITTFAKSIAGGFPLSGITGRAEVMDAIGPGGLGGTYGGSPLACAAALAVIEVFEEEKLLERSNAIGQTIKSAIGELASRYPQIAEVRGLGSMIAIELMENGKPAPEYCPQVLTEARNRGLILLSCGTYGNVLRILVPITAPDEQIQRGLEIMAECFEAVLGK Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS03990 RR42_RS03990 aspartate:proton symporter Glt Specifically important for asparagine utilization. Asparagine is probably cleaved in the periplasm (by RR42_RS12610 or RR42_RS26140) and RR42_RS03990 is 60% identical to aspartate transporter AO356_01905 from Pseudomonas fluorescens FW300-N2C3 C4-dicarboxylate ABC transporter MKLNRLPTLIFIAMLLGVLAGTAAHHYAPDPAAAKSIADHLSILTDVFLRMIKMIIGPLVFATLVSGIASMGDGKAVGRIGMKAMAWFIAASITSLLLGLLMANLLRPGDGMNLALPAADAASNLKTGALNLREFIAHMFPKSFVEAMATNEILQIVVFSLFFGFALGTLKDGIGKPVLAGIEGLSHVMLKITNYVMAFAPVGVFGAVAAVITAEGLGVLVVYAKLLGAVYLSLALLWVALIAGGYFFLGRDVFRLLKMVRAPLMIGFATASSESAYPKVIEQLGRFGVKERITGFVLPLGYSFNLDGSIMYTSFAALFVAQVYGIHLSLSQQVTMLLVLLVTSKGIAGVPRASLVVVAAVLPMFGLPEAGILLVLGIDHVLDMGRTVTNVLGNAIATTVVAKSEGAIGAPVPEEADDPAADGNRGLTPVQVLAGK Burkholderia phytofirmans PsJN BFirm BPHYT_RS22245 BPHYT_RS22245 D-alanine transporter MctP Specifically important for utilization of D-alanine as a carbon source. Also has phenotypes on pyruvate and D-alanine, which might also be substrates. Also important for utilization of dAMP and DNA, which is not explained. sodium:solute symporter MSDVNPVNPVAMTVFIAFFVLVTVIGFFAARWKRGDLTQLHEWGLGGRQFGTVISWFLVGGDFYTAYTVIAVPALVYSVGAYGFFALPYTIIVYPFVFAVMPKLWKIAHAKNHITAADYVQGEYGGKWFPAAVAITGIVATMPYIALQLVGMQVVIKGLGVTGEMPLIVAFVILALYTYASGLRAPAMIAFVKDIMIYIVVIAAVWLIPAKLGGYAHVFDAADTYFKAKGGATGIILKPTQFTAYASLALGSALAAFMYPHTMTAVLSSSSANTVRKNAIFLPAYTLLLGLIALLGYMAIAAGVHVKSASDMVPALFNTLFPSWFVGFAAAAIAISALVPAAIMSIGAANLFTRNLWRPLVSPNISPEGEASTAKIVSLVVKFGALLFIVFLPTQYAIDLQLLGGVWILQIFPAIVFSLYTRRLNTPGLFLGWLAGIVLGTGLAISQGLKPVFALHLGDAVYPVYIGLIALTVNIVVSFVVSVLSPRRVVAAA Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_1918 N515DRAFT_1918 fructose porter FruP Specifically important for growth on fructose. MFS transporter, FHS family, L-fucose permease MAFAAPPAPSKTSLPGAARERYTDYPMAMGVLTSIFFMWGFLTCLNDILIPHLKAVFKLNYAEAMLVQFTFFGAYFLMSLPAGLLVARLGYKKGIVAGLAVAGVGAAGFWPAAAMHFYPAFLGALFVLATGITVLQVAANAYVALLGPEKSASSRLTLAQALNSLGTFLAPKFGGLLILSAAVLSAEQIAKLSPAEQVAYRVQEAQTVQGPYLGLAIVLFLLAVFVYLFRLPALTEKTEQASVKQHSLVSPLRHPHVLFGVLAIFFYVGGEVAIGSFLVNYLSMPDIGNMSEQAAANWVAYYWLGAMIGRFIGSALLAKLSPRKLLAIFAAINMALVLTTMMTKGTVAMYSVVSIGLFNSIMFPTIFSLGIERMGPMTGEASSLLIMAIVGGAIVPFVQGLFADHIGVQHAFFLPLLCYAYIVFYGLYGSRIKSDTPVAATH Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS05235 HSERO_RS05235 L-fuconate dehydratase (EC 4.2.1.68) Specifically important for fucose utilization. fuconate dehydratase MTKITALRVLDVRFPTSQSLDGSDAMNPDPDYSAAYVILDTDNAALKGHGLTFTIGRGNEICCAAIRAMEHLVVGLELEWIAADMGRFWRHVTSDSQLRWIGPDKGAIHLATGAVVNAAWDLWAKAEGKPVWKLVADMSPEELVRTIDFRYITDCITPDEALALLREKEAGKAERLRVLEQEGYPCYTTSAGWLGYEDAKLRRLCQEAIDQGFNHVKLKVGRDLADDKRRVTIAREVLGPERKLMIDANQVWEVHQAIDWVNQLAFAQPWFIEEPTSPDDVEGHRKIREGIGAVKVATGEMCQNRVLFKQFIMRDAIDVVQIDSCRLGGVNEILAVMLMAAKYGKVVCPHAGGVGLCEYVQHLSMIDYLCISGSKEGRVTEYVDHLHEHFVDPCVVKNAAYMPPSRPGFSIEMKPQSLEQYRFRG Bacteroides thetaiotaomicron VPI-5482 Btheta 350803 BT1275 L-fuculose kinase fucK (EC 2.7.1.51); D-ribulose kinase (EC 2.7.1.47) Specifically important for L-fucose utilization, along with fucose isomerase BT1273 and fuculose-phosphate aldolase BT1274. Also important for D-arabinose utilization, so it is probably a D-ribulokinase as well. L-fuculose kinase (NCBI ptt file) MKDTTRNTYLAVDFGGGSGRVIAGSLLQGKLELEEIHRFTNRQVKLGNHVYWDFPALFEDMKTGLKLAAQKGYHVKGIGIDTWGVDFGLIDKKGNLLGNPVCYRDARTDGMPDKVFQILDAQKHYACTGIQVMPINTLFQLYSMQQNQDVLLEVAQRLLFMPDLFSYYLTGVANNEYCIASTSELLDARQRNWSMDTIRALGLPEHLFGEIILPGTVRGTLKEEIGRETGLGPVDIIAVGSHDTASAVAAVPATEGQVAFLSSGTWSLLGVEVDEPILTEEARLAQFTNEGGVGGHIRFLQNITGLWILQRLMSEWKLRGEEQSYDTILPQAADAEIDTIIPVDDAEFMNPENMETALLNYCRNHSLKVPGNKAEMVKCVLQSLAFKYREAVAQLNRCLPSPIHRLNIIGGGSQNKLLNQLTANALGIPVYAGPVEATAMGNILTQAMAKGEISSLREIREVVSHSVTPQVYYPEK Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_1233 N515DRAFT_1233 2-dehydro-3-deoxygalactonokinase dgoK (EC 2.7.1.58) Specifically important for galactose utilization. 2-keto-3-deoxygalactonate kinase (EC 2.7.1.58) MSAGLIGLDWGSTHLRAYLYGADGHALESRALPHGIRQLPAGGFPEAFSSAVRDWPALPVLACGMVGSRNGWQEVPYLDTPTGVERLAQHLTRIAAPDGHALYLVPGLHDTHRPDVMRGEETQIAGVLAREPATTRLLLPGTHSKWVRLRDGIVTDFATVMTGELYGLLRQHSILGAALPEARDDADAFRRGVAAARGSGPAGALSLLFSARALMLDGVLDPAAVPDYLSGLLIGEELRMALAAGWADADDAIPMVGEGPLCDRYRRAADTFGLRLARAPDGTTADGLWRIAAAAGLVPAPATITS Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS05160 HSERO_RS05160 2-dehydro-3-deoxygalactonokinase dgoK (EC 2.7.1.58) Specifically important for galactose utilization. 2-dehydro-3-deoxygalactonokinase MNQNHHDCALIALDWGTSSLRCYRYDGSGQVVERRAHPWGIMNLPAVEHGDDAQAPYRAALEAACGDWIAAAPEAALIAAGMVGSKQGWREAAYLTVPLAPDGIGRKLTEVDTGLGRSLWIIPGLLQNSALPNVMRGEETQVIGALQQQRQSELLIGLPGTHSKWVRVVEGRIEHFDTFMTGEVYGALCGHTILGRTMHKPDVPDDAAFVRGARVAQGPQGQAGVLSNIFSSRTLGLTGELAPEAQPDYLSGLLIGHEIAALKSLYPAQQAPIVLIGDAGLCRRYRLALELYGLGPVSEADAATEAGLWILARHAGLVA Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_1229 N515DRAFT_1229 D-galactanolactonase Specifically important for galactose utilization. It is not certain whether the galactose dehydrogenase (N515DRAFT_1230) forms the 1,5-lactone or the 1,4-lactone. L-arabinonolactonase (EC 3.1.1.15) MNARVVHHPANTLGEGILWCEREQALYWTDIQAATLWRHRPADGATRSWEMPERLGCLALCEADGWLLLGLATRLAFFRPEDDLLLPLVSVEPDLPTRLNDGACDRQGRFVFGTLHEPAAGETRQPIGAFYRLNADLTLERLNLPGIGISNSVAFSPDGRTMYFCDSPSRVIQCCDYGDRCGEPRVFARVDDERGEPDGSAVDAQGCLWNAQWGLGRVVRYAPDGRVDRIVEVPATQPTRPAFGDSPLDTLYITSARDGLSSAALATQPLAGALFAADAGASGLPEPRFRGAPPGFGRSS Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_5129 D-galacturonate transporter ExuT Specifically important for D-galacturonate utilization. Hexuronate transporter MNLNEPINAQRIGQAVGNYRWTICALLFFATTVNYLDRQVLSLLAPDLSTQFGWSNSDYANIASVFQFVYAISMLFAGRVVDKIGTKTAYVVAICIWSTGAVMHAFAVPMGEGIGAVSSALGIAMIPVSIAGFMVSRAVLAIGEAGNFPIAIKATAEYFPKKERSFATGIFNSGANVGAILAPICVPLIASLWGWEAAFIVIGMLGFVWVGVWIALYEKPEQQKRLSAQELAYIRSDQVVPVVTRPVPGVADKKVSWFKLLTYRQTWAFAFGKFMTDGVWWFFLFWLPTYLSAQYGMKGQAIVMPLAVLYSMTMIGSIGGGWFPSYFMSRGDAPYDGRMKAMLVIAFFPLLVLLAQPLGYISFWVPVLLIGVGASAHQAWSCNIFTTVSDMFPQKSIASVVGIGGLAGGLGGVVMTKIGGWVIDHYKLIGDIHTGYMIMFAICALAYLVAWSVMKALVPRHKEITDL Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS19855 CA265_RS19855 D-galacturonate transporter ExuT Specifically important for D-galacturonate utilization. MFS transporter MNQPKTSKYRWTICLLLFLATTINYLDRQVLSLTWTDFIKPEFHWDNNDYGNITALFSIFYAISMLFAGRFVDKMDTKKGFLWAIGVWSVGACLHAFCGIATAGIINGNWFVGFEGAKDVIARVNDTGLIVSVSVTLFIFARFVLAVGEAGNFPAAIKATAEYFPKKDRAFATSIFNAGATVGALAAPITIPFIAKAYGWEMAFIIIGALGFVWMGLWIFVYNKPELHKRVSPEELAYIQQDVINDRKLADYVEETKEKVSFIDCFKYKQTWAFAFGKFMTDGVWWFFLFWTPAYLKSVYGMDSTQSALPLFVLYMITLLSIIGGWLPTYFVDKKGMNPYEGRMKAMLIFAFFPLLALAAQPLGHITYWIPVIIIGIAGAAHQAWSANIFSTVGDMFPKKAIATITGIGGMAGGLGSFIINKGSGLLFDYTGKNEIVFMGFKGEEAGYFIIFSICAVCYLIGWTVMKTLVPKYKVIELK Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS23010 HSERO_RS23010 D-galacturonate transporter ExuT Specifically important for D-galacturonate utilization. hexuronate transporter MVTLVTLALIVNYLARNTLSVAAPTMMKELDMSTQQYSYIVVAWQICYAVMQPVAGYILDAVGTKIGFGIFALAWSLVCAAAAFATGWQSLAFFRALLGITEAAGIPGGVKASTEWFPAKERSVAIGWFNIGSSIGALCAPPLVVWTILHGGWKMSFVVVGALGVIWFVLWMLFYKSPRDQKLLSPEERAYILEGQEKSPEKVQRESWTKIVRSRNFWSIAIPRFLSEPAWQTFNAWIPLYMATERHMNIKEIAMFAWLPFLAADIGCVLGGYLSPLFHKHLKVSLFTSRKLVMLVGSLSMIGPACVGFVDSPYVAIALLSIGGFAHQTLSGALYSITSDVFTKNQVATATGLTGMSGYLGATLFTLLFGILVTQIGYGPLFVLLAAFDLVAVAVVFAIARPRPEAIA Bacteroides thetaiotaomicron VPI-5482 Btheta 353631 BT4105 D-galacturonate transporter ExuT Specifically important for D-galacturonate utilization. Also important for utilization of galacturonate-containing polysaccharides polygalacturonate and rhamnogalacturonan from potato, and probably important for pectin utilization as well hexuronate transporter (NCBI ptt file) MTNYRWTICAMLFFATTVNYLDRQVLSLTWDEFIKPEFHWDESHYGTITSVFSIVYAICMLFAGRFVDWMGTKKGFLWAIGVWSAGACLHAVCGIVTEAQVGLHSAAELAGATGDVVVTIATVSMYCFLAARCILALGEAGNFPAAIKVTAEYFPKKDRAYATSIFNAGASIGALIAPLTIPILAKAFGWEMAFIVIGGLGFIWMGFWVFMYDAPSKSKHVNKAELEYIEQDQNEAGAGPKTEEKDEKKMRFWQCFSYKQTWAFVFGKFTTDGVWWFFLFWTPSYLNSQFGIKTSDPLGMGLIFTLYAITMLSIYGGKLPTIFINKTGMNPYAARMKAMLIFAFFPLVVLLAQPLGTFSPWFPVILIGIGGAAHQSWSANIFSTVGDMFPRTAIASITGIGGMAGGIGSMILQKVAGNLFVYASGTTMVDGKEVEMTKELLEQGAQFVHPAMTFMGFEGKPAGYFVIFCVCAVAYLIGWVIMKALVPKYKPIVLD Shewanella sp. ANA-3 ANA3 7025963 Shewana3_3111 transmembrane glucosamine N-acetyltransferase NagX Specifically important for glucosamine utilization. NagX proteins are distantly related to human HGSNAT (uniprot:Q68CP4), which is a transmembrane acetyl-CoA:alpha-glucosaminide N-acetyltransferase. hypothetical protein (RefSeq) MSTTAPESITNTGVNAQEAAAKKRQSKPRLMSLDALRGFDMFWILGGEALFGALLMLTGWAGWQWGDTQMHHSEWNGFRFYDLIFPLFIFLSGVALGLSPKRLDKLPMQERMPVYRHGIKRLFLLLLLGILYNHGWGTGAPADPEKVRYASVLGRIAFAWFFAALLVWHTSLRTQVLVALGILVAYGAVQLWLPFPGGQAGVLSPTESINAYVDSLLLPGVSYQGRTPDPEGVLSTLPAVVNALAGVFVGHFIVKSHPKGEWAKVGLLSVAGGVCLALGWLLGGVIPVNKELWTSSFVLVTSGWSMLLLALFYALVDVLKWQKLAFIFVVIGTNAIIIYLASSLVDWKYIAQSVFGGVIAVLPENAQPLGAVIGLLTVQWLVLYWMYRRNIFVRI Shewanella amazonensis SB2B SB2B 6936760 Sama_0947 transmembrane glucosamine N-acetyltransferase NagX Specifically important for glucosamine utilization. NagX proteins are distantly related to human HGSNAT (uniprot:Q68CP4), which is a transmembrane acetyl-CoA:alpha-glucosaminide N-acetyltransferase. hypothetical protein (RefSeq) MQATQTKAAKPRLMSLDALRGFDMFWILGGEKLFIALFALTGWSFWQLADAEMHHSEWHGFTFYDLIFPLFIFLSGVALGLSPKRLDKLAPAERNPIYRHAVKRLFLLLALGVLYNHGWGTGIPAHSDEVRYASVLGRIAFAWFFAALLVWHTSLRTQIATALAILFGYAAIQLWLPVPGGQAGVLTPSGSINAWVDTHFLPGITYQHRPYDPEGILSTLPAIVNALMGVFVGRFIVKPDARGDWAKAGILTGAGGLSLVLGWSLDSVLPVNKDLWTSSFVLVTTGWNLLFLALFYVLVDVLGAKRLAFPFVVIGVNSIIIYLASSLMNWEYLSKSLFGGVIHALPMPAQALAAAIGFLLVQWALLYWMYRKGIFIRI Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1106 Echvi_1106 transmembrane glucosamine N-acetyltransferase NagX Specifically important for glucosamine utilization. NagX proteins are distantly related to human HGSNAT (uniprot:Q68CP4), which is a transmembrane acetyl-CoA:alpha-glucosaminide N-acetyltransferase. Uncharacterized conserved protein MPKQRILALDVFRGITIFAMILVNNPGSWSHVYAPLLHAKWHGCTPTDLIFPFFLFIVGVAIELSLGGQLKKGTPKGFLLRKSLIRALKLIGLGLLLTAIPYFDLAHLRFPGVLQRIGLVYFISTVMYLYWSPKALVFSSGILLIGYWLCMTFIPVPGIGPANLEPGTNLAAWIDQQVLTGHMWSQTKTWDPEGLFSTLPAIVTCLLGVACGKILTGNSSHKARLTKWGIAGVTLVFGGLAWSLFFPLNKALWTSSFVLYTAGWAFLGLAACYWILDVKGWKKWSLPFVIYGMNAITVFFLSGVIAKLFGLIKVNWEGTRVSLKLFLQEALFNGWLAPKDASLCGAILMMIILFIPAYFMWKRNIIIKV Pseudomonas putida KT2440 Putida PP_1167 PP_1167 D-glucuronate / D-galacturonate TRAP transporter, large permease component Specifically important for utilization of D-glucuronate and D-galacturonate putative TRAP dicarboxylate transporter, DctM subunit MEAFILLGSFIVLILIGMPVAYALGLSALIGAWWIDIPLQAMMIQVASGVNKFSLLAIPFFVLAGAIMAEGGMSRRLVAFAGVLVGFVRGGLSLVNIMASTFFGAISGSSVADTASVGSVLIPEMERKGYPREFSTAVTVSGSVQALLTPPSHNSVLYSLAAGGTVSIASLFMAGIMPGLLLSAVMMGLCLIFAKKRNYPKGEVIPLREALKIAGEALWGLMAMVIILGGILSGVFTATESAAVAVVWSFFVTMFIYRDYKWRDLPKLMHRTVRTISIVMILIGFAASFGYVMTLMQIPSKITTAFLTLSDNRYVILMCINFMLMLLGTVMDMAPLILILTPILLPVITGIGVDPVHFGMIMLVNLGIGLITPPVGAVLFVGSAIGKVSIESTVKALMPFYLALFLVLMAVTYIPAISLWLPSVVL Pseudomonas putida KT2440 Putida PP_1169 PP_1169 D-glucuronate / D-galacturonate TRAP transporter, solute receptor component Specifically important for utilization of D-glucuronate and D-galacturonate TRAP dicarboxylate transporter, DctP subunit MTFKRKLLLAVLPFAFSVAMPASALDIKFAEIHPAGYPTVVAEQNMGKKLEDASNGEITFKMFAGGVLGSEKEVIEQAQIGAVQMTRVSLGIVGPVVPDVNVFNMPFVFRDHDHMRKIIDGEIGQEILDKITNSDFNLVALAWMDGGSRSIYTKKPVRSLEDLKGMKIRVQGNPLFIDMMNAMGGNGIAMDTGEIFSALQTGVIDGAENNPPTLLEHNHFQSAKYYTLTGHLILPEPVVMSKTTWNKLSPEQQALVKKVAREAQMEERALWDAKSAASEEKLKAAGVEFITVDKKPFYDATASVREKYGAQYADLMKRIDAVQ Pseudomonas putida KT2440 Putida PP_1168 PP_1168 D-glucuronate / D-galacturonate TRAP transporter, small permease component Specifically important for utilization of D-glucuronate and D-galacturonate putative TRAP dicarboxylate transporter, DctQ subunit MPNRPRQCGARRPAALVMPMKSLFLSVNDTLYRSCIWIAGLSILAMTLIIPWGIFARYVLGTGSSWPEPVSILLMVVFTFVGAAASYRAGAHMAVGMITDRLPPLQRQLVALLVQLLMIVVCVFMTYYGTRLCITTWNQSLASLPGVRVGMTYAPIPVGGVLTLVFVLEKLLLGDQSNRKVVRFDLVEENEGAA Burkholderia phytofirmans PsJN BFirm BPHYT_RS24000 BPHYT_RS24000 L-histidine ABC transporter, substrate-binding component Specifically important for histidine utilization. ABC transporter substrate-binding protein MKVKRTTAAKTLIGAVLGAAAIFAAPAQAKDWKTVTIALEGGYAPWNLTLPGGKLGGFEPELVANLCERIKLQCNLVAQDWDGMIPGLQAGKFDVLMDAISITPEREKIIAFSKPYAATPATFAVADAKVLPKAAPGAGVVKLSGDPKADQPTVDALRKQLKGKTIGIQSGTVYTKFINDGFKDIATIRVYKTSPERDLDLANGRIDASFDDVTYYAANIDKKETASIVMAGPKIGGPIWGPGEGLAFRKQDADLKAKFDTAISAALADGTVKKLSNKWFKTDVTP Burkholderia phytofirmans PsJN BFirm BPHYT_RS24005 BPHYT_RS24005 L-histidine ABC transporter, permease component 1 Specifically important for histidine utilization. ABC transporter permease MALIQMLGFGPEGWGGVLLLAALMTVALTLAALAVGAVFGALVAAAKLSRFRTLRVIGDIYTTVFRGVPELLVIYLFYFGGSTLVTSVGQLFGAEGFVGVPPFVVGALAVGMISGAYQAEVYRSAVLAVSRGELEAARSIGMPTLTMARRILIPQVLRFALPGIGNVWQLSLKDSALISVTGLAELLRTSQVAAGSTHQYFTFFVVGGALYLIMTSISNRVFNRAEAHVGRSFKRNFARN Burkholderia phytofirmans PsJN BFirm BPHYT_RS24010 BPHYT_RS24010 L-histidine ABC transporter, permease component 2 Specifically important for histidine utilization. ABC transporter permease MHFDFDFLFDTIKQLLAAVPTTLGLFFCSLILGGLLSLVIVTMRVSPHWLPNRFARAYILVFRGSPLLIQMFLVYYGMGQFGVIRESFLWPVLREPYMCAVLSLALCTAGYTAEIIRGGLMAVPVGQIEAGYSIGLSGFALLRRVIGPIALRQCLPAYSTEAVLLVKSTALASLVTVWEVTGVAQQIIQQTYRTTEVFICAALIYLFLNFVIVRLLGMLETRLSRHLRAARPAAVSRPVSATTEARRAAP Burkholderia phytofirmans PsJN BFirm BPHYT_RS24015 BPHYT_RS24015 L-histidine ABC transporter, ATPase component No fitness data for the gene, but the other components of the putative transporter are upstream (BPHYT_RS24000:BPHYT_RS24010) and are specifically important for histidine utilization. ATP-binding protein MNATAPVALSVKNIHKSFGDHHVLKGISLDAHQGDVISILGASGSGKSTFLRCLNLLETPDDGSVSLAGEELKMKRRGDGKLQPSDRRQVDRVRSQLGMVFQNFNLWSHMTVLENLIEGPMRVQKRSRAESVEEAEALLAKVGLAEKRGHYPAHLSGGQQQRVAIARALAMHPKVMLFDEPTSALDPELVGEVLRVMRSLAEEGRTMLVVTHEMGFARHVSNRVMFLHQGQVEADGTPDEVFVECKSDRFRQFVSSHQDRTTN Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS21295 RR42_RS21295 L-lactate dehydrogenase, LutA subunit Specifically important for utilization of L-lactate or D,L-lactate. (Also important on various nitrogen sources with lactate as the carbon source.) This is related to the LutABC system from Bacillus subtilis (PMC3347220, PMC2668416). oxidoreductase MKQRRYPPAPAQVYLFATCLVDMFVPQAGLDAVRLLEREGLTVHFPRGQSCCGQPAYSSGNPEQARAVALAQLDLFAEPWPVIVPSGSCAGMMRHHWPQLFAQDPVAGPKAALLAERVYELSEFLLHVLKVRFDVSGVAGQPPETVVLHTSCAARREMGTRDHGVALVDALPGVTRTEHQRESECCGFGGTFSLKHPDISGAMVQDKIASACATGCDRLVSADCGCLLNIGHAARHQGAPLPVEHIASFLWRRTGGAAKEQA Marinobacter adhaerens HP15 Marino GFF4148 HP15_4088 L-lactate dehydrogenase, LutA subunit Specifically important for utilization of L-lactate or D,L-lactate. This is related to the LutABC system from Bacillus subtilis (PMC3347220, PMC2668416). protein of unknown function, cysteine-rich region domain protein MSQLFYDAAPNATRVSPEREADRHYPEKPEAVTLFGTCVVDLFFPEAGLDTIRLLEREGVRVHFPQEQSCCGQPAWTSGYRDEAKAVARAQLDILDRSGLPVVVPSGSCAGMFRHHYPALFADEPDTLKRVEALAERTFELTEFLLKVCRVQLADRGAPSKIALHTSCSARREMNTHLHARELLQQLEGVERIDHDHESECCGFGGTFSVRMPEVSGAMVKDKTRSLIDSGAVEMVTADGGCLMNINGSLEKQKESFRGRHLASFLWERTNGDNAGEVA Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS21285 RR42_RS21285 L-lactate dehydrogenase, LutB subunit Specifically important for utilization of L-lactate or D,L-lactate. (Also important on various nitrogen sources with lactate as the carbon source.) This is related to the LutABC system from Bacillus subtilis (PMC3347220, PMC2668416). (Fe-S)-binding protein MHFVPAADFKARSRAALDDPKLRSSFRGAMDFLQAKRAVQFPDGDELEQLRDLGEAIRQHALSQLPDLLVQLEDKLTAAGVQVHWAETADEANAIVHGIAQARQASRVIKGKSMASEEIELNHYLAERGIDCIESDMGEYIVQLAGEKPSHIVMPAIHKTRGDIAELFEQHIPGTPYTEDVDELIQTGRRALRQEFVNADIGLSGVNFAAADTGTLWLVENEGNGRLSTTVPDVHIAIMGMEKVVARLEHIVPLASLLTRSATGQAITTYFNLISGPRRAGERDGPREVHLVLLDNGRSQAYADEQLRATLQCIRCGACMNHCPVYTRIGGHAYGTTYPGPIGKIISPHLLGLDATADLATASSLCGACGEVCPVRIPIPQLLIRLRTEANRDPSEQVAHPLRGQGTKFSRGEHLVWRFWSGAFAHPLAYRLFRWAATRLRVLTPKHQLGWTRHRAPLTPAPRSLSDLLRERGQAE Marinobacter adhaerens HP15 Marino GFF4149 HP15_4089 L-lactate dehydrogenase, LutB subunit Specifically important for utilization of L-lactate or D,L-lactate. This is related to the LutABC system from Bacillus subtilis (PMC3347220, PMC2668416). iron-sulfur cluster binding protein MSQRIPVTELTPDFRGRAEEALADGQLRNNFRVAMDSLMTKRANAFPDADEREGLRELGNRIKAGALSRLPDLLEQLEQKLTENGVKVHWAETVEEANSLVHGIIEARKGSQVVKGKSMVSEEMEMNDYLAERGVECLESDMGEYIVQLDNEKPSHIIMPAIHKNARQVSKLFHDKLGEPETEDVNQLIQIGRRTLRRKFMEADVGVSGVNFAIAETGTLLLVENEGNGRMSTTAPPVHIAVTGIEKVVPNLRDVVPLVSLLTRSALGQPITTYVNLISGPRKPDELDGPEEVHLVLLDNGRTGAFADAQMRQTLNCIRCGACMNHCPVYTRVGGHTYGEVYPGPIGKIITPHMAGLDKVPDHPSASSLCGACGEVCPVKIPIPELLQRLRQENVKNPEQPQQVKGGGAKYSRTERWIWRGWQMLNTRPALYRSFLWAATRFRALAPKKAGPWTENHSAPVPARRSLHDLAARHLDQNGGRPS Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS21290 RR42_RS21290 L-lactate dehydrogenase, LutC subunit Specifically important for utilization of L-lactate or D,L-lactate. (Also important on various nitrogen sources with lactate as the carbon source.) This is related to the LutABC system from Bacillus subtilis (PMC3347220, PMC2668416). lactate utilization protein C MSTLSARERMLGRLRAAAPATTADASQLDARIDAHYDARREAATPAELAQAMQAALGASHALAWCASAEAWPAQLAGKLAAAGVRRLLLDPAAEQGAALMRALPASVAPLSYARPIEAWKAELFDTVDAGFTVARSGIAATGTLVLAPDAQTPRTVSLVPPLHIALVYAETLHPDLHCAARAERWSAGMPTNLVLVSGPSKTSDIQQTLAYGAHGPRELWVIIVTGSAGTGAAQ Marinobacter adhaerens HP15 Marino GFF4150 HP15_4090 L-lactate dehydrogenase, LutC subunit Specifically important for utilization of L-lactate or D,L-lactate. This is related to the LutABC system from Bacillus subtilis (PMC3347220, PMC2668416). protein containing DUF162 MSARANILGKLRNSLAGTTPRPDEFDERLVTAPWRYAPEDRIERLRSLMEAVHTEVHPCRSDNWPELVAELLNKRNLTNLLCAPSKEHGRALQAYFEATEQKVELLAYDQPVEAWKEELFWSVEASLTGTLGGIAATGTLVLWPDCHEPRLMSLVPPVHIALLKASEIHDNLYDMMVAQDWAAGLPTNVLLVSGPSKTADIEQVLAYGAHGPRELIVLVLEDA Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS24665 CA265_RS24665 maltose transporter MalT Specifically important for maltose utilization. MFS transporter MSLKTIFENPKLTLVQIINMSVGFFGIQFGWDLQRANMGRIYENLGANPDQVPLLFLAAPLTGLLVQPIIGYLSDRTWHPKWGRRRPYFMIGAIVSSIALIFMPHSSVLWMAAGLLWILDVFGNIAMEPFRAFVTDKLPDSQVNRGFIMQSMMIGLGGSVASALPWIMNNVFHLTNTAEQGSIPENVKFSFYIGAFFFFAAVLWTVFTTKEYPPQDVDFKEKVKESNKGFGGGAREIFHALRNMPKRMQIVSLVQFFTWPGLFLMWFYYTTAVAVNVFGGKDAADPVYAQGADFGSLTLAYYSVITFLFALVLPKIADALGRKTTHALCLICGAIGLISVAWVHDKNMLYLCMTGVGIAWASILSMPYAMLSGSLPKDKIGIYMGIFNFFIVLPEIIASLGFGWLMRNVLNNDRLLAVQLGGGLMILAAVICYVFIREPKKTDEVLAAKLGVEENRSV Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS33495 RR42_RS33495 L-phenylalanine:H+ symporter AroP Specifically important for utliization of phenylalanine as the nitrogen source. aromatic amino acid transporter MVPNASDNTDATLKRGLKNRHIQLIALGGAIGTGLFLGIAQTIKMAGPSVLLGYAVAGIIAFFIMRQLGEMVVDEPVAGSFSHFANKYCGSFAGFMSGWNYWVLYILVSMAELSAVGIYVQYWWPHIPTWASALGFFLLINAINLTSVKSFGEMEFWFSIVKVLAIVGMIVFGGYLLASGTAGPQASVSNLWQHGGFFPNGISGLVMAMAVIMFSFGGLELVGITAAEADEPEKTIPKATNQVIYRILIFYVGALGVLLSLYPWEKVVTGGSPFVLIFHAMNSDIVATVLNAVVLTAALSVYNSGVYCNSRMLFGLAKQGNAPKALLKVNKRGIPLAALGVSALATAACVVINYFMPGEAFELLMGLVVSALIINWAMISIIHLKFRRDKRAAGQETRFKSLGYPLTNYVCLAFLAGILYVMYLTPGLRISVYLIPAWLAVLGLSYRLRQKQKRAEPALPERVSA Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_25255 AO353_25255 large subunit of pyruvate transporter (CstA) Specifically important for pyruvate utilization. Related to E. coli cstA, which is involved in pyruvate transport along with ybdD (PMID:29358499). Also similar to pyruvate transporter btsT (formerly yjiY). It is not certain if AO353_25255 functions with a ybdD-like component: the downstream gene, AO353_25260, is ybdD-like and has subtle defects during growth on pyruvate. carbon starvation protein A MTRLAKHLAWFAVAVLGAFALSVVALRRGEAINALWIVVAAVAIYLVAYRYYSLFIANKVMQLDPGRATPAVVNNDGLDYVPTNKHILFGHHFAAIAGAGPLVGPVLAAQMGYLPGTLWLIAGVVLAGAVQDFMVLFMSTRRNGRSLGDMVREEMGRVPGTIALFGCFLIMIIILAVLALIVVKALADSPWGMFTVMATIPIAMFMGVYMRYIRPGRIGEISVVGVLLLLGSIWLGGQIAADPVWAKAFSFTGIQITWMLIGYGFVAAVMPVWLILAPRDYLSTFLKIGTIMALAIGILITMPELKMPALTQFIDGTGPVWKGGLFPFLFITIACGAVSGFHALIASGTTPKLLASEGHARYIGYGGMLMESFVAIMAMVAASVIEPGVYFAMNSPAAIVGGDVVQVAQTVSSWGFMITPEALQAVAKDIGETTVLARAGGAPTLAVGIAQILHSVLPGENTMAFWYHFAILFEALFILTAVDAGTRAGRFMLQDLLGSFVPALKRTESWTANLIATAGCVAMWGYLLYQGVIDPLGGINTLWPLFGISNQMLAGIALMLSTVVLIKMKRQRYIWVTLLPAAWLLICTTTAGFIKLFDANPAIGFLSLAKKYSDALANGQILAPAKDITQMQHVIYNAYTNATLTALFLFVVFSILFYAIKVGISAWGSKERTDKESPFQAIPEA Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_6034 D-ribose ABC transporter, ATPase component RbsA Specifically important for ribose utilization. Also involved in utilization of ribonucleotides, which might be hydrolyzed before uptake. Ribose ABC transport system, ATP-binding protein RbsA (TC 3.A.1.2.1) MSVCAPNAVLSVSGIGKTYAQPVLTGIDLTLMRGEVLALTGENGAGKSTLSKIIGGLVAPTTGQMRFQGRDYRPGSRSQAEELGIRMVMQELNLLPTLSVAENLFLDNLPSHGGWISRKQLRKAAIEAMAQVGLDAIDPDTLVGELGIGHQQMVEIARNLIGDCHVLILDEPTAMLTAREVEMLFEQITRLQARGVSIIYISHRLEELARVAQRIAVLRDGNLVCVEPMANYNSEQLVTLMVGRELGEHIDMGPRKIGAPALTVKGLTRSDKVRDVSFEVRAGEIFGISGLIGAGRTELLRLIFGADTADSGTVALGASAQVVSIRSPADAVGHGIALITEDRKGEGLLLTQSISANIALGNMPVISSGGFVNNGDEMSLAQRQINAMRIRSSSPTQLVSELSGGNQQKVVIGRWLERDCTVMLFDEPTRGIDVGAKFDIYALLGELTRQGKALVVVSSDLRELMLICDRIGVLSAGRLIDTFERDSWTQDDLLAAAFAGYQKRDALFNEAAPRDLP Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_6035 D-ribose ABC transporter, substrate-binding component RbsB Specifically important for ribose utilization. Also involved in utilization of ribonucleotides, which might be hydrolyzed before uptake. Ribose ABC transport system, periplasmic ribose-binding protein RbsB (TC 3.A.1.2.1) MKLPFAGRLLAVAMLAAASAALPVSSAFAETPEKPKVALVMKSLANEFFLTMEDGAKAYQKDHSGDFELISNGIKDETDTAGQTRIVEQMILSKVNALVIAPADSKAMVPVIKKAVDAGITVINIDNQLDPAVVKSKNITVPFVGPDNRKGARLVGEYLAKQLKAGDEVGIIEGVSTTTNAQQRTAGFKDAMEAAQIKVVSLQSGDWEIDKGGKVASSMLSEYPNIKALLAGNDSMAVGAVSAVRAAGKAGKVQVVGYDNINAIKPMLKDGRVLATADQFAARQAVFGIETALKIIKGETVDSGANGVIETPVELVTK Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_6033 D-ribose ABC transporter, permease component RbsC No fitness data for this gene, but the other putative components are upstream (Pf1N1B4_6035:Pf1N1B4_6034) and are specifically important for ribose utilization. Ribose ABC transport system, permease protein RbsC (TC 3.A.1.2.1) MNTASLAGKRSGNFYGLGTYLGLAGALLAMVALFSVLSSHFLSYDTFSTLANQIPDLMVLAVGMTFVLIIGGIDLSVGSVLALAASAVSVAILGWGWSVLPAALLGMAVAALAGTITGSITVAWRIPSFIVSLGVLEMARGLAYQMTGSRTAYIGDAFAWLSNPIAFGISPSFIIALLIIFIAQAVLTRTVFGRYLIGIGTNEEAVRLAGINPKPYKILVFSLMGLLAGIAALFQISRLEAADPNAGSGLELQVIAAVVIGGTSLMGGRGSVISTFFGVLIISVLAAGLAQIGATEPTKRIITGAVIVVAVVLDTYRSQRASRRT Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_15980 AO353_15980 trehalose PTS system, EII-BC components TreB Specifically important for trehalose utilization. trehalose permease IIC protein MSHDYPTIASELLHSLGGADNLEQAAHCVTRLRLALKDPQRVDSATLNQIDLVKGSFFTGGLFQVVIGPGEVEKVYAALRQQTGLAASTIADVKQKGADKTNAMQRLVRVFSDVFMPILPALIIAGLLMGVNNLIGAKGMFIAGKTLLEAYPTLDGVWSLINLMANTSFVFLPALVGWSAAKRFGGSEILGIVLGLMLVHPDLLNAWNYGKAVAGLDGQSLPYFDIFGWFKIEKVGYQGQILPILMAAYVMSVIEKWLRARVPNAIQLLVVPITTIVVTGVLALAVIGPVTRHLGILITEGVVTLFDLAPMVGGAIFGLLYAPLVITGMHHMFLAVDLQLISTQGGTFIWPMIVMSNLAQGSAALGVFYMTRSARDKSMASTSAISAYFGITEPAMFGVNLRYKFPFYAALSGSALGCMFLSLNKVQASAIGVGGLPGFISIIPQFIPMFIVGMVIAMVVPFVLTCGMSMKIVRAGYRVA Pseudomonas simiae WCS417 WCS417 GFF4503 PS417_23050 trehalose PTS system, EII-BC components TreB Specifically important for trehalose utilization. trehalose permease IIC protein MSHDYSTIAREILENLGGSDNLEQAAHCVTRLRLALKDPSLVNSSALNQVDLVKGSFFTGGLFQVVIGPGEVEKVYAALREQTGLAAATIADVKKKGADKTNAMQRLVRVFSDVFMPILPALIIAGLLMGVNNLMGAQGMFIEGKTLLEAYPNLDGLWSLINLMANTSFVFLPALVGWSAAKRFGGSEILGIVLGLMLVHPDLLNAWNYGKAVAGLDGQSLPYFDIFGWFKIEKVGYQGQILPILMAAYVMSVIEKGLRARVPNAIQLLVVPITTIVVTGVLALAIIGPVTRHLGILITEGVVTLFDLAPMVGGAIFGLLYAPLVITGMHHMFLAVDLQLISTQGGTFIWPMIVMSNLAQGSAALAVFYTTRNARDKSMASTSAISAYFGITEPAMFGVNLRFKFPFYAALVGSALGSIFLALNKVQASAIGVGGLPGFISIVPQSIAVFVIGMVIAMVVPFVLTCGLSMKIVRPGYRVA Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1875 Echvi_1875 xylulokinase (EC 2.7.1.17) Specifically important for xylose utilization. Also important during utilization of some nitrogen sources (with glucose as the carbon source), which is not explained. Sugar (pentulose and hexulose) kinases MRKLFIGYDIGSSSVKATLLDGDTGKVVASDGQPKIEMPIDSPQKDWAEQDPQMWWKYVIETTQAIIQQGGVKPGELQAIGISYQMHGLVMVDKEQQVIRPSIIWCDSRAVETGNSAFEALGSEFCLSHLLNSPGNFTASKLKWVKDHEPANYEKIHKVMLPGDFIAMKLTGEIFTSESGLSEGVFWDFKENRVSQPLLDHYGIDREILATAIPSFAEGGKVNAAAAKVLGIAEGIPVTYRAGDQPNNAFSLNVLEAGELATTAGTSGTVYGVSSSPVYDPQSRVNTFLHVNHMADNPHYGVLLCVNGTGILNSWLKKMLGGESIDYEAMNKLAAEVPVGAEGLSFVPFGNGAERIMENKTVGAHLAGLNLLKHDKRHVLRAGQEGIVSALTFGFNIMKNMGLTLDTVKAGRANMFLSPLFREAFVNMNEVNLEFYDTDGSQGAARGAGVGAKHFASPQEAFNGLEKVASYVPEPKLVSAYKEVYQQWEERLRKIQ Burkholderia phytofirmans PsJN BFirm BPHYT_RS16915 BPHYT_RS16915 L-arabinono-1,4-lactonase; galactonolactonase specifically important for utilization of L-arabinose and D-galactose; it is not certain whether the galactose dehydrogenase (BPHYT_RS16920) forms the 1,5-lactone or the 1,4-lactone. gluconolaconase MSASGSPGTAALLLDTKCTLGEGATWCAQTGHFYWTDIEGARLWRYDPRDCSNMSWHMPERLATFALCADPRYLLLGLATHLAFFELATGETRRIIDVEAGLNTRVNDGRCDRQGRFVFGTKDEGAPLQAIGGFYRLGHDLSLERLPLPAPAISNSIAFSPDGATMYYCDSPTREIRACDYRADGSIANDRLFTRLTDATGEPDGSTVDRDGGLWNAQWGGRRVVRYGPDGMETERVDVPTAQPSCVALGGTQLDTLYITSARCDLDAAALANDPHAGGVFIATLGRRGLPEPVFQGAPA Cupriavidus basilensis FW507-4G11 Cup4G11 RR42_RS19540 RR42_RS19540 branched-chain alpha-ketoacid:ferredoxin oxidoreductase, fused (EC 1.2.7.7) Specifically important in nitrogen source L-Valine. This belongs to the indolepyruvate ferredoxin oxidoreductase family, and the mutant phenotype on valine suggests that 3-methyl-2-oxobutanoate (the product of valine transaminase) is a substrate indolepyruvate ferredoxin oxidoreductase MNAPLTPPVSDAIRRALANVSLEDKYTLERGRVYISGTQALVRLPMLQRERDRAAGLNTAGFISGYRGSPLGALDQSLWKAKQHLAAHDIVFQAGLNEDLAATSVWGSQQVNMYPDARFEGVFGMWYGKGPGVDRTSDVFKHANSAGSSRHGGVLVLAGDDHAAKSSTLAHQSEHIFKACGLPVLYPSNVQEYLDYGLHAWAMSRYSGLWVSMKCVTDVVESSASVELDPHRVEIVLPQDFILPPGGLNIRWPDPPLEQEARLLDYKWYAGLAYVRANKIDRIEIDSPHARFGIMTGGKAYLDTRQALANLGLDDETCARIGIRLYKVGCVWPLEAHGARAFAEGLQEILVVEEKRQIMEYALKEELYNWRDDVRPKVYGKFDEKDNAGGEWSIPQSNWLLPAHYELSPAIIARAIATRLDKFELPADVRARIAARIAVIEAKEKAMAVPRVAAERKPWFCSGCPHNTSTNVPEGSRALAGIGCHYMTVWMDRSTSTFSQMGGEGVAWIGQAPFAGDKHVFANLGDGTYFHSGLLAIRASIAAGVNITYKILYNDAVAMTGGQPIDGKLSVQDVANQVAAEGARKIVVVTDEPEKYSAAIKLPQGVEVHHRDELDRIQRELREVPGATILIYDQTCATEKRRRRKRGTYPDPAKRAFINDAVCEGCGDCSVKSNCLSVEPLETELGTKRQINQSSCNKDFSCVNGFCPSFVTAEGAQVKKPERHGVSMDNLPALPQPALPGLEHPYGVLVTGVGGTGVVTIGGLLGMAAHLENKGVTVLDMAGLAQKGGAVLSHVQIAAHPDQLHATRIAMGEADLVIGCDAIVSAIDDVISKTQVGRTRAIVNTAQTPTAEFIKNPKWQFPGLSAEQDVRNAVGEACDFINASGLAVALIGDAIFTNPLVLGYAWQKGWLPLSLDALVRAIELNGTAVEKNKAAFDWGRHMAHDPEHVLSLTGKLRNTAEGAEVVKLPTSSGALLEKLIAHRAEHLTAYQDAAYAQTFRDTVSRVRAAESALVGNGKPLPLTEAAARNLSKLMAYKDEYEVARLYTDPIFLDKLRNQFEGEPGRDYQLNFWLAPPLMAKRDEKGHLVKRRFGPSTMKLFGVLAKLKGLRGGVFDVFGKTAERRTERALIGEYRALLEELTRGLSAANHATAITLASLPDDIRGFGHVKDDNLAKVRTRWTALLEQFRHPETAQRVA Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS17015 HSERO_RS17015 sorbitol dehydrogenase (EC 1.1.1.14); xylitol dehydrogenase (EC 1.1.1.9) Specifically important for utilizing Xylitol. Automated validation from mutant phenotype: the predicted function (1.1.1.14, 1.1.1.9) was linked to the condition via a SEED subsystem. This annotation was also checked manually. sulfurtransferase MQALVLEATRELKLREIDLPQQMGAQDVRIRIHTVGICGSDLHYYTHGSIGPFKVEAPMVLGHEASGTVIEVGSAVSHLKVGDRVCMEPGIPRLDSPATLRGMYNLDPAVRFWATPPIHGCLTGSVVHPAAFTYRLPDNVSFAEGAIVEPLSIGLQAATKARMKPGDTAVVIGAGTIGAMTALAALAGGAARVILADVVAEKLAHFADNPAVITVDVTRETLTDVVRQATDGWGADVVFEASGHAGVYQTLLDLVCPGGCAVLVGMPPAPVALDVVAMQTKEVRLESVFRYANIFPRALALISSGMIDVKPFISRKFPFSQSIRAFEEAASGRPQDVKIQIEMEG Klebsiella michiganensis M5al Koxy BWI76_RS01820 BWI76_RS01820 maltose ABC transporter, permease component 2 (MalG) Specifically important for utilizing D-Maltose monohydrate. maltose transporter permease MAMVQPKSQKLRLFTTHLLLLVFIAAIMFPLLMVIAISLREGNFATGSLIPESISWEHWRLALGFSVEHADGRVTPPPFPVLLWLWNSIKVAGITAIGIVALSTTCAYAFARMRFPGKATLLKGMLIFQMFPAVLSLVALYALFDRLGQYVPFVGLNTHGGVIFAYMGGIALHVWTIKGYFETIDGSLEEAAALDGATPWQAFRLVLLPLSVPILAVVFILSFIAAITEVPVASLLLRDVNSYTLAVGMQQYLNPQNYLWGDFAAAAVLSAIPITVVFLLAQRWLVNGLTAGGVKG Klebsiella michiganensis M5al Koxy BWI76_RS01825 BWI76_RS01825 maltose ABC transporter, permease component 1 (MalF) Specifically important for utilizing D-Maltose monohydrate. maltose ABC transporter permease MalF MDVVKKKHWWQSPQLTWSVIGLLCLLVGYLVVLMYAQGEYLFAIMTLILSSVGLYIFSNRKAYAWRYVYPGLAGMGLFVLFPLICTIAIAFTNYSSTNQLTFERAQQVLMDRSFQAGKSYNFALYPAGDEWKLALTDGESGKNYLSDAFKFGGEQKLALKEADALPEGDRATLRVITQNRTALNQLTAVLPDESKVIMSSLRQFSGTQPLYALANDGTLTNNQSGVKYRPNAEVGFYQAINADGSWGSEKLSPGYTVTIGWDNFTRVFQDEGIQKPFFAIFVWTVVFSVLTVILTVAVGMVLACLVQWEALKGKAIYRVLLILPYAVPSFISILIFKGLFNQSFGEINMMLSALFGIKPAWFSDPTTARTMIIIVNTWLGYPYMMILCMGLLKAIPDDLYEASAMDGATPFQNFFKITLPLLIKPLTPLMIASFAFNFNNFVLIQLLTNGGPDRLGTTTPAGYTDLLVSYTYRIAFEGGGGQDFGLAAAIATLIFLLVGLLAIVNLKATRMKFD Klebsiella michiganensis M5al Koxy BWI76_RS01830 BWI76_RS01830 maltose ABC transporter, substrate-binding component MalE Specifically important for utilizing D-Maltose monohydrate. maltose ABC transporter substrate-binding protein MalE MKIKTGARILALSALTTMMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVSVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEISPDKAFQDKLYPFTWDAVRYNGKLIAYPVAVEALSLIYNKDLVPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKFENGKYDVKNVGVDSAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSKVNYGVTLLPTFKGNASKPFVGVLSAGINAASPNKELAKEFLENYLMTDQGLDEVNKDKPLGAVALKSFQEKLEKDPRIAATMANAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVEAALKDAQSRITK Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS06125 CA265_RS06125 galactokinase, -1-phosphate forming (EC 2.7.1.6) Specifically important for utilizing D-Galactose. Automated validation from mutant phenotype: the predicted function (2.7.1.6) was linked to the condition via a SEED subsystem. This annotation was also checked manually. galactokinase MNAQHLKNTFKKLFNAEPILVRSPGRINIIGEHTDYNGGFVMPAAIDKAIYVAISKRGDDEIHLFSESYQQFDISSINSLKKSENSWANYILGIADQLKERGYQLGGFNFYIDGDVPLGAGLSSSAAVECATGFALDQLFSLSVSRMDIALIAQKAEQTFAGVNCGIMDQFASVFGKKDQAIMLDCRSMKHIYIPLKLDGYKLLLLNTNVKHALADSAYNKRRSQCEQGVAWVKAHYPNVSTLRDVDLTMLETYVKPMDLEVYNKCRFVVEEIGRLLTAAEQLENGNLQALGKLMFETHEGLSKDYEVSCKELDFLVEAVKPLDYVLGARMMGGGFGGCTINIVKEEKIADLVEELSSKYLLQFGLKLDSYTVQTDNGTSLFN Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_03985 AO356_03985 L-phenylalanine transaminase (EC 2.6.1.57) Specifically important for utilizing L-Phenylalanine. aromatic amino acid aminotransferase MHFDAIGRVPGDPILGLMEAYGADSNPSKFDLGVGVYKDAQGLTPILESVKRAEQRLVERQTTKTYIGGHGDAAFGQLINELVLGADSPLISEKRAGATQTPGGTGALRLSADFIAQCLPGRGVWLSNPTWPIHETIFAVAGVKASHYPYVGADNRLDFEAMLATLNQAPKGDVVLLHACCHNPTGFDLSHEQWRQVLEVVRSRDLLPLIDFAYQGFGDGLEQDAWAVRLFAQALPEVLVTSSCSKNFGLYRDRTGALIVCAQDGEKLVDVRSQLANIARNLWSTPPDHGAAVVATILGDPELKSLWADEVQAMRLRIAQLRSGLLEALESHGLRERFAHIGVQRGMFSYTGLTPEQVKHLRERHSVYMVGTGRANVAGIDATRLDLLAEAIADACK Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_07335 AO356_07335 fructose-specific PTS system (fructose 1-phosphate forming), EI, Hpr, and EII-A components Specifically important for utilizing D-Fructose. PTS fructose transporter subunit IIA MLELTLEQISMAQTAVDKDAALQLLADKLVADGLVAEGYLAGLQAREAQGSTFLGQGIAIPHGTPQTRDLVYSTGVRLLQFPEGVDWGDGQIVYLAIGIAAKSDEHLRLLQLLTRALGETDLGQALRRAGSAEALLKLLQGAPQELALDAQMIGLGVSADDFEELVWRGARLLRQADCVSNGFAGVLQQVDALPLGDGLWWLHSEQTVKRPGLAFVTPDKPIRYLGQPLSGLFCLASLGEAHQALLERLCALLIEGRGHELGRATSSRKVLEVLGGELPADWPSARIGLANAHGLHARPAKILAQLAKSFDGEIRVRIVDGQDSAVSAKSLSKLLSLGARRGQVLEFIAEPSIANDALPALLAAIEEGLGEEVEPLPPPSAPRETVMAEVATVMLAPESGSLIQAVAAAPGIAIGPAHIQVLQAIDYPLRGESAAIERERLQNALNQVRSDIQGLIERAKAKAIREIFITHQEMLDDPELTDEVDTRLKLGESAQAAWMGVIEAAAKEQEALQDALLAERAADLRDVGRRVLAQLCGVETPNEPDQPYILVMDEVGPSDVARLDPTRVAGILTARGGATAHSAIVARALGIPALVGAGAAVLLLAPGTSLLLDGQRGRLHVDPDAATLQRAKEERDTREQRLKVAAEQRHEPALTRDGHAVEVFANIGESAGVASAVEQGAEGIGLLRTELIFMAHSQAPDEATQEAEYRKVLDGLAGRPLVVRTLDVGGDKPLPYWPIAKEENPFLGVRGIRLTLQRPQVMEAQLRALLRSADSRPLRIMFPMVGSVDEWRQARAMTERLRLEIPVADLQLGIMIEVPSAALLAPVLAKEVDFFSVGTNDLTQYTLAIDRGHPTLSAQADGLHPAVLQLIDITVRAAHAHGKWVGVCGELAADPLAVPVLVGLGVDELSVSARSIAEVKARVRELSLAQVQTLAQAALAVGSADDVRALVEAL Pseudomonas stutzeri RCH2 psRCH2 GFF3291 Psest_3355 fructose-specific PTS system (fructose 1-phosphate forming), EI, Hpr, and EII-A components Specifically important for utilizing D-Fructose. phosphoenolpyruvate-protein phosphotransferase MLELNAQHIHMHQAAADKPAALALLGEVLVADGLVAAGYLEGLRAREAQGSTFLGQGIAIPHGTPETRDQVFTTGVRLLHFPAGVDWGNGQLVYLAIGIAARSDEHLRLLQLLTRALGEGDLSEGLQQAESPEAIIGLLQGAPQALALDGELVSLGVAADDFDELAWQGVKLLKRAQCVEPGFNASLPLGQSLPLGDGLWWLSSEQSVQRPGLAFVTPVSNLEHQGQPLNGLFVLASMGEAHQAMLERLCNLLIEGRGQELSQATSSRTVLEALGGDVPADWPSAQVPLANAHGLHARPAKVLTEIAQAFEGEIRVRLAGTESAGVSVKSLSKLLAMGAHRGQLLEFMAEPAIASDALPALVRAVEEGLGEEVEPLPAPGEASEPPVTAQGPAESAIDQAALRAGDQVNGIAASPGIAIGPVLVRKPQVIDYPKRGESPVIELQRLDAALDKVHADIGTLIDESQVASIRDIFTTHQAMLKDPALREEVQVRLQKGLSAEAAWMEEIESAAQQQEALHDKLLAERAADLRDVGRRVLACLTGVEAEQAPDEPYILVMDEVAPSDVATLNAQRVAGILTAGGGATSHSAIIARALGIPAIVGAGPGVLGLARNTLLLLDGERGELLVAPSGAQLEQARSERAAREERKHLANERRMDAAVTRDGHPVEIAANIGAAGETPEAVAMGAEGIGLLRTELVFMNHSQAPNQATQEAEYRRVLEALEGRPLVVRTLDVGGDKPLPYWPMPAEENPFLGVRGIRLSLQRPDILETQLRALLASADGRPLRIMFPMVGNIDEWRTAKAMVDRLRVELPVADLQVGIMIEIPSAALIAPVLAQEVDFFSIGTNDLTQYTLAIDRGHPTLSGQADGLHPAVLRLIGMTVEAAHAHGKWVGVCGELAADALAVPLLVGLGVDELSVSARSIALVKARVRELDFAACQRLAQQALMLPGAHEVRAFVGEHC Pseudomonas stutzeri RCH2 psRCH2 GFF849 Psest_0863 maltose ABC transporter, substrate-binding component MalE Specifically important for utilizing D-Maltose monohydrate. Maltose-binding periplasmic proteins/domains MNKKFWCIATVGLAATFSLPLPALAAIEEGKLVVWINGDKGYKGLAEVGKKFTAETGIPVEVAHPDSATDKFQQAAATGNGPDIFIWAHDRIGEWAKSGLLTPVTPSADTKSGIADFSWQAVTYDNKLWGYPISVETIGLIYNKALVDTPPKTFDDVMALNEKLAAQGKRAILWDYNNTYFTWPLLSAKGGYVFEHADGGYDVKSTGVNNAGAKAGAQVLRDLIDKGVMPKGADYSVAEAAFNKGDSAMMISGPWAWSNIEKSGIDFGVAPIPAIDGEPGKPFVGVAAALLNAASPNKDLAVEFLENYLLQVEGLKTVNADVPLGAVANTAYMEELSANPHIKATFENAQMGEPMPNVPEMGAFWSSMAAALTNITSGRQDVDAALDDAAKRITR Pseudomonas stutzeri RCH2 psRCH2 GFF850 Psest_0864 maltose ABC transporter, permease component 1 (MalF) Specifically important for utilizing D-Maltose monohydrate ABC-type sugar transport systems, permease components MNARAELPSPAMTRPTSWGLPRFLTTGVRWLLWLAFNALSLYLVVALYVQKQMAFALLGLVVTGIASYLFINRRMYAQRYIFPSVAGMLVFVIFPLLYTVGIGFTNYSGTNLLSQAQVERYHLSQTYLAGERFRFTLHQSPDGERLRVDKGELGVFVSPPLTGEPDPEAPLSLLPAESVEGLGEALALREVIQRRKVLEQWVMQAPDGSLLRLYGLREVAAVEPQYRQDGPGVLVETRTGARLTADMERGFYVDETGKAVPPGFTVFTGFANFSRVLTEPSIREPFMQIFAWTFAFAGLTVVFTLAVGLVLASLLQWELVRGKAFYRLMLILPYAVPGFISILVFRGLFNQNFGEINLLLEGLFGIRPDWFSDPSLARTMILIVNTWLGYPYMLLLCMGLLQAIPRDQYEASAIDGASPLDNLLRITLPQLIKPLMPLLIACFAFNFNNFVLITLLTRGGPDIIGATTPAGTTDLLVSYTYRIAFQDSGQDFALAAAIATMIFILVGAMALLNLKLSKVKV Pseudomonas stutzeri RCH2 psRCH2 GFF851 Psest_0865 maltose ABC transporter, permease component 2 (MalG) Specifically important for utilizing D-Maltose monohydrate. ABC-type maltose transport systems, permease component MAMVQPKSARYRLWATHAALLAFVAAILFPLLMVISISFREGNFATGSLFPENPTLEHWSLALGIPYTHADGSVTQPPFPVLLWLWNSVKIAFVSSILILLLSTTSAYAFARMRFGGKAPILKSMLIFQMFPPVLSLVAIYALFDQLGQHVSWLGVNSHGAVIVASLGGMALHIWTIKGYFESIDASLEEAAIVDGATTWQAFFHILLPMSVPILAVVFILAFITSVTEYPIASVLLMDVDKLTLSVGAQQYLYPQNYLWGDFAAAAVLSGLPITAVFLYCQKWIVGGLTAGGVKG Pseudomonas stutzeri RCH2 psRCH2 GFF857 Psest_0871 maltose ABC transporter, ATPase component MalK Specifically important for utilizing D-Maltose monohydrate. ABC-type sugar transport systems, ATPase components MASVTLRDICKSYDGTPITRHIDLDIEDGEFVVFVGPSGCGKSTLLRLIAGLEDITSGDLLIDNQRVNDLPPKDRSVGMVFQSYALYPHMTVAENMAFGLKLASVDKREIKRRVEAVAEILQLDKLLERKPKDLSGGQRQRVAIGRTMVREPKVFLFDEPLSNLDAFLRVQMRIEIARLHQRIRSTMIYVTHDQVEAMTLADKIVVLNAGEIAQVGQPLHLYHYPKNRFVAGFLGSPQMNFVEVRAISASPETVTIELPSGYPLTLPVDGSAVSPGDPLTLGIRPEHFVMPDEADFTFHGQITVAERLGQYNLLYLTLERLQDVITLCVDGNLRVTEGETFAAGLKADKCHLFRENGEACTRHYREPAIYG Pseudomonas putida KT2440 Putida PP_3358 PP_3358 hydroxycinnamoyl-CoA hydratase-lyase (EC 4.1.2.61) Specifically important in carbon source p-Coumaric acid. This is the second step in p-coumaric acid catabolism. (Hydroxycinnamoyl-CoA is a synonym for p-coumaryl-CoA.) hydroxycinnamoyl-CoA hydratase-lyase MSKYEGRWTTVKVELEAGIAWVTLNRPEKRNAMSPTLNREMVDVLETLEQDADAGVLVLTGAGESWTAGMDLKEYFREVDAGPEILQEKIRREASQWQWKLLRLYAKPTIAMVNGWCFGGGFSPLVACDLAICANEATFGLSEINWGIPPGNLVSKAMADTVGHRQSLYYIMTGKTFDGRKAAEMGLVNDSVPLAELRETTRELALNLLEKNPVVLRAAKNGFKRCRELTWEQNEDYLYAKLDQSRLLDTTGGREQGMKQFLDDKSIKPGLQAYKR Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_2777 Echvi_2777 fused D-3-phosphoglycerate dehydrogenase / phosphoserine phosphatase (EC 1.1.1.95; EC 3.1.3.3) # Important for fitness in defined media, unless serine is added as a nitrogen source. The N-terminal part is distantly related to the phosphoserine phosphatase from Arabidopsis, and no other candidate was found for this step. The C-terminal part is 52% identical to E. coli phosphoglycerate dehydrogenase. Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like MTTDKKFIIDFDSTFTQVEALDILGEISLRNDPKRDEKLQAIKDITDLGMEGKLNLRESLERRIEILQANKSQIAELIDALKQKVSKSFQRNREFFQENAENIYILSNGFKDFITPVVAAYGLKEENVFANDFIYDEAGNIIDLNKENLLSNNNGKPATIKSLKLEGDVYVIGDGYTDYEIKASGLANKFYAFTENINRPKVSSKADHIAPSLDEILYVNKMNKKFSYPKSRINVLLLENVHPIGVEIMKQEGYNVEVVSSAMSEEELCEKIKNVSIIGIRSKTQITKKVLENANRLMAVGAFCIGTNQIDLETCQEKGIAVFNAPFSNTRSVVELAISEIIFLMRNLHDKTLKMHQGIWNKSASGSFEVRGKKLGIIGYGNIGAQLSVLAENMGMNVFYYDIVERLALGNATKIDSLDELLETCDIISLHVDGRTENKNILNKEKIFKMKKGAILVNLSRGHVVDVPALRDALESGHLAGAAVDVFPTEPKNNDEPFESELIGCPNTILTPHIGGSTLEAQENIAQFVPGKIIEYINSGNTFNSVNFPNIQLPFLKDAHRLIHIHQNAPGVLAKINQVLASYKINIVGQYLKTNEKIGYVITDIDKRYSNDVIDALKEIEGTIRFRILY Burkholderia phytofirmans PsJN BFirm BPHYT_RS17700 BPHYT_RS17700 imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) # Important for fitness in minimal media, unless histidine is provided as a carbon or nitrogen source. imidazoleglycerol-phosphate dehydratase MRLAEVVRNTSETQIRVKINLDGTGQQKLATGVPFLDHMLDQIARHGLFDLEIEAHGDLHIDDHHTVEDTGITLGQAVAKAIGDRKGIVRYGHSYVPLDEALSRVVIDFSGRPGLEFHVPFTRARIGTFDVDLSIEFFRGFVNHAGVTLHIDNLRGLNAHHQMETVFKAFGRALRMATELDERAAGQIPSTKGSL Phaeobacter inhibens BS107 Phaeo GFF1303 PGA1_c13190 ABC transporter for D-Sorbitol, permease component 1 Specific phenotypes on D-Sorbitol; D-Sorbitol. ABC transporter permease protein MARAVTPRRKAINTALAWAVGLLIFFPILWTILTSFKTEAQAISDPPVFLFFDWTLENYSVVQERSDYMRFLWNSVIIAGGSTILGIIIAVPAAWSMAFVPSKRTKDILLWMLSTKMLPAVGVLYPIYILFIKMGLLDNRFGLVVVLMLINLPIIVWMLYTYFKEIPGEILEAARMDGATLKEEILYVLTPMAIPGIASTLLLNIILAWNEAFWTLNLTAAKAAPLTAFIASYSSPEGLFYAKLSAASTMAIAPILILGWFSQKQLVSGLTFGAVK Burkholderia phytofirmans PsJN BFirm BPHYT_RS16105 BPHYT_RS16105 ABC transporter for D-Sorbitol, permease component 1 Specific phenotypes on D-Sorbitol. mannitol ABC transporter permease MSQVASTPVSNPTAMTVPAKSPFAAIRRGIPGVIAWLVALLLFFPIFWMTITAFKTEQQAYASSLFFIPTLDSFREVFARSNYFSFAWNSILISAGVTILCLILAVPAAYAMAFFPTRRTQKVLLWMLSTKMMPSVGVLVPIYLLWKNSGLLDSVSGLVIVYTLINLPIAVWMSFTYFAEIPRDILEAGRIDGAATWQEIVYLLMPMSLPGLASTALLLVILSWNEAFWSINLSSSNAAPLTVFIASYSSPEGLFWAKLSAASLLAVAPILIVGWLSQKQLVRGLTFGAVK Phaeobacter inhibens BS107 Phaeo GFF1304 PGA1_c13200 ABC transporter for D-Sorbitol, permease component 2 Specific phenotypes on D-Sorbitol; D-Sorbitol. ABC transporter permease protein MATQHSRSAARIMMAPAVILLLGWMLVPLTMTLYFSFKKYLPLRGGDLGWVGFDNYARFLSSSAFWPSVQATLVIVGGVLAITVILGVFLALLLNQPMWGQGIVRILVIAPFFVMPTVSALVWKNMFMDPVNGLFAHLWKAFGAEPVSWLSEASLQSIILIVSWQWLPFATLILLTAIQSLDSEQLEAAEMDGAPPVARFGYITLPHLSRAITVVVLIQTIFLLSIFAEIFVTTQGSFGTKTLTYLIYQRVLESQNVGLGSAGGVYAIILANIVAIFLMRIVGKNLDA Burkholderia phytofirmans PsJN BFirm BPHYT_RS16110 BPHYT_RS16110 ABC transporter for D-Sorbitol, permease component 2 Specific phenotypes on D-Sorbitol. sugar ABC transporter permease MRPLRLPIMHAHPQTEKERETRKANSARWLATPSVAVLVLWMAIPLAMTIWFSFSRYNLLNPDLKGFAGFDNYKYLASDPSFGPSIGHTLELIISVLVITVVGGVLMAILFDRKFYGQGIARLLAIAPFFVMPTVSALIWKNMILHPVYGLIAQGMRAMGMQPIDWFAEYPLTAVIMIVAWQWLPFAFLILFTAIQSLDQEQKEAARIDGAGPFSMFFYITLPHLKRAIAVVVMMETIFLLSIFAEIYTTTGGGPGTATTNLSYLIYSLGLQQFDVGLASAGGILAVVLANIVSFFLVRMLAKNLKGEYEK Shewanella amazonensis SB2B SB2B 6936374 Sama_0562 D-mannose transporter (MFS superfamily) Specific phenotype on mannose and no other transporter is apparent in the fitness data. glucose/galactose transporter (RefSeq) MAFVSSTTPQNGSAAPAQSHQQLLFGAMTSLFFIWGFITALNDILIPHLKGIFDLSYTQAMLVQFCFFGAYFLVSPLAGVLIARIGYLRGIIFGLSTMATGCLLFYPASSLEQYALFLLALFVLASGITILQVSANPFVARLGPERTAASRLNLAQALNSLGHTLGPLFGSLLIFGAAAGTHEAVQLPYLLLAAVIGIIAVGFIFLGGKVKHADMGVDHRHKGSLLSHKRLLLGALAIFLYVGAEVSIGSFLVNYFAEPSIGGLDEKSAAELVSWYWGGAMIGRFAGAALTRRFNPAMVLAANAVFANLLLMLTIVSSGELALVAVLAVGFFNSIMFPTIFTLAIEGLGELTSRGSGLLCQAIVGGALLPVIQGVVADNVGVQLSFIVPTFCYFYICWYAFFARNRMNGETAS Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_28540 AO356_28540 D-mannose transporter Specific phenotype on D-mannose as the carbon source. No other transporter was apparent in the fitness data. hexuronate transporter MFGQGRSLIIIMLFLAGVINYLDRSALSVAAPFIQKDYGLSTGEMGMIFSSFFVGYAAFNFIGGWAADRYGAKTTLLLAMVLWSLFSGLTVLTVGFASLVLIRILFGMGEGPLSVTTSKMVNNWYTPKRRARAIGASMSGTPLGGAISGPVVGFIAVTYGWKISFIIIMLIGLVWAAVWFKFVKERPEGEGAEDILRAEGQGELAAQPVFPLRFYLKQPTVLFTSLAFFSYNYTLFFFLTWFPSYLTMAHGLNVKDMSIATVIPWVLGFLGLALGGFISDFVFKKTGRMMFSRKVVLVTCLLACAVCIACAGMVTTLYPAVILVALAVFFLYLTGAIYWAIIQDTVPAARVGGVSGFMHFLANTSGIVGPTLTGFLVQFTGSFTSAFLLAGLLTVIGAVCVARYVKPLSVADTGNAAAQSPQPVSALGRS Pseudomonas simiae WCS417 WCS417 GFF4325 PS417_22150 D-mannose isomerase (EC 5.3.1.7) Specifically important for: D-Mannose. D-mannose isomerase is the first step in mannose catabolism. This gene is similar to the putative mannose isomerase Sama_0560 (PMID:20836887, PMCID: PMC4436071). sugar isomerase MITQPLPASSWLNAPAHYVWLAAEGQRLLAFAKASRLPDGFGNLDDKGQLPADAHAETMNTARMTHSFAMAHALGLPGYAELVAHGVAALSGALRDSEHGGWFAAPHALDGNRGKAAYLHAFVALAASSAVVAGAPGASTLLNDAIHIIDHFFWSEEEGVMLESFAQDWSGVEAYRGANSNMHATEAFLALADVTGDTRWLDRALRIVERVIHTHAAGNQFMVIEHFDTHWHPLLGYNEDNPADGFRPYGITPGHGFEWARLVLHLEAARLQAGLVTPEWLVADAKRLFASACEYAWSVDGAPGIVYTLDWNHRPVVRERLHWTHAEASAAAQALLKRTGELHYETWYRRFWEFCETHFIDRLHGSWHHELSPHNQPSSNIWGGKPDLYHAWQAVLLPALPLAPSMASAIGTGRYVTNW Phaeobacter inhibens BS107 Phaeo GFF1644 PGA1_c16670 D-mannose isomerase (EC 5.3.1.7) Specifically important for: D-Mannose. often annotated as N-acylglucosamine 2-epimerase, but the phenotype confirms that it is mannose isomerase. putative N-acylglucosamine 2-epimerase MSTHSAVGDLSAPGVWLEDTGHQAYLIADARRQLDFFAGSLRAEPGFHTLDAAGRPLPDDKQELHTTTRLVHSYALAHICGYAGAEQMIDHGMAYLNSHHRDQIHGGYLWALSGDAIADDRKLAYGHVFVLLAAASAKLAGHPGADALLSDVAEVLDQRFWETGPKRFADEWNRDWTPFSTYRGMNANMHGVEALLTAYEATGETVFLDRAGHILDFFVDEVAAAESWRLPEHYTETWQIDRTYAGDPMFRPAGTTPGHSFELGRLMLQHWDLAGRRDTGAPTRARSLIEQALADAWLVDGGFAYTLDFEGKVAMRNRFWWPVTEAIGAVATLVKLDGRVEDEQWYRRLWGFAQAHFIDEDRGGWYPEIDGNGQVTRTIFTGKPDIYHALQACLLPLGALPLGHVAGLKKLSAPLLS Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2078 D-mannose isomerase (EC 5.3.1.7) Specifically important for: D-Mannose. Often annotated as N-acylglucosamine 2-epimerase instead D-mannose isomerase (EC 5.3.1.7) MAIPPYPDFRSAAFLRQHLRATMAFYDPVATDASGGQFHFFLDDGTVYNTHTRHLVSATRFVVTHAMLYRTTGEARYQVGMRHALEFLRTAFLDPATGGYAWLIDWQDGRATVQDTTRHCYGMAFVMLAYARAYEAGVPEARVWLAEAFDTAEQHFWQPAAGLYADEASPDWQLTSYRGQNANMHACEAMISAFRATGERRYIERAEQLAQGICQRQAALSDRTHAPAAEGWVWEHFHADWSVDWDYNRHDRSNIFRPWGYQVGHQTEWAKLLLQLDALLPADWHLPCAQRLFDTAVERGWDAEHGGLYYGMAPDGSICDDGKYHWVQAESMAAAAVLAVRTGDARYWQWYDRIWAYCWAHFVDHEHGAWFRILHRDNRNTTREKSNAGKVDYHNMGACYDVLLWALDAPGFSKESRSAALGRP Shewanella amazonensis SB2B SB2B 6936372 Sama_0560 D-mannose isomerase (EC 5.3.1.7) Specifically important for: D-Mannose. This is the first step in D-mannose catabolism. Also see PMID:20836887, PMCID: PMC4436071 hypothetical protein (RefSeq) MKFYNRDFLLSHSQSILDFYDPRVLDASGGYFHNYYDDGSLFEPGFRQLVSSCRITVNYARAADILDKPEYLAHARHGLNYLLNVHLQADERFAWTLKSHRPEDMTQQAYGYAFALLAFAACRKSGILKDNNKLLWIYNLLEQRFWQPEYGLYADEIGADGVLSDYRGQNANMHLCEAMIAAFEASGEGRFLDRAMEIADKIANRQAALTGGIIWEHFTPGFAINWEYNKDDPKNLYRPWGFQGGHQTEWAKLLLSLARHSHQPWLISRAKTLFDTAFEKSWDKEHGGMVYGFGPNGDWCDDDKYFWVQAESFAAAAMLYQQTGEQKYLDAYNALWNYAWQHFVDHEHGAWFRVLYRDNRKYSNEKSTAGAKCDYHTLGACFDSLRDLT Burkholderia phytofirmans PsJN BFirm BPHYT_RS02050 BPHYT_RS02050 D-mannose isomerase (EC 5.3.1.7) Specifically important for: D-Mannose; D-Sorbitol; D-Fructose. Often annotated as N-acylglucosamine 2-epimerase, but phenotype on mannose is consistent with annotation as mannose isomerase. Its role on sorbitol (which is probably oxidized to sorbose or fructose by BPHYT_RS16120) or fructose is unclear - this might be a polar effect on fructokinase (BPHYT_RS02045), as there is a stronger phenotype for insertions with the antibiotic resistance marker in the non-coding orientation N-acylglucosamine 2-epimerase MTQSDPLHPANGAAAAPPVESFRSRDFLLSHVQDTLRFYAPNVFDPSGGFFHFFRDDGSVYDKTTRHLVSSCRYVFNYAMAYRQFGDPQHLEYARHGLRFLREAHWDAQHEGYDWEIEWRDGKKRTLDATRHCYGLAFVLLAYSHAAMAGIEEAKPMIGATFELMEHRFWDAAAGLYADEASPDWRVSSYRGQNANMHTTEALLAAHEATRHLVYLDRAERVASNITLRQAKLSQGLVWEHFHADWSVDWHYNEEDSSNIFRPWGFQPGHQTEWAKLLLILERFRPLPWLLPRAIELFDAAMAHAWDEDHGGLYYGFGPDGTVCDHDKYFWVQAETFATAALLGKRTGNERFWDWYDEIWRYSWAHFVDHEYGAWYRILTCDNRKYSDEKSPAGKTDYHTMGACYEVLAHALPDGAAAAPESAEQTK Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1776 Ga0059261_1776 Fructokinase (EC 2.7.1.4) Specifically important for utilizing D-Fructose. Automated validation from mutant phenotype: the predicted function (2.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Transcriptional regulator/sugar kinase MPLDSFGQAGLMGDEPLLLGAVEAGGTKFLCGIADRTGSVLAQTRIPTTTPAETLDAATAFFAEHVARHGPLSAFSVGSFGPLSLDPIAPDYGSITSTPKPGWQDVDLLGYFRQMIDAPMALDTDVNCAAVGERLFGSGRGLDTFCYVTVGTGIGVGLLVGGAPHGGANHPEAGHIRLPRAPGDHDFAGICPFHGDCLEGLACGPAMKARWGAAAETLPGDHPAWDIEADYLAGLCATLTYIVRPDRIILGGGVMESHLMHARVRRTLVAKLAGYDASMRSLDMDEYVVPPTAGPSAGLTGAFALAYRIVTRQWPMHWAATGSLIAPSITEFANA Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_3036 Fructokinase (EC 2.7.1.4) Specifically important for utilizing D-Mannose. Automated validation from mutant phenotype: the predicted function (2.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. Fructokinase (EC 2.7.1.4) MYLVCGEALFDFFSENDASGLASKVNFKAIAGGSPFNVAVGLRRLGVDAALLAGLSTDYLGRRLLQVLQDEGVCLDYLLEFAAPTTLAMVAVGANGSPQYSFRGEGCADRQLQAEHLPTLGPEVRGLHIGSFSLVVQPIADTLLALVRRESGKRLISLDPNVRLNPEPDIDLWRKRVATLVELADLIKVSDEDLHLLYPDQDPAQVIEGWLQHRCQLVFLTRGGEGATVFSRAHGSWSAPACSVKIADTVGAGDTFQAALITWLTEQQLDSVEGVKQLGREQIDRMLKFAVRAAALTCSKTGPDLPYRKQLDLR Shewanella amazonensis SB2B SB2B 6936373 Sama_0561 Fructokinase (EC 2.7.1.4) Specifically important for utilizing D-Mannose. Automated validation from mutant phenotype: the predicted function (2.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. carbohydrate kinase (RefSeq) MSKRVLCFGEALIDFLCTGSDEDDGLMLPCYRQYPGGAPANAAVAVAKLGGQARFAGLVGKDTFGDFLANSLVRYGVDISLLGRHSSAPTSLAFVHLNDDGDRSFSFYRDGGADTLFDASVAEASWFENTAVLHLCSNTLTTAQSAEATLTMADRAVAAGLAVSVDVNLRHNLWQGGAACKATVMSLVHKAHVLKFAQEELEYLAGSEPQGFIQQLLDSGCKLLLITDGGNPIRAFTGKQCLTLPVPKMDVVDTTAGGDGFIGGLLHRIARDGLDTLLESETTFKDALGFAIGCGALAVSRPGAFPALPGLAEAEAFQASMGDVLHTISVDDSRLPKPCQRSW Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_25910 AO353_25910 Fructokinase (EC 2.7.1.4) Specifically important for utilizing D-Mannose. Automated validation from mutant phenotype: the predicted function (2.7.1.4) was linked to the condition via a SEED subsystem. This annotation was also checked manually. fructokinase MYLVCGEALFDFFSENAASSQASTVNYKAIAGGSPFNVAVGLRRLGVDSALFAGLSTDYLGRRLQQVLADEGVRADYLLDFDAPTTLAMVAVGANGSPHYSFRGEGCADRQLTLAHLPELSDEVRGLHIGSFSLVVQPIADTLLALVRRESGKRLISLDPNVRLNPEPDIELWRSRIAELMKYADLIKVSDEDLSLLYPGREPQSVIDSWLEHRCQLVFLTRGGQGATVFSRRHGSWSAPASKVVIADTVGAGDTFQAALITWLTEQQLDSVDGLQRLSREQIDAMLRFAISAAALTCSKTGPDLPYRHQLEMR Dinoroseobacter shibae DFL-12 Dino 3609413 Dshi_2797 Fructokinase (EC 2.7.1.4) Important for utilizing Sucrose, which is catabolized via fructose. PfkB domain protein (RefSeq) MILCAGEALIDMLPRALPDGTAGFAPVAGGAVFNTAVALGRLGADVGLVTGLSRDLFGEVLMTALAAADVDSDMAVLSDRPTTLAFVTLTDGHAQYAFYDENTAGRMLAPADMPDPGPEVGTLFFGGISLAVEPCAAAYEALCLKAAAGRVVMLDPNIRPGFIKDETTFRARIDRMLAVTDIVKVSDEDLAWLMGPGDLAESAAALRARGPAVVCVTRGGAGVEAHTATGITHVAAEAVEVVDTVGAGDTFNAGFLAGLAEAGALDKDRLRALDAPVLTSALRLGAQAAAITVSRAGANPPWRDELPR Azospirillum brasilense Sp245 azobra AZOBR_RS32325 AZOBR_RS32325 Fructose PTS system (E-I, HPr, and E-IIA components) Specifically important for utilizing D-Fructose. This gene includes components E-I (PEP-protein phoshpotransferase), HPr, and E-IIA. Components E-IIB and E-IIC are in the adjacent gene AZOBR_RS32335. PTS fructose transporter subunit IIA MAPDANTAIMPTDLLRPELLRLSASPAGKEEAIREAAQLLIAAGCIDSAYAASMLRREAVANTFLGHGVAIPHGMVEDRGMVRRSGIAVLQVPGGIAWNPGQTAHLVVAIAAQSDAHIAVLRRLTRLMQDEARLTALFTVTDPAALAAALGEDAPVAAPATPGGDLAERFDWVVDYPTGLHARPATAWVETARASAARIQVRHGDLVADAKALVALLQLGLRAGDSVVVSAEGDDAVAALARMKATITRLTAREKADAAAAAQKARAPVRGWTPPNPLPAVPGIAASPGLAIGPVHVLPRAAVSVPDEPVPLIEGGDRLHEALSLTRQNLKALADDTARRLGPSEAAIFAAQAEILNDTDLVTLACQLMVEGHGVAWSWHQAVERTAAGLAALDNPVLAARAADLRDVGQRVLARIDPALRTGGAPDLPDTPCILIAEDLSPSDTAALDMARVIGLATAQGGPTSHTAILARTLGLPAMVAGGAALMELANGTPAILDGQSGRLHLSPAAADIADARAWIAREEARKAEEEARRGLPARTRDGHEVEIGANVNRPDQVAVALSQGAESVGLMRTEFLFLERGDAPGEDEQYETYRGMLTALEGRPLIVRALDIGGDKQVPHLQLPHEENPFLGVRGARLLLRRPELLETQLRALYRAAKDGGAKDGGALSIMFPMITALGEVQALRAACERIRAELDAPAVPLGIMVEVPAAAIQADVLARHVDFFSIGTNDLTQYALAIDRQHPELAAEADSLHPAVLRLIRLTVEGAERHGRWVGVCGGIAGDPFGAALLTGLGVRELSMTPRDIPAVKDRLRGSDLSALKDAAQRALDCETADAVRALDGGAA Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_1146 fructose-specific PTS system (fructose 1-phosphate forming), EI, Hpr, and EII-A components Specifically important for utilizing D-Fructose. Phosphoenolpyruvate-protein phosphotransferase of PTS system (EC 2.7.3.9) MLELTIEQISMGQSAVDKATALQLLADRLVTDGLVADGYLAGLQAREAQGSTFLGQGIAIPHGTPQTRDLVFSTGVRLMQFPDGVDWGDGQIVYLAIGIAAKSDEHLRLLQLLTRALGETDLGQALRRASTAEALLKLLQGAPQELALDAQMIGLGVSADDFEELVWRGARLLRQADCVSNGFAGVLQQVDALPLGDGLWWLHSEQTVKRPGLAFVTPDKPMRYLGQPLSGLFCLASLGEAHQALLERLCALLIEGRGHELGRATSSRAVLEVLGGEVPADWPSARIALANTHGLHARPAKILAQLAKSFEGEIRVRIVDGHDSAVSVKSLSKLLSLGARRGQVLEFIAEPTIAADALPALLAAIEEGLGEEVEPLPAVSQHREVIADVAEVLLAPASGSLIQAIAAAPGIAIGPAHIQVQQVIDYPLRGESAAIERERLKQALADVRRDIEGLIERSKAKAIREIFITHQEMLDDPELTDEVDTRLKQGESAEAAWMAVIEAAAKQQESLQDALLAERAADLRDIGRRVLAQLSGVETPAEPEQPYILVMDEVGPSDVARLDPTRVAGILTARGGATAHSAIVARALGIPALVGAGAAVLLLKPGTPLLIDGQRGRLHVDADAATLQRATEERDTRELRLKAAAEQRHQPALTTDGHAVEVFANIGESAGVTSAVEQGAEGIGLLRTELIFMAHSQAPDEATQEVEYRRVLDGLAGRPLVVRTLDVGGDKPLPYWPIAKEENPFLGVRGIRLTLQRPQVMEAQLRALLRAADNRPLRIMFPMVGSVDEWRQARDMTERLRLEIPVADLQLGIMIEVPSAALLAPVLAKEVDFFSVGTNDLTQYTLAIDRGHPTLSAQADGLHPAVLQLIDITVRAAHAHGKWVGVCGELAADPLAVPVLVGLGVDELSVSGRSIAEVKARIRELSLTQTQTLAQQALAVGSANEVRALVEAL Pseudomonas simiae WCS417 WCS417 GFF780 PS417_03965 fructose-specific PTS system (fructose 1-phosphate forming), EI, Hpr, and EII-A components Specifically important for utilizing fructose and mannose. The phenotype on mannose is not explained. PTS fructose transporter subunit IIA MLELTVEQISMGQVAVDKSAALHLLAEKLVADGLVAEGYLSGLQAREAQGSTFLGQGIAIPHGTPETRDQVFSTGVRLLQFPEGVDWGDGQIVYLAIGIAAKSDEHLRLLQLLTRALGETDLGQALRRAGSAEALLKLLQGAPQELALDAQMIGLGVSADDFEELVWRGARLLRQADCVSNGFAAVLQQVDALPLGDGLWWLHSEQTVKRPGLAFVTPDKPMRYLGQPLNGLFCLASLGEAHQTLLERLCALLIEGRGQELGRATSSRAVLEVLGGELPPDWPAARITLANAHGLHARPAKILAQLAKSFDGDLRVRIVDGPVGAVSVKSLSKLLSLGARRGQVLEFIAEPSIAGDALPALLAAVEEGLGEDVEPLPTLSVQPEVLDIEPELSAPLAGSQVQAIAAAPGIAIGPAHIQVLQVFDYPLRGESCAIERERLHSALADVRRDIQGLIERSQSKAIREIFVTHQEMLDDPELTDEVDTRLKQGESAEAAWMSVIEAAAKQQESLQDALLAERAADLRDIGRRVLAQLCGVETSQEPSEPYILVMDEVGPSDVARLDPARVAGILTARGGATAHSAIVARALGIPALVGAGPAVLLLAAGTPLLLDGQRGRLHVDADAATLQRATVERDTREQRLQAASAQRHEPALTRDGHAVEVFANIGESAGVASAVEQGAEGIGLLRTELIFMAHPQAPDEATQEAEYRRVLDGLAGRPLVVRTLDVGGDKPLPYWPIAEEENPFLGVRGIRLTLQRPQIMEAQLRALLRSADNRPLRIMFPMVGSVDEWRAARDMTERLRLEIPVADLQLGIMIEVPSAALLAPVLAKEVDFFSVGTNDLTQYTLAIDRGHPTLSAQADGLHPAVLQLIDITVRAAHAHGKWVGVCGELAADPLAVPVLVGLGVDELSVSARSIPEVKARVREFSLSEAQGLAQKALAVGSPAEVRALVEAV Dinoroseobacter shibae DFL-12 Dino 3608251 Dshi_1655 glucokinase (EC 2.7.1.2) Specifically important for utilization of D-glucose and glucose-containing disaccharides (D-maltose, D-trehalose, and perhaps sucrose) Glucokinase (RefSeq) MTSLRDAPALVADIGGTNTRVALADGPVLRAGSVEKYRNADYSSLDSVLRSYLEKMEVAGCSGACVALAGPVRNGIGHLTNLDWRMDEDLLSEATGAPVVALLNDLQAQGFALGHLEAACLRPVISRPPPAAQETRLMIGLGTGFNAASVLYTPAGRIVTPSEAGHANLPVRTEQELRLCRFVETAHGFPAVEDVLSGRGLERVYNFLSPTPDQPQRLSAAEVMAAAAREERQALDALELFIGLLGTVAGNLSLIHLPFGGVYLCGGVARHIGPYLGSMGFAEAFANKGRFADFMRDFPVWLVEDDFAALTGCASFLDERCRN Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2066 glucose ABC transporter, ATPase component Specifically important for utilizing glucose. Also mildly important for mannose utilization and likely transports it as well. SN-glycerol-3-phosphate transport ATP-binding protein UgpC (TC 3.A.1.1.3) MASSLDIAGINKRFGKGDKSVEVLRKVDIHVAPGEFLILVGPSGCGKSTLLNIIAGLDEPTEGEIRIGGKNVVGMPPRDRDIAMVFQSYALYPTLSVADNIGFALEMRKMPKPERQKRIDEVAAMLQISHLLDRRPSQLSGGQRQRVAMGRALARQPQLFLFDEPLSNLDAKLRVEMRAEIKRLHQASGITSVYVTHDQVEAMTLGSRIAVMKGGVVQQLGTPDEIYNRPANTYVATFIGSPTMNLLRGAVTGGQFGIQGAALNLAPPPSSANEVLLGVRPEHLVMQETAPWRGRVSVVEPTGPDTYVMVDTAAGSVTLRTDAQTRVQPGEHVGLALAPAHAHWFDAQSEERLVA Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2064 glucose ABC transporter, permease component 1 Specifically important for utilizing glucose. Also mildly important for mannose utilization and likely transports it as well. ABC-type sugar transport system, permease component MSKNTFETWLPKLVVAPAFVLGFAFIYGLMVWNGVLSLTVSRMLPNYEWAGLAQYERLWEMDRWWVALKNLGIFGVGYVGGSLLIGVVLAVLLDQKIRAEGALRTIYLYPMALSFVVTGTAWKWLLNPGLGIEKMVRDWGFPNFEFGWLVDTEMAIYCVVIAGIWQSAGFAMALFLAGLRGIDDSIIKAAQVDGASLPRIYWRIVLPALRPVFFSTLMVLSHLAIKSFDLVMALTAGGPGFATDVPATFMYTMSFSRGQIGLGAASATMMLATVAALVIPYLYSELRTKAHDR Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2065 glucose ABC transporter, permease component 2 Specifically important for utilizing glucose. Also mildly important for mannose utilization and likely transports it as well. Maltose/maltodextrin ABC transporter, permease protein MalG MTAKPSLLPSVGRFLVYAVLALATAFFLLPLYAMLVTSFKYAEEIRSTSLLALPGSLNWSAWGTAWQSACTGVDCNGLRPFFMNSVAMAVPAVLISTVWGALNGYVLSLWKFRGSDALFGMLLFGVFMPFQVVLLPMSQVLGWLGLSSSITGLVLVHCLAGLAGTTLFFRNYYAAIPKELVNAARMDGASFFQIFWRIVLPLSTPIVMVTLIWQFTNIWNDFLFGVVFSGTDSKPVTVGLNNLANTSSSVKAYNVDMAAAIIAGLPTMVIYVLAGKFFVRGLTAGAVKG Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2062 glucose ABC transporter, substrate-binding component Specifically important for utilizing glucose. Also mildly important for mannose utilization and likely transports it as well. ABC-type sugar transport system, periplasmic component MWKMTKIAAVAVGLAAAMSASAGEVEVLHYWTSGGEAKSVAELKKIMQGKGHTWRDFAVAGGGGDSAMTVLKSRVISGNPPSAAQTKGPAIQEWASEGVLANMDTLAKAEKWDELLPKVVADVMKYKGAYVAAPVNVHRVNWMWGSSEALKKAGVAAMPKTWDEFFAAADKLKAAGLVPVAHGGQNWQDFTTFESVVLGVGGAKFYQDALVKLDNTALTSDTMKKSLETFRRIKGYTDPGAPGRDWNLATAMLIQGKAGFQLMGDWAKGEFLAAGKAPGKDFLCAAAPGSANAFTFNVDSFILFKLKDAAAQKAQSDLASSIMSPAFQEVFNLNKGSIPVRAGQPMDKFDDCAKASAKDFVDTAKSGGLVPSAAHGMAIAPATEGAIKDVVSQFWNDDKVSVADAMKKIAAAAKTK Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_05200 AO356_05200 D-mannose isomerase (EC 5.3.1.7) Specifically important for: D-Mannose. Often annotated as N-acylglucosamine 2-epimerase, but this is also distantly related to the D-mannose isomerase Sama_0560. The putative fructokinase AO356_00035 is also important for consuming mannose, which would complete the pathway. sugar isomerase MDTFQPAFSSWLNAPAHQQWLAAEGLRLLAFAKASKLPDGFGNLDELGRLPADARAETMNTARMTHSFAMAHIQGLPGFAELVDHGIQALNGRLRDAEHGGWFATTRPDEDGAGKAAYLHAFVALAASSAVVAQRPGAAALLDEAVRIIDEHFWCEEEGALRESFNRDWSEEEAYRGANSNMHATEAFLALADATDDPRWLVRALRIVERVIHGHAAANDYLVVEHFDRHWQPLHEYNQDNPADGFRPYGTTPGHGFEWARLLLHLEAARVQIGMLTPGWLAQDAQKLFDQNCRHGWDVDGAPGIVYTLDWDNRAVVRHRLHWVHAEAAAAASALLKRTDEAKYEAWYRCFWEFCDKHFIDRCNGSWHHELDPQNRPSADIWPGKPDLYHAWQAVLIPRLPLAPSMASALARLSSPAPV Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_03400 AO353_03400 D-mannose isomerase (EC 5.3.1.7) Specifically important for: D-Mannose. Often annotated as N-acylglucosamine 2-epimerase, but this is also distantly related to the D-mannose isomerase Sama_0560. The putative fructokinase AO353_25910 is also important for mannose utilization, which would complete the pathway. sugar isomerase MNTAPPAFSSWLNAPAHQQWLADEGLRLLAFAKASKLPEGFGNLDEHGQLPADAQAHTMNTARMTHSFAMAHIQGLPGFAELVDHGINALNGLLRDAEFGGWFAAPDHRDGDTGKAAYLHAFVALAASSAVIAQRPGAEALLNDAIAIIEQHFWSEEEGAMRESFNRDWSEEEPYRGANSNMHATEAFLALADVTQDSRWLNRALRIVERVIHRHAASNDHLVVEHFDRDWQPLRDYNQANPADHFRPYGTTPGHGFEWSRLLLHLEAARGQAGMLTPGWLLSDAQQLFANNCLHGWDVDGAPGIVYTLDWDNRPVVRQRLHWVHCEASAAASVLLKRTGEAQYETWYRRFWEFSDRCLIDRIHGSWHHELDPQNRPSTEIWGGKPDLYHAWQAVLIPRLPLAPSMASALAQGSVSVLM Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_597 D-mannose isomerase (EC 5.3.1.7) Specifically important for: D-Mannose. Often annotated as N-acylglucosamine 2-epimerase, but this is also distantly related to the D-mannose isomerase Sama_0560. This organism has a fructokinase (Pf1N1B4_4844, no data) which probably utilizes the resulting fructose. N-acylglucosamine 2-epimerase (EC 5.1.3.8) MDTFQPAFSSWLNAPAHQQWLAAEGLRLLAFAKAAKLAEGFGNLDEKGRLAANAQAETMNTARMTHSFAMAHIQGLPGFAELVDHGIQALSGPLRDAEHGGWFATPEHRDGNTGKAAYLHAFVALAASSAVVAQRPGAQALLDDAIHIIDSHFWSEEEGAMRESFNRDWSVEEAYRGANSNMHATEAFLALADVTEDNRWLIRAQRIVERVIHDHAAVNDYLVVEHFDRDWQPLRDYNYDNPADGFRPYGTTPGHGFEWARLLLHLEAARVQAGILTPGWLATDAQKLFDHNCRHGWDVDGAPGIVYTLDWDNRAVVRHRLHWTHAEASAAASALLKRTGDEQYERWYRLFWEFCDSHFIDRCDGSWHHELDPLNRPSADIWAGKPDLYHAWQAVLIPRLPLAPSMAIALAQLSQSVAV Sinorhizobium meliloti 1021 Smeli SMc03109 SMc03109 Mannokinase (EC 2.7.1.7) Specifically important for utilizing D-Mannose. Mannose is catabolized via mannose-6-phosphate isomerase (SMc03111) so this is mannokinase. hypothetical protein MFIGIDWGGTKMEVIALDRDGETRARHRVPTPTSGYEDCIRAVVELVASAESTAGERGSIGIGIPGSPNPRTGIVRNSNAVLINGKPLGRDLAAALGREVRLANDANCLAVSEAVDGAGKDAGVVFGVIVGTGHGGGLAIGKKVHAGYQGVAAEIGHYPLPWMTKDEYPGHRCWCGKLGCLDMYACGTGLELDYRMTTGTDRRGRDIIEAKRAGDPVAIGVYGRFVDRLARSLALLTNIVDPDVFVLGGGMSNVDEIYGELPASITRYLFGDSFETPIRKAVHGDSSGVRGAAWLWKD Sinorhizobium meliloti 1021 Smeli SMc03111 SMc03111 mannose 6-phosphate isomerase (EC 5.3.1.8) Specifically important for utilization of mannose (mannose 6-phosphate is formed by SMc03109) mannose-6-phosphate isomerase MGMDIHLQAGELAGWLNDAALPLWRQKGFDGEGGGFVETIDMKGEPTRDDRRSRVQPRQVYCFAAAGRRGWDGDWRTAAEGGLLYFDRVYGQPGGFYGALANADGKLIDASFDLYNQAFALLAFAHLAEVLPERGAEMVGRSDKLRRQLEARCKHPLAGFEEDDPPRLPLGSNPHMHLFEACLASEEVEGFDRVAWANLADEIAHLAMDRFIDAESGALREFFDHDWAPFPGEKGRIVEPGHLFEWAWLLLRWAERRGNAQAIVKARRLFEIGEKDGTCPDRDVVVMTLFDDFSVADPTARLWPQTEWLKAAIRFAALTEGAERERYLASAGRAAAALQRFLNVPVRGLWRDKQKADGSFVEEPAPASTFYHILCAIYELEDCLKRM Dinoroseobacter shibae DFL-12 Dino 3608245 Dshi_1649 alpha-glucosidase / maltase / trehalase / sucrase (EC 3.2.1.48; EC 3.2.1.20; EC 3.2.1.28) # Very important for fitness during growth on maltose, trehalose, or sucrose. 60% identical to Halomonas HaG, which is most active on maltose and sucrose and has some activity on trehalose (PMC3298133). Dshi_1649 is also important for utilization of glucose, which is not explained. The glucose phenotype is variable and might reflect polar effects on Dshi_1648, a component of the glucose/maltose/trehalose/sucrose transporter. alpha amylase catalytic region (RefSeq) MNAEAQMREVKSLAADPDWWRGAVIYQIYPRSFQDSNGDGIGDLLGIVERMPYIASLGVDAIWISPFFTSPMKDFGYDISDYFDVDPMFGSLADFDALIETAHMYGLRVMIDLVLSHTSDQHPWFEESRSSRDNPKADWYVWADAKPDGTPPNNWLSIFGGSGWHWDARRCQYYLHNFLTSQPDLNFHCADVQDALLGVGRFWLDRGVDGFRLDTINFYVHDAELRDNPPLPPEERNSNIAPEVNPYNHQRHLYSKNQPENLEFLAKFRAMMEEYPAIAAVGEVGDAQYGLEILGQYTRGETGVHMCYAFEFLAQEKLTAKRVAEVLNKVDEVASDGWACWAFSNHDVMRHVSRWDLTPGAQRGMLTLLMCLRGSVCLYQGEELGLPEAEVAFDDLQDPYGIEFWPEYKGRDGCRTPMVWQSDNMSGGFSIHRPWLPVSTEHLGLAVAVQEEAPDALLHHYRRALAFRRAHPALVKGDISDVTVVGDVISFLRKDPEETVFVAINMSDAPGAVDLPPGNWMQIGAELNSGGTSPDGRVHLGPWQPCIALKAP Pseudomonas simiae WCS417 WCS417 GFF2490 PS417_12700 ABC transporter for D-Mannitol and D-Sorbitol, ATPase component Specific phenotype on D-Sorbitol; D-Mannitol. Also important for D-mannose utilization, but is closely related to a P. aeruginosa system that is apparently not a mannose transporter (the substrate-binding component PA2338 does not bind mannose, see PMC6829864). ABC transporter ATP-binding protein MANLKIKNLQKGFEGFSIIKGIDLEVNDKEFVVFVGPSGCGKSTLLRLIAGLEEVSEGTIELDGRDITEVTPAKRDLAMVFQTYALYPHMSVRKNMSFALDLAGVDKKLVESKVSEAARILELGPLLERKPKQLSGGQRQRVAIGRAIVRNPKIFLFDEPLSNLDAALRVQMRLELARLHKELQATMIYVTHDQVEAMTLADKVVVLNSGRIEQVGSPLELYHQPANLFVAGFLGTPKMGFLKGKVTRVESQSCEVQLDAGTLINLPLSGATLSVGSAVTLGIRPEHLEIASPGQTTLTVTADVGERLGSDTFCHVITANGEPLTMRIRGDMASQYGETLHLHLDPAHCHLFDTDGVAVARPLRAAA Pseudomonas simiae WCS417 WCS417 GFF2493 PS417_12715 ABC transporter for D-Mannitol and D-Sorbitol, periplasmic substrate-binding protein Specific phenotype on D-Sorbitol; D-Mannitol. Also important for D-mannose utilization, Also important for D-mannose utilization, but closely related to a P. aeruginosa system that is apparently not a mannose transporter (the substrate-binding component PA2338 does not bind mannose, see PMC6829864). sugar ABC transporter substrate-binding protein MKFTAKALLASTCMMTCMTLSAVSFGAQTLTIATVNNSDMIRMQKLSKTFEAEHPEIKLNWVVLEENVLRQRLTTDIATQGGQFDVLTIGMYEAALWGAKGWLEPMKDLPASYDLDDVFPSVRDGLSVKGSLYALPFYAESSITYYRTDLFKDAGLTMPEHPTWTQIGEFASKLTDKTKEQYGLCLRGKAGWGENMALITTLANGYGARWFDEKWQPEFNGPEWKDALNFYVDNMKKSGPPGASSNGFNENLALFNSGKCAIWVDASVAGSFVTDKTQSKVADHVGFTFAPHEKTDKGTSWLYSWSLAIPTSSKAKDAAKVFTSWATSKEYGELVAKTDGIANVPPGTRKSTYNDEYMKAAPFAKVTLESLKVADPTKPTLKPVPYIGIQLVTIPEFQAIGTQVGKFFSGALTGQQTVDAALTAAQTTTEREMKRAGYPK Pseudomonas simiae WCS417 WCS417 GFF2491 PS417_12705 ABC transporter for D-Mannitol and D-Sorbitol, permease component 1 Specific phenotypes on D-Mannitol; D-Sorbitol. Also important for D-mannose utilization, but closely related to a P. aeruginosa system that is apparently not a mannose transporter (the substrate-binding component PA2338 does not bind mannose, see PMC6829864). mannitol ABC transporter permease MTLQQSRRLQSLLLGTLAWAIAILIFFPIFWMVLTSFKTEIDAFATPPQFIFTPTLENYLHINERSNYFSYAWNSVLISFSATALCLLISVPAAYSMAFYETQRTKGTLLWMLSTKMLPPVGVLMPIYLLAKSFGLLDTRIALIIIYTLINLPIVVWMVYTYFKDIPKDILEAARLDGATLWQEMVRVLLPIAKGGLASTVLLSLILCWNEAFWSLNLTSSSAAPLTALIASYSSPEGLFWAKLSAVSTLACAPILIFGWISQKQLVRGLSFGAVK Pseudomonas simiae WCS417 WCS417 GFF2492 PS417_12710 ABC transporter for D-Mannitol and D-Sorbitol, permease component 2 Very important for utilization of D-sorbitol, D-mannitol. Also important for D-mannose utilization, but closely related to a P. aeruginosa system that is apparently not a mannose transporter (the substrate-binding component PA2338 does not bind mannose, see PMC6829864). sugar ABC transporter permease MNTTTPKNRLANPGWFLVSPSVALLLLWMIVPLGMTLYFSLIRYNLLYPGENEFVGLENFTYFITDSGFLPGATNTLLLVGSVLLISVVFGVLISALLEASEFLGRGLVRVLLISPFFIMPTVGALIWKNLIFHPVSGILAAVWKFFGAEPVDWLAHYPLLSIIIIVSWQWLPFAILLLMTAMQSLDQEQKEAARLDGAGAIAIFWHLTLPHLARPIAVVVMIETIFLLSVFAEIFTTTNGGPGYASTNLAYLIYNQALVQFDVGMASAGGLIAVVIANIAAIILVRMIGKNLTDKP Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2942 ABC transporter for D-Sorbitol, permease component 1 Specific phenotypes on D-Sorbitol. The homolog in P. simiae WCS417 is probably a mannitol transporter as well. Various polyols ABC transporter, permease component 2 MTVRRRSNFPLGLLALRTAAAWGVALLLFFPLGWLFLTAFKTELQAIAVPPLFVFTPTLENFHEVQERSDYLLYAKNSVITSVLSTVLGLMLAAPAAYAMAFFKGKYTKDILMWMLSTKMMPAVGALVPIYVLAQKSHLLDTQLALIIVFALSNLPIMVWMLYSHFKDIPHEILEAARMDGATLWQEVRLVLLPLGMGGLASTGLLCLVLSWNEAFWSLNLSAAKAGTLATLIASYSSPEGLFWAKLSAASLMAIAPIVVFGWFSQKQLVQGLTFGAVK Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2943 ABC transporter for D-Sorbitol, permease component 2 Specific phenotypes on D-Sorbitol. The homolog in P. simiae WCS417 is probably a mannitol transporter as well. Various polyols ABC transporter, permease component 1 VELRTSPPIAHATACPFSAAFFRCFDGLSMNRRLLPRLLLTPAMATLFLWMIVPLVMTIYFSLIRYNLMQPDQTGFAGLENFEFFVTDPSFGTAVVNTILLLGSVILITVVLGVAIALLINEPFPGRGIVRVLLISPFFVMPTVNALMWKNMMMNPIYGVLAQVWIFFGAAPVDWLTDHPLFSVIVMVSWQWLPFATLIFMTALQSMNHEQLEASRMDGANYLQQLRYLYVPHLGRSVAVVVMIELIFLLSIFAEIYTTTAGGPGDASTNVTFLIFKQALLNFDAGVASAGALFAVVLANIAAVFLIRMVGKNLDK Shewanella sp. ANA-3 ANA3 7023408 Shewana3_0638 smc-like chromosome partitioning protein (DUF3584) This gene has a conserved motility defect. and some close homologs are important for resisting cisplatin. DUF3584 is distantly related to smc proteins. hypothetical protein (RefSeq) MPSLIRIVLIDTHLPGVVELALNGHTNICGTNASGKTTLQRLVPVFYGEYPSRVVPSTRDSFERWYLPHDSSYIIYEYQKADGLLYQAVLASAGDGKGVNYRFIGKGFELSDYIKTQNGDTILCHTMAELGRELKRQGVATTNLLNTREYRAIIQNDRTLLSTGSNRSELRAYAHQFALCEGEHSLRHIEKLAKAVHSKEGKMETVKSMIAAILEEDGVNPPSSRLNPQRVEAWIRESQLIQGFEVIRPEFEKLEQEFNQLLSAEMRLSSLSRGYRNDETLEADRLEIQQTLSKELNLKLRMLDDEWKEVRDELNLDLSAAKGDVAKCEYELDAIEDQHGAFLDANIEQAKADLDMLPNWRADMENLSERHKLQTEKHQDIEAAYNARRSKIGEQLNRELEGLHAEQDKQREARDKQREVARADLDALEAQWRSQMDAGKASFSEQEYQFKLNAAELKLRVDGVTYTEEEKLSLAIFDERIHRADEEQESCNAKVERLTGEERKLRAKRDQANEALRIASLRVNERQTALDELHHMLFPQSHTLLEFLRKEAQGWEQSLGKVIAPELLHRTDLHPTVTGESDTVFGVHLDLKAIDVPEYAASEQELRIRLSKAEEALQSAQELQAEAESQLVAINGELDKLSRELTFARTAYKNSRDDLRRLFDEKRSEQDKINKALAERKAFAQQRLTQLDGELKQLKHQHQLWLEEQKEQALEARMEKQAYWQEVIGALDNQLGQIKATIDARRESAKAEQKACETWYKNELKSRGVDEDNILKLKQQIRELETKISRAEQRRSEVLRFDDWYQHTWLIRKPKLQTQLSDVKRAASEIDQQLKAKTQEVKTRRQQLETERKASDAAQIEASENLTKLRAVMRKLAELKLPANNEEAQGSLGERLRQGEDLLLKRDYLMGSVKQYVEHFDSVIASKSGSGLAETWERAREESSFINDKGIRLLDYRKLVPQLEQLLNVMVPQSIMALREQGRIFGVDLTAFYDVLADIDRRIASQSARITREVGEELFLDGVSESAVRIRSKISELEFWPELEQFVKAFKQWKADGFNGLPDEEYTNSMRRALDIIGRAALTGGIAKLLEIELRLKEGNSDLIIRTDRQLNESSSHGMAYLILCKFLLAFTRLLRGRADVTIHWPIDELGTLHHTNVKKIFDACGNNNISVLGAFPNPESEVLNLFENRYIINKQTKKLQVVKPKANPIADMLSKRLSKEAI Shewanella sp. ANA-3 ANA3 7023409 Shewana3_0639 predicted chromosome partitioning protein (with smc-like Shewana3_0638) conserved cofit with smc-like (Shewana3_0638) hypothetical protein (RefSeq) MSAAMNESNQTVLVGTGAIIELLLKGEFICRTTNEDGWRALKNNSTRERVEAYLNQINRTVASAAEGDVFFCGYLQLGESERKVISSQFKDICQALIPMVEWLVLVQEASGQDAPLSEGAPVRLTELQSRIEDTPAFREQLAKLSQYRLFGSTSTNSDAQIKLVFKRLVELGYLVRPNVEKQIYIATGKLDYLYEVIRFIDETEGLSLEAQAETATQRDLL Shewanella sp. ANA-3 ANA3 7023410 Shewana3_0640 predicted chromosome partitioning protein (with smc-like Shewana3_0638) conserved cofit with smc-like (Shewana3_0638) hypothetical protein (RefSeq) MSSNLHQAGVKLLKQLGRHADIIMDAYLAGSLKEESHDPAVVEKLKQAGILWRPEPDQELRLKRSVRALLEEGLSDERNRQIDSNVGSALATIKTLADHYKEARHSSDYSAAEAYLSDLSEHVYSFADSLRYSIRVLWGRINNEFGYVGTINAKIRENELAQSQVSELLNGLEMFQFSELGEIAGDIRELRKLLVTTLQETMSDCAQELSVVQGRLLELLGRFRQIRGRTRLLKGWLLYTDLHPDYRPADHVSHKEIPSLFNRAEVLLAPASVDVHNASQEFELMNIVAHIKAISRQGIVETVREQDVAVPLTQNEDFDIPDNPLKQAVDTYFVDVIESGLRQSALDYLAEKALPWDAESWIYQVIGGYEGLPDEHKAYFELEPLGEPHPIYSGNFIIRDVELWLA Shewanella oneidensis MR-1 MR1 203090 SO4006 predicted chromosome partitioning protein (with smc-like SO4008) conserved cofit with smc-like (SO4008) hypothetical protein (NCBI ptt file) MMSSNLHQAGVKLLKQLGRHADIIMDAYLAGSLNEDAHDPAVVEKLKQAGILWRPEPDQELRLKRSVRALLEEGLSDERNRQIDSNVGSALATIKTLADHYKEARHSSDYSAAEAYLSDLSEHVYSFADSLRYSIRVLWGRINNEFGYVGTINAKIRENELAQSQVSELLNGLEMFQFSELGEIAGDIRELRKLLVTTLQETMSECAQELSVVQGRLLELLGRFRQIRGRTRLLKGWLLYTDLHPDYRPADHVSHKEIPSLFNRAEVLLAPASVDVHNASQELELMNIVAHIKAISRQGVIETVREQDVSVSLTQSEDFDIPDNPLKQAVDAYFVDVIESGLRQSALDYLAEKALPWDAESWIYQVIGGYDGLPDEHKAYFELEPLGEPHPIYSGNFIIRDVELWLA Shewanella oneidensis MR-1 MR1 203091 SO4007 predicted chromosome partitioning protein (with smc-like SO4008) conserved cofit with smc-like (SO4008) hypothetical protein (NCBI ptt file) MSAMNESNQTVLVGTGAIIELLLKGEFICRTTNEDGWRALKNNSTRERVEAYLNQINRTVASAAEGDVFFCGYLQLGESERKVISSQFKDICQALIPMVEWLVLVQEASGQDAPLSEGAPVRLTELQSRIEDTPAFREQLAKLSQYRLFGSTSTNSDAQIKLVFKRLVELGYLVRPNVEKQIYIATGKLDYLYEVIRFIDETEGLSLEAQAETATQRDLL Shewanella oneidensis MR-1 MR1 203092 SO4008 smc-like chromosome partitioning protein (DUF3584) Conserved phenotypes: important for motility and cisplatin resistance. DUF3584 is distantly related to smc proteins. hypothetical protein (NCBI ptt file) MLIDTHLPGVVELALNGHTNICGTNASGKTTLQRLVPVFYGEYPSRVVPSTRDSFERWYLPHDSSYIIYEYQKADGLLYQAVLASAGDGKGVNYRFIAKGFELSDYIKSQNGDTILCHTMAELGRDLKRQGIATTNLLNTREYRAIIQNDRTLLSTGSNRSELRAYARQFALCDGEHSLRHIEKLAKAVHSKEGKMETVKSMIAAILEEDGVNPPSSRLNPQRVEAWIRESQLIQGFEVIRPEFEKLEQEFNQLLSAEMRLSSLSRGYRNDESLEADRLEIQQTLSKELNLKLRMLDDEWKEVRDELNLDLSAAKGDVAKCEYELDAIEDQHGAFLDANIEQAKADLDMLPNWRADMENLSERHKLQTEKHQDIEAAYNARRSKIGEQLNRELEGLHSEQDKQREARDKQREVARGDLDALEAQWRSQMDAGKASFSEQEYQFKLNAAELKLRVDGVTYTEEEKLNLAIFDERIHRADEEQESCNAKVERLTSDERKLRAKRDQANEALRIASLRVNERQTALDELHHMLFPQSHTLLEFLRKEAQGWEQSLGKVIAPELLHRTDLHPSVTGESDTVFGVNLDLKAIDVPEYAASEQELRIRLSKAEEALQSAQELQAEAESQLVAINGELDKLSRELTFARTAYKNSRDDLRRLFDEKRSEQDKINKALAERKAFAQQRLTQLDGELKQLKHQHQLWLEEQKEQALEARMEKQAYWQEVIGALDNQLGQIKATIDARRESAKAEQKACETWYKNELKSRGVDEDNILKLKQQIRELETKISRAEQRRSEVLRFDDWYQHTWLIRKPKLQTQLSDVKRAASEIDQQLKAKTQEVKTRRQQLETERKASDAAQIEASENLTKLRAVMRKLAELKLPANNEEAQGSLGERLRQGEDLLLKRDYLMGSVKQYVEHFDSVIASKSGSGLAETWERAREESSFINDKGIRLLDYRKLVPQLEQLLNVIVPQSIMALREQGRIFGVDLTAFYDVLADIDRRIASQSARITREVGEELFLDGVSESAVRIRSKISELEFWPELEQFVKAFKNWKADGFNGLPDEEYTNSMRRALDIIGRAALTGGISKLLEIELRLKEGNSDLIIRTDRQLNESSSHGMAYLILCKFLLAFTRLLRGRADVTIHWPIDELGTLHHTNVKKIFDACGNNNISVLGAFPNPESEVLNLFVNRYIINKQTKKLQVVKPKANPIADLLSKRLSKEAI Shewanella loihica PV-4 PV4 5210688 Shew_3116 predicted chromosome partitioning protein (with smc-like Shew_3118) conserved cofit with smc-like (Shew_3118) hypothetical protein (RefSeq) MSSNLHQAGVTLLKQLGRHADLIMDVYLSGSVTEEGERAGAIDKLRKADILWQPEGEQGLRLKRSVRALLEEVLSDERNRQIDANVGSSLATIKTLADHYKEARQAADYSASEAYLADLSEQVYSFTEGLKYSIRVLWSRINNEFGYVGTINAKIRENELAQSQVTELLNGLEMFQFSELGEIAGDIRELRKLLVTRLQETLSDCTQELSVVQGRLLELLGRFRQIQGRTRLLKGWLLYTDMHPDYEVADHVSHKQLPTLFNRAEAILAPAAVDVTNTAQEVELLAMVSQIKSISRAGRDLVMRDHDVPFALVEAEDFDIPDNPLKLAVDEYFCAVIDSGLRQSALDYHQAKSLSWDTESWLYQVICGYEGLPEEHRRYFELEPIGERHPVYSGNFIIRDVELWLA Shewanella loihica PV-4 PV4 5210689 Shew_3117 predicted chromosome partitioning protein (with smc-like Shew_3118) conserved cofit with smc-like (Shew_3118) hypothetical protein (RefSeq) MSSSTQTVLVGQGALIEALLRGEFICRTSNEDAWRALKSQATRDNVEQYLNQINRTLASAGEGEVFFCGYLQLGDDERKVISSQFRDICHALIPLVEWLVLVQEASGQDAPLSEGAAVRLNELQTRIEDTPAFREQLAKISHYRLFGSSSTQVDAQIKLVFKRLVELGYLLRPNQEKQIYIATGKLDYLYEVIRFIDETEGLSLEAQAETATQRDLI Shewanella loihica PV-4 PV4 5210690 Shew_3118 smc-like chromosome partitioning protein (DUF3584) Conserved phenotypes: important for motility and cisplatin resistance. DUF3584 is distantly related to smc proteins. hypothetical protein (RefSeq) MPSLNRIVLINTHLPGVVELALDGHTNICGTNASGKTTLQRLVPVFYGEYPSRVVPSTRDSFERWYLPHDSSYIIYEYRRDDGLLTQAVLASAGDGKGVNYRFIGKGFELEDYVKSQQGESILCHNMAELGREMKRAGVAVTNLLNTREYRAIIQNDRTLLSTGSNRSELRAYARQFSLCQHEHTLRHIEKLAKAVHSKEGKMETIKSMIAAILEEDGVNPPSSRLNPQRVEAWIRESQLIQGFEQIRPEFDKLEQEFNQLLSAEQRLAGLKRGYGKDEAQEIERQELNQQRSKDLGNKLRQLDDEWKELRDELNLDLSAAKGDVAKIEHELDIIEDQHAGFLDADIEQAKLDLEQLPSWRASLENLTERHKLQTEKHQDIEAAYNARRSKIGENLNRELEQLDKEQDKHREARDKQQEVGREELAALEQSWREQMEAGRAKHNEQEYQLKLTAAELQMQVNGVTYSEEEKLTLAVFDERISRADEEQEACNAMVDRLAGEERKLRAKRDQANESLRQAGLRVIERQGALDELHQVLFPQSHTLLEYLRKEVDGWEESIGKLINPELLHRSDLHPAKSAGGDSFCGVELDLKALTTPEYAASEQELRGRYSEAEEALANAKQLQAEAEEALVAINAELDKLNRELTFAKTAYKNSRDDLRRLFDEKRAEQEKINQALSARKADSQKRLARLDSEMKQLKAQHQEWIDEQNEQALEARMEKKAYWQEVVGALDVQLSQVKQNINDRRHAAKTEQKACEQWYKDELKSRGVDEAKIVKLKQEIRDLESSISKAEQRRSEVLRFDDWYQHTWLARKPKLQTELSQVKMAVTELSQQLTTKANEIKHQRQQYDSERKQSDAIQVEASENLTKLRAVMRKLAELKLPSSQDEMQGGLTERLRQGEELLLRRDQLMGSVKQYIEHFDSVIASKSGSSLSETWERAREESSFVNDKGIRLLDYRKLVPQLEQLLNVMVPQAIMGLREQGRNFGIDLTAFYDVLADIDRRIASQSARITREVGEELFLDGVSESAVRIRSRISELEFWPELEEFVKAFKQWKAEGFADLPDEHYTSSMRRALDIIGRAALTGGIAKLLEIELRLKEGNSDLVIRTDRQLNESSSHGMAYLILCKFLLAFTRLLRGRADVTIHWPIDELGTLHHGNVKKIFDACENNNISVLGAFPNPESEVLNLFANRYIINKQTKKLQVVKPQVNPIADKLSQRFAKEAV Shewanella amazonensis SB2B SB2B 6936404 Sama_0592 smc-like chromosome partitioning protein (DUF3584) Conserved phenotypes: important for motility and cisplatin resistance. DUF3584 is distantly related to smc proteins. hypothetical protein (RefSeq) MSSLQRIVLIDTHLPGVVELALDGHTNICGTNASGKTTLQRLVPVFYGEYPSRVVPSTRDSFERWYLPHDSSYIIYEYRRGDGMLYQAVLSSNGDGKGISYRFIAKGFELDDYVKARNGDALVCHTAAELGREMKRAGIAHTNLLNTREYRAIIQNDRTLLSSGTNRVELRSYARQFALCDAEHTLRHIEKLAKAVHSKEGKMETVKSMIAAILEEDGVNPPTSRINPQQVENWIRECQLIAGFEEIRPEFDKLEQEFNQLLSAELRLAGLHKGYKDDEVLEAERQERCQTASKEYNFRLRQLDDEWKEKRDELNQEISAARGDVSKFEHELEVIEDQHGAFLDADIETAKGDLEQLPLWRTDLENLSERHKLLTDKHQDVEAAYNARRSKIVEQLNRDLEVLDQDLDKQRDARERQAAAARSDLEKLEQFWRDQLEAGKNRFREEEYELKLAASEEKLRQDAVTYTEEEKLNLAVFDERIERADEEQEASNANVERLALEERRLRSRRDQASEALRLASIRVSERQNALDELKTMLFPQSHTLLEFLRKEAPGWEEHLGKVIAPELLHRTDLHPFNASSGADGNSLFGIGLDLKALDIPEYAQSEQELRSRLAKAEEALGSAREVQEAAEEQLVTINGELEKLSRELTFARTAFKNAREDLRRLFDEKRAEQDRVNKALAERKQLAGKRLVTIEHQLKQLGRDHQDWLEETKEESLEARMEKNAYWQEVVGALDAQIASVKTGIESRRANAKAETKACEQWYKNELKSRGVDEDKIVGLKADIRTLERKIADAEGRRADVLRYEDWYQHTWLSRKPRLAEELAKVRRAQSELEQQLARLSAEVKTQRSELESGRKASDAAQVEASENLTKLRSLLRKLADLKLAPTDDEAQGSIGERLRQGEELLLKRDYLVGSVKQYVEHFDTVIAAKSGSGLAETWERAREEATSINDKGIRILDYRKLVPSLEQLLNVMVPQSIMALREQGRIFGVDLTAFYDVLADIDRRIASQSARITREVGEELFLDGVSESAVRIRSRISELEFWPELEVFVAAFRRWKSDGFAGLPDEHYTNSMRRALDIIGKAALSGGIAKLLEIELRLREGNSDLIIRTDRQLNESSSHGMAYLILCKFLLAFTRLLRGSAQVTVHWPIDELGTLHHNNVKKIFDACENNNISVLGAFPNPESEVLSLFKNRYIINKQTRKLQVVKPKSNPIADKLASRISREAV Shewanella amazonensis SB2B SB2B 6936405 Sama_0593 predicted chromosome partitioning protein (with smc-like Sama_0592) conserved cofit with smc-like (Sama_0592) hypothetical protein (RefSeq) MSEANFSGIGTGLVGHGALIERLLRGEFICRVTDEDGWRALKSPAVRERIETYLNQINRTVASAGEGEVFFCGYAQLGEAERKVISSQFKDICQALIPLVEWLVLVQEASGQDTPLTEGAPVRLTELQGRIEETPAFREQLGKLSQYRLFGSTSSNVDAQLKLVFKRLVELGFLTRPNVEKQIYIATGKLDYLYEVIRFIDETEGLNLEAQAETATQRELI Shewanella amazonensis SB2B SB2B 6936406 Sama_0594 predicted chromosome partitioning protein (with smc-like Sama_0592) conserved cofit with smc-like (Sama_0592) hypothetical protein (RefSeq) MSSNLHQSGVRLLRMLGRHAETVMDVYLSGAVDEANADAGVLKKLTEAGILWRPEEDEGLRLTRSVRALLEEGLKDERNRQINANVGSALATIKTLANHYKEARSHSDYSAAEAYLADLSEHVYAFTENLRYSIRVLWGRINNEFGYVGTISAKIRENELAQSQVSELLNGLELFQFSELGEIASDIRELRKLLVTTLQETLSDCTQELSVVQARLLELLGRFRQIQGRTRLLRGWLLYTDMHPDYEPMDHVAHRKVPMLFNRAEAMLADAHVDVHNQSQEQELMEMVARIKSISRLDLKPAVKAAETSVVLSAAEDFDIPENPLKQDVDDYFVAVIDSGKRQSALVYLQEKALPWDSESWIYQVIGGFEGLSEEHKSFFELEPLGEPHPVYTGNFIIRDVELWLS Kangiella aquimarina DSM 16071 Kang B158DRAFT_0994 B158DRAFT_0994 putative adhesin (DUF1302) Similar to PA3923, which binds laminin (PMC6890786) and is involved in biofilm formation (PMC8547006), so this is probably an adhesin. Protein of unknown function (DUF1302). MKNTGLNHKSSPMTRLSQIAAGVALAVSAASSQAVNWDTENYDVNFDTTLSVGVGVRVEERDRNLVGKSNLYQIENGQPISNAYLSGDVPPGAWSNNSDDGNLNFDKGDFFSQVIKGVHELDIRHKDGDQGLFARGLWYYDRILMDTELPFRNLDSYGGQDGRNTAREEQGYDARMLDMYVWKTFEFDSGNVMQVRLGEQVVSWGESTFIQHSLSEANPVDLRTLRNPGAELKEAFIPTSMIWTSFDLSESWNMEAFYQFEFEEVKFDEPGTYFSTRDFLGLKGEEVHLGFAQYPEGQPGTVALRDETRFADDQGQFGVKVGYFTEYGTEFGFYYMNYHNRRPIISANAANAEGVVTGFLEYPEDIQMYGLSFNTATDSGLSVAGEISYRVDEPLQVDDVELLFATLEPIGQIPSGTSQVANGVGLGEEISGYRLLDTVQAQMTVTSLLGPVFGSDQTAFLVEVGANQILDMPSQDELRFESEGTFRSGNPDRAIDYNGNGTIDGLFGFDPTGTSPCGFTNPTTGQRIRTECEGMTENGFADEFSWGYRMAMRWDYNNVFSGWNMSPRIVFQHDVSGNTPAPISNFLEGRKSLSAGVSLSTLSAWKWDFAYNSYFGGGSANLISDRDHVSLALSYSF Kangiella aquimarina DSM 16071 Kang B158DRAFT_0995 B158DRAFT_0995 adhesin-associated sorting protein (DUF1329) Conserved cofit with a putative adhesin (B158DRAFT_0994). DUF1329 is distantly related to lolB, which inserts lipoproteins into the outer membrane. So we predict that DUF1329 is involved in sorting the adhesin to the outer membrane. Protein of unknown function (DUF1329). MTKVMNKWLLAGAVVSAMCTSVASAKVSEEKAAQLGGEIYTPMGSIRAGNEDGTIPAWTGGITEDMIPEGYQEGDHHPDPFAGDEKLFTIDASNYQQYAEHLTVGQIALFKAYPDRFKMHIYPTRRSASYPQHVLDAVKANATRAELIQEGNGIKGAAIGIPFPFPENGLQLIWNSITRYRGVSVEREVGQAAPLPDGDYVLVKLKDELHHIYNQPDMTPEKLEEGNVLFLFRQNVTAPARLAGTALLVHETMDQVKEPRKAWTYNTGQRRVRRAPNVAYDAPGTASDGLRTTDDFDMFNGAPDRYNWTITGKKEIYIPYNTYKLHSDEVTYDEIIQPGVINSDLVRYEKHRVWVLEANLKEDTRHQYKKRVFYIDEDSWQIAAEEMYDERGELWRVAMAYLVNYYDVPTLWSTLEAYYDLPSGRYLVIGLDNQENMYNFKVEFSDSHFTPSALRRAGIR Kangiella aquimarina DSM 16071 Kang B158DRAFT_0996 B158DRAFT_0996 adhesin-associated BNR repeat protein Conserved cofit with a putative adhesin (B158DRAFT_0994). This is also predicted to be an outer membrane protein. Uncharacterized protein related to plant photosystem II stability/assembly factor MKAIIKYAFPLVLLFTGIQVSSSAETEPALIADKAVKSLLLDVEMLESGRLVTVGERGHILLSDDQGIEWRQVPVPTREQLTAVDFLDDKRGIAVGFSQTILMTNDGGESWQLTHHEESFEQPALFDVQFINGDKIVAVGSYGLYLESSDGGETWEAQEVEGLADYYGFFSHFYSIQKVTDDYWVMAGEKFIDGVDEDGFETSSALAAETRDGGETWQKLPTPYDGSFFGIEVDDKGYLYVYGLRGNLYISKDAGQSWQGQFLSTASGFHDMAILDENRWVLVGTGGVLVYKTLTSTDIKKRKDLKGRAAVVAVDEDTLVVVGDGGVERLSLSQQ Kangiella aquimarina DSM 16071 Kang B158DRAFT_0997 B158DRAFT_0997 adhesin-associated MmpL efflux pump Conserved cofit with a putative adhesin (B158DRAFT_0994). The MmpL family is involved in efflux of lipids or siderophores (see IPR004869); we speculate that this exports a lipid or saccharide that is attached to the adhesin. Predicted exporters of the RND superfamily MTKNKLESIVSKVFFSKRALWISLFAVFTAVMVYFVTQLRVDASFEKNIPLKHEYMQTYIEYQDQFGGANRVLVALEDTSGNIFNASFFEALKETTNRVAGIAGVNQPQVESLFTPNTRYIEASEQGLEGGPVIPARFDGSERALKQVEENILKAGIVGRLVSNEFESAMVSAQLLSEYNPTDVEVTGENGEQMVQTDFVRVAHDLEKIRTDIEAKYPNVEVHIIGFSKMIGDVSDAAGGVIVFFLIALAITALLVYWYSRSIKLTALPILTSIIAVVWQLGLLTALGYGIDPMSILVPFLIFAIGVSHGVQMINGVQHNVAHGMKTYNAAIAACAALIVPGGIALLSDTVGFLTLQLIEIDIIRELAVTASIGVAVLILTNLLLLPLLLSYTHFSDKFVQSVRDREHAREKWWKKIAGFARKPASTIIIIVSLLLGIIGYWQSLNMKVGDLQSGAPALRQDSTYNLDNKYITDTYAIGTDVIYVLAKTKTDGCTYYDIMNNIDQFQWEMNNVKGVQSTISLPQVAKVVNGMLSEGNLKWKMLPKDEAVLVQSISRVETSTGLLNSDCSVMPVMIFLDDHKAETIERLVSAVKDFRANKAHEEVEYLLATGPVGVMAATNEAVSAAQIPMMIWVYLAVTLLCLISFRSVRGTICVILPLVVVSFLAQALMTWLQIGLTVATLPVIALGVGIGVDYGIYIFSRMVGFIRSGMSVADAYFETLKLTGNAVLFTGLTLAIGVSTWLMSALQFQADMGIMLTFMFLVNMLGAIILLPALAALLYRR Pseudomonas stutzeri RCH2 psRCH2 GFF1089 Psest_1122 putative adhesin (DUF1302) Similar to PA3923, which binds laminin (PMC6890786) and is involved in biofilm formation (PMC8547006), so this is probably an adhesin. Protein of unknown function (DUF1302). MTKTTRQGIFQPKSLALAVALSIAAPAYAVNFNIGEIEGQFDSSMSIGASWSTTDRDMDLVGINNGGTGFTQTGDDGRLNFKKGETFSKIFKGVHDLELRYRDSGAFIRGKYWYDFELKDESRLFKDISDSNRKEAAQSSGAQILDAFVYHNYALGDLPGTVRVGRQVVSWGESTFIGNSINSINPLDAAAFRRPGAEIKEGLIPVNMFYVSQSLTDRLSMEAFYQIEWDQTIADNCGTFFAVDVVQDGCDTNYHVGNPAIAPLQPVAAAFGQGFEVTPEGVILPRAGDRDARDSGQYGLALRWLGDATEYGAYFMNYHSRTPNVSTQTAGLATAAQLGNIIGTAESIAPGSGAGLASSVMLGNGSYYLEYPEDIQLYGLSFSTTLPTGTAWSGEISYRPNAPVQLNTQDVTRALLNPIAPGTSPIESSFGAENRGYNRKEITQIQTTFTHFFDQVLGAGRVTVVGEIGYAHVGGLESTSELRYGRDAIYGSVDDPTALARYGRHGFVTANSWGYRLRTIADYNNVFAGINLKPNLSFSHDVDGYGPNGLFNEGSKAVSIGLDAEYQNTYTASLSYTDFFGGDYNTLVDRDFLAFSVGVNF Pseudomonas stutzeri RCH2 psRCH2 GFF1090 Psest_1123 adhesin-associated sorting protein (DUF1329) Conserved cofit with a putative adhesin (Psest_1122). DUF1329 is distantly related to lolB, which inserts lipoproteins into the outer membrane. So we predict that DUF1329 is involved in sorting the adhesin to the outer membrane. Protein of unknown function (DUF1329). MKTTRKLFSVLAFSLLASSVMAAVSPEEAAKLGTSLTPLGAEKAGNADGSIPEWTGGLKTDAAPLKNGHLTNPFKDEQPKFVITAQNAEQYKDKLTAGQLAMFKRYPETYKIRVFPTHRSVAVPDEIYQAAKKSAVNTELVEGGNGIANFTDSRYYAFPIPKNGLEVVWNHITRYRGGNVRRNIVQATPQTNGSYTMVHFEDEVAFPLGMTDLDPERAKNALLFFKQRVTAPSRLAGNVLLVHDSLDQVKDPRQAWIYNAGQRRVRRAPQVAYDGPGTASDGMRTTDNFDMFSGAPDRYDWKLVGKKELFIPYNSYEIASSDLKYKDVIKAGHVNQDLARYELHRVWEIEATLKSGERNIYAKRRFFVDEDSWTIVQSELYDGRGQLWRVGEAHSLQYYQHKVPAYAFEALYDIISGRYIAIGMSNEEKPHEYGYRASARDFTPAALRNAGVR Pseudomonas stutzeri RCH2 psRCH2 GFF1883 Psest_1923 adhesin-associated BNR repeat protein Conserved cofit with a putative adhesin (Psest_1122). This is also predicted to be an outer membrane protein. Uncharacterized protein related to plant photosystem II stability/assembly factor MSEPVLRRTLSGRAKVANQARASRFHSSVAGMLSLCGTFSLLLLAASAPAQAATDGQTRYSIESAKAASNLLLDITQAGDRIVAAGDRGHILYSDDEGTSWTQAKVPTRQLLTAIDFIDAKHGWAVGHDALVLATADGGESWAVQYEEREREAPLLDVWFEDTQHGIAVGAYGALIETIDGGQSWDDISERLDNEDGFHLNAITHIEGSGLFVVGEMGGMFRSADMGETWERVDSPYKGSFFGVVGGSEPGVVIAFGLRGHLFRSTDFGDSWQAIELSNGNGQALESGLADGSLLRDGRIAVVGHGGAVLTSDDQGRSFKLVNRPDRRSLSGVTSDSQGNLILVGQGGVRIASPSGADLAPKQ Pseudomonas stutzeri RCH2 psRCH2 GFF1884 Psest_1924 adhesin-associated MmpL efflux pump Conserved cofit with a putative adhesin (Psest_1122). The MmpL family is involved in efflux of lipids or siderophores (see IPR004869); we speculate that this exports a lipid or saccharide that is attached to the adhesin. Predicted exporters of the RND superfamily MTKHQQKPASFLERLIFNNRPAVVVLCLLISAFLFYQAAQVRPQTSFEKMIPLAHPYIQKMLEHQNDLANLGNTVRISVEAVEGDIFSKEYMETLRQIHDEVFYIHGVDRSNMKSLWSPSVRWTEVTEEGFAGGEVIPQTYDGSPESLDDLRDNILKSGQIGRLVANNFKSSIIDVPLLESYPDPEDQSRQIKLDYQKFSHELEEKIREKYQAQNPNVKVHIIGFAKKVGDLIDGLVGVALFFIVAIGITFVLLLWFTRCLKSTIAVLITTLIAVTWQLGLLHTLGFGLDPYSMLVPFLVFAIGISHGVQKINGIAMASGYTEDPVTAARMAFRQLFIPGMVALLSDAVGFVTLLLIDIGVIRELAIGASLGVAVIILTNLILLPVAISYMGISQRAIKQAREEASRDHPFWRALSNFASPKVAPISITIAVVALAGGLWYGQNLKIGDLDQGAPELHPDSRYNLDNDFVIRNYSTSSDVLVVMVKTAPEGCSHYDTLAAMDELMWKMQNTEGVQSAVSMVSVARQGIKGMNEGSLKWETLSRNPHVLNNSIARAEGMYNSDCSLAPVLVFLNDHKAETLEHVVAAAKDFAEENNREGLEFVLAAGNAGIEAATNEVIAASETTMLIAVYLAVSIMCLLTFRSLAATLCVILPLVLTSILGNALMAFMGVGVKVATLPVIALGVGIGVDYGIYIYSRLESFLRQGMTLQEAYYQTLKSTGKAVIFTGVCLAIGVVTWVFSAIKFQADMGMMLTFMFLWNMVGAIWLLPALARFLIKPEKLRQKA Shewanella amazonensis SB2B SB2B 6937424 Sama_1588 putative adhesin (DUF1302) Similar to PA3923, which binds laminin (PMC6890786) and is involved in biofilm formation (PMC8547006), so this is probably an adhesin. hypothetical protein (RefSeq) MKSVKKGFNKTALSLGVASALSLGSIPAQAVSFDWGEVQGSFDSTFTLGASWRVEKRDWDGQIGKVNHPRFDWSNYSAFGNTKYTSAEIWAQPGSYSSNNDLSNLLYSQGDTTSEIFKGLHELSLKYENFGLFARGMYFYDRKLNDGDFGFSDPITGKEFDPCADKRAKELQCKDIRLLDAFVYANFDFNDGQNPLTVRVGNQVVSWGESTLIAHGIGVINPVDLNILNAPGAELKEAFRPQGMVWASLGVTENLSLEAFYQYDWQPIWVPTPGSIFATNDFAGYGGYQQNAQLGFNANPDINLDFIQAEYEKLAQMIVAGAFSSPEGTQSLIRAALAYPTKVTLIQDEAEASDDGQYGIKLGYYAPELGETEFGLYYMNYHSRRPLISGTAANFDLVPLLTDMTTVGMNAGNIDRNLILGLESFSKAQIVYPEDIQLYGFSFNTLIGDTSVAGEIAHRQDEPLQIDDVELLFAAMPQQLANSNVVGGDYSYLDGLSQYTSYFNKDVNPGDYAEGFIRVDTTQAQFTLTHLFGPTLGTDNLTMLAEVGGIWIHDMPSPDELRLNGPGTARSGGKEGYEAIIQVLHNGPETNPFPTDFAWGYRIVAKADYNNLFAGINVSPRVIWSHDVDGITPDPLFLFTEGRKSVAVGINFDYQSRWGADLSYNSFFGGVGTTNAMSDRDYVSFNIKYSI Shewanella amazonensis SB2B SB2B 6937425 Sama_1589 adhesin-associated sorting protein (DUF1329) Conserved cofit with a putative adhesin (Sama_1588). DUF1329 is distantly related to lolB, which inserts lipoproteins into the outer membrane. So we predict that DUF1329 is involved in sorting the adhesin to the outer membrane. hypothetical protein (RefSeq) MKKLAILSAAVMFALGGGAAVAKVSEAEAAKLGTSLTPMGGEMAASADGSIPAWNGGITAAPAGYKKGDHHPDPYSADKVEYTVTKANLEQYKSLLTPGQIKLFELYPDTFKMNVYKTQRSASAPQWVYDATKANASRAELVQGGNGVVGAAVGIPFPIPQNGLEAIWNHILRFRGVDIETQRNQAAPAKGGGYTLVELSEQLRFEYSQPDMTPEKLKENNTLALFKQVVTQPARLAGTALLVKETLDQEALPRQAWTYNTGQRRVRKAPNVAFDTPGTVSDGLRTTDDYDMFNGSPSRYNWELVGKKEILIPYNDYKLHSDKVKYDDILTPGHINPDLVRWEKHRVWEVKATLKDGMRHIYKTRVFFLDEDSWQVSATDMYDNRDELYRVAFAHGLNYYEVPAHWSTLEVFHDLQSRRYLAIGLDNEGSMYDFDAKLSASDFTPDALRREGVR Shewanella amazonensis SB2B SB2B 6937426 Sama_1590 adhesin-associated BNR repeat protein Conserved cofit with a putative adhesin (Sama_1588). This is also predicted to be an outer membrane protein. BNR repeat-containing protein (RefSeq) MLLRVLLPLSLLSLAAMSAQAADSPGHQLQPNAIKSLLLDVVNAGEYLVAVGERGHVLLGNGSWQQVETPTDAQLTKVFFLNNQLGWAVGHDATIIHTQDGGKTWNKQFSAPERERPFMDVLFVDDKRGFAVGAYGLFFTTFDGGKQWQEVFHQELLFEEDLAYLNELKDTDPEAYAIERASLLPHFNRLLRLNDGRLLMVGELGLVAVSDNNGDSFTRLPFDYEGSMFSAIQQGDSVYVMGLRGHVFEAGLALDDWQQLDLPVESSINGALADDKGTIYFVGNAGVILSKPDGEEVSLVARRQGENLVAAAKDSRGKVWLVGAKGVFALEDAQKH Shewanella amazonensis SB2B SB2B 6937427 Sama_1591 adhesin-associated MmpL efflux pump Conserved cofit with a putative adhesin (Sama_1588). The MmpL family is involved in efflux of lipids or siderophores (see IPR004869); we speculate that this exports a lipid or saccharide that is attached to the adhesin. hypothetical protein (RefSeq) MLERLVNGFESFLFRHRGWVISIFVLLTAFLGYQASQLKMDAAFVKNIPLNHSYMQTYLKHQKDFGGANSIMVAVEDTSGNIFNPVFFDALKNVHDQLFFIPGIERSQVKSLFSPSTRFTEVVEDGFAGGPVIPADYVNDDIGLAVVRDNIEKAGIVGRLIAEDYSAAMVSAQLMDFDPQTGEPLDTIALAAKLENELRGKYETDTIKVHIIGFAKMAGDVADGAKGVLLFFLIAIAITAVMVFLFSRSLVLTLLPLSCSLIAVVWQLGLLTVVGFGLDPMSILVPFLVFAIGVSHGVQIINAVRQRVLDGQQTKAAAASAFRSLLVPGGVALLSDTVGFITLLAIDIGIIRELAISASLGVAVIIFTNLILLPIVISFFEIKTKEGNGRAERSKAFWQPFSRFADIRVAAVVLLATAGVYALGLKGASEMKIGDLQGGAPALHADSRYNQDTFFITDHFSITTDVMTIITEAYPEACTYHDALERIGEFEWQVGNTPGVESTASLASIARKVNAGFNEGNPKWEVLPRNTSSLVQAVGQIPTTSGLLNGDCSVMPVYLFLKDHKAETIEAVVAKVKAVSAELNTDKIQFKLASGPVGVMAATNEAVAEAQTPMMLYVYGAVFVLCLVSFRSLRATIAVILPLYVVSTLAQALMTKLEIGLAVSTLPVIALGVGIGVDYGIYILSTMAVKLRDGMAVQQAYLEALQERGSAVIFTGLTLAIGVSTWFFSALKFQMDMGILLTFMFLVNMLGAIIILPALTAVFWPNRR Pseudomonas putida KT2440 Putida PP_0765 PP_0765 putative adhesin (DUF1302) Similar to PA3923, which binds laminin (PMC6890786) and is involved in biofilm formation (PMC8547006), so this is probably an adhesin. conserved exported protein of unknown function MKSANLFWRRAKLPLAVSLASTLASPAFAVSFNIGEIEGQFDSSLSIGASWSTANPNKNLIGVNNGGKGLSQTSDDGHLNFKKGETFSKIFKGIHDLELKYGDTGVFVRGKYWYDFELKDENREFKDISDSNRKEGAKSSGAELLDAFVYHNYSIGDQPGSVRFGKQVVSWGESTFIGGGINSINPIDVSAFRRPGAEIKEGLIPVNMFYISQSLTDNLSAEAFYQLEWDQTVVDNCGTFFSQPDIIADGCTDNLRVLNSSRTVPGAAQQFLATRGVNINEEGVMVRRGADRDARDSGQFGVAMRYMFEPLDTEFGAYFMNYHSRAPIFSATGAPPSVFAGLSALPAQLRALAPLIVAGNSEYFVEYPEDIRLYGLSFSTTLPTGTAWSGEVSYRPNAPVQLNTTDILFAGVRPIGGALSNASLLTGTPGQDLHGYRRKEITQFQTTLTHFFDQVMGASRMTVVGEVGVTHVGGLENAHDTRYGRDPVFGPGPLPSTGGADTCQALNGSTIAGAGAGASTANLNRKCENDGYTTSTSWGYRGRVIWDYNDVFAGINLKPSVAWSHDVSGYSPGPGANFEEGRKAVSLGLDAEYQNTYTASLSYTNFFDGKYSTVDDRDFVALSFGVNF Pseudomonas putida KT2440 Putida PP_0766 PP_0766 adhesin-associated sorting protein (DUF1329) Conserved cofit with a putative adhesin (PP_0765). DUF1329 is distantly related to lolB, which inserts lipoproteins into the outer membrane. So we predict that DUF1329 is involved in sorting the adhesin to the outer membrane. conserved exported protein of unknown function MNKTRSLLQAGVLGLSLLATSVMAAVSADEAAKLGSTLTPMGAEKAGNADGSIGPWEPLSKTAGSVDGKGFLSDPYGSEKPLFTITAQNADQYKDKLSPGQLAMFKRYPNTYKIPVFKTHRGATVPADVFAAIKENATKTTLVEGGNGLSNFRTAVPFPIPKSGLEVIWNHITRYRGGSVSRLVTQATPQQNGSFNPVYFSDQFVFRDKMKDYDPNNPGNILFYFKQEVTAPARLAGTVLLVHETLDQVKEPRKAWIYNAGQRRVRQAPQVSYDGPGTAADGLRTSDNLDMFNGAPDRYDWKLEGKKELYIASNAFKLDDPKLKYADIIKAGHINQDLARYELRRVWHVVATLKPGQRHIYAKRDFYIDEDTWQAAVIDQYDGRGQLWRVSEAHAQPYYNVEVPWYTLEAIYDLQSGRYLALGMKNEEKRAYDFGFSASKADFQPAALRQSGIR Pseudomonas putida KT2440 Putida PP_2018 PP_2018 adhesin-associated BNR repeat protein Conserved cofit with a putative adhesin (PP_0765). This is also predicted to be an outer membrane protein. BNR domain protein MWADSAQAAAADQYSTESAKASQSLLIDATHAGKRLVVVGDRGHILFSDDQGSTWTQARVPTRQLLTAVFFLDDKRGWAVGHDAQILASTDGGATWSKQFEDLAREAPLLDVTFLDAQHGFAVGAYGALLETTDGGQHWQDVAERLDNPDQLHLNGIAQVRDAGLFIVGEQGGMFRSTDNGQTWAKVQGPYEGSLFGVIGTARPQTLLAYGLRGNLFRSSDFGDNWQPIELKAARGTLEFGLAGATLVDDGTLVLVGNGGSVLRSTDDGQTFSVYNRADRLALAGVSGLANGGLLLVGQGGVHLASAEGADQPAPEVRP Pseudomonas putida KT2440 Putida PP_2019 PP_2019 adhesin-associated MmpL efflux pump Conserved cofit with a putative adhesin (PP_0765). The MmpL family is involved in efflux of lipids or siderophores (see IPR004869); we speculate that this exports a lipid or saccharide that is attached to the adhesin. putative multidrug efflux transporter, RND family MTSRESITMHPHHQDKATLLERLIFNNRPVVIALCVLVSIFLFWQATQIRPSTSFEKMIPLQHPFIEQMMEHRNDLANLGNTVRISVEAVNGDIFDKDYMETLRQIHDEVFYIPGVDRAGLKSLWSPSVRWSEVTEEGFSGGEVIPNTYNGSQDSLDTLRDNVLKSGQVGRLVGNNFKSSIVDVPLLESYPDPQDPGKQVKLDYQQFSHLLEEKIRDKFQAQNPNVKIHIVGFAKKVGDLIDGLVMVAMFFGVALVITLVLLYWFTWCIRSTVAVLITTLVAVVWQLGLMHAVGFGLDPYSMLVPFLIFAIGISHGVQKINGIALQSSDADNALTAARRTFRQLFLPGMIAILADAVGFITLLIIDIGVIRELAIGASIGVAVIVFTNLILLPVAISYVGISKKAIERSKKDATCEHPFWRLLSNFASAKVAPVSVVLALLAFAGGLWYSQNLKIGDLDQGAPELRPDSRYNQDNNFIISNYSTSSDVLVIMVKTPSEKCSVHSTMAPIDELMWTMENTPGVQSAISLVTVSKQVIKGMNEGSLKWETLSRNPDILNNSIARADGLYNGDCSLAPVLVFLNDHKAETLERVTAVAKAFADSHDKEGLQFLLAAGNAGIEAATNEVIKSAELTILILVYICVAVMCLITFRSFAATLCIVLPLVLTSVLGNALMAYMGIGVKVATLPVVALGVGIGVDYGIYIYSRLESFLRAGLPLQEAYYQTLRSTGKAVLFTGLCLAIGVCTWIFSAIKFQADMGLMLTFMLLWNMFGALWLLPALARFLIKPEKMVGKEGGSIFAH Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_04594 H281DRAFT_04594 putative oxepin-CoA hydrolase (EC 3.3.2.12) H281DRAFT_04594 is specifically important for phenylacetate utilization via the oxygenase pathway. This pathway requires an oxepin-CoA hydrolase, which is often provided by a (R)-specific enoyl-CoA hydratase (R-ECH) domain which is fused to 3-oxo-5,6-didehydrosuberyl-CoA semialdehyde dehydrogenase ("PaaZ"). But P. bryophila has a PacL-like semialdehyde dehydrogenase (H281DRAFT_05724), which lacks the R-ECH domain. H281DRAFT_04594 has an (S)-specific ECH domain and is probably the missing oxepin-CoA hydrolase. (There are no chiral centers in the oxepin-CoA reaction.) H281DRAFT_04594 is also related to paaF (2,3-dehydroadipyl-CoA hydratase), but that activity is probably provided by H281DRAFT_05725. short chain enoyl-CoA hydratase /Enoyl-CoA hydratase MSAELLTSRPTESESTLVLTLSNPGARNALHPDMYAAGIEALDSVERDPSIRAVVITGADNFFCAGGNLNRLLENRAKDPSVQAQSIDLLAEWISALRLSSKPVIAAVDGAAAGAGFSLALACDLIVAADDAKFVMSYARVGLTPDGGGSWFLAQALPRQLATEVLIEGKPIGAARLHELGVVNKLTKPGTARDAAIAWADELGKISPNSVARIKTLVCAAGTQPLSEHLVAERDNFVASLHHREGLEGISAFLEKRAPVYK Paraburkholderia bryophila 376MFSha3.1 Burk376 H281DRAFT_00361 H281DRAFT_00361 (3S)-hydroxyadipyl-CoA dehydrogenase (EC 1.1.1.35) / enoyl-CoA hydratase domain H281DRAFT_00361 is specifically important for phenylacetate utilization via the oxygenase pathway. This pathway require a (3S)-hydroxyadipyl-CoA dehydrogenase (forming 3-oxoadipyl-CoA), which is probably provided by the aldehyde dehydrogenase domain of H281DRAFT_00361. H281DRAFT_00361 is 49% identical to PimB from Rhodopseudomonas palustris; the pim operon is involved in dicarboxylic fatty acid degradation (PMID:15758219), which is consistent with activity on (3S)-hydroxyadipyl-CoA. H281DRAFT_00361 also has an enoyl-CoA hydratase domain, whose role (if any) in phenylacetate utilization is not clear. short chain enoyl-CoA hydratase /3-hydroxyacyl-CoA dehydrogenase MSLTTSTDVVTRELRGKVLLVTIDHAPVNALSADVRRGLLAAIEAADSDPSVQAVLIVGAGRNFIAGADIREFGKPPVPPSLPDVCNRIEACTKPVVAAIHGAALGGGLEVALAAHYRLAVDGAKLGLPEVQLGLLPGAGGTQRTPRLIGAQAALDLMLSGRHANAQEALALGLVDRLGSSDDILAEGLAYVHELLAGHAPVRRTRDATALNDRASSLAAVATARAETAKKSRGLFSPLKIVDAVEAAIAQPFEDGLRRERQLFLECLDSPQRAGLVHAFFAEREVLKAPETRDTKPRALNAIGVVGGGTMGAGIAVAVLDAGLPVTMIERDEASLARGRAHIEKVYDGLIAKGRMSAEKKAQLMARWTGSTSYDALADADLVIEAVFEDLSVKQAVFAELDRVCKPGAVLATNTSYLDIDAIAASISRPADVIGLHFFSPANIMKLLEVVVPKAVSADVVATAFELAKKLRKTPVRAGVCDGFIGNRILAVYRSAADAMMEDGASPYQIDAAVRAFGFPMGPFQVVDLAGGDIGWAARKRRAATRNPAARYVQIADRLCERGWFGQKTGRGFYLYPEGSRSGQPDPEVEAIIDAERVRAGITPREFSDDEIIRRYMAAMINEGANVVHERIALRPLDVDVTFLYGYGFPRYRGGPMKYADMIGLPRILADIREFAKEDPLFWRASPLLIDLVERGADFASLNHAA Bacteroides thetaiotaomicron VPI-5482 Btheta 353936 BT4410 endo-hyaluronase # Specifically important in carbon source Hyaluronic acid sodium salt from Streptococcus equi. 68% identical to endo-hyaluronanase ALJ61728.1 (PMID:30850540). Probably functions with the BT4411, which has a similar phenotype and is probably a hyaluronic acid binding protein. hypothetical protein (NCBI ptt file) MNRMKHLICVFLLATFGSFSFKANAYTERDMLQKAADETTLKNVLVMKQAWVPYPAYTDRAAWDSLMGSNKQRLIAAGEKLLDYKWQLIPATAYLEYERTGNRKIMEVPYDANRQALNTLMLAELAEGKGRFIDQLLNGAYMSCEMNSWVLSAHLPRQSSKRSLPDFREQIIDLGSGGYGALMAWVHYFFRKPFDKINPVVSLQMRKAIKERILDPYMNDDDMWWMAFNWQPGEIINNWNPWCNSNALQCFLLMENNKDRLAKAVYRSMKSVDKFINFVKSDGACEEGTSYWGHAAGKLYDYLQILSDGTGGKISLLNEPMIRRMGEYMSRSYVGNGWVVNFADASAQGGGDPLLIYRFGKAVNSNEMMHFAAYLLNGRKPYATMGNDAFRSLQSLLCCNDLAKETPKHDMPDVTWYPETEFCYMKNKNGMFVAAKGGFNNESHNHNDVGTFSLYVNTIPVILDAGVGTYTKQTFGKDRYTIWTMQSNYHNLPMINGIPQKYGQEYKATNTTCNEKKRVFSTDIAAAYPSEAKVKNWIRSYTLDDRKLTITDSYTLEEAVAPNQVNFMTWGNVTFPSQGKIQIEVKGQKVELDYPTLFKAELETIQLDDPRLSNVWGKEIYRITLKTNEKKETGNYKFVIQQIK Bacteroides thetaiotaomicron VPI-5482 Btheta 354178 BT4652 heparan sulfate cleaving enzyme # Specifically important in carbon source Heparin sodium salt from porcine intestinal mucosa. 66% identical to the heparan sulfate cleaving enzyme ALJ58962.1 (PMID:30850540) conserved hypothetical protein (NCBI ptt file) MKQRYYIFLLFVAMLSYSGYAQKSILRLSQQTLMHEVRETPSPLGGQHIAVNPPRFMWPDKFPHLGPVLDGVEEEDHKPEVTYRIRIARDPEFKSEVMTAERNWAFFNPFKLFEKGKWYWQHAYLDKDGKEEWSPVYHFYVDEQTRTFNPPSLQEVLAKFSQSHPRILLDAKDWDQIIERNKNNPEAQLYIQKARKCLNHPLKHLEEEIDTTQVVKLTNIVQYRSALIRESRKIVDREEANIEAMVRAYLLTKDEVYYKEGIKRLSEILSWKDSKYFAGDFNRSTILSMSTSAYDAWYNLLTPAEKQLLLETISENAHKFYHEYVNHLENRIADNHVWQMTFRILNMAAFATYGELPMASTWVDYCYNEWVSRLPGLNTDGGWHNGDSYFHVNLRTLIEVPAFYSRISGFDFFADPWYNNNALYVIYHQPPFSKSAGHGNSHETKMKPNGTRVGYADALARECNNPWAAAYARTILEKEPDIMKKSFLGKAGDLTWYRCITDKALPKEEHSLAELPMTKVFNETGIATMHTSLGDIEKNTMLSFRSSPYGSTSHALANQNAFNTFYGGKAIFYSSGHRTGFTDDHCMYSYRNTRAHNSILVNGMTQTIGTEGYGWIPRWYEGEKISYMVGDASNAYGKITAPIWLKRGELSGTQYTPEKGWDENKLKMFRRHIIQLGNTGVYVIYDELEGKEAVTWSYLLHTVELPMEMQELPDEVKVTGKNKDGGISVAHLFSSAKTEQAIVDTFFCAPTNWKNVTNAQGKAVKYPNHWHFSSTTIPCKTARFLTVMDTHGNNRADMKVVRQGNTVQVGDWIITCNLTEKGKAAISVTHQAEKVSLKYDAGKKEGATIITDQVQGKQVNKVLTDYLPDFEI Desulfovibrio vulgaris Hildenborough JW710 DvH 206625 DVU1186 mazG phosphoribosyl-ATP diphosphatase (EC 3.6.1.31) # Important for growth in minimal media, except when histidine is provided. Belongs to the MazG family of pyrophosphatases. Replaces the typical HisI. See PMID:29324779. MazG family protein (TIGR) MTKDNASLARLTDVIDRLLAPEGCPWDKEQTPESLCDYLVEECFELVEAIRSGNADEVREEMGDVMFLLAFLGRLYADKGAFTLDDAMANNAAKMIRRHPHVFSDTTYADRDEFLRNWESIKRAEKADAEGEPQGVYDSLPASLPPLLKAYRIHSKAARVGFTWPEDEDVERQVEAEWLELLDVLAGDDKAAQENELGDLIFSLVELGRRKGIKANTALDMTNLKFLRRFRRMEALARERGLDFPALSLDDKDELWNEAKAAEAAAR Desulfovibrio vulgaris Hildenborough JW710 DvH 209400 DVU0464 prephenate and/or arogenate dehydrogenase # important for fitness in defined media, and rescued by added tyrosine. This is the second or third step in tyrosine synthesis from chorismate via prephenate; it is not clear if dehydrogenation or transamination occurs first. prephenate dehydrogenase (TIGR) MKIALVGDKGRMGRLLTSRFSAAGCEVAGVDRPLTPDTVRPAVQGADVVILCVPVEVLAEVLSIVAPLLSPKQVLADITSVKVRPMEVMQAFHAGPVVGTHPLFGPDPQDDHLPVAVTPGSSARDADVTLVEQCFRMIGCDTFRTTAQEHDRAAAMIQGLNFISSVAYLATLAHNEELLPFVTPSFRRRLDAARKMLTEDAALFEGMFEANPASQDAVRSFRSFLNIASAGDVDVLVDRARWWWRTHDDRGGARQ Desulfovibrio vulgaris Hildenborough JW710 DvH 207036 DVU1585 Methionine synthase (cobalamin-dependent) (EC 2.1.1.13) # Important for fitness in most defined media experiments and cofit with metF (DVU0997) vitamin B12-dependent methionine synthase family protein (TIGR) MPDFRQALRAGRRLLFDGGLGTMLQARGLPAGVSPEQFCLDRPDVLRGIHADYVRAGADILTTNTFGGSRFKLGDGFDVVDFNRRMAAIAREAADASGRQAFVAGSIGPTGHFVKPLGEVEPAALVAAFREQVRGLVAGGADLLMIETQFDLAEARAAVVAARAECSLPIAVSMTFENGVSLTGSTPEVFVATMLNLGVDLLGTNCSAGPDQMHDVVASLLASASVPVLVEPNAGLPELIDGKTVFRLPPAPFAEKTAAFAAMGARVLGGCCGTTPDHIAALRQAVADIPATLPVDSGVGIVLTTRSHLVRVGGDAPVRIIGERINPTGKKQLIAELQAGDFSLALRFSDEQVEAGAPILDVNVGAPMVDEEVLLPDLVQRLITRHGVPLSIDSSNAAAIERALPYCPGSTLVNSISGEPGRMERLGPLCRDHGAPFILLPLKGRKLPVAATERIAIIEELLVQAEGLGIPRRLVMVDVLALAVSSKAEAARQCLETIRWCTANGFATTIGLSNISFGLPARELLNGTFLAMAAGAGLSSCIAHPGNGRIRETVACADVLLARDANAERFIDAYAAWTPATQGGPVASGPGLASQPPATTLEEAVVKGDRDGVTAIVESELAAGADPFDLVQTKLIPAINEVGVKYERREYFLPQLIRSAETMQTAFRRLQPLLEEMRGAEVRPVIIMATVEGDIHDIGKNIVSLMLGNHGFEVVDLGKDVKAETIVDAAETHGARIIGLSALMTTTMVRMEDTVKLVRARGLDVKVIVGGAVVTKAFADAIGADGYSADAVEAVRLAKSLLAG Desulfovibrio vulgaris Hildenborough JW710 DvH 207038 DVU1587 N-acetylglutamate synthase (EC 2.3.1.1) # Important for fitness in minimal media, unless arginine is provided. acetyltransferase, GNAT family (TIGR) MAPFIRKATVPDVKRIHAILMECAGQRLLLPRSLNDLYSRIRDFVVVDADEGGAILGCCALSITWEDIAEIRSLVVLESLRGQGWGRRLVEACMSDAVTLGLYRVFTLTYQVEFFNKLGYSVVGKEVLPQKVWADCIHCPQFPECDETAMLIEL Desulfovibrio vulgaris Hildenborough JW710 DvH 206250 DVU0823 argJ Glutamate N-acetyltransferase (EC 2.3.1.35) # Important for fitness in minimal media unless arginine is provided. Some homologs also catalyze the formation of N-acetylglutamate synthase, but the dedicated synthase (DVU1587) is also required, so DVU0823 probably catalyzes the acetyltransferase reaction (which is necessary to convert N(2)-acetylornithine to ornithine) only. arginine biosynthesis bifunctional protein ArgJ (TIGR) MSASPKGFRFATVSAGFRKEARPDLALIVSDTPATAAGVFTTNRFQAAPVVVARENLSARPVARAVVINSGQANACTGDEGMTNCRTTLDLVGKACGIPAAEVLPASTGVIGAQLHMDKWREAAPRLAAALGQNTHHDFARAIMTTDAFPKVAERELAIAGTTVRLVGMAKGAGMICPNMATMLSVVLCDAAVTPEAWQRLFLDAVDRTFNRVTVDGDTSTNDTVFGLANGASGVTVEGEDLAKLGEALTDVLARLAYMLVQDGEGATKVMRVKVSGAVDDAEAEAVARTVGHSQLVKTAMYGRDANWGRIVAAVGRSGASFKAEDVVVTLCGVELFRNGQPTDLDFDTLLREPLKGRDVTVDIELGAGTGHYELLASDLTHDYVNCNADYRS Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_3768 N515DRAFT_3768 N-acetylglutamate synthase; N-acetylglutamate kinase (EC 2.3.1.1; EC 2.7.2.8) Important for fitness in most defined media, except when arginine is provided. Contains both acetylglutamate kinase (TIGR00761) and N-acetylglutamate synthase (PF04768) domains. N-acetylglutamate kinase MEAHKHTRKTIVRLLSSMGSAKEIQQYLKRFSQLDAKRFAVVKVGGAVLRDDLPALTSSLTFLQQVGLTPIVLHGAGPQLDEELSAAGIQKQTVNGLRVTSPKALAIVRKVFQEQNLRLVEALQGMDTRATSVPSGVFTSEYLDRDVYGLVGKVSSINLAPIEASLRAGSIPVIASLGETAEGQILNINADFAANELVRVLQPYKIVFLTGTGGLLDDKGRIIDSINLSTEYEHLMAQPWINGGMRVKIEQIADLLSSLPLTSSVSITQPSELAKELFTHKGSGTLVRRGEKVLRYESWEGIDLARMRELIESSFGRKVVADYFERTRPYRIYVSENYRAAMILTQEEGLAYLDKFAVLDDAQGEGLGRAVWQVMREENPQLFWRSRHGNQVNIFYYAESDGCFKQERWKVFWYGLKNFGEIERCVAHCAVRPATLMD Bacteroides thetaiotaomicron VPI-5482 Btheta 352922 BT3395 N-succinylglutamate kinase (EC 2.7.2.-) Important for fitness in most defined media, except when arginine is provided. Bacteroidetes use succinylated intermediates, and a close homolog from B. fragilis prefers N-succinylglutamate as a substrate (see PMC7311316 and references therein), so this is N-succinylglutamate kinase, not N-acetylglutamate kinase. putative acetylglutamate kinase (NCBI ptt file) MREKLTVIKVGGKIVEEEATLLQLLNDFAAISGHKVLVHGGGRSATKIAAQLGIESKMVNGRRITDAETLKVVTMVYGGLVNKNIVAGLQARGVNALGLTGADMNVIRSVKRPVKEVDYGFVGDVEKVDASLLADLIHKGVVPVMAPLTHDGQGNMLNTNADTIAGETAKALSALFDVTLVYCFEKKGVLRDENDDDSVIPEITRAEFEQYVADGVIQGGMIPKLENSFEAINAGVTEVVITLASAIKDNEGTRIKK Bacteroides thetaiotaomicron VPI-5482 Btheta 353285 BT3759 N-succinylglutamylphosphate reductase (EC 1.2.1.-) Important for fitness in most defined media, except when arginine is provided. Hits TIGR01850, which is described as N-acetyl-gamma-glutamyl-phosphate reductase, but Bacteroidetes use succinylated intermediates for arginine synthesis (see PMC7311316). N-acetyl-gamma-glutamyl-phosphate reductase (NCBI ptt file) MIKAGIIGGAGYTAGELIRLLLNHPETEIVFINSSSNAGNRITDVHEGLYGETDLRFTDQLPLDAIDVLFFCTAHGDTKKFMESHNVPEDLKIIDLSMDYRIKSDDHDFIYGLPELNRRATCTAKHVANPGCFATCIQLGLLPLAKNLMLTGDVSVNAITGSTGAGVKPGATSHFSWRNNNISIYKAFDHQHVPEIKQSLKQLQNSFDSEIDFIPYRGDFPRGIFATLVVKTKVALEEIVRMYEEYYAKDSFVHIVDKNIDLKQVVNTNKCLIHLEKHGDKLLIISCIDNLLKGASGQAVHNMNLMFNLEETVGLRLKPSAF Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_3847 Echvi_3847 N-succinylglutamylphosphate reductase (EC 1.2.1.-) Important for fitness in most defined media, except when arginine or citrulline is provided. Hits TIGR01850, which is described as N-acetyl-gamma-glutamyl-phosphate reductase, but Bacteroidetes use succinylated intermediates for arginine synthesis (see PMC7311316). N-acetyl-gamma-glutamyl-phosphate reductase, common form MTKIKTAIIGAAGYTGGELLRILVHHPSCELVYIHSNSQKGKKIDEVHPDLIGDSDLVFTDEVKTTGLDAVFLGLPHGQAKAFLAENKFDDQTVIIDLSTDFRDESNGFLYGLPEVNASQTGQAKRIANPGCFATGIQLALAPAIAAGLAKSDIHITGITGSTGAGKKLSETTHFSQRNQNVSVYKLFTHQHLKEISQTFGQLQTGFDQHLLFVPYRGNFSRGIWVTAYFPFEGSLEEAYKIYHDFYQNAAFTHVSEKDIDLKQVVSTNKCIVHLKKEAGQLVIYSAIDNLLKGASGQAVQNYNLAFGLNEKEGLRLKSVAF Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_3769 N515DRAFT_3769 N-acetylglutamylphosphate reductase (EC 1.2.1.38) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01850. N-acetyl-gamma-glutamyl-phosphate reductase MSIDKKTIGIVGARGHTGAELIRLIATHPALELGFVSSRELDGQRVAEHVDGYAGELRYANLDPAAVAAQGADVVVLALPNGKAAPYVEAIDAAKPETLILDLSADYRFNERWYYGLPELTRGKWRGERRISNPGCYATAIQLSIAPLKDVLAAPPVSFGVSGYSGAGTTPSDKNNPEKLRDNLMPYSLTGHTHEQEASRHLGLPVEFMPHVAPHFRGLTVTTNLYLVRPMKREEILQRFRHAYDGEKLVKVVDEAPWVSQIAHRHHAEVGGFAVSVDGKRVVIVATLDNLLKGAATQAIQNINRAIGVDEYTSIPLEG Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_0351 Ga0059261_0351 N-acetylglutamylphosphate reductase (EC 1.2.1.38) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01850. N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) MSVSVFIDGAAGTTGLEIRERLATRSDISLIGLDDAHRKDAGKRAEAINSADFVILCLPDDAAREAVALIANDTTRVIDASTAHRVADGWTYGFAELEPAQAAAIAEARYVSNPGCWPTGFLALVRPLVRAGLIPPDWVLTAGGASGYSGGGKSMIAEFEDGSEPTGFRAYGLDLEHKHLPEMQKHARIDHAPIFQPAVARSYRGMLIEVPLPLQMLPRKPAPAQIEQVLADAYRDSPIVRVLPSDDVSLVRIEDDAGTDRLTIRVFGNAERGQARLVATLDNLGKGAGGAAVQNLNIMAGFDQTAGLVL Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS18540 CA265_RS18540 N-succinylglutamylphosphate reductase (EC 1.2.1.38) Important for fitness in most defined media, except when arginine or citrulline is provided. Hits TIGR01850, which is described as N-acetyl-gamma-glutamyl-phosphate reductase, but Bacteroidetes use succinylated intermediates for arginine synthesis (see PMC7311316). N-acetyl-gamma-glutamyl-phosphate reductase MKIKAGIIGGAGYTGGEMLRILVNHPNVEIAFVNSTSNAGNLISDVHTDLIGDTDLKFVSDIPQDIDVLFLCVGHGDAKKFLTANPIKDNIKIIDLSQDFRLHANASFSTKDFVYGLPELNRDKIKAAKNIANPGCFATCIQLGLLPLAAKGLIQNEVHINATTGSTGAGQSLSTTSHFSWRNNNLSIYKAFEHQHLNEISESLLQLQPSISEALNFIPQRGAFTRGILAAMYLESDLSLEEAQNIYEAYYSAHPFTHVSRKNIDLKQVVNTNKALVHLEKHGGKLFIISIIDNLLKGASGQAVQNMNLMFGLDETAGLKLKAAYF Sinorhizobium meliloti 1021 Smeli SMc01801 SMc01801 N-acetylglutamylphosphate reductase (EC 1.2.1.38) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01850. N-acetyl-gamma-glutamyl-phosphate reductase MKPKIFIDGEHGTTGLQIRVRMAGRTDLELLSIPEAERRNAAMREDLLNSADIAILCLPDDASREAVAMVAGNNRVRIIDTSTAHRVAPDWAYGFAEMDKAQPQRIRDARHVANPGCYPTGAIALIRPLRQAGILPDGYPVTVNAVSGYTGGGKQMIAQMEDDQNPDHIGAPHFLYGLTLKHKHVPEMKMHGLLERAPVFSPSVGKFAQGMIVQVPLYLEDLAAGATLETIHRALVDHYAGQSIVEVVPLDESAKLARIDATELAGSDAMKLFVFGTKGGAHVNLVALLDNLGKGASGAAVQNMDLMLSA Bacteroides thetaiotaomicron VPI-5482 Btheta 353284 BT3758 N-succinylornithine aminotransferase (EC 2.6.1.81) Important for fitness in most defined media, except when arginine is provided. Similar to acetylornithine aminotransferases (such as argD from B. subtilis), but Bacteroidetes use succinylated intermediates for arginine synthesis (see PMC7311316). acetylornithine aminotransferase (NCBI ptt file) MKLFDVYPLYDINIVKGQGCKVWDENGTEYLDLYGGHAVISIGHAHPHYVEMISNQVATLGFYSNSVINKLQQQVAERLGKISGYEDYSLFLINSGAEANENALKLASFYNGRTKVISFSKAFHGRTSLAVEATNNPTIIAPINNNGHVTYLPLNDIEAMKQELAKGDVCAVIIEGIQGVGGIKIPTTEFMQELRKVCTETGTILILDEIQSGYGRSGKFFAHQYNHIQPDIITVAKGIGNGFPMAGVLISPMFKPVYGQLGTTFGGNHLACSAALAVMDVIEQDNLVENAKAVGDYLLEELKKFPQIKEVRGRGLMIGLEFEEPIKELRSRLIYDEHVFTGASGTNVLRLLPPLCLSMEEADEFLARFKRVL Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_3848 Echvi_3848 N-succinylornithine aminotransferase (EC 2.6.1.81) Important for fitness in most defined media, except when arginine or citrulline is provided. Similar to acetylornithine aminotransferases (such as argD from B. subtilis), but Bacteroidetes use succinylated intermediates for arginine synthesis (see PMC7311316). Ornithine/acetylornithine aminotransferase MKPFDVYPLIDVTPVKASGSTIWDDQGNEYLDLYGGHAVISIGHSHPHYTKRIKEQLDNIAFYSNSVQIPIQKELATKLGQLSGYPDYDLFLCNSGAEANENALKLASFETGKKGFIAFTKGFHGRTSGAVALTDNPKIIAPFNAHEGVHILPFNDLEAVEKQLATGTIAGVIVEGIQGVGGIQVPDPAFLLGLSALTKQYGAKLILDEVQSGYARSGKFFAHQWVEGLKPDLITVAKGMGNGFPIGGVLISPEFKASHGLLGTTFGGNHLACAAALAVLEVIDEENLITAAAENGKAIMAALEKVAGVTEVRGKGLMIGFDLATEAGPVRAALIHEHKIFTGSAGGKHTIRLLPPLNIEPKALTLFLEKLETVLNVKQST Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_3767 N515DRAFT_3767 N-acetylcitrulline deacetylase (EC 3.5.1.-) Important for fitness in most defined media, except when arginine is provided. 70% identical to argE¡¯ from Xanthomona campestris (Q8P8J5), which is active on both N-acetylornithine and N-acetylcitrulline. But only the N-acetylcitrulline activity is expected to be relevant (see N-acetylornithine carbamoyltransferase N515DRAFT_3763) acetylornithine deacetylase MSQLLDDTLRHLRALVSHDTRNPPREIGTGGIFDYLREQLAGFEVTVTDFGAGAVNLYAVRGKPKYLFNVHLDTVPDSPHWSADPHVLRVEGDRAIGLGACDIKGAAAALVAVANATQGDMALLLSTDEEANDARCIAGFLKDHPVYEAVIVAEPTKGEAVLAHRGIHSVQMRFSGKAGHASGEQKPSDSAVHQAVRWGVAALDYVESQAHERFGGLTGLRFNIGKVEGGIKANVIAPTADVRFGFRPLPSMDADRMLETFRTLVEPQPVEFGETFRGDSLPAGDTATAETRRLAARDLADELGIPVGNAVNFWTEAALFSAAGYISFVYGPGDIAQAHAADEWVALEQLDHYAQTIYRIVDRGSA Bacteroides thetaiotaomicron VPI-5482 Btheta 353076 BT3549 N-succinylcitrulline desuccinylase (EC 3.5.1.-) Important for fitness in most defined media, except when arginine is provided. Distantly related to succinyl-diaminopimelate desuccinylases, so this probably provides the missing N-succinylcitrulline desuccinylase activity. See PMC7311316. acetylornithine deacetylase (NCBI ptt file) MKYDIPTMTAEAVSLLKSLISIPSISREETQAADFLQNYIEAEGMQTGRKGNNVWCLSPMFDLKKPTILLNSHIDTVKPVNGWRKDPFTPREENGKLYGLGSNDAGASVVSLLQVFLQLCRTSQNYNLIYLASCEEEVSGKEGIESVLPGLPPVSFAIVGEPTEMQPAIAEKGLMVLDVTATGKAGHAARDEGDNAIYKVLNDIAWFRDYRFEKESPLLGPVKMSVTVINAGTQHNVVPDKCTFVVDIRSNELYSNEDLFAEIRKHIACDAKARSFRLNSSRIDEKHPFVQKAVKMGRIPFGSPTLSDQALMSFASVKIGPGRSSRSHTAEEYIMLKEIEEAIGIYLDLLDGLKL Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_3851 Echvi_3851 N-succinylcitrulline desuccinylase (EC 3.5.1.-) Important for fitness in most defined media, except when arginine is provided. Distantly related to succinyl-diaminopimelate desuccinylases, so this probably provides the missing N-succinylcitrulline desuccinylase activity. See PMC7311316. Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase and related deacylases MLQTFSNAMQQLKAEAKELLKQLIETPSLSREEDHTAKLLEEYLTSKGIPAKRLQNNVWATNKHFDPNLPNVLLNSHHDTVKPNNGYTKDPFKAIEEEGKLYGLGSNDAGGCLVSLIAAFVHLYDQKLPFNLILAATAEEEVSGKNGIALLLEELPTIALAIVGEPTLLDVAVAEKGLMVIDATVTGKAGHAARNEGINALYEALPDLNTLKDYSFKRVSEYLGESKVSATIIQAGSQHNVVPDKCVYTLDVRVTDSYTLQEALDELKGFLKADLQPRSMRLNSSALPKGHRIWEVIHQLSLKCYGSPTLSDQALIPYPSIKIGPGDSARSHTPDEFIHLKEIDQGIDRYVDILNGYADLTN Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS18500 CA265_RS18500 N-succinylcitrulline desuccinylase (EC 3.5.1.-) Important for fitness in most defined media, except when arginine is provided. Distantly related to succinyl-diaminopimelate desuccinylases, so this probably provides the missing N-succinylcitrulline desuccinylase activity. See PMC7311316. acetylornithine deacetylase MSLENIQKESLDLLRQLIRIQSFSKEEDRTANLIAQFLEERGIKTQRKMNNVWAYNKHFDATKPTLLLNSHHDTVKPNSGYTRDPYDAAIEGDKLFGLGSNDAGGCLVSLIGTFLYYYEQEGLKYNICLAATAEEEISGNNGLELVLPDLGELEFGIVGEPTEMNLAIAERGLLVLDCVSHGKAGHAAREEGENAIYKALKDIEWFRNYQFPKVSEVFGPLKMTVTIINAGSQHNVVPANCTFTVDVRVTDAYTNEEVLEIIRANVDCDVTPRSIRLKPSSIDKNHPVVQAGVALGKTTYGSPTTSDQALLDIPSVKCGPGFSGRSHMADEFLYVREVAEGVEGYVNMLRPVVIG Bacteroides thetaiotaomicron VPI-5482 Btheta 353243 BT3717 N-succinylornithine carbamoyltransferase (EC 2.1.3.11) Important for fitness in most defined media, except when arginine is provided. Over 90% identical to the N-succinylornithine carbamoyltransferase of B. fragilis (E1WKT5) ornithine carbamoyltransferase (NCBI ptt file) MKKFTCVQDIGDLKSALAEAFEIQKDRFKYVELGRNKTLMMIFFNSSLRTRLSTQKAALNLGMNVMVLDINQGAWKLETERGVIMDGDKPEHLLEAIPVMGCYCDIIGVRSFARFEDRDFDYQETILNQFIQYSGRPVFSMEAATRHPLQSFADLITIEEYKKTARPKVVMTWAPHPRPLPQAVPNSFAEWMNATDYDFVITHPEGYELAPQFVGNAKVEYDQMKAFEGADFIYAKNWAAYTGDNYGQILSKDREWTVSDRQMAVTNNAFFMHCLPVRRNMIVTDDVIESPQSIVIPEAANREISATVVLKRLIEGLE Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_3849 Echvi_3849 N-succinylornithine carbamoyltransferase (EC 2.1.3.11) Important for fitness in most defined media, except when arginine is provided. 45% identical to the N-succinylornithine carbamoyltransferase of B. fragilis (E1WKT5) Ornithine carbamoyltransferase MKYYTQFENKSLADQLIQKALEYKKAPLSDNNLGRGKRIGLLFLNPSLRTRVSTQIAASNLGMESIVLNMDKESWALEMEDGVIMNQGKAEHIRDAAGVLGSYFDILALRAFPSLTNKDEDSEDFILHQFAKHSGLPLISLESAIRHPLQSLADMVTIQEHKQKEKPKVVLTWAPHIKAIPHAVANSFAEWSIGCGHDVTITHPEGYELDERFTQGATIEHDQDKALANADFVYVKNWSAFNEYGKILCTDESWMLNEQKLSQAPNAKVMHCLPVRRNVELSDEILDGPRSLVQHQAKNRVFAAQAALSELLK Bacteroides thetaiotaomicron VPI-5482 Btheta 353286 BT3760 arginosuccinate synthetase (EC 6.3.4.5) Important for fitness in most defined media, except when arginine is provided. 32% identical to argininosuccinate synthase from Leishmania (H9BG20). argininosuccinate synthase (NCBI ptt file) MEEKKKKVVVAFSGGLDTSFTVMYLAKEKGYEVYAACANTGGFSEEQLKTNEENAYKLGAVKYVTLDVTQEYYEKSLKYMVFGNVLRNGTYPISVSSERIFQALAIARYANEIGADAIAHGSTGAGNDQIRFDMTFLVLAPNVEIITLTRDMALSRQEEIDYLNKHGFSADFTKLKYSYNVGLWGTSICGGEILDSAQGLPETAYLKHVEKEGSEQLRLTFEKGELKAVNDETFDDPIQAIQKVEEIGAAYGIGRDMHVGDTIIGIKGRVGFEAAAPMLIIGAHRFLEKYTLSKWQQYWKDQVANWYGMFLHESQYLEPVMRDIEAMLQESQRNVNGTAILELRPLSFSTVGVESEDDLVKTKFGEYGEMQKGWTAEDAKGFIKVTSTPLRVYYNNHKDEEI Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_3766 N515DRAFT_3766 arginosuccinate synthetase (EC 6.3.4.5) Important for fitness in most defined media, except when arginine is provided. 35% identical to argininosuccinate synthase from Thermus thermophilus (P59846). argininosuccinate synthase MSKDIVLAFSGGLDTSFCVPYLKERGWNVHTVFADTGGVDAEERAYIEARAQELGVASHVTVDGGPAIWNGFVKPFVWAGEGYQGQYPLLVSDRYLIVDAAIQRCAELGTRAIAHGCTGMGNDQVRFDLAVKALGDYEIVAPIREIQKEHTQTRAYEQAYLEERGFPVRAKQKSYTINENLLGVTLSGGEIDLWKAPGEGARGWCKPRAEWPSEKLSVTLGFEHGEAVSLNGEKLPGAKILARLNELFAPYGVGRGMYTGDTTIGLKGRIVYEAPGLISLLAAHRALEEAVLTKQQNRFKPEIARKWVEVVYEGFFHDPVKTDLEAFLASSQQQVNGDVVLETSGAQVTAVEVRSPHILNAKGATYAQSADWGVAEAEGFIKLFGMSSTLWAEVNRKG Bacteroides thetaiotaomicron VPI-5482 Btheta 353259 BT3733 arginosuccinate lyase (EC 4.3.2.1) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00838. argininosuccinate lyase (NCBI ptt file) MAQKLWEKSVQVNKDIERFTVGRDREMDLYLAKHDVLGSMAHITMLESIGLLTKEELEQLLAELKTIYASVERGEFIIEEGVEDVHSQVELMLTRRLGDVGKKIHSGRSRNDQVLLDLKLFTRTQIREIAEAVEQLFHVLILQSERYKNVLMPGYTHLQIAMPSSFGLWFGAYAESLVDDMQFLQAAFRMCNRNPLGSAAGYGSSFPLNRTMTTDLLGFDSLNYNVVYAQMGRGKLERNVAFALATIAGTISKLAFDACMFNSQNFGFVKLPDDCTTGSSIMPHKKNPDVFELTRAKCNKLQSLPQQIMMIANNLPSGYFRDLQIIKEVFLPAFQELKDCLQMTTYIMNEIKVNEHILDDDKYLFIFSVEEVNRLAREGMPFRDAYKKVGLDIEAGKFTHDKQVHHTHEGSIGNLCNDEISALMQQVVDGFNFCGMEQAEKALLGR Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_3852 Echvi_3852 arginosuccinate lyase (EC 4.3.2.1) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00838. argininosuccinate lyase MKLWQKNTTSTKEVEQFTIGRDPEFDIVLAPFDVLGSLAHATMLESIDLLTKEELAILKKGLKDIYQEIQEGTFTIDPGVEDVHSQVEFLLTERYGDVGKKLHSGRSRNDQVAVDLKLYYRAVIQEVLDDAKALFDLLLTLAEKHQNDLMPGYTHTQLAMPSSFGLWFGAMAESLAEDMELWLAAYNLADRNPLGSAAGYGSSFPLNRTMTTRLLGFKDMHYNVINAQNNRGKTEKAIAFAMAGMAGTLNRLSADIIIFMNQHFGFVKFPDNLTTGSSIMPHKKNPDVFELIRAKANQIQSGPQNLMMQMTNTTTGYHRDLQLLKETTFPDFEKLKDCLQITKFMLEHIEIKPDILEDKFYKHLFSVEVVNDLVLQGMPFRDAYKKVGLDIESDDFAPDHTVNHSHEGSIGQLCLDEIRTKMETALAKFDFSAIETSYQKLLEA Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_3770 N515DRAFT_3770 arginosuccinate lyase (EC 4.3.2.1) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00838. argininosuccinate lyase MTQPLWQKSGIQIDARIMRFLAGDDVVLDREFFLHDITASKAHVEGLAKIGVVSADEAAALKRELDALAADFSAGDFVLDESYEDGHSAIEARLTERLGDAGRRVHTGRSRNDQILVATRLWLKDQLAVLETHCRAIAEVCLERAAQPALPLPGYTHIQRAVVSSTAMWFAGFAEGFIDNTLRARQTAALIDCNPLGTAAGYGVNLPLDREHTTQALGFARMQVSPVYAQLSRGKFEMAVLEAIAAALLDVRRLAWDLSLFTTAEFGFVKLPSEYTTGSSIMPNKRNPDVVELLRASYASVAAARTEIEQLLSLPSGYQRDLQFSKGSLFHGCRHGLAALELVPDLLARMEWHEPAMRAAIEPAMYATDVAIEQAAAGVPFRDAYRAAADAAASAGAGRTPEGSLAARVSPGAGHDLRLDELKARLAALTPGH Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS18485 CA265_RS18485 arginosuccinate lyase (EC 4.3.2.1) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00838. argininosuccinate lyase MKIWQKNIDVNQFVESFTVGKDRELDLQMAKFDVLGSLAHTQMLETINLLTAEELKTVQHELKNIYAEIEAGNFTIEDSVEDVHSQVEWLLTQRIGEAGKKIHSGRSRNDQVLVDLKLFFRACIEDMVGQTSTLFNQLIELSNTHKDKLVPGYTHLQIAMPSSFGLWFGAYAESLADDMELMLAAWKICNKNPLGSAAGYGSSFPLNRTLTTHLLGFETLNYNVVYAQMGRGKTERILAQAMSAVAATLAKMAMDVCLFINQNFGFISFPAELTTGSSIMPHKKNPDVFELIRSRCNKIQALPNEIAMMITNLPSGYHRDLQLLKENLFPAITSLNECLEIATFMFQNITIKDDILKDKKYDYLFSVEVVNDLALQGVPFREAYKIVGEQIENGSFAPSGQIHHTHEGSIGNLCNEQISAAMQAVLSQFGFGKVNKAIEDLVK Bacteroides thetaiotaomicron VPI-5482 Btheta 353741 BT4215 shikimate dehydrogenase (EC 1.1.1.25) A conserved essential gene. This activity is necessary to explain chorismate biosynthesis. 36% identical to shikimate dehydrogenase from Aquifex aeolicus (O67049). shikimate 5-dehydrogenase (NCBI ptt file) MEKYGLIGYPLRHSFSIGYFNEKFRSEGINAEYVNFEIPNINDFMEVIEENPNLCGLNVTIPYKEQVIPFLNELDRDTAKIGAVNVIKIIRQPKGKVKLVGYNSDIIGFTQSIQPLLQPQHKKALILGTGGASKAVYHGLKNLGIESVFVSRTHKTDDMLTYEELTPEIMEEYTVIVNCTPVGMYPKVDFCPNIPYELLTPNHLLYDLLYNPNVTLFMKKGEAQGAVTKNGLEMLLLQAFAAWEIWHR Caulobacter crescentus NA1000 Caulo CCNA_00003 CCNA_00003 shikimate dehydrogenase (EC 1.1.1.25) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00507. shikimate 5-dehydrogenase MTNAITGAAIVGGVCGQPIKHSMSPVIHNAWIAAAGLDAAYVPFAPAADRFETFVDGLRGGAVRGLNVTIPFKERALAVADTASDLARMAGAANLLVFNEDGSVHADNTDGPGLLGAIAIQAPGFDVTAAPVVILGAGGAARGAVAALLLAGAPRIAVVNRTVARAQDLADTFGEKVVAKGEDALPALLPEAGLIINATSLGLGGGAGPSADLTLTPKTAVVMDMVYKPLRTEFLRRAEAAGRRTVDGLEMLLRQAIPTFETIYGQAPSPKIDVRVLALKLLGEV Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS19745 CA265_RS19745 shikimate dehydrogenase (EC 1.1.1.25) A conserved essential gene. This activity is necessary to explain chorismate biosynthesis. 33% identical to shikimate dehydrogenase from Geobacillus kaustophilus (Q5KWX7). shikimate dehydrogenase MKTYGLIGYPLSHSFSKKYFTEKFQNEGIAGHQYELFPIADIKSLPDLLNENPSLCGLNVTIPHKVNVLCYLNEVDEAAEKIGAVNCISIKSFEGKNYLKGYNTDAYGFEESLKPLLGPQHTKALVFGDGGAAKAVKYVLEKLNIQYQLVVRTAVPGAILYSEVSPEILASHQLLINTTPLGMSPNVDTFPEIDYSLLGPGYLAYDLVYNPLETAFLAKAAERGAAIKNGLEMLYKQAEKAWAIWNK Caulobacter crescentus NA1000 Caulo CCNA_03103 CCNA_03103 shikimate kinase (EC 2.7.1.71) Important for fitness in most defined media, and highly cofit with shikimate 5-dehydrogenase (CCNA_00003). 39% identical to shikimate kinase from Acinetobacter baumannii (A0A0M3KL09) shikimate kinase MTETDQTPDTAPEAAPEVAPIVSDDLAPLRAKTIVLVGLMGVGKSSVGRRLANVLGLPFRDADNEVEAAAGRSISEIFAELGEPAFRDGERRVIARLLDEPPHVLATGGGAFVNAETRALINEKAVSVWLKADVELLARRVSRKDNRPLVRGKDPVKVLTELAEARYPAYAEAQVHVETGDTPHMVAVEAILTALRQAHA Bacteroides thetaiotaomicron VPI-5482 Btheta 351931 BT2403 aspartate kinase / homoserine dehydrogenase (EC 2.7.2.4; EC 1.1.1.3) Important for fitness in most defined media. 37% identical to a bifunctional aspartokinase/homoserine dehydrogenase from Arabidopsis (O81852). aspartokinase/homoserine dehydrogenase (NCBI ptt file) MKVMKFGGTSVGSVNSILSVKRIVESAGEPVIVVVSALGGITDKLINTSKMAAAGDSAYEGEFREIVYRHVEMIKEVIPAGAGQVALQRQIGELLNELKDIFQGIYLIRDLSPKTSDTIVSYGERLSSIIVAELIDEAKWFDSRTFIKTEKKHNKHTIDADLTNQLVKEAFHSIPKVSLVPGFISSDKVSGDVTNLGRGGSDYTAAIIAAALDASSLEIWTDVDGFMTADPRVISTAYTISELSYVEATELCNFGAKVVYPPTIYPVCHKNIPIIIKNTFNPDGVGTVIKQETSNPQSKAIKGISSINDTSLITVQGLGMVGVIGVNYRIFKALAKNGISVFLVSQASSENSTSIGVRNADADLACEVLNEEFAKEIEMGEISPILAERNLATVAIVGENMKHTPGIAGKLFGTLGRNGINVIACAQGASETNISFVVDSKSLRKSLNVIHDSFFLSEYQVLNLFICGIGTVGGSLVEQIRCQQQKLMMENGLKLHVVGIIDAAKAMFSREGFDLANFREELQKKGKDSNLQTIRDEIVGMNIFNSVFVDCTASPDIASLYKDLLQHNVSVVAANKIAASSAYENYRELKTIARQRGVKYLFETNVGAGLPIINTINDLIHSGDKILKIEAVLSGTLNYIFNKISADIPFSRTIKMAQEERYSEPDPRIDLSGKDVIRKLVILAREAGYHIEQEDVEKNLFVPNDFFEGSLDDFWKRVPSLDADFEARRQVLEKEHKHWRFVAKLEDGKASVGLQEVGANHPFYGLEGSNNIILLTTERYKEYPMMIQGYGAGAGVTAAGVFADIMSIANV Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_2000 Echvi_2000 aspartate kinase / homoserine dehydrogenase (EC 2.7.2.4; EC 1.1.1.3) Important for fitness in most defined media. 40% identical to a bifunctional aspartokinase/homoserine dehydrogenase from Arabidopsis (O81852). aspartate kinase MKIIKFGGSSIANYENIQKVFSIIEQKSEKEAFALVFSAFGGVTEQLLQCANIAQQSEESYHTILQELEKRHLEIVKKLVPVQQQSTALTFVKVRFNELGDLFHGIYLIKECSNRTMDYVLSFGERLSNFILAAGLQAKGIGTSYVDARDLVKTDDRFGHAKVNFKTTNKLIQDHFKSHDDIKVITGFIGSTEKGETTTVGRSGSDYTASIFAAALGAEQVEIWTDVSGVMTADPRLVYTAFTIPQLSYNEAMELSHFGAKVVFPATMQPAMKEDIPIYIKNTFKPDEAGTRISKDSGEGKIIKGISSMDNISILNVQGPGLVEVVGVSQRFFGTLANNGINIILISQASSEHSICVAIASKDASRAKSVIEEEFRYEIQSGEMDEIQIVPDMAVIAVVGENMQHNPGASGRMFQALGRNNVNVAAIAQGSSELNISAVITQADLQKALNALHEAFFLSDYKVLHLFLVGVGLIGKALTKMIHQQLKNLQEENMLDIQIHGMANSRYMKFHEDGFDLATVGPPDENDEPMDMDKFIGTMTEMNFSNSVFVDCTASQDVADIYEQILDSKVGIVTPNKKANSGPLETYKKLKKLAGQRGVRFFYETNVAAGLPVINTLQDLMLSGDHVHRIEAVLSGSMNYIFSELEKGMPFSEVVAQAKEKGYTEPDPRDDLSGMDVARKILILGREAGQDLHFEDVEIQSMVPEDCEDAASVPEFFKKLQKHDGHFQQLLDEANAKGEKLRFMATLENGKAKVGLNSLDSEHPFFTLKGSDNMILFTTERYNDFPMIVRGPGAGADVTAAGVFADIIRLGNYSR Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_4002 N515DRAFT_4002 aspartate kinase / diaminopimelate decarboxylase (EC 4.1.1.20; EC 2.7.2.4) Important for fitness in most defined media. Contains TIGR00657 and TIGR01048. aspartate kinase MKFGGTSVATLPRWQNIRELVASRRAEGARVLVVVSALTGITDALKQMCAQEDKGKRVEAARAIAQRHYDLLDHMQLAVPATLAERLSELAMLAEDGPGAMGELAWAALVQAHGELMSSALGAAFLSHAGLPTEWLDARDCLAAVALPNQNERTKLLSAMVEARPDPALNARLAELGEVFITQGFIAREAQGRTVLLGRGGSDTSASYFGALLKAQRVEIWTDVAGMFTANPRQVPGARLLQRLDYEEAQEIASTGAKVLHPRCLSPLREPRVPMLIKDTNRPELEGTVIGPEVREHAPSVKAISARKGITLVSMESVGMWQQVGFLADVFAQFKQHGLSVDLIGSAETNVTVSLDPTENLLDSDAIAALASDLAKVCRVKVIAPCAAITLVGRGMRSMLHTLSGVLAEFGQIRVHLISQSSNNLNLTFVVDENVVDDLLPHLHELLIAAGALRTDDSALFGPSWQALYGSGEVAAPAASWWRTAERERLLRLGAERTPRYVYHLPTVRQQARELKSLGAVDRLHYAVKANTHPAILKALAEEGFGFECVSPGELKAVLAAVPESAPLLFTPNFAPRADYEWALTTRATISLDALYQLENWGELFRGREIVLRVDLGRGLGHHEKVRTGGSGSKFGLPVELVDSFLRLADAHGVIVRGLHAHLGSGILDEGHWGEVYGQLASLAERIGSVAFLDIGGGLGVPSHPGEARLDIAALDRVLRSVKAAYPHYQLWMEPGRYLVADAGVLLARVTQQKGKGSWRYLGVDTGMNSLIRPALYEAWHEIVNLTRLDEPATGLFQVVGPICESGDVLGTDRRLPEAQEGDVVLVAQAGAYGKVMSSPYNMRDEAEEVILD Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS23475 CA265_RS23475 aspartate kinase; homoserine dehydrogenase (EC 2.7.2.4; EC 1.1.1.3) Important for fitness in most defined media. The entire protein is 40% identical to a bifunctional aspartokinase/homoserine dehydrogenase from Arabidopsis chloroplast (O81852). bifunctional aspartate kinase/homoserine dehydrogenase I MKVLKFGGTSVGSAENIKTLLRLVGEEKQKNSPVVVLSAMSGVTNLLTEMAEMAERGEDYDTHLKEIEAKHFAVIRSLLPAAAQNPVFTRLKIFFNELEDLLQAVANLRELSLQTKDQILSYGERCSTFMISHIASKNIGDSIYVNGSDLIKTDSNFGQAKVETELTEMLINNFYQENKDKVLFVTGFIASNAAGRVTTLGRGGSDYTAAVWGAALNAEEIEIWTDVNGMMTADPRMVKKAFSLPELSYTEAMELSYFGAKVIYPPTMIPAFMKKIPIVIKNTFEPDFAGTYIKSDVKASSLPIKGISSIDHISIINLTGSGMVGKAGFSGRLFSLLSREQINVVLITQSSSEHSITFAVKPTDASQAISLIKKEFELELDAKKLELPEVENNLAVLAIVGENMKRTPGMSGRLFNALGRNGINVRAIAQGSSEYNISVIISKDDLSKAVNAVHDAFFTDLKRTLNVFCLGTGNIGKTLFNQLKEQMPFLAANNDLQVKVTGISNTRKMIFSADGLSLENWETELNTNGEPADLAGFVAKMKALNLPNCVFVDNTAAESPIEFYQGIFESSISVVTCNKKGNSADYAQYKSFKDTARKFGVDFYYETNVGAGLPIIRTLRELMMSGDKVARIEAILSGTISYIFNNFKGEAGFYETVKEAQELGYTEPDPRDDLNGKDFMRKMLILARDAGYPLEASDVKIDNILPEACLNASSVEDFYSELQANAAYFENLKQTAANDGKVLRYIGKLEDGNVEISLQMVDDSHPFYMLSGSDNIISFTTDRYKSRPLVVKGPGAGAEVTAAGVFADIINVGTLNK Caulobacter crescentus NA1000 Caulo CCNA_01969 CCNA_01969 aspartyl-tRNA(Asp/Asn) synthetase (EC 6.1.1.23) A conserved essential gene. This activity is necessary to explain asparagine biosynthesis. 43% identical to the enzyme from Bacillus subtilis (O32038) aspartyl-tRNA synthetase MTTMHAYRTHNCGALRASDTGAAVRLSGWIHRKRDHGGLVFIDLRDHYGLTQLVLHPETPGFNVVERLRAESVIRVDGEVIARDASVVNPNLPTGEIEIRVSAVEVLSEAAELPLPVFGEPDYPEEIRLKHRYLDLRRETLHKNIVLRSRVIQSIRNRMFAQGFNEFQTPILTASSPEGARDFLVPSRLHPEKFYALPQAPQQFKQLLMVSGFDRYFQIAPCFRDEDLRADRSLEFYQLDVEMSFVTQEDVFAAIEPVMHGVFEEFSNGKPVSPINGTHTFTNDFGQSFEHKGFERLTYAQSMAWYGSDKPDLRNPIKMANVSEHFRDGGFGLFAKILGADAKNQVWAIPAPTGGSRAFCDRMNSWAQGEGQPGLGYVFWSEDQGGWGGPIAKNLGEPTQALMESLGLGAGDAAFFVAGDPAVFAKFAGLARTRVGTELKLVDENQFKFCWIVDFPMFEWNEEEKKVDFSHNPFSMPQGGLEALETQDPLTIRAYQYDIVCNGYELCSGAIRNHKPEIMLKAFATAGYGPEVVEEQFGGMLNAFRYGAPPHGGLAPGIDRIVMLLADQVAIREVIAFPLNQQGQDLLMNAPANVLDKQLKELHIRTAPPIKV Dinoroseobacter shibae DFL-12 Dino 3609247 Dshi_2633 aspartyl-tRNA(Asp/Asn) synthetase (EC 6.1.1.23) A conserved essential gene. This activity is necessary to explain asparagine biosynthesis. Related to both tRNA(asp)-specific enzymes (as from E. coli) and tRNA(asp/asn) enzymes (as from Pseudomonas aeruginosa) aspartyl-tRNA synthetase (RefSeq) MHAFRTHTCAELTKDAVGQTVRLSGWVHRVRDHGGVLFIDLRDHYGMTQVLCDPDSPVFSQVEKVRSEWCIRIDGTVKARDESLINPKIPTGEIEVFIRDMEVLGTAEELPLPVFGDQEYPEETRLKYRFLDLRRESLHDNIMLRSKVVQSIRKRMWDIDFTEFQTPIITASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLIMVGGFDKYFQIAPCFRDEDPRADRSPTDFYQLDLEMSFVSQQDVFDTIQPVIAGIFEEFGGGRRVDTDWPLISYRDSALWYGTDKPDLRNPIKMQIVSDHFAGSGFAIFAKLLEQEGTEIRAIPAPGGGSRKFCDRMNKFAQEQGLPGMGYIFWRDQGQGMEAAGPLAKNIGPERTEAIRQQLGLQVGDAAFFLGGKPASFEAVAGRARTVIGEELGLIDQDRFAFAWIVDFPMYEKDDEGRIDFSHNPFSMPQGGMAALEGDPLEVLGYQYDLACNGYELVSGAIRNHKLDIMYKAFEIAGYGADEVEKRFGGMVNAFKYGPPPHGGCAAGIDRIVMLLADTANIREVIMFPMNQRAEDLMMNAPSEPTGEQLRDLSLRVIPQE Desulfovibrio vulgaris Miyazaki F Miya 8501305 DvMF_2038 aspS aspartyl-tRNA(Asp/Asn) synthetase (EC 6.1.1.23) A conserved essential gene. This activity is necessary to explain asparagine biosynthesis. aspartyl-tRNA synthetase (RefSeq) MSDQKLDVQQEHQQYIEPLGDWVRSHDCATLTAADTGAEVCLMGWVQYRRDHGGLIFVDLRDRQGLTQIVFSPDVNPAAHERAHIIRSEYVLAIRGTVRPRPEGMTNPGMKTGEIEVYVSEWKLLNTSKTPAFVIEDRTEASENLRLQYRYLDLRRPRMANNFIVRHKAAQATRRYLDELGFLEIETPYLTKSTPEGARDFLVPSRLNQGQFYALPQSPQLFKQLLMMSGMERYYQIVRCFRDEDMRADRQLEFTQIDIEMSFVDEEQVMAMAEGLMARVFRDALDREIATPFPRMSYDDAMARYGVDKPDTRFGLELQDVTHIVRGSNFKLFATAELVKAMRVPGGETMTRKEIDEFTEFVKIYGAQGLAWIKIRPDEWQSPIAKFLSDEERAGLKDALGLETGDIVFFQAGAPGMVNAALGNLRVRLGEHLGLIDENAFNFLWVTDFPLFEYDEEEKRYVACHHPFTSPKDGHMDVMVENPAAARARAYDMVLNGYELGGGSIRNHTAEKQRRMFAALGFSPEEAEAQFGFLTQALEMGAPPHGGIAFGMDRLAMLLTGSSSIRDVIAFPKTQKATCLLTQAPDSVSARQLRDLGLRLRETGKDGAPNAPQG Phaeobacter inhibens BS107 Phaeo GFF2422 PGA1_c24530 aspartyl-tRNA(Asp/Asn) synthetase (EC 6.1.1.23) A conserved essential gene. This activity is necessary to explain asparagine biosynthesis. 41% identical to an aspartyl-tRNA(Asn) ligase from Bacillus halodurans (Q9KDG1) aspartyl-tRNA synthetase AspS MHDYRSHTCAELNKSNVGETVRLSGWVHRVRDHGGLLFIDLRDHYGVTQVMADPDSPVFAEIEKVRSEWCIRIDGNVKARDESLVNDKIPTGEIEVFIRDIEVLGKSEELPLMVFGEQEYPEETRLRYRYLDLRREKMQKNMLLRSNMIQSIRRRMWDKGFNEYQTPIITASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLMMVSGFDKYFQIAPCFRDEDPRADRSPTDFYQLDLEMSFVTQQDVFDTIQPVMQGVFEEFGKGRKVDSEWPQVSYKDAAKWYGTDKPDLRNPIKMQDCSEHFRGSGFAIFANLLENEGTEIRAIPAPKGGSRKFCDRMNKFAQGEGLPGMGYIFWRDQGEGMEAAGPLAKNIGPERTEAIRQQLGLGVGDAAFFLGGKPKTFESVAGRARTVIGEELGLTDKDRFAFCWIVDFPIYEKDEETGKIDFEHNPFSMPQGGMDALLSDPLAVKGYQYDLACNGYELVSGAIRNHKPEIMFKAFEIAGYGKEEVEKRFGGMVNAFQYGAPPHGGCAAGIDRMVMLLADEANIREVIMFPMNQRAEDLMMSAPSEPMSDQLMELGLRVIPQDQ Synechococcus elongatus PCC 7942 SynE Synpcc7942_1313 Synpcc7942_1313 aspS aspartyl-tRNA(Asp/Asn) synthetase (EC 6.1.1.23) A conserved essential gene. This activity is necessary to explain asparagine biosynthesis. Similar to both aspartyl-tRNA(Asp) synthetases (as from Arabidopsis chloroplasts & mitochondria) and to aspartyl-tRNA(Asn) synthetases (as from Bacillus subtilis) aspartyl-tRNA synthetase MRTHYCGELRAEQVGTSVTLYGWVDRRRDHGGVIFVDLRDRTGTVQIVSDPERTPESYHQAEGLRNEYVVKITGRVSGRPAESLNPKLPTGEVEIYADRIEILNAVRRQLPFQVSSADEETVREDLRLRYRYLDLRRDRMNRNLQLRHQVVKAIRRFLEDEEQFIEIETPVLTKSTPEGARDYLVPSRVNPGEWFALPQSPQLFKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFLSQEEIIDLNERLIAHIFKTVKGIELPRPFPRLTYAEAMDRYGSDRPDTRFGLELVDVSDVVADMGFKVFSGAVKSGGKVKILPIPDGNDRISNVRIKPGGDIFKEATEAGAAGLAYIRVRENGEIDTIGAIKDNLSDEQKAEILRRTQAQPGTLLLFGAGSTDIVNKSLDRVRQFLGKELGLIDPEALNLLWVVDFPMVEWNADEKRYEALHHPFTAPNPQDLEDLTTARAQAYDIVLNGLEIGGGSLRIYQRDIQERVFETIGLSHEEAQAKFGFLLEAFDFGTPPHGGIAYGLDRLVMLLTGEESIRDAIAFPKTQQARCLLTEAPADVSDRQLKELYVASTWQPPIKERD Bacteroides thetaiotaomicron VPI-5482 Btheta 351386 BT1858 (R)-citramalate synthase (EC 2.3.1.182) Important for fitness in most defined media. Sometimes annotated as 2-isopropylmalate synthase, but that is probably BT1861. 2-isopropylmalate synthase (NCBI ptt file) MDTTLRDGEQTSGVSFVPHEKLMIARLLLEDLKVDRVEVASARVSEGEFEAVKMICDWAARRNLLQKVEVLGFVDGHTSVDWIQRTGCRVINLLCKGSLKHCTQQLKKTPEEHIADIINVVHYADEQDIGVNVYLEDWSNGMKDSPEYVFQLMDGLKQTSIRRYMLPDTLGILNPLQVIEYMRKMKKRYPNTHFDFHAHNDYDLAVSNVLAAVLSGVRGLHTTINGLGERAGNAPLSSVQAILKDHFNAMTNIDESRLNDVSRVVESYSGIVIPANKPIVGENVFTQVAGVHADGDNKNNLYCNDLLPERFGRKREYALGKTSGKANIRKNLEDLGLELDEDAMRKVTERIIELGDKKELVTQEDLPYIVSDVLKHGAIGEKVKLKSYFVNLAHGLKPMATLKIEINGKEYEESSSGDGQYDAFVRALRKIYKVTLGRKFPMLTNYAVSIPPGGRTDAFVQTVITWNYDEQVFRTRGLDADQTEAAIKATMKMLNLLEE Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_0120 Echvi_0120 2-keto-3-deoxy-D-arabino-heptulosonate-7-phosphate synthase / chorismate mutase (EC 2.5.1.54; EC 5.4.99.5) Important for fitness in most defined media. The N-terminal DHAP region is only 33% identical to the Pyrococcus enzyme (Q8U0A9) but the active site and substrate-binding residues are conserved. The C-terminal chorismate mutase region is diverged but hits PF01817 and no other chorismate mutase was found in the genome. 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase MKDHLKTSEWGLGLKGHVIIAGPCSAETPEQVEKVCLEMKEQNIIPSMFRAGIWKPRTRPGSFEGIGEDGLKWMEIVRHHLNIPITTEVGNTAHVELALKHKVDVLWIGARTTVNPFAVQEIAEALKGTDIPVMVKNPMNPDLQLWIGALERLHAVGINKLAAIHRGFSDAYDKRFRNKPNWSMPIHLKREWKGMEVINDPSHIVGKRDGILEISQRAINFGLDGLMIETHHDPDNAWSDAKQQVTPAQLKDILSKIDFKTPLDSEKPSEKLHDLRSAIDHMDDQLIDLLAERFAVIDQIGAHKREHKLTVFQSDRWKEVMDSRTDKGVKKGLSEKFMKELLFSIHEESVKRQEKQLRAGDPVNKNA Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS11635 CA265_RS11635 chorismate mutase (EC 5.4.99.5) Important for fitness in most defined media. The N-terminal DHAP region is only 36% identical to the Pyrococcus enzyme (Q8U0A9) but the active site and substrate-binding residues are conserved. The C-terminal chorismate mutase region is diverged but hits PF01817 and no other chorismate mutase was found in the genome except for a paralog that has little phenotype (CA264_13110) 3-deoxy-7-phosphoheptulonate synthase MKLNLNIQSLNTWLNVNNEPLIISGPCSAETEEQLLTTAHLLAATGKVSVLRAGIWKPRTRPGEFEGIGSIGLEWLKRAKAETGLPTAVEVANAKHVEEALAAGVDILWIGARSTVNPFTVQEIADALKGHDVPVLIKNPVNPDLQLWIGAIERINGAGITKIGAIHRGFSSFEKSSFRNEPMWELAIQLKTLCPELPIINDPSHICGNRELIPYISQKALDLDMQGLMIESHVDPSVAWTDAKQQVTPAALAELVDRLTVREPEAPNEAFADKLADLRKSIDKIDDVLLQKLGERMAIVEKIGEFKRDNQVTILQVNRWDAIIKKGHAFAKALKLDLNFTEKFLELVHGESIRKQTEIMNAGKAEQGIAAEQHTEVKA Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_2395 Echvi_2395 4-hydroxy-tetrahydrodipicolinate reductase (EC 1.17.1.8) A conserved essential gene. This activity is necessary to explain lysine biosynthesis. 34% identical to dapB from Thermotoga maritima (Q9X1K8). dihydrodipicolinate reductase MNILILGYGKMGKIISQIAEERGHTIAAKIDESNIHELDKLDTTKVDAAIEFSQPDAAVQNLSWAIKHNIPVVCGTTGWLDKKPEIERLTLSNGGAFFYASNYSIGVNILFKVNSFLAKIMNEQPAYTVKMEEIHHTEKKDAPSGTAITLAESIIDRVDRVKRWDLDKDVNGNEHSLPITAKRIDPAPGTHIVTYQSEIDDIEIKHTAHSRKGFALGAVLVAEWIKDKKGVLSMDDYLTF Desulfovibrio vulgaris Miyazaki F Miya 8499684 DvMF_0450 4-hydroxy-tetrahydrodipicolinate reductase (EC 1.17.1.8) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00036. dihydrodipicolinate reductase (RefSeq) MSTSIIVTGAGGRMGSTICRMAQEDPVLTLAAVVERPERLASLDVWKCPSGSDPDAVFATVPGGVVVDFTSPEASMANARAAARAGVSHVIGTTGLTAEQKAELADLARTARIFWAPNMSIGVNVLLKILPQLVQQLGEQYDLEMVELHHNRKKDSPSGTALRLAECLAEARGWNLPDVANYHREGIIGERPKDEIGIQTIRGGDVVGVHTIYAMGPGERIEITHQAHSRENFAQGALRAAKWLPQQQPGTLYSMLDML Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS15670 CA265_RS15670 4-hydroxy-tetrahydrodipicolinate reductase (EC 1.17.1.8) A conserved essential gene. This activity is necessary to explain lysine biosynthesis. 34% identical to dapB from Thermotoga maritima (Q9X1K8). 4-hydroxy-tetrahydrodipicolinate reductase MKLALLGYGKMGQIIEKFAVERGHEIVLKITIDNQEDLTRQNLKSADVAIDFSTPDSVLKNIDACFDANVPIVVGTTGWYGKLQEVKDDCNNSNNTLLYGSNFSIGVNLFFKLNQTLAKLMNNYPAYEVQVEEIHHTQKLDAPSGTAITLAEGIVDNLDRKQEWLNEVVGTDVELFPKAEQLLIESHRIENIPGTHTVIYSSEVDEIEIKHTAHNRAGFALGAVVAAEWLKDKKGFFSITDIFE Caulobacter crescentus NA1000 Caulo CCNA_01982 CCNA_01982 glutamyl-tRNA(Glx) synthetase (EC 6.1.1.24) A conserved essential gene. This activity is necessary to explain glutamine synthesis. Similar to both glutamyl-tRNA(Glu) and glutamyl-tRNA(Glx) synthetases (i.e. from E. coli or the organellar enzyme from Arabidopsis, which is probably transamidating, see PMID:3340166) glutamyl-tRNA synthetase MSNPTPTGVVTRFAPSPTGFLHIGGARTALFNWLYARHTGGKFLIRVEDTDRERSTEAAVAAIFEGLDWLGLKSDDEVIFQHTRAPRHVEVVHELLAKGRAYRCWMSIEELEVAREKARAEGRAIRSPWRDAPEGDLSAPHVIRFKGPLDGETLVNDLVKGPVTFKNIELDDLVLLRADGAPTYNLAVVVDDHDMGVTHVIRGDDHLNNAARQTLIYQAMDWAVPAFAHIPLIHGPDGAKLSKRHGAQAVGEFADLGYIPEGMRNYLARLGWGHGDDEVFTDEQAISWFDVADVVKAPARLDWAKLNHINAQHLRKADDARLTALALAAAETRGEPLPADAAERIARTVPEVKEGAKTILELVDHCAFALKTRPLALEEKTQKQLTEETVERLKRLRDQLAAAPDFDAATLETVLKSFAESEGVGFGKFGPALRGVLTGGAQAPDLNKTMAALSRDEAIGRLDDALAPRA Azospirillum brasilense Sp245 azobra AZOBR_RS01680 AZOBR_RS01680 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase MIIYPAIDLKDGACVRLLRGEMSQATVFNTEPADQARLFESQGFEWLHLVDLNGAFEGKPVNGKAVESILGAVAIPVQLGGGIRDLKTIAHWLEKGVSRVILGTVALREPELVREACREFPGKVAVGIDAREGYVAVAGWAETSTIKALDLALKFEDSGVAAIIYTDINRDGAMGGVNVEATSDLAFHLTTPVIASGGVSSIDDLIALKKEEDTGIEGVICGRALYDGRIDPKTALDLLSPAPVTGKAG Burkholderia phytofirmans PsJN BFirm BPHYT_RS17685 BPHYT_RS17685 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase MLLIPAIDLKDGQCVRLKQGDMDQATIFSEEPAAMARHWVDRGARRLHLVDLNGAFAGKPKNEDAIRAIIEEVGGEIPVQLGGGIRDLNTIERYLDDGLSYVIIGTAAVKNPGFLQDACTAFGGHIIVGLDAKDGKVATDGWSKLTGHEVADLARKFEDYGCESIIYTDIGRDGMLQGINIEATVRLARAVKIPVIASGGLSNLTDIESLCEVEDEGIEGVICGRAIYSGDLDFAAAQTLADRLRESDDA Bacteroides thetaiotaomicron VPI-5482 Btheta 350907 BT1379 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (NCBI ptt file) MIEIIPAIDIIDGKCVRLSQGDYDSKKVYNENPVEVAKEFEANGVRRLHVVDLDGAASHHVVNHRVLEQIATRTSLIVDFGGGVKSDEDLKIAFESGAQMVTGGSVAVKDPELFCHWLEVYGSEKIILGADVKEHKIAVNGWKDESACELFPFLEDYINKGIQKVICTDISCDGMLKGPSIDLYKEMLEKFPNLYLMASGGVSNVDDIIALNEAGVPGVIFGKALYEGHITLKDLRIFL Caulobacter crescentus NA1000 Caulo CCNA_03852 CCNA_03852 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide isomerase MAPMILYPAIDLKDGQCVRLLHGDMDKATVFNTSPADQAQRFVQDGFSWLHVVDLNGAIEGKSVNTAAVEQILESISIPVQLGGGIRTLEGVEAWIEAGVSRVILGTVAVHDPELVKKAARLWPEQIAVAVDVRDGKVAVDGWTGLSDLSAIDLSRRFEDAGVAALIITDISRDGALTGVNVEGVGELADAVSIPVIASGGVAAVADIERLKARQGVEIAGAILGRSLYAGTIKPSEALIAAAA Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_2515 Echvi_2515 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase MEIIPAIDIIGGKCVRLTQGDYGQKKEYADNPLEVAKKFEGAGIKRLHLVDLDGAKAKTIVNRAVLENITSHTSLKVDFGGGVQSDETIQMAFDAGASQVTGGSIAVKNPALFEGWLEKHGSEKIILGADAKNRKIAISGWEETTEADVVDFIKDYHAKGARYVICTDVAKDGLLQGPSVDLYREIIQEIPGIRLIASGGVAEVRDLEVLEKIGVFGTIVGKAFYEGRVSLEELATFAD Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS20320 HSERO_RS20320 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase MLLIPAIDLKDGHCVRLKQGDMDQATVFSEDPAEMALHWLKQGARRLHLVDLNGAFAGKPKNEAAVKAILKAVASFAEENEVEEIPVQLGGGIRDLDTIERYLDDGLSYIIIGTAAVKNPGFLHDACSAFPGQIIVGLDAKDGKVATDGWSKLSGHEVVDLAQKFEGYGCEAIVYTDIGRDGMMGGVNIEATVRLAQAVTIPIIASGGVHNVGDVEALCRVEDEGIEAVICGRSIYEGTLDLRSGQDRADELTRELEANRLSGSK Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1047 Ga0059261_1047 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (EC 5.3.1.16) VIVFPAIDLKAGQVVRLAEGDMTRATVYGENPAAQAEAFAKAGATHLHVVDLDAAFAGESINGGAVAAILARFPGKVQLGGGIRNRASVERWIDMGVSRVVIGTAALEDPDFVREAAAAHPGQIVVAVDARDGFVATKGWADVSTVSIAELGHRFEDAGVAALLFTDVGRDGLLKGCNVEATAALAAEVSIPVIASGGVADISDIHALAGKPGIEGVITGRALYDGRLDLAEALKAAAKVAQ Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS03615 CA265_RS03615 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino]imidazole-4- carboxamide isomerase MYIIPAIDILDGKVVRLREGDYNQKTEYAVSIPEMIEKYRSNGTDFIHIIDLNGAKGDFSNQKTLFEIIKKTEMKVQYGGGIRTIEQVTNLLDAGIHRVIVGTQAITNPDFLPQLSEAFAKKDDYANRIVIAIDVLDEVIKYSGWMESSPIKLMDYVDKCLSLGFFRFLCTDISKDGKLGGAAIDLYEKLLEHSPMIKLIASGGVSSMQDIYDLAKYPIRSVVVGKAIYEDRITIEEIKEWNLKALSSI Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_1624 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase (EC 5.3.1.16) MLIIPAIDLKDGACVRLRQGRMEDSTVFSDDPVSMAAKWVEGGCRRLHLVDLNGAFEGQPVNGEVVTAIAKRYPNLPIQIGGGIRSLETIEHYVKAGVSYVIIGTKAVKDPAFVAEACRAFPGKVIVGLDAKDGFVATDGWAEISTIQVIDLAKQFEADGVSAIVYTDIAKDGMMQGCNVSYTAALAAATKIPVIASGGIHNLGDIKSLLDAKAPGIIGAITGRAIYEGTLDVAEAQAFCDSYKG Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_359 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase (EC 5.3.1.16) MLIIPAIDLKDGACVRLRQGRMEDSTVFSDDPVSMAAKWVEGGCRRLHLVDLNGAFEGQPVNGEVVTAIAKRYPNLPIQIGGGIRSLETIEHYVKAGVSYVIIGTKAVKDPAFVAEACRAFPGKIIVGLDAKDGFVATDGWAEISTIQVIDLAKQFEADGVSSIVYTDIAKDGMMQGCNVPFTAALAAATKIPVIASGGIHNLGDIKTLLDAKAPGIIGAITGRAIYEGTLDVAEAQAFCDSYKG Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_12085 AO353_12085 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase MLIIPAIDLKDGACVRLRQGRMEDSTVFSDDPVSMAAKWVEGGCRRLHLVDLNGAFEGQPVNGEVVTAIAKRYPNLPIQIGGGIRSLETIEHYVKAGVSYVIIGTKAVKDPAFVAEACRAFPGKVIVGLDAKDGFVATDGWAEISTVQVIDLAKQFEADGVSAIVYTDIAKDGMMQGCNVSYTAALAAATRIPVIASGGIHNLGDIKSLLDAKAPGIIGAITGRAIYEGTLDVAEAQAFCDSYKG Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_09800 AO356_09800 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase MLIIPAIDLKDGACVRLRQGRMEDSTVFSDDPVSMAAKWVEGGCRRLHLVDLNGAFEGQPVNGEVVTAIAKRYPNLPIQIGGGIRSLETIEHYVKAGVSYVIIGTKAVKEPEFVAEACRAFPGKVIVGLDAKDGFVATDGWAEVSTVQVIDLAKRFEADGVSAIVYTDIAKDGMMQGCNVPFTAALAAATKIPVIASGGIHNLGDIKALLDAKAPGIIGAITGRAIYEGTLDVAEAQAFCDSYKG Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_3839 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase (EC 5.3.1.16) MLIIPAIDLKDGACVRLRQGRMEDSTVFSDDPVSMAAKWVEGGCRRLHLVDLNGAFEGQPVNGEVVTAIAKRYPNLPIQIGGGIRSLETIEHYVKAGVSYVIIGTKAVKEPEFVAEACRAFPGKVIVGLDAKDGFVATDGWAEVSTVQVIDLAKRFEADGVSAIVYTDIAKDGMMQGCNVPFTAALAAATRIPVIASGGIHNLGDIKALLDAKAPGIIGAITGRAIYEGTLDVAEAQAFCDSYKG Pseudomonas stutzeri RCH2 psRCH2 GFF155 Psest_0155 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase MLIIPAIDLKDGACVRLRQGLMDDATVFSDDPVAMAAKWVEAGCRRLHLVDLNGAFEGQPVNGEVVTAIAKRYPDLPIQIGGGIRTLETIEHYVRAGVSYVIIGTKAVKEPGFVTEACRAFPGKVIVGLDAKDGFVATDGWAEVSSVQAVDLARRFEADGVSAIVYTDIAKDGMMQGCNVEATVALANASRIPVIASGGIHNIGDIQKLLDTNTPGIVGAITGRAIYEGTLDVAEAQALCDLKYKDE Pseudomonas putida KT2440 Putida PP_0292 PP_0292 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide isomerase MLIIPAIDLKDGACVRLRQGRMEDSTVFSDDPVSMAAKWVEGGCRRLHLVDLNGAFEGQPVNGEVVTAIAKRYPNLPIQIGGGIRSLETIEHYVKAGVSYVIIGTKAVKQPEFVAEACKAFPGKVIVGLDAKDGFVATDGWAEVSSVQVIDLAKRFEADGVSAIVYTDIAKDGMMQGCNVPFTKALAEATRIPVIASGGIHNLGDIKALLDAKAPGIIGAITGRAIYEGTLDVAEAQAFCDNYQG Sinorhizobium meliloti 1021 Smeli SMc02570 SMc02570 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase MILFPAIDLKDGQCVRLKLGDMEQATVYNPDPAAQARAFEEQGFEWLHVVDLNGAFAGETVNGAAVDAILKATKNPVQLGGGIRTLEHIENWLSRGLKRVILGTVAVRDPALVIEACRKFPGRVAVGIDAKGGKVAVEGWAEASELGVVELARKFEGAGVAAIIYTDIDRDGILTGINWASTLELADAVSIPVIASGGLASMDDIRRMTEPDAQKLEGAISGRALYDGRIDPKEALDLIREARKGKL Pseudomonas simiae WCS417 WCS417 GFF309 PS417_01575 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00007. 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase MLIIPAIDLKDGACVRLRQGRMEDSTVFSDDPVSMAAKWVEGGCRRLHLVDLNGAFEGQPVNGEVVTAIAKRYPSLPIQIGGGIRSLETIEHYVKAGVSYVIIGTKAVKDPAFVAEACRAFPGKVIVGLDAKDGFVATDGWAEISTVQVIDLAKQFEADGVSAIVYTDIAKDGMMQGCNVPFTAALAAATKIPVIASGGIHNLGDIKSLLDAKAPGIIGAITGRAIYEGTLDVAEAQAYCDAYNG Bacteroides thetaiotaomicron VPI-5482 Btheta 349730 BT0202 histidinol-phosphate aminotransferase (EC 2.6.1.9) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01141. histidinol-phosphate aminotransferase (NCBI ptt file) MKTLQELTRPNIWKLKPYSSARDEYKGAVASVFLDANENPYNLPHNRYPDPMQWELKTLLSKIKKVSPQHIFLGNGSDEAIDLVFRAFCEPEKDNVVAIDPTYGMYQVCADVNNVEYRKVLLDENFQFSAEKLLAATDERTKLIFLCSPNNPTGNDLLRSEIEKILREFEGLVILDEAYNDFSEAPSFLEELDKYPNLVVFQTFSKAWGCAAIRLGMAFASEAIIGILSKIKYPYNVNQLTQQQAIAMLHKYYEIERWIKTLKEERDYLEEEFAKLSCTVRMYPSDSNFFLAKVTDAVKIYNYLVGEGIIVRNRHSISLCCNCLRVTVGTRVENNTLLAALKKYQG Desulfovibrio vulgaris Hildenborough JW710 DvH 206463 DVU1029 hisC histidinol-phosphate aminotransferase (EC 2.6.1.9) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01141. histidinol-phosphate aminotransferase (TIGR) MTAPSMSRPDDVRPEVLDFKPYVPGLSIDEIRDRFGLADVVKLASNENPLGTSPVVQRTLKTKADLAFRYAQSGNPRLTRAIAAHHGVAPERVVAGNGSDEIIDLLIRVRATPGKHNIVAFRPCFSIYELQAKFCGLEFRQADLRPDFTFDWDAFLAATDENTAIAFVTTPDNPSGWCPPVSELEHVARTLPPSCLFVIDEAYMDFCGDEAAHSLLSRLDAFPNIAVLRTFSKSFGLAGLRLGYGILPERLADYLHRVRLPFSVNILAEEAGLAALEDTVFRSETLRVTAEGRAYIAEGLTALGCEVMPSWANFIMFRPPTDATDLFEALLRRGIIIRPLKSYGLPQHLRVSVGNADENRRFIEACKEILPHA Marinobacter adhaerens HP15 Marino GFF2483 HP15_2427 histidinol-phosphate aminotransferase (EC 2.6.1.9) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01141. histidinol-phosphate aminotransferase MSKFWSPLVNDLVPYVPGEQPKMANLVKLNTNENPFGPSPKVIEAIQAELNDGLRLYPDPEGESLRETIAAYHKITPEQIFLGNGSDEVLAHIFFGLFQHGEPILFPDITYSFYPVYCGLYNIESKKVPLTESFEINPEDFKQPNGGVIFPNPNAPTGRYLELQYVEEILAANPNRVVVVDEAYIDFGGESAITLVDKYPNLLVSQTLSKARSLAGLRVGFAVGHPDLIEALNRVKNSFNSYPLDRLALAGAKAAYEDEAWFRKCCDGVISERERVTAVLEGLGFEVLPSKANFIFARHKEQPGEVLAKGLREQGIIVRHFNKPRISEFLRITIGTVEQNDALIARLESL Desulfovibrio vulgaris Miyazaki F Miya 8500145 DvMF_0908 histidinol-phosphate aminotransferase (EC 2.6.1.9) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01141. histidinol-phosphate aminotransferase (RefSeq) MCADKTASAGAPTGLPLASPSAVRPEVCGFKPYTPGLSIDEIRDRYGLAHVIKLASNENPLGTSPVVQHALRHKADLAFRYAQSGNPRLTAAIAAHHGVPAERVVAGNGSDEIIDLIVRVRAVPGVHNVVAFNPCFSIYELQTRLAGVEFRQAPLAADFSFDWDGLMALVDDATAVVFVTTPDNPSGFCPPVADLERLAHALPAGCLLVVDEAYMDFCGDESAHSLLARVDEFPNLAVLRTFSKSFGLAGLRLGYGILPVQLADYLRRVRLPFSVNILAEEAGLAALADDVFRTETLRVISEGRAALTEGLTALGCHVYPSKANFVMFRPAPTCKSAAHLFEELLRRGIIIRPLKSYGLPDLLRVSVGSPDENAAFLKAAGEIMAHA Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_3251 histidinol-phosphate aminotransferase (EC 2.6.1.9) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01141. Histidinol-phosphate aminotransferase (EC 2.6.1.9) MSKFWSPFVKNLVPYVPGEQPKLTRLVKLNTNENPYGPSPKALAAMQTELNDNLRLYPDPNSDLLKGAVARYYGVQSNQVFLGNGSDEVLAHIFHGLLQHDQPLLFPDISYSFYPVYCGLYGIQFDAVPLDAQFQIDPADYAKPNGGIIFPNPNAPTGCLLALEAVEQILKANPDSVVVVDEAYIDFGGETAISLVDRYPNLLVTQTLSKSRSLAGLRVGLAVGHPELIEALERIKNSFNSYPLDRLANVGGAAAFDDREYFDRTCRLVIEHREWVVAQLQAKGFEVLPSAANFIFARHPRHDAAGLAAKLREQGVIVRHFKQERIAQFLRISIGTPEQNQALIEALGEL Pseudomonas stutzeri RCH2 psRCH2 GFF3234 Psest_3297 histidinol-phosphate aminotransferase (EC 2.6.1.9) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01141. histidinol-phosphate aminotransferase MSKFWSPFVKDLVPYVPGEQPKLSKLVKLNTNENPYGPSPRAIAAMQAELNDSLRLYPDPNGERLKQAVADYYGVQPAQVFVGNGSDEVLAHAFHGLFQHAGPLLFPDISYSFYPVYCGLYGIAYETVALDEQFQIDVADYNRPNGGIIFPNPNAPTGCLLALEAIERLLQANTETVVLVDEAYVDFGGESAIALVDRYPNLLVTQTLSKSRSLAGLRVGLAVGHPDLIEALERIKNSFNSYPLDRIAIAGAAAAFEDRAYFQQTCQQVIDSREAVVAAMQGLGFEVLPSAANFIFARHPQRDAATIAASLREQGVIVRHFKQRRIEQFLRITIGTPEQNQALLEALG Pseudomonas putida KT2440 Putida PP_0967 PP_0967 histidinol-phosphate aminotransferase (EC 2.6.1.9) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01141. Histidinol-phosphate aminotransferase MSRFWSPFVKDLVPYVPGEQPKLARLVKLNTNENPYGPSPKALEAMRGELNDNLRLYPDPNGDRLKQAVAEYYGVTPAQVFVGNGSDEVLAHIFHGLFQHDAPLLFPDISYSFYPVYCGLYGIAFEQVALDEQFQIRIEDYKKPNAGIIFPNPNAPTGCLMPLQAVEELLQANRDSVVVVDEAYIDFGGETAISLVDRYDNLLVTQTLSKSRSLAGLRVGLAVGHPDLIEALERIKNSFNSYPLDRAAIVGAAVAFEDREYFEETCRKVIDSREVLVGQLQAKGFEVLPSAANFIFARHPQQDAGELAARLREQGVIVRHFKQPRIAQFLRITIGTPEMNQALLDALS Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS20310 HSERO_RS20310 phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM PF01502. phosphoribosyl-AMP cyclohydrolase MSISAKWLNKVKWDEVGLVPVIAQEVGSNDVLMFAWMNREALARTVEIGQAVYWSRSRKKLWHKGEESGHFQKVHEIRLDCDEDVVLLKVEQVAGIACHTGRHSCFFQKFEGSADSGEWVTVEPVLKDLQPGAGGGPAATAAEPEAKPKRVRKSIPKPVDSDKTPS Azospirillum brasilense Sp245 azobra AZOBR_RS19500 AZOBR_RS19500 ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00070. ATP phosphoribosyltransferase catalytic subunit VSASQPLVLALPKGRILKELRPLLAHAGIEPEAAFDDADSRLLRFATNIPNLSIIRVRSFDVATFVAFGAAHLGVAGNDVLMEFDYPEIYAPLDLGIGKCRLSVAEPVELGESDDPSRWSHVRVATKYPEVTRKHFAARGVQAECVKLNGAMELAPTLGLCRRIVDLVSTGSTLKANGLVEIEHIADVTSRLIVNRAAFKTRPEEISGWIDRFREAVNARQA Burkholderia phytofirmans PsJN BFirm BPHYT_RS17715 BPHYT_RS17715 ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00070. ATP phosphoribosyltransferase MSAMPQTSSSPAVSAPLTLALSKGRIFEETLPLLAAAGIEVAEDPETSRKLILPTTDANLRVIIVRATDVPTYVEYGAADFGVAGKDVLLEHGGSGLYQPVDLDIARCRMSVAVAAGFDYANAVRQGARLRVATKYVETAREHFAAKGVHVDLIKLYGSMELAPLVGLADAIVDLVSSGNTLRANNLVEVEEIMQISSRLVVNQAALKLKRAALRPILDAFERASKAGAATA Caulobacter crescentus NA1000 Caulo CCNA_03626 CCNA_03626 ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in many defined media, and cofit with histidinol dehydrogenase (CCNA_02431). Hits TIGR00070. ATP phosphoribosyltransferase MSTPMIFAIPSKGRLKDQVEAWLADCGFKLEMTGGARGYSAELSGLPGVSVRLLSAGDIAAGLDSGDLHLGVTGEDLLRERGDDMDSRVMLLRALGFGRADLVVTAPKNWLDVDTMADVDEVGHAHLARTGRRLRVATKYVTQTRAFFARHGVADYRIVESSGATEGAPAAGAAELVVDITTTGATLAANGLKILSDGVILKSQAQLTASLTAGWNGEQLDALRRLLSVVEAKGRAGKLATLVWPAEQDRAAQDAVAAFIARGGSRRANGALLATADLFDAAAALAEAGVEPVTVSRPDYVFESRSAVLDRFAEALKSKI Desulfovibrio vulgaris Hildenborough JW710 DvH 209044 DVU0114 hisG ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00070. ATP phosphoribosyltransferase (TIGR) MSIRTPMKLGIPKGSLEEATINLLARSGWKIRKHHRNYFPEINDPELTARLCRVQEIPRYIEDGILDVGLTGKDWLLETGSDVVVVSDLVYSKVSNRPARWVLAVAGDSPYTRPEDLAGKRIATELLGVTKRYFADAGIEVNVQYSWGATEAKVVEGLADAIVEVTETGTTIKAHGLRIISEVLLTNTVLIANRAAWEDPCRRRKIEQIDLLLQGALRADSLVGLKMNVPTRCLDAVLDQLPSLNSPTVAGLRDNTWFAVEIVVDNGVVRDLIPRLREAGAEGIIEYALNKVI Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS20350 HSERO_RS20350 ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00070. ATP phosphoribosyltransferase MTQQLTLALSKGRIFEETLPLLKAAGITVSEDPESSRKLILPTNDPDVRVIIVRASDVPTYVQYGAADFGVAGKDVLLEHGGEGLYQPIDLNIAKCRLSVAVQEGFDYANAVRQGARLRVVTKYVNTAREHFAAKGVHVDLIKLYGSMELGPLVGLSDAIVDLVSTGGTLRANKLVEVEHIIDISSRLVVNQAALKLKRERLQPILDAFEKASKAK Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1280 Ga0059261_1280 ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00070. ATP phosphoribosyltransferase MSEPIILAVPKGRILEEALPLLAHAGIIPEPAFADEGSRALRFKTNRPDIDLIRVRAFDVATFVAHGAAQLGIVGSDVLAEFAYSELYAPVDLGIGYCRLSVAEPAALAATDDPRGWSHVRVATKYPSLTRRHFEARGVQAECIKLNGAMELAPLLDLAPRIVDLVSSGRTLKENGLVEVETIMEVSSRLVANRAAFKTRPEIVPLIDAFRRAVEAKAA Marinobacter adhaerens HP15 Marino GFF2485 HP15_2429 ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00070. ATP phosphoribosyltransferase MTDSITIALSKGRILEETLPLLAEAGIELIDDVKKSRKLVFPTTDPNVRVLIIRATDVPTYVQYGGADLGVTGKDVLMEHGGEGLYEPLDLNISRCRLMTAGPKDQTPPSGRIKVATKFVNLARRYYSAQGRQADIIKLYGAMELAPILGLADEIVDIVDTGNTLKANGLEARELIEHISSRLVVNRASMKMKHERINPIIEKMSAAVDKRRT Desulfovibrio vulgaris Miyazaki F Miya 8501229 DvMF_1963 hisG ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00070. ATP phosphoribosyltransferase (RefSeq) MSGNNMLKIGIPKGSLEEATVNLFARSGWKIRKHHRNYFPEINDPELTARLCRVQEIPRYLEDGVLDVGLTGKDWLLETGADVVTVSDLVYSKVSNRPARWVLAVAGDSPYVRPEDLAGCTIATELLGVTRRYFEDAGIPVKVQYSWGATEAKVVEGLADAIVEVTETGTTIKAHGLRIIAEVLLTNTVLIAGKAAWADPWKRAKIEQIDLLLQGALRADSLVGLKMNVPAHNLDAVLDQLPSLNSPTVAGLRDSTWYAVEIVVENDLVRDLIPRLRAAGAEGIIEYSLNKVI Phaeobacter inhibens BS107 Phaeo GFF2940 PGA1_c29870 ATP phosphoribosyltransferase (EC 2.4.2.17) A conserved essential gene. This activity is necessary to explain histidine biosynthesis. Hits TIGR00070, and no other candidates for this step were identified in the genome. ATP phosphoribosyltransferase HisG MSLKLGVPSKGRLMEKTFEWFAKRGITLSRTGSDREYAGAVAGIDGIDLVLLSAGEMPRELAAGRIHLGVTGTDLVQEKLPLWEQQVEEIAGLGFGHADLILAVPQIWVDVETIDDLDAVAAAFRAKHGHRLRIATKYHRLVREYLMDAGVADYQLVDSQGATEGTVKNETAEMVADITSTGETLRANHLKLMSDGLILRSQATLWRSRVAKYSAKEKATLGDLLERLHG Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_1067 ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00070. ATP phosphoribosyltransferase (EC 2.4.2.17) MLTIALSKGRILDDTLPLLAEAGIVPTENPDKSRKLIIPTTQADVRLLIVRATDVPTYVEHGAADLGVAGKDVLMEYGGQGLYEPLDLRIALCKLMTAGRVGDVEPKGRLRVATKFVNVAKRYYAEQGRQVDIIKLYGSMELAPLIGLADKIIDVVDTGNTLRANGLEPQDFIADISSRLIVNKASMKMQHARIQALIDTLRKAVESRHRG Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_5001 ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00070. ATP phosphoribosyltransferase (EC 2.4.2.17) MLTIALSKGRILDDTLPLLAEAGIVPTENPDKSRKLIIPTTQEDVRLLIVRATDVPTYVEHGAADLGVAGKDVLMEYGGQGLYEPLDLQIAQCKLMTAGKVGAVEPKGRLRIATKFVNVAKRYYAEQGRQVDIIKLYGSMELAPLIGLADKIIDVVDTGNTLRANGLEPQDFIAAISSRLIVNKASMKMQHARIQALIDTLRKAVESRHRG Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_05115 AO353_05115 ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00070. ATP phosphoribosyltransferase MLTIALSKGRILDDTLPLLAEAGIVPTENPDKSRKLIIPTTQADVRLLIVRATDVPTYVEHGAADLGVAGKDVLMEYGGQGLYEPLDLQIAQCKLMTAGKVGAVEPKGRLRIATKFVNVAKRYYAEQGRQVDIIKLYGSMELAPLIGLADKIIDVVDTGNTLRANGLEPQDFIAAISSRLIVNKASMKMQHARIQALIDTLRKAVESRHRG Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_06970 AO356_06970 ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00070. ATP phosphoribosyltransferase MLTIALSKGRILDDTLPLLAEAGIVPTENPDKSRKLIIPTTQADVRLLIVRATDVPTYVEHGAADLGVAGKDVLMEYGGQGLYEPLDLRIARCKLMTAGKVGAPEPKGRLRVATKFVNIAKRYYAEQGRQVDIIKLYGSMELAPLIGLADKIIDVVDTGNTLRANGLEPQDFIADITSRLIVNKASMKMQHARIQALIDTLRKAVESRHRG Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_3253 ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00070. ATP phosphoribosyltransferase (EC 2.4.2.17) MLTIALSKGRILDDTLPLLAEAGIVPTENPDKSRKLIIPTTQADVRLLIVRATDVPTYVEHGAADLGVAGKDVLMEYGGQGLYEPLDLQIARCKLMTAGKVGAPEPKGRLRVATKFVNIAKRYYAEQGRQVDIIKLYGSMELAPLIGLADKIIDVVDTGNTLRANGLEPQDFIADITSRLIVNKASMKMQHARIQALIDTLRKAVESRHRG Pseudomonas stutzeri RCH2 psRCH2 GFF3236 Psest_3299 ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00070. ATP phosphoribosyltransferase MLTIALSKGRILDDTLPLLAAAGIVPTENPDKSRKLIIPTTQDDVRLLIVRATDVPTYVEHGAADLGVAGKDVLMEYGGQGLYEPLDLRIANCKLMTAGKVGAPEPKGRLRVATKFVNVAKRYYAEQGRQVDIIKLYGSMELAPLVGLADKIIDVVDTGNTLRANGLEPQELIAHISSRLVVNKASMKMQHARIQALIDILHAAVQQHQH Pseudomonas putida KT2440 Putida PP_0965 PP_0965 ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00070. ATP phosphoribosyltransferase MLTIALSKGRILDDTLPLLAEAGIVPTENPDKSRKLIIPTTQDDVRLLIVRATDVPTYVEHGAADLGVAGKDVLMEYGGQGLYEPLDLQIAQCKLMTAGVVGAAEPKGRLRVATKFVNVAKRYYAEQGRQVDIIKLYGSMELAPLINLADKIIDVVDTGNTLRANGLEPQELIATISSRLVVNKASMKMQHARIQSLIDTLRAAVESRHRG Sinorhizobium meliloti 1021 Smeli SMc00917 SMc00917 ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00070. ATP phosphoribosyltransferase catalytic subunit MTVTIALPSKGRMKDEASAIFERAGMKIAAVGSDRSYRGRVEGWDDVEIAYLSASEIAREIGSGAVDFGVTGEDLVREGLADADARVDFAARLGFGHADVVVAVPEIWYDVDTMADLGDVAADFRARHGRRLAIATKYWRLTQQFFSGSHGIQLYRIVESLGATEGAPASGSADIIVDITSTGSTLKANHLKILSDGVILRSEACLVRARKATHEGNPVIDRIVAAVRAVL Pseudomonas simiae WCS417 WCS417 GFF870 PS417_04415 ATP phosphoribosyltransferase (EC 2.4.2.17) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00070. ATP phosphoribosyltransferase catalytic subunit MLTIALSKGRILDDTLPLLAEAGIVPTENPDKSRKLIIPTTQDDVRLLIVRATDVPTYVEHGAADLGVAGKDVLMEYGGQGLYEPLDLRIALCKLMTAGRVGDVEPKGRLRVATKFVNVAKRYYAEQGRQVDIIKLYGSMELAPLIGLADKIIDVVDTGNTLRANGLEPQEFIADISSRLIVNKASMKMQHARIQALIDTLRKAVESRHRG Desulfovibrio vulgaris Hildenborough JW710 DvH 209219 DVU0285 hisH IGP synthase, amidotransferase subunit (EC 4.3.2.10) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01855. imidazole glycerol phosphate synthase, glutamine amidotransferase subunit (TIGR) MLAILDYKAGNQTSVRRALDHLGIPCVITADPEVIQGAAGVIFPGVGAAGQAMNELVTTGLDEVLRRQVQAGRPLLGICVGCQIMLDYSQENDTKALGIIPGECRLFNPAWTDEDGAPIRVPHMGWNHIVQRRPCELLKGIEPEAEFYFVHSYYPAPPEEYVIATCTYGAEFCAIHGGPGLWAVQFHPEKSGRPGLRLLANFHRYCTEAADAQ Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS20325 HSERO_RS20325 IGP synthase, amidotransferase subunit (EC 4.3.2.10) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01855. imidazole glycerol phosphate synthase MNKIVVVDYGMGNLRSVAQALRHVAPEADVRISGEVADIRAADRVVLPGQGAMPDCMRSLRESGVQDAVIEASRTKPLFGVCVGEQMLFDWSEEGDTPGLGLLPGKVVRFDLEGMRQDDGSLFKVPQMGWNHVHQTSRHPLWEGIADNAFFYFVHSYYAVPAESAHVVGQTPYGRDFACAVARDNIFATQFHPEKSASAGLQLYRNFVHWKP Desulfovibrio vulgaris Miyazaki F Miya 8501586 DvMF_2305 hisH IGP synthase, amidotransferase subunit (EC 4.3.2.10) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01855. imidazole glycerol phosphate synthase subunit HisH (RefSeq) MLAILDYKAGNQTSVRRALDHLGIPCVITADPAVIAGAHGVIFPGVGAAGQAMNELLTTGLDKVLKDQVQAGKPLLGICVGCQIMLDYSQENDTKALGIVPGECRLFNAAWTEEDGTPIRVPHMGWNSIVQKRPCELLKGIEPEAEFYFVHSYYPAPPESYVIATCTYGEEFCAIHGGPGLWAVQFHPEKSGRPGLALLRNFYAYCKEASRA Azospirillum brasilense Sp245 azobra AZOBR_RS01690 AZOBR_RS01690 phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR03188. phosphoribosyl-ATP pyrophosphatase MSDDKAAATAEVLDRLYATVQARKGADPETSYTAKLFHRGTAKIAQKVGEEAVETVIEAVRGDKAAVASESADLLYHLMVLWADAGLEPAAVWEKLAQREGTSGIAEKNARKA Burkholderia phytofirmans PsJN BFirm BPHYT_RS17670 BPHYT_RS17670 phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR03188. phosphoribosyl-ATP pyrophosphatase MTQSTQTTSSDSASTTDTLMRLAAIIDSRKGGDPDVSYVSRLFHKGDDAVLKKIGEEATEVVLAAKDARHGGAPKALVGEVADLWFHCLVMLSHFDLSPADVLAELERREGMSGIEEKALRKSRDREQNGD Caulobacter crescentus NA1000 Caulo CCNA_03854 CCNA_03854 phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR03188. phosphoribosyl-ATP pyrophosphatase MSQRLTDVLQRLAATIEARKGGDPSVSYTAKLLNDPALAAKKLGEEAVETVIAAVAQGSDALAAESADLLYHWLALMAASGVSLDAVAEKLEAREGTSGIAEKASRA Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_1051 Ga0059261_1051 phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR03188. phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) MAADILDTLEAVIRERRTGDPATSYVAKLTAKGRAKIAQKLGEEAVEAAIAAVQDDRDGLTGEAADLIFHLLVLLADTGLSLDDVRAELARREGISGIDEKASRHAD Marinobacter adhaerens HP15 Marino GFF3253 HP15_3195 phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) Important for fitness in many defined media, and highly cofit with ATP phosphoribosyltransferase HP15_2429. Hits TIGR00070. phosphoribosyl-ATP pyrophosphatase MSDVLENLARVLEARKEADPETSYVASLHAKGLNKILEKVGEECTETLLAAKDAEHSGETRDVVYETADLWFHSMVMLSRLGLGPKDILDELASRFDLSGLEEKASRNK Pseudomonas fluorescens FW300-N1B4 pseudo1_N1B4 Pf1N1B4_1566 phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) Important for fitness in many defined media and cofit with phosphoribosyl-AMP cyclohydrolase (Pf1N1B4_1565). Hits TIGR03188. Phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) MSDTLTRLAQVLEERKGAAADSSYVASLYHKGLNKILEKVGEESVETIIAAKDAAISGDCSDVIYETADLWFHSMVMLAQLGQHPQAVLDELDRRFGLSGHAEKASRPSA Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_303 phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR03188. Phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) MSDTLTRLAEVLEERKGAAADSSYVASLYHKGLNKILEKVGEESVETIIAAKDAAVSGDCSDVIYETADLWFHSMVMLAQLGQHPQAVLDELDRRFGLSGHAEKASRPSA Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_12360 AO353_12360 phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR03188. phosphoribosyl-ATP pyrophosphatase MTDTLTRLAQVLEERKGAAADSSYVASLYHKGLNKILEKVGEESVETIIAAKDAAISGDCSDVIYETADLWFHSMVMLAQLGQHPQAVLDELDRRFGLSGHVEKASRPSA Pseudomonas fluorescens FW300-N2C3 pseudo5_N2C3_1 AO356_09525 AO356_09525 phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR03188. phosphoribosyl-ATP pyrophosphatase MSDTLTRLAQVLEERKGAAADSSYVASLYHKGLNKILEKVGEESVETIIAAKDAAISGDCSDVIYETADLWFHSLVMLAQLGQHPQAVLDELDRRFGLSGHVEKASRPSA Pseudomonas fluorescens FW300-N2E2 pseudo6_N2E2 Pf6N2E2_3783 phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR03188. Phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) MSDTLTRLAQVLEERKGAAADSSYVASLYHKGLNKILEKVGEESVETIIAAKDAAISGDCSDVIYETADLWFHSLVMLAQLGQHPQAVLDELDRRFGLSGHVEKASRPSA Pseudomonas stutzeri RCH2 psRCH2 GFF3874 Psest_3944 phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR03188. phosphoribosyl-ATP pyrophosphohydrolase MSDTLTRLAEVLEARKGAAPDSSYVASLYHKGLNKILEKVGEESVETILAAKDAAVSGDASDLIYETADLWFHSMVMLAALGQHPQAVLDELDRRFGLSGHAEKAARPQT Pseudomonas putida KT2440 Putida PP_5015 PP_5015 phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR03188. Phosphoribosyl-ATP pyrophosphatase MSDTLNRLAEVLEERKQAAPDSSYVASLYHKGLNKILEKLGEESVETIIAAKDAQISKDYSDVIYETADLWFHSLVMLSALGQHPQAVLDELERRFGLSGHDEKAARQPSA Pseudomonas simiae WCS417 WCS417 GFF363 PS417_01850 phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR03188. phosphoribosyl-ATP pyrophosphatase MSDTLNRVAQVLEDRKGADADSSYVASLYHKGLNKILEKLGEESVETIIAAKDAQISGDCSDVIYETADLWFHSLVMLAQLGQHPQAVLDELDRRFGLSGHAEKASRPSA Desulfovibrio vulgaris Miyazaki F Miya 8500664 DvMF_1412 homoserine dehydrogenase (EC 1.1.1.3) Important for fitness in most defined media and strongly cofit with homoserine kinase (DvMF_0971). 37% identical to homoserine dehydrogenase from Lactococcus lactis (P52985). homoserine dehydrogenase (RefSeq) MGSDSDKPGGKRLVIGMAGFGTVGSGLARVLDENRQWITERTGREMVIKTILVRDLAKPRAWPVPQGATLTADPAVLTDDPEIDVLVELMGGIAAPHAIIKRALEAGKHVVTANKALLAEDGYDLYRLAEQKNVGLHHEASVAGGIPIVQTLKESLAGNRIGSLVGILNGTANYILSEMTSNGLDFATALAQAQELGYAEADPTLDIEGHDTAHKLVLLIRLAYGMDYPYAELPVQGIAGIDRMDIEFARELGFRIKLLAQVREVDGKLEAGVFPTLVKHTFLIARVGGAYNAIRLEGNAVGPVFLHGLGAGSLPTASAVLADLMTVARGAAPHNTGFQRQVPPRADILPPADAESSYYVRAMVPDNPGVLRDLAGAMADHSISIAQAIQKGQHPQGVPLVFMTHAAKASAIQGAIAQVQAAGLLLAPPVCYRVLQ Caulobacter crescentus NA1000 Caulo CCNA_03750 CCNA_03750 threonine deaminase (EC 4.3.1.19) Important for fitness in most defined media. Hits TIGR01127. threonine dehydratase MTLDLAAIQAAAGRLQGQIERTPCRHSKTLSKITGAEVWVKFENLQFTAAYKERGALNKLMLLSETEKQRGVIAASAGNHAQGLAYHGARLGVPVTIVMPKTTPFVKVQHTRDFGATVVIEGETYDDANAHARKLRDEQGLTFVHPFDDYDIMAGQGTIALEMLEDAPDLEILPVPIGGGGLISGVATAAKALKPDIRIIGCEPAMYPSFTAKMRGVAAHCGGQTIAEGVAVKQVGELTYGVVRPLLDDVLLLEEPYLEQAVSLYCNVEKTIAEGAGAASLAALLAYPERFRGKKCGLILCGGNIDTRLLASVLTRELVRAQRLASLRIIGDDRPGLLSTVASVIGAMGANIIEVNHNRLALDVPAKGAEFDITIETRDAQHTQEVMEALRESGYPPRVV Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_3694 Ga0059261_3694 threonine deaminase (EC 4.3.1.19) Important for fitness in most defined media. Hits TIGR01127. threonine ammonia-lyase, medium form MVYGPPMATQAATAAQPLPVTLADVQAAAARIMGAVVHTPTLHSKTLSDLTGATVYLKFENLQFTAAYKERGALNTLLQLDDAARAKGVIAASAGNHAQGLAYHGNRLGIPVTIVMPKSTPTVKVMQTESHGATIILEGETFDEAYAHARQLEASNGYTFVHPFDDPRIIAGQGTVFLEMLADAPAIDTLIVPIGGGGLISGALTVAKAADKPIEVVGVQAELFPSMFNRFTGAHEPIGGDTLAEGIAVKEPGGLTAQIVEALVDEIMLVSERSLEEAVSLLLQIEKTVVEGAGAAGLAALMTQPERFRGKTVGVILTGGNIDTRLLANVLLRDLARSGRLARLRIRLQDRPGALYQVARIFQEQTVNILELSHQRIFTNLPAKGLSLDVECETRDRAHLERLISALQEAGYEVRLIELA Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS15860 CA265_RS15860 threonine deaminase (EC 4.3.1.19) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR02079. threonine dehydratase MNTTTPNTLDFQSASQRLKGVVKRTPLEFNAGLSAHYNANIYLKREDLQIVRSYKLRGAYNKISSLPQDALINGVVCASAGNHAQGVAYSCKKLGIKGVIFMPEITPKQKVKQTYMFGGDNVEVVLVGDTFDDCLKEALAYSAEKSATFIPPFDDEKVIEGQATVGVEIYEDLPDLDMIVMPVGGGGLASGVSAYMKTVKPEVKLVGVEPLGAPSMVTAMEYGGPFTLEEIDRFVDGAAVKRIGHITYEYCKELLDQMHLIPEGKICTTILKLYNEDAIVVEPAGALSVAALDQLKDQITGKTVVCIVSGGNNDIERMQEIKEKSLLFEGLKHYFIVRFPQRPGALKLFVNEVLGPQDDITRFEFIKKTNKENGPALVGIELSNKNDYASLLQRMKDFKFEIIELNQDQTLFEYLV Bacteroides thetaiotaomicron VPI-5482 Btheta 351604 BT2076 acetohydroxybutanoate synthase regulatory subunit (EC 2.2.1.6) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00119. acetohydroxyacid synthase small subunit (NCBI ptt file) MSDKTLYTIIVHSENIAGLLNQVTAVFTRRQINIESLNVSASSIKGVHKYTITAWTDKDTIEKVVKQIEKKIDVIQAHYFTEDEIYFHEIALYKVSTPAFQETPEASKVIRRYNARIVEVNPVFSIVEKNGMSEEITSLYEELRALKCVLQFVRSGRVAITTSCFERVNEFLDGQEAKYKQSKKEQE Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_2057 Echvi_2057 acetohydroxybutanoate synthase regulatory subunit (EC 2.2.1.6) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00119. acetolactate synthase, small subunit MNRYTVSLFTENFIGILNRVTLIFTRRGVNIDALTASESKEDGVHRITIEVTTTEDQVIQIVKQTEKIIDVIKSFYYKDDEVVYQEIALYKIPISSLDPGLEKVIRQYNARIISAEKEFVVIEMTGHKEDTKALLEILKDFNILEFARSGRVAVAKPMGTIEQYLNN Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS15810 CA265_RS15810 acetohydroxybutanoate synthase regulatory subunit (EC 2.2.1.6) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00119. acetolactate synthase small subunit MSTENTIEHKIDKADLDGKQEYTITVYAENRIGLLNRIAIIFSKRKINIESLNTSPSEIDGIHRFNIVIHEGYEVVRKLARQIEKQIEVLKVYFNTNEEIIWQELALYKVSTDEIAEKVTVERLLRQYGASAVVIRKDYTVFAVTGHREETDALVKALEPYELIEFVRSARVAIIKDSAGFHEKLKEFEAFEPGEELVENEFLEKGQKIFTM Bacteroides thetaiotaomicron VPI-5482 Btheta 351389 BT1861 2-isopropylmalate synthase (EC 2.3.3.13) Important for fitness in most defined media. Hits TIGR00973 and 47% identical to the 2-isopropylmalate synthase from Leptospira interrogans (Q8F445). 2-isopropylmalate synthase (NCBI ptt file) MDNRLFIFDTTLRDGEQVPGCQLNTVEKIQVAKALEALGVDVIEAGFPISSPGDFNSVIEISKAVTWPTICALTRAVQKDIDVAVDALKFAKHKRIHTGIGTSDSHIKYKFNSNREEIIERAVAAVKYARRFVDDVEFYAEDAGRTDNEYLARVVEAVIKAGATVVNIPDTTGYCLPSEYGAKIKYLIDHVDGIDNAILSTHCHNDLGMATANTIAGVLNGARQVEVTINGIGERAGNTALEEIAMIIKSHHEIDIQTNINTQKIYPTSRMVSSLMNMPVQPNKAIVGRNAFAHSSGIHQDGVLKNVETYEIIDPHDVGIDDNSIVLTARSGRAALKNRLSLLGVNLDQEKLDKVYEEFLKLADKKKDINDDDVLVLAGADRSQNHRIKLEYLQVTSGVGVRSVASLGLNISGEKFEACASGNGPVDAAIKALKKIVDRHMTLKEFTIQAISKGSDDVGKVHMQVEYDNQIYYGFGANTDIIAASVEAYIDCINKFKA Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_3833 Echvi_3833 2-isopropylmalate synthase (EC 2.3.3.13) Important for fitness in defined media unless leucine is provided. 55% identical to 2-isopropylmalate synthase from Leptospira interrogans (Q8F445). Isopropylmalate/homocitrate/citramalate synthases MDKRQVLIFDTTLRDGEQVPGCKLNTPQKIEIARQLESLGVDVIEAGFPISSPGDFKSVVEISKSVSEPIICGLSRGVAKDIEVAAEALKYAKRPRIHTGIGTSPSHIKYKFKSTPDQILERAVAAVKHAKSFVEDVEFYAEDAGRTDNEYLARICEAVVKAGATVLNIPDTTGYCLPDEYGAKIKYLMDNVKGIENVIISAHCHNDLGLATANSISAVMNGARQIECTINGIGERAGNTSLEEVAMIMKQHPRLNVYNKINSRLLNPISRLVSERMGMHVQPNKAIVGSNAFAHSSGIHQDGVIKNRETYEIIDPEEVGVTESMIVLTARSGRAALAFRLHKIGYTITKLQLDDIYQLFLEHADMKKEITDEDLHEIMKVSSVPGNVEA Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS15855 CA265_RS15855 2-isopropylmalate synthase (EC 2.3.3.13) Important for fitness in defined media unless leucine is provided. 54% identical to 2-isopropylmalate synthase from Leptospira interrogans (Q8F445). 2-isopropylmalate synthase MIHDPNKVYIFDTTLRDGEQVPGCQLDTNQKVEIAKSLELLGVDVIEAGFPVSSPGDFNSVIELSKAVTNPIICALTRANKNDIDVAADALRYAKRPRIHTGIGSSDFHIKHKFNSTREEILERAVEAVRYSKKFVEDVEFYAEDAGRADIEFLAKMVEAVIAAGATVVNIPDTNGYCLPDQYGSKILFLKENVKNIDKAIISVHCHNDLGLATANSIAGLQNGARQVECTINGIGERAGNTSMEEVVMILKTHKILGLNTQIDATRFYEMSHMVRNQMNMPVQPNKAIVGGNAFSHSSGIHQDGFLKNRENYEIIKPEDVGFPDATIVLTARSGRHALKHHLDRLGHKLEKDHLDIVYKQFLVLADSKQGINDQDLNQLVALHLA Bacteroides thetaiotaomicron VPI-5482 Btheta 350902 BT1374 diaminopimelate decarboxylase (EC 4.1.1.20) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01048. diaminopimelate decarboxylase (NCBI ptt file) MKGIFPIDKFRTLQTPFYYYDTKVLRDTLSAINQEVAKYPSYSVHYAVKANANPKVLTIIRESGMGADCVSGGEIRAAVRAGFPANKIVFAGVGKADWEINLGLEYGIFCFNVESIPELEVINELAAAQNKIANVAFRINPDVGAHTHANITTGLAENKFGISMQDMDRVIDVALEMKNVKFIGLHFHIGSQILDMGDFIALCNRVNELQDKLEARRILVEHINVGGGLGIDYGHPNRQSVPDFKSYFATYAGQLKLRPYQTLHFELGRAVVGQCGSLISKVLYVKQGTKKKFAILDAGMTDLIRPALYQAYHKMENITSEEPVEAYDVVGPICESSDVFGKAIDLNKVKRGDLIALRSAGAYGEIMASGYNCRELPKGYTSDELV Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_1295 Echvi_1295 diaminopimelate decarboxylase (EC 4.1.1.20) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01048. diaminopimelate decarboxylase MTIDNQQYQVQGVPLLDIASEYGTPVYVYDGQKILDQVATLQNAFSSVNLKIKYATKALSNINILKLMKKAGTGVDAVSIEEVKLCLHVGYEPSEIMFTPNCVAFEEIQEAVDLGVMINIDNIPMLEHFGTYYGNSVPLCIRLNPHILAGGNAKISVGHIDSKFGISILQLKHVLKIVEVHNLKVAGLHVHTGSDILDAEVFLKGAEILFDAAKEFKDLQFLDFGGGFKVGYKEGDITTDMVEVGRKVSAAFKEFCKNYGRELEIWFEPGKFLVSECGYLLVNANVVKSTPASTFIGVDSGLNHLIRPMMYDAYHGVENISRVTGPDRVYTIVGYICETDTIAADRKLKEVKEGDVLAIKNAGAYGFSMASNYNSRLRPAEVLVLDGKAHLIRARESFEDILRHQIDIGL Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_2051 Ga0059261_2051 diaminopimelate decarboxylase (EC 4.1.1.20) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01048. diaminopimelate decarboxylase MDHFNRKNGVLHAENVSIPAIAAEVGTPVYVYSTATLERHASALKNALAGLPSVHLAFAIKANPNLAVLGVLARQGYGADVVSGGELKRALAAGMPAEDVVFSGVGKTRAELQLGLDEGIGQFNLELEEEGEVLADLAHAQGKTAPAVLRVNPDVDAGTHAKISTGKAENKFGVAIDRALEIFDRLAKRPGLNLRGVAIHIGSQLTELAPLEAAYKRVGELVAQLRAAGHTITHVDLGGGLGVPYHAGQTVSTAEEFGAMVARVTQGWNVTLMFEPGRFICGNAGVLVTEVIWVKPAAGNPYVIVDAAMNDLARPALYDAYHEFEAVEPTGEKFVANIAGPVCETGDTFAMGREIDVVKSGDLAVFRTAGAYGATMASTYNSRALVPEVLVSGDRFAVVADRIQPETIMGAERVPEWVR Desulfovibrio vulgaris Miyazaki F Miya 8499710 DvMF_0476 vitamin B12-dependent methionine synthase without a reactivation domain (EC 2.1.1.13) Important for fitness in most defined media and strongly cofit with the ATP-dependent co(II)balamin reductase (DvMF_1398). This lacks the usual reactivation domain for converting co(II)balamin to co(I)balamin; that activity is instead provided by DvMF_1398. homocysteine S-methyltransferase (RefSeq) MPDFRQALRSGRRLVFDGGMGTMLQSRGLPPGVSPELFCLARPDVLVGIHADYLRAGADVLTTNTFGGCIHKLGTGPGAPDVVEFNRAMARAAREAVLASGREAFVAGSVGPSGHFMRPLGDLDPAELVAAFRAQIRGLVQGGVDLILAETQFDLAEARAIVLAARAECDLPVGVSMTFENGVSLTGTRPEVFVQSMLNMGVDLVGTNCSAGPEQMAEVADELLAISEVPVLVEPNAGLPELVDGKTVFRLGPDDFARHTARFAASGVRMLGGCCGTTPDHIAALRGALDNLSGGLVPDPARRDGIVLTTRAQAVHIGAGSPIRIIGERINPTGKKLLTAELQAGEFAQALRFADEQVEAGAPLLDVNVGAPMVDEAVLLPALVERLVARHSLPLSLDSSNADAIAAALPFHPGSPLVNSISGEPGRMEHLGPLCRDHGAPFILLPLKGRKLPVTAAERIAIIEELLQQADSLRIPRRLVMVDVLALAVSSKAEAARHCLDTIRWCAAQGLPTTIGLSNISFGLPARELLNSTFLAMAAGAGLSSCIAHPGNARIREAVAASSVLLGLDANAESFIEGYSGWTPGGDATGATPAGVAGGTGGGTGGVKAKAATLEEAVIRGDREGALALVERALSEGADPFSLVQEKLIPGITEVGRRYERREYFLPQLIRSAETMQHAFRKLQPLLEAQRGHEARPVIIMATVEGDIHDIGKNIVTLMLGNHGFDVVDLGKDVKAADIVEAAERHGARVIGLSALMTTTMVRMEDTVRLVRERGLPVKVMVGGAVVTPAYAEAIGADGYSADAVEAVRVAKELLTVQ Acidovorax sp. GW101-3H11 acidovorax_3H11 Ac3H11_2452 O-succinylhomoserine sulfhydrylase (EC 2.5.1.48) Important for fitness in defined media and highly cofit with homoserine O-succinyltransferase Ac3H11_4277. The closest characterized homolog is a methionine gamma-lyase (Q84AR1, 36% identical) but this family also includes sulfhydrylases. O-acetylhomoserine sulfhydrylase (EC 2.5.1.49) / O-succinylhomoserine sulfhydrylase (EC 2.5.1.48) MTTPQNQSFTTQIVHADRLGGAEQGAIHQPIHTSVQYGYDKVEDLIAVFQGTAKGGFNYARQGTPTTAALEAKITKMERGHGTIVFSSGMAGICAVFLTLLKAGDHLVASQFVFGNTNSVLGTLADLGVEVTTVDVTDAANVAAALRPNTRMVFVETIANPGTQIPDLEGIGALCKAHGALYVVDNTVASPYLFRAATVGAGLVVNSLTKSIGGLGDALGGAITDTGLYDWSRYPNIFAAYRKGDAKGWGLQQLRKKGLRDMGGTLSSHAAHQLALGAETLALRMDRTSATALALAQWLEAHPAIARVHYPLLPSHPQHAFAKKHLKAGSWLLSFELRDPDQCLPVCNRLQLPIKATGLADTRTLIIPVAHTIFWEAGPAVRASMGIADSMIRLSVGLEEVEDLLADFEQALAGA Herbaspirillum seropedicae SmR1 HerbieS HSERO_RS16440 HSERO_RS16440 O-succinylhomoserine sulfhydrylase (EC 2.5.1.48) Important for fitness in defined media and strongly cofit with homoserine O-succinyltransferase HSERO_RS00455. The closest characterized homolog is a methionine gamma-lyase (Q8L0X4, 37% identical) but this family also includes sulfhydrylases. hypothetical protein MNDKKTYGFTTTILHSDRQKGIEHGSLHKPIHTSVTFGYEDARQLAEVFQGKQPGYRYGRQGNPTVAALEDKITKMEDGKSTICFATGMAAIGAIVQGLLREGDHVVSSAFLFGNTNSLWMTVGAQGAKVSMVDATDVKNVEAAITANTRLVFVETIANPRTQVADLKRIGELCRERGILYVVDNTMTSPYLFRPKTVGAGLVVNSLTKSIGGHGNALGGALTDTGEFDWTRYPHIAENYKKNPAPQWGMAQIRAKALRDFGGSLGPEAAHHIAVGAETIALRQERECKNALALAQMLQADERVAAVYYPGLESHPQHALSKALFRSFGSLMSFELKDGIDCFDYLNRLRLAIPTSNLGDTRTLVIPVAHTIFYEMGAERRASMGIAESLIRVSVGLEDTDDLVADFRQALDA Bacteroides thetaiotaomicron VPI-5482 Btheta 350056 BT0528 phosphoribosylanthranilate isomerase (EC 5.3.1.24) Important for fitness in most defined media and strongly cofit with anthranilate phosphoribosyltransferase (BT0530). 37% identical to phosphoribosylanthranilate isomerase from Thermotoga maritima (Q56320) putative N-(5'-phosphoribosyl)anthranilate isomerase (NCBI ptt file) MINGKIIKVCGMREAQNIRDVESLQRVDMMGFIFYPKSPRYIYELPAYLPVHARRVGVFVNEDKDVITMYADRFGLEYIQLHGKESPEYCQSLRTSGLKIIKAFSVARPKDLNHVSEYEKTCNLFLFDTKCEQYGGSGNQFDWNILHTYNGQVPFLLSGGINSHSANALKAFDHPRLAGYDLNSRFELKPGEKDPERIRIFLNELKS Bacteroides thetaiotaomicron VPI-5482 Btheta 353459 BT3933 prephenate dehydrogenase (EC 1.3.1.13) Important for fitness in defined media. Distantly related (under 25% identity) to the prephenate dehydrogenase portion of E. coli tyrA. This is sometimes annotated as chorismate mutase as well, but it lacks that domain. chorismate mutase/prephenate dehydratase (tyrA) (NCBI ptt file) MRILILGAGKMGSFFTDILSFQHETAVFDVNPHQLRFVYNTYRFTTLEEIKEFEPELVINAVTVKYTLDAFRKVLPVLPKDCIISDIASVKTGLKKFYEESGFRYVSSHPMFGPTFASLSNLSSENAIIISEGDHLGKIFFKDLYQTLRLNIFEYTFDEHDETVAYSLSIPFVSTFVFAAVMKHQEAPGTTFKKHMAIAKGLLSEDDYLLQEILFNPRTPGQVANIRTELKNLLEIIEKKDAEGMKAYLTKIREKIK Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_2298 Ga0059261_2298 prephenate and/or arogenate dehydrogenase (EC 1.3.1.13) Important for fitness in defined media. 31% identical to arogenate dehydrogenase from Arabidopsis (Q9LMR3). The substrate could be prephenate (dehydrogenation first) or arogenate (transamination followed by dehydrogenation). Prephenate dehydrogenase MKRFGIIGFGRFGQLAARHLRDHFSVVVTDTADVGEAAAAIGVKTGSLADAADCDVVMLAVPVQAMAATIAAIAPLVRPGALVLDVASVKMLPARWMLEALPESVDIVATHPLFGPQSARGGLEGQPLVVCAVRGERHHKVAEFGRSLGLSVSITTAEEHDREMAYVQALTHLIGRALVNIRIPDEELKTNSYQHLLELCGLIRDDSKELFFAIQNLNPYAEEITRQFIAEANGLLAESLKAGNRSAAD Bacteroides thetaiotaomicron VPI-5482 Btheta 353462 BT3936 prephenate and/or arogenate dehydratase (EC 4.2.1.51) Important for fitness in defined media. 35% identical to the prephenate dehydratase and ACT (regulatory) domains of D3U717 from Petunia. It is uncertain whether dehydration occurs first or transamination (to arogenate) occurs first. prephenate dehydratase (NCBI ptt file) MKKIAIQGTLGSYHDIAAHKYFEGEEIELICCANFEDVFTSIRKDSQVIGMLAIENTIAGSLLHNNELLRQSGTQIIGEYKLRISHSFVCLPEESWEDLTEVNSHPIALMQCRDFLNQHPQLKVVEGEDTARSAEIIKKENLKGHAAICSKTAAERYGMKVLQEGIETNKHNFTRFLVVADPWQVDELRQHHAKATNKASMVFTLPHTEGSLSQVLSILSFYNINLTKIQSLPIIGREWEYQFYVDVSFNDYLRYKQSIAAITPLTKELKILGEYAEGKSNV Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_0123 Echvi_0123 prephenate and/or arogenate dehydratase (EC 4.2.1.51) Important for fitness in defined media unless phenylalanine is provided. 34% identical to prephenate/arogenate dehydratase from Oryza sativa (Q6Z3Y3). It is uncertain whether dehydration occurs first or transamination (to arogenate) occurs first. Prephenate dehydratase MTSTPHQQKVAIQGIKGSYHYQVALNQFGQDIHVIECLTFSDLVKSITSNDADIGVLALENSIAGAILPNYDLMDRNNLQVIGEFYLPISHQLMVLKGQSIDDITEVRSHPMALLQCKAFFEQYPQIKLIEDLDTASVAKEISEQHLQGVGAIAGKSAAEFYGLDILASDIQTIKNNITRFCIVKNAADAKPVIGFDKASIKVTIKNEQGSLAKVLTTMSAYRLDLTKIQSLPVIDQPWHYAFFIDLLFENLEDYQQALKELKANGHQIKVLGEYKNTK Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS11630 CA265_RS11630 prephenate and/or arogenate dehydratase (EC 4.2.1.51) Important for fitness in defined media unless phenylalanine is provided. 34% identical to prephenate/arogenate dehydratase from Oryza sativa (Q6Z3Y3). It is uncertain whether dehydration occurs first or transamination (to arogenate) occurs first. prephenate dehydratase METTKRVAIQGIKASFHEEAAYKFFGKDIETVECNSFKETCDKLEKNDADFVVMAIENSIAGSLLPNYTLIRDFGFSVVGEVYLPIQLHLMALPGVKFEDIKVVTSHPIAIRQCIDFFYDYPHIKIVESNDTAACAKRIQEEQLTDTMAIANSLAAELYSLNILERRVESNKKNYTRFLILKKDKTDEGKKINKASICFQVGHKAGSLATVLNIFAEQDVSLTKIQSMPVLGKRNEYYFYVDLEWPSTEKYDKAIRKALKYTSNFNILGEYQKNDKV Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_2633 Echvi_2633 gamma-glutamylphosphate reductase (EC 1.2.1.41) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00407. gamma-glutamyl phosphate reductase MKILSTQKKNDVLASMIKIIDKNREKILTANKADLDAFQRDDQALYDRLVVNDAKIDGMIQAVQEVKDQDDPVGKEISKRTLANGLDITNKTAPFGTIMIIYESRPDVTIEAAVLAFKANSKILLKGGKEAVNSNKVLVECWHEALEENGLSKDWIELFTLNREQTQAFLKNPSEKLDLIVPRGGERLIAFVKEHAQCAVLVSGRGNNFAYVAEDADWELAKKVIINAKTNKISGCNALDKILVDEKLPDFESKLADLAKSLASYKVELVAEKELVPAIEGAKEVPSEDTWYEEFLALKALIGKVNGLDEAIAKINKYSGGHSATILTTDKDKAATFMEQVDSAAVYHNASTRFTDGGQMGVGAELAISTDKLHHRGPLGLEQLVTNKYYVFGSGQIRD Bacteroides thetaiotaomicron VPI-5482 Btheta 353245 BT3719 glutamate 5-kinase (EC 2.7.2.11) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01027. glutamate 5-kinase (NCBI ptt file) MKQEFTRIAVKVGSNVLARRDGTLDVTRMSALVDQIAELNKSGVEIILISSGAVASGRSEIHPQKKLDSVDQRQLFSAVGQAKLINRYYELFREHGIAVGQVLTTKENFSTRRHYLNQKNCMTVMLENGVIPIVNENDTISVSELMFTDNDELSGLIASMMDAQALIILSNIDGIYNGSPSDPASAVIREIEHGKDLSNYIQATKSSFGRGGMLTKTNIARKVADEGITVIIANGKRDNILVDLLQQPDDTVCTRFIPSTEAVSSVKKWIAHSEGFAKGEIHINECATDILSSEKAASILPVGITHIEGEFEKDDIVRIMDFLGNQVGVGKANCDSAQAREAMGKHGKKPVVHYDYLYIE Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_4033 Echvi_4033 glutamate 5-kinase (EC 2.7.2.11) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01027. glutamate 5-kinase MIHRKANTIVIKIGSNVLTQADGTPDTMRMKALVRQMVYLREQGQEIVLITSGAVAYGRTSTVFEEKTDPVIQKQILAAVGQIELIRQYKQLFGDHNTPIAQIMVTKSDFRDRKHFLNMKNCLEGLLKNNIIPVINENDTVSVTELMFTDNDELAGLVAAMLDAKDLIILSNVEGIFKGHPSDPEAVLIEKVDADTPSMANFISSSKSSFGRGGMLTKMNMAKKSADLGIGVTIANGKREDVLVDYFHNRLRCTYFEPSKAKQSPKKWIAHSEHYSTGEVIINSGAENALRSDKITSLLPIGVLEIRGDFSKGDIIRILSEDGRKIGLGKSAYGAKVAAEKKGLSNQKPLIHYDYLYLHQDS Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_3512 Ga0059261_3512 glutamate 5-kinase (EC 2.7.2.11) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01027. glutamate 5-kinase MHLFPPASCPRLVVKIGSALLVDPEGAIRRDWLEGIAADIAARVRAGQQIAVVSSGAIALGARRLKLAKGGRASLEDAQAAAATGQIALSQVWAEVLAANGLTAAQMLVTLDDLEDRRRYLNAAATLGRLLSLGVVPVINENDSVATAEIRFGDNDRLAARVAQAADASGVVLLSDIDGLYDRNPALPGAVHIPVVERIDGRVEGMADRGSASGMGSGGMVSKIEAARIAASAGVSLAIANGRVDRPLSADARHTVFLPEKRTRARKAWLAGRLTAKGSIIVDAGAAQALTEGRSLLAIGATAIRGMFFRGDLVTIEGPNGPIARGLSEYDAPDAQAILGTRSDDQGEILGYAPRSTLVHRNHMALL Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS20855 CA265_RS20855 glutamate 5-kinase (EC 2.7.2.11) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01027. glutamate 5-kinase MKLGYKKIVVKVGSNVITQANGLPDEGRIKHLVNQLADIKKQGIEVILVSSGAVASGRSLIKVSEKQDAVTTRQLLAAIGQVKLINTYANFFAAHAIQCAQVLVTKEDFRDRAHYLNMKNCLQILLQNEVIPVVNENDVVSVTELMFTDNDELAGLIASMLNADALIILSNVNGIYNGDPKVEGSAVIEEINGSVANLASFIQTGKSQFGRGGMITKSTMAQKVAKLGITVHIANGTKDNVLTSLLNNELVHTRFVPEKSKSGKKKWIAHSETAATGVVKLNDGAKTVLTSSKATSLLPVGIIEIQTDFLKGDIIKIVDEKNNLIGLGIAEYGSDKARERIGQKKQKALVHYDYFYSAI Bacteroides thetaiotaomicron VPI-5482 Btheta 353283 BT3757 pyrroline-5-carboxylate reductase (EC 1.5.1.2) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00112. pyrroline-5-carboxylate reductase (NCBI ptt file) MKIAIIGAGNMGGSIARGLAKGSLIADSDIIVSNPSAGKLEKLKEEFPGISTTLSNTEAATGADVVILAVKPWFVESVMRELKLKSKQTLVSVAAGISFEELAHFVIAPEMPMFRLIPNTAISELESMTLIAARNTNDEQNLFMLRLFNEMGMAMLIPEDKIAATTALTSCGIAYVLKYIQAAMQAGIEMGIRPKDAMEMVAQSVKGAAALILNNDTHPSVEIDKVTTPGGITIKGINELEHNGFTSAVIKAMKASK Caulobacter crescentus NA1000 Caulo CCNA_00528 CCNA_00528 pyrroline-5-carboxylate reductase (EC 1.5.1.2) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00112. pyrroline-5-carboxylate reductase MTPILLLGAGRMGGALIQGWQAAGAFDAADLIIRDPHVDAAAFAGAVVNPPLETLGAAKTVLLAVKPQIWREAIADVVPHLAPDAVIVSIAAGVRAADISQAFGGRRVARVMPTTAVAIGQGAASLYADDAEALARARALFAPLAAVAELASEDLMHAATAVSGSAPAYLYAFIEALEAAGAAQGLDPAQSARLARATIIGAAALMAQSGEEPAELRKQVTSPGGTTAAALSVLMGAGGFGDLLPKALDAAVARSKELGG Desulfovibrio vulgaris Hildenborough JW710 DvH 207819 DVU2332 proC pyrroline-5-carboxylate reductase (EC 1.5.1.2) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00112. pyrroline-5-carboxylate reductase (TIGR) MQTTLGCIGCGNMGSAILRGLSGREGLRLVGCDPTGAKLAALADAGVEGVADIAAAVRASDIVLVAVKPGQVGAVLGAAMPELDSGKVVVSIASGVSVGSLREMSGGRCPVVRVMPNTPAMVGAGVFALCFEDATLDEVRRTLVKELFEALGRVLVLPEEKFNAFTAVVGCGPAYVFHFMEAVVEAAVTLGFPRHEATDMVVDLFAGSVKLAATSGTHLSLLREAVCSPAGNTIAAMNQFDRDAVRGRIIDAILAAYRRGQEMER Desulfovibrio vulgaris Miyazaki F Miya 8502455 DvMF_3161 pyrroline-5-carboxylate reductase (EC 1.5.1.2) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00112. pyrroline-5-carboxylate reductase (RefSeq) MGTVLGCIGCGNMGAAILRGLSGRQGLSLLGYNPTPAKVLALADAGVRAMPDAATLAAQADVVLLGVKPYLVPDVLRAIAPSLTPGKVVVSIASGVSIAAMKAAIAEAGGPECPVVRVMPNTPAMVGKGVYALCFEDPALDVPRRDLVRGLFESIGTVIVLPEARFTAFTAVVGCGPAYVFYFMEAVTEVAVTLGFTRQDATELVKGLFSGSVALAEQSGTHLSVLREQVCSPAGNTIAAMNQLDREAVRGRIMDAVLAAYRRGLEMEK Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS18505 CA265_RS18505 pyrroline-5-carboxylate reductase (EC 1.5.1.2) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00112. pyrroline-5-carboxylate reductase MKKIAIIGSGNIGLSLAKGLVKANYTTTKNIILTRRNTANLYKFAQERYKVTANNADAAADADVIILAVLPQQLNVVLEEIQSAINPAKHLVISVISGVSCAAVREKLDSNVQIIRAMPNTAIAIGQSMTCIASDNASPQNLEDVTRMFETVGSVVKINEDLMTSATALCACGIAFFLRGIRAASQGGVEIGFHADEALKMAVQTAKGAADLLLLHGTHPESEIDKVTSPKGCTIAGLNEMEHNGYSSSLIKGIKLSALKAGNLYTKEG Shewanella loihica PV-4 PV4 5208627 Shew_1136 pyrroline-5-carboxylate reductase (EC 1.5.1.2) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00112. pyrroline-5-carboxylate reductase (RefSeq) MTQKKICFIGAGNMTRSITSGLVKGGYAPELIHATNPSEGKLIALKQDLGIRVSHDNLQAADEADVIVLAVKPQLMQQVCEAMSGLNLKDKLIVTIAAGVTAERYHAFFKQPIQLIRTMPNTPTQIGLGMTGLYAEQGVSAQDRELCEQLMQTGGETVWVEKEEDLNQVIALAGSSPAYFFLMMEAMIDSAKQDGVDEQTAREMVQQAALGAAAMVKQNPQLSPAQLRENVTSKGGTTAQALAAFERAGLREIVRTAMHDCMDRAQEMAKQF Desulfovibrio vulgaris Hildenborough JW710 DvH 206336 DVU0908 ATP-dependent reduction of co(II)balamin Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM PF14574. iron-sulfur cluster-binding protein, putative (TIGR) MQPHPETTPVTSCTIIDATDRSIRQTLGETSTLARLIWVDAGLASPPLCSGLARCGRCRVRITEAAPAPHEDDREFFSAEDISAGWRLACRHAPAHGMVVHVPLPVMPHRHASRPKHPGPFRLAVDLGTTSLQWSLLAPDGTVAAQGSETNPQMGAGSDVMSRIAMARSDKGRGRLRELVLQALRRIVADVEGTPATADAVPPAGSGDEPTTACGYESRVEELCVAGNTAMTAILADESVEGLASAPYRLEMRGGTALALPGLPPAWIPPLPAPFVGGDLSAGYLAVLTDHAPAFPFVLADLGTNGEFVLALSPERTLVTSVALGPALEGIGLTFGTVAQRGAITSFTLTPGGLVPYVLDGGEADGISGTGYISLVHALLRAGLLDVDGRFIQSPSSPLAARMARSIVSHRGEPCLPLARGLYLAARDIEEILKVKAAFSLAFERLLATAQMPSHALSGIHLAGALGQHALPADLEGLGFIPPGSGGRTRAVGNTSLRGAELLLTSPPLRDTLNTWREGCTVVDLTAAPDFSAAFLRHMHFHF Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS22635 CA265_RS22635 phosphoserine phosphatase (EC 3.1.3.3) Important for fitness in most defined media and strongly cofit with 3-phosphoglycerate dehydrogenase (CA265_RS09010). CA265_RS22635 is distantly related (28% identity) to the chloroplast phosphoserine phosphatase of Arabidopsis (O82796). CA265_RS22635 also has a 3-phosphoglycerate dehydrogenase domain, but given the auxotrophic phenotypes of the other 3-phosphoglycerate dehydrogenase, it may not be catalytically active. phosphoserine phosphatase MPKQKAYYIIDFDSTFTQVEALDELARISLKNHPDKEAIFQKIEDYTNFAMEGKLSFSESLAQRVKLLEANEDHLKQLIKHLKKKVSTSFSRNAEFFKKHADEVLIVSGGFKEFITPVVSQYHIKKENIYANTFVTTGDGKIIDYDHANPLSEEGGKVKLLQHLKLEGELFGIGDGYSDFQLRESGIINKFFAFTENIARESIVSKADHVTPSFDEFLYVNDLPRAISYPKNRILCLVIGDVDPLTIAILKNDGLSIRHKTSFEDKYVKDVGIILLADGEKINKEQLKNAAKLKTIGYLGNAKNKIDLDLCTKQGIVVFDDPKNNPRNIDFIPKRVADFMNTGATYLSSNFPNLQLPKIEKSHRLIHIHKNVPGIMAKINTVFAKHDINIVSQFLMTNPEIGYAITDINAEYDKQLFKSLKKIEHTIKFRVLY Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_2001 Echvi_2001 homoserine kinase (EC 2.7.1.39) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00191. homoserine kinase MKKVTAFAPATVANVSCGFDILGFAVEEMGDKVTVSLADEPGVRVVRIEGDGGRLPYEVDKNTCGVALKAFLAAIDYKGGLEVELYKGLPLGSGMGSSAASSVAALEAANQLLGNPLDKKALLPFAMKAEGVACGAEHADNVAPSLLGGFVLIRSYHPLDVTKLHVPKGLYCALVHPHLELNTADSRSVLRQQVPLKDAITQSGNIAGLVAGLYQEDMGLISRSLQDVIAEPSRSVLIPGFDEIKSAIKEVGALGVGISGSGPTTFILAPSREVAERASEICQEVFDKIGLEVDLYVSAVNTKGTYVINKA Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_0576 N515DRAFT_0576 homoserine kinase (EC 2.7.1.39) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00191. homoserine kinase MNAQLAAQNPEPMARSPQRALSAQALAPASVGNVGIGFDILGHSVAGAGDRARVRRIDEPVVRIAAIEGCVVDLPLDPAQNTAGMALMALRKALGLRHGFELVLHKGIALGSGMGGSASSCVAALVAANALLERPLPMESLYGFALEGEAVASGGRHGDNVGPMLLGGLVLATRDRLVRVPVPDAWHCALVHPHMVLETRKARAALAGAYQLGEFVAQSANLSLMLAGCWQGDAGLVREGLNDVLVEPRRAPLIPGFARVKQAAMDHRAMGASISGAGPSVFGWFEQRDEAKAAAAAMAAAFAEAGLDSDTLVSPIAGPSAALIDVERKA Sphingomonas koreensis DSMZ 15582 Korea Ga0059261_3253 Ga0059261_3253 homoserine kinase (EC 2.7.1.39) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00938. homoserine kinase (EC 2.7.1.39) MAVYTQVSAEALAGFLARYDVGELVSAKGIAEGVENSNYLVETTRDRFILTLYEKRVEAADLPYFMGLLDHLAAKGLPVPPAIKDRGGVEIQELNGRPACLIKFLSGISLSHPTPAQARAAGEAMAQMHRAVADFPLDRPNSMGVDTWQPLFEKCGHSLDQIVPGLYDDLGFAIARVVPAWTRNDFDRCAIHADLFPDNVLMRGDQVTGLIDFYFACTDIRVYDLAVMHSAWSFDAHGRNYDPAVGDALIAGYEASFPLTEVERAAFPTLAAGACIRFSLSRAWDWLNTPADALVMRKDPLAYVRRLKHYAPDLVKHVA Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS23470 CA265_RS23470 homoserine kinase (EC 2.7.1.39) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00191. homoserine kinase MKDSIKVFAPATVANVVCGFDVLGFAVNEPGDEVEMRFTDTPGVVIKGITGDDGRLPLDAAKNTVSASVQHYLKHINRLDVGVEIELHKKMPIGSGLGSSSASTVAGLFAINKLMGDLLSTKELVPFAMKGEELACGYGHADNVAPALLGGFVLVRSYDPLDVISLPTPAGMYAAIVYPEVDVPTKDARQMIRSKVALKDAVTQWGNVAGLVSGLFMNDFDLIGRSMKDVLVEPTRSILIPGFEEMRKLAMENGAIGFGISGSGPSVFSLTKDEETARKITKSQQQHLHKININSKAFVSPVNAEGPKVL Dyella japonica UNC79MFTsu3.2 Dyella79 N515DRAFT_0575 N515DRAFT_0575 threonine synthase (EC 4.2.3.1) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00260. threonine synthase MSEPLLYHSTRGAAHGAGIGEAIAAGLAPDGGLYVPEALPSRRPDDFDPDGTLADTAARLLRPFFAGHALAAELPAICAEAFCFDAPLRPLPQHPGAAMLELFHGPSAAFKDFGARFLASCFRRLRKAGEAPLTILVATSGDTGAAVAAAFHRQPGVEVVILYPDGLVSPRQAHQLGCFGDNVRALRVAGRFDDCQRMVKAALNDTALQAQRPLSSANSISLGRLLPQMAYYAHASLRWWREHRRPLNFIVPTGNLGNALAAVWVREMGLPVGAIELACNANETLPDYFAGTPYAPRAAVATLANAMDVGAPSNFERLRWTFPYDDDLRGQLSSHSVDDDTIRATVRRHALEHGEVFCPHTATAMHRLDLRQEKADWAVVSTAHAAKFESVVEPLIGRGVAVPPALQAMLARPAQAEAIEASDDALKQWLLPQPAHVRRLG Desulfovibrio vulgaris Miyazaki F Miya 8501211 DvMF_1945 threonine synthase (EC 4.2.3.1) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR00260. threonine synthase (RefSeq) MPCPTSCPAPGHDFPTARTRMEYVCLGCGERRGIDELLYTCPSCGGVYLLEDLDFDTLAEQRTGPEWRALFDARAATRTTALRGIFRFYELMAPVLEEEDIVYLGEGNTPIVEAAPVLRDAVGIPFAFKNDGQNPSASFKDRGMACAFSYLKALVRKHGWDEVLTVCASTGDTSAAAALYASYVGGPVKSVVLLPHGKVTPQQLSQPLGSGATVLEIPGVFDDCMKVVEHLAENYRVALLNSKNSWRILGQESYAFEVAQWYGWDMKGQCVFVPIGNAGNVTAIMAGFLKLLRLGVIDALPRVIGVQSHHADPVWRYYSQPDPATRTYAPVTVQPSVAQAAMIGNPVSFPRVKALADRFIAEGGERAFSVVQVTEQEIMDAMIRGNRHGHIACTQGGECLAGLIKARELGLVSQGEHAVLDATAHSLKFAGFQDMYFTNSFPPEYGVTPDASLANAPALVVSPEDKARLSPEAYTLAAAKAVVARLGLAKKA Bacteroides thetaiotaomicron VPI-5482 Btheta 350058 BT0530 anthranilate phosphoribosyltransferase (EC 2.4.2.18) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01245. anthranilate phosphoribosyltransferase (NCBI ptt file) MKQILYKLFEHQYLGRDEARTILQNIAQGKYNDVQVASLITVFLMRNISVEELCGFRDALLEMRVPVDLSEFAPIDIVGTGGDGKNTFNISTAACFTVAGAGIPVVKHGNYGATSVSGASNVMEQHGVKFTSDVDQMRRSMEQCNIAYLHAPLFNPALKAVAPIRKGLAVRTFFNMLGPLVNPVLPTYQLLGVYNLPLLRLYTYTYQESKTKFAVVHSLDGYDEISLTNEFKVATCGNEKIYTPEGLGFARYQDTDLDGGQTPEDAAKIFDNIMNNTATEAQKNVVVINAAFAIQVVRPEKTIEECIALAKESLESGRALATLKKFIELNNK Pedobacter sp. GW460-11-11-14-LB5 Pedo557 CA265_RS05010 CA265_RS05010 anthranilate phosphoribosyltransferase (EC 2.4.2.18) Important for fitness in most defined media. Semi-automated annotation based on the auxotrophic phenotype and a hit to HMM TIGR01245. anthranilate phosphoribosyltransferase MKKILNHLFENKSFSREEAKNILISISEGAFNSSQIAAFITAYAMRNITVQELQGFRDAMLDMCVKVNLSGYDLIDLCGTGGDGKDTFNISTLSSFVVAGAGHHVAKHGNYGVSSGCGSSNVMEYLGYTFTNNEDTLKRNLDAAGICFLHAPLFNPAMKIVAPIRKELGVKTFFNMLGPMVNPGQPKYQMVGVFSLELARLYAYLYQDTDKSYTIVHALEGYDEVSLTCDVKTFSNKGEQILTLQDMGFDKVEVNAIKGGDTVESSAKIFMDVLNGKATDVQNNVVLCNSALAIKTIKPQQSFADCFYEAEESLMSKKALNSFKQLLAC Bacteroides thetaiotaomicron VPI-5482 Btheta 352858 BT3331 Outer membrane binding protein for chondroitin sulfate and hyaluronic acid (susD-like) Specifically important in carbon source Hyaluronic acid sodium salt from Streptococcus equi; carbon source Chondroitin sulfate A sodium salt from bovine trachea. The adjacent susC-like protein BT3332 has similar phenotypes. putative outer membrane protein, probably involved in nutrient binding (NCBI ptt file) MKALKITIIALLAGFSMVSCDFLDKEPTKLTPENYFNTPAEANSFLTGIYAILSQPTFYGGDYMYLVAGDDLSHYGGSGRGPASTGLICNNATTSDNAVTAFWYALYSGINRANMFLENIDKVNGFDAGVKEQYIAEARFLRAFYYFNLVECWGDVPFKTVSTQSVTNLNIPRTDKQEIYDFIISEMADAAETGLKSASDLAYKPGRISQSTAWGILARVYLFRAGEHYREGRNATQAEKKDYFERASFYAQKVMTAGHKLAANYWDPFIDMCSDKYNTTANESIWEAEFAGNNTSDTQAEGRIGNIIGLAGPDLSSKSDVTGAKDPGYGYAFIYSTPKLYNLYVNNGDTKRFNWSIAPFEYKEAGGKNTGVTHREFEQGKLAEVMSQYGQQRGTYQYADDTEKTTATKNFSRMCGKYRREYEADKKDKNYTSINFPILRYADVLLMIAEAENEANNGPTTLAYQCMKEVRERAGLNELPDMTQEEFRQTVKDERAMELCFEYTRRFDLIRWGEYVKNMRALVTEAQSGNNWTQGPTNVYTYFNISSTYNYFPIPDAEMSVNKDITQNNPGW Bacteroides thetaiotaomicron VPI-5482 Btheta 352859 BT3332 TonB-dependent receptor for chondroitin sulfate and hyaluronic acid (susC-like) Specifically important in carbon source Hyaluronic acid sodium salt from Streptococcus equi; carbon source Chondroitin sulfate A sodium salt from bovine trachea. The adjacent susD-like protein BT3331 has similar phenotypes. putative outer membrane protein, probably involved in nutrient binding (NCBI ptt file) MLSILGMLLLSVPFVLAQVLVKGTVKDNLGEGVPGASVQVKGTSQGTITDLDGKFTLNIPQKNATLVISFIGYVTVEQKADSQKPMVITLKEDTKTLDEVVVVGYQEVRRRDLTGSVAKANMADVLTAPVASFDQALGGRIAGVNVTSGEGMPGGNMSIVIRGNNSLTQENSPLFVIDGFPIEDSSAASTLNPSDIESLDFLKDASATAIYGARGANGVVIITTKKGKVGRAQLSYDGSFGVQHVTRTIPMMDAYEFVKLQNEMYPTVVAGSYLMNYEGKQWTLDDYKNIPQYNWQDEIFKTAWQQNHTVRLAGGTEGVRYNASLSYFDQDGTLIETGYKRMQGRMNTVVRRGKLNMSLTTNYSRSIQTGSTPSSTSYSGMNNLFYSVWGYRPVTSPDTPLSFLMDSSTDNAVDSSNDYRFNPIKSQKNEYRKSYTNNLQMNGFAEYEVLKGLKLKVSAGYTYDSRKQDQFNNSNTRYGGPTSTDKVNAQVTRQERLTWLNENTLTYQTNIKKKHFLNVLGGITFQNSDYEIYSFRTTHIPNESLGMAGMSEGQAGTTTSAKSSWAMLSYLGRVTYNYMSKYYATVSFRADGSSKFNKDNRYGYFPSGSLAWSFSEEEFMKPLKSVLSSGKVRLSWGLTGNNRIGEYDYYALLAVLKSRVGSYTSTNSLPSGVYPFDNDATNAGVVPTSLPNKDLKWETTEQWNAGLDLGFFDERIGITMDIYRKTTRDLLLDASLPFSSGYYSATKNIGKVRNDGLELSLNTVNFQTRAFKWTTNFNISFNKNKVLALSENQTALLTAAQFDQNYNGQSSYIAKVGLPMGLMYGYVYEGTYKYDDFNKSGNSYSLKPGVPHYSTETNTQPGMPKYADLNGDGVVDSNDRTIIGRGLPIHTGGFTNNFEYKGIDLSIFFQWSYGNDIMNANRLFFESSNNRSRELNQFASYANRWTPENPTSDIPAATNSSSNRVISSRIIEDGSYLRLKNVTVGYTFPAKLVKKWKIDKARVYVAAQNLWTCTGYSGYDPEVSVRNSALTPGLDYSSYPRAYSISFGVSLGF Bacteroides thetaiotaomicron VPI-5482 Btheta 350967 BT1439 Outer membrane binding protein for vancomycin (SusD-like) Specifically detrimental during vancomycin stress in BHIS media, along with the adjacent SusC-like protein BT1440 putative outer membrane protein, probably involved in nutrient binding (NCBI ptt file) MKKIKIQSILTAVAGLFLATSCSSSFLDTEPTDAVSSDQVAVAGNAERLFNGAWYNLFEYGTTYANIGYRALQCQDDMMASDVVSRPKYGFNSSYQFNDVAIPSDGRTSFAWYLIYKTIDNCNTAISIKGDSEELRQAQGQALALRAFCYLHLVQHYQFTYLKDKDAPCVPIYTEPTTSGTKPKGKSTVAQVYQQIFDDLNLAQDYLTNYVRKGDGQKFKPNTDVVNGLMARAYLLTGQWGEAAKAAEAARKGYSLMTTTAEYEGFNNISNKEWIWGSPQTLSQSDASYNFYYLDATYVGAYSSFMADPHLMDTFVKGDIRLPLFQWMREGYLGYKKFHMRSDDTADLVLMRSAEMYLIEAEAKVRDGVALDQAVAPLNTLRTARGVGNYDVTGKTKEQVIDEILMERRRELWGEGFGITDVLRNQKAVERMALSEDMQKTEVDCWQEGGSFAKRNPLGHWFLNFPDGKAFSANSSYYLYAIPEKEINANPNL Bacteroides thetaiotaomicron VPI-5482 Btheta 350968 BT1440 TonB-dependent receptor for vancomycin (SusC-like) Specifically detrimental during vancomycin stress in BHIS media, along with the adjacent SusD-like protein BT1439 putative outer membrane protein, probably involved in nutrient binding (NCBI ptt file) MRIYLRLLVAFLLLSAGNVVYAEAQQEKRVTGTVTSEGEPLPGVSVQVKGASSGTITDIDGNYSIEAPANGTIVFRFVGLRTVEQAVNNRNVINVTMESESKELEEVMVVAYATAKKYSFTGAASTMKAGEIEKLQTSSVSRVLEGTVSGVQASASSGQPGTDAEIRIRGIGSINASSAPLYVVDGVPFDGSVNSINPDDIASMTVLKDAASAALYGSRGANGVIIITTKQGQQDSKATVKVKATLGGSSRAVRDYDRVNTNQYFELYWEALRNQYAKSSDYTPATAATQASKDLVTKLMGGGPNPYGTQYPQPVGTDGKLAAGARPLWNSDWSDAMEQQALRTELNLSVSGGGKANQYFFSAGYLNDKGIALESGYQRFNLRSNVTSEMTSWLKGSINLSFAHSMQNYPVSSDSKTSNVITAGRTMPGFYPICEMNTDGSYKLDDNGDRIYDFGSYRPSGSMANWNLPATLPLDKSERMKDEFSGRTYLEATIIEGLKFKTSFNFDLINYNTLDYTNPKIGPALENGGGSSRLNSRTFSWTWNNIASYDKTIGDHHFNVLAGMEAYSYRYDELTASRTKMAQPDMPELVVGSQLTGGSGYRIDYALVGYLTQALYDYQNKYFFSASFRRDGSSRFAPETRWGNFWSLGTSWRIDRESFMASTANWLSALTLKMSYGAQGNDNLGTYYASKGLYTIVSNLGENALVSDRMATPNLKWETNLNFNVGVDFSLFNNRFSGSFDFFTRRSKDLLYSRPIAPSLGYGSIDENVGALKNTGIEMVLNGTIINQNGWVWKLGMNLTHYKNKVTELPLKDMPQSGVNKLQVGRSVYDFYMKEWAGVDPDNGNPLWYMDEKDANDNLTGKRVTTSDYASANYYYVNKSSLPKVYGGFNTSLSWKGFDLSAIFAYSIGGYIYNRDITMILHNGSLEGRDWSTEILKRWTPENRYTDVPALSTTSNNWNSASTRFLQNNSYMRLKNLTLSYDLPKQWISKLALSSVQVFVQGDNLFTIHRNQGLDPEQGITGITYYRYPAMRTISGGINLSF Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_4214 Echvi_4214 lysine/tyrosine outer membrane transporter, TonB-dependent receptor component # Specifically important in nitrogen source L-Lysine; nitrogen source L-tyrosine disodium salt. Echvi_4214 is a TonB-dependent outer membrane transporter that is required for utilization of lysine. Mutants also have a defect in tyrosine utilization. It probably functions with Echvi_4215, which is cofit and part of a conserved gene cluster. Inner membrane protein Echvi_4216 (PFam PepSY_TM) is also conserved nearby but does not have a phenotype; it may have a regulatory role. Outer membrane receptor proteins, mostly Fe transport MKTFLPLGKIYFYTALCMLMSGLPAVAQTIPATTLKGRIFDTEESPVPGVIVRIKDSPLTAISSLDGSYQITDIPEGEVEVLLSCLGYQDHASKVSIEKNKPTVHLDFALEESMTELDGVIIEGQSVKTEIETKGFAVEVVETDKAALQSVQTNDLLNRTAGIRVRQNGGIGSRVDYNLNGMSGNSVRIFIDGLPISTYGPSFSLNSIPPALIERIEIYKGVIPAHLADDALGGAINVVLKKGAVNSLMAAVSYGSFNTLQGNLNAVYRDKRSGFTTKISGFYNYSDNDYEVWGKFVRNILPNGRYDYVRAKRFNDSYRSVGGKFDIGFTDVKWADQFFISYTGSDDYNEIQHGTYMSIPYKGRFTTSQSNVFGLTYSKEDLFTKGLAVNFNGSFSKRAEVVTDTVKWNYNWFGEISLDLDGEPILRPDGAQQGAPTINHIDRNVSTFRAGAQYELHPQHKLIFGQSFFNIDRFQQDEMRNAVERQFVGTRDLQKHITSLGYEFNLMHSRLKGNVFGKYYVQNIERMDPILVEGPNGSERQEDRVTSSRNTTGMGMAYSFRAWKQILFLASAEQAVRMPSEGEIFGSPGDNIVENLSIRPEISNNLNLGFKLGEFRKNAHEFSFSGSGFIRDTKDKIIQQINPRINDAVQTNPFENLGRTKAIGFEGQATYSYKKALRATVNFSRFNSVFNTKYDPNGNLYEKFGQQIPNEPYFTINSTLEYTLKDVFQQGSSLRLSHYFSFVERFYTTWLEIEDFRTPRQYVHDLGATYTLPNQRLSISADLRNVFDKQVYDNFAVQKPGRAFYLKINYAIHNFK Echinicola vietnamensis KMM 6221, DSM 17526 Cola Echvi_4215 Echvi_4215 lysine/tyrosine outer membrane transporter, accessory component # Specifically important in nitrogen source L-Lysine; nitrogen source L-tyrosine disodium salt. Echvi_4215 is an outer membrane lipoprotein that has very similar phenotypes as an adjacent TonB-dependent receptor (Echvi_4214). Jackhmmer searches found that Echvi_4215 is distantly related to DUF4374; both Echvi_4215 and DUF4374 have conserved proximity to TonB-dependent receptors. Echvi_4215 and relatd proteins are probably accessory proteins for uptake, analagous to the SusD family, but not homolgous. (SusD-like proteins are not found in proximity to Echvi_4214 or its homologs.) hypothetical protein MLRTNMLKSKILHMGAVVAALSLTSCNNEDDPTPQPEQNADRWVTVAGALMGDSPGDGNGGTKIYAVSYEDAINPEIEIDVFDNGEPVKSNRTARLQISEDGSTLFNIAYGGENGGEFSKFDVAGGSSYVQQDVTVNISQYVGTAPRWSKLYNGDQNGIAVNVANIAANNAAENSTEPFQYYRGTATVLDVDLQDVLIRATKDYEIPLTEEEELAGHCIFRLDAPVLNQAGDKLLIGTWMRKYDVATGERESEWDRLGTKTVVVDYPSLENPTIITSTQANGDCSGYRSNVNQLAEDGSIYQATSRDTDGSHILRITPENEYDNTFALSLDEALGLNDVYVDAWKYVNNGIGYAMIRHGEEDQGYIARLDLNQQTAYLVNEIPDDPDVRFNQFQGFMVSGNDLLVPVSPLGKDGNIYILHSQTGEVSVGAKLINKPGNHFIGAF Bacteroides thetaiotaomicron VPI-5482 Btheta 349800 BT0272 TonB-dependent receptor for (+)-arabinogalactan (SusC-like) # Specifically important in carbon source (+)-Arabinogalactan putative outer membrane protein, probably involved in nutrient binding (NCBI ptt file) MRNIFKYGLLAMAIAVTSVGVRAQDIPVSGVVKDKSNNSTLPYASVIVKNESGKTVPQLSTTTDDNGRFSTKVKSGYRLVFSFLAFDSLSVKVTKPSERMQIYLSPTENMLDETVVVGFKRVSKAAVTASVTVIKAEDLVNTPVANPMELLQGRVPGLNIQMNNGTPGGLPSFSIRGVSDISVQSSGDGEFMMGLTPPLFVVDGIPQEDVTGYDAAGLLSGATVSPLAMIPLEDIANIQVLKDAAATSLYGSKGAYGVILIETKRGETAKPKVSYSANFVVKTPPRLRDVLAGGAERALRIMQILGNDTSAYHGYNEIHKLQALSDSLNPYYNNNTDWQGVFYQTTYNQTHNLSFSGKPNEKFDYKINANYYTEKGIVKNTDFNRYGIRAAVGYKPNDRFHLDLNLATTLTRNSNGSGNAFSQSGVAAGSAASSLLPPPSMYTASNSALSVFSVQADNQNVVYDASMNIMYLLPFDIRWRSTLGYKYGTVENEKFTPGILNANRATWNNGSEYSYNMYVRSLLSRTVKLGIVNFDLQGGFELSSEKYSGNFIMLNGLASDHIWSSGMPSMAAGRSNFSDKKNTFALIIDPQLSLPGGKYVFTPNIRPEINSSYGSQAKWAINPSLGFRWNFSRESFAKKWKFLDAGALRVTWGRSTTYKASIYDIWGSYNLSKDTYNGVSIIPIDKNAMPNPDLKPVTSTSWNLGTDLSFLNNKIMFVAEAYYKQIDNQLSSIELANHNAFNSVRSTKTSLVNYGLEFSLNVRPLSRQSNWDLNVATSLAINKDVIAKLPNEVRQIINSDAEVVNKLGSNAMGNYLYVYKGVYATDEDVPVNPLTGERLRMGGNTSTQAYFKAGDPIWVDVNGDYIIDEKDKVIVGNSQPRMTGGISINLRYKAFSINTNCSFTLRRDIINKALADRFRAYGTPVAGKVNLTGSGALTPIEAYNFWTEDNIYAQYPNPFDYTRSSIIQPFRYDQTLFMEDGSYFKINGISVAYTIPKKMLDFFRISRCQLNFSMNNIYTFSKYSGINPENVNNLGYDTSGGYPNGRTVTFGVSMDF Bacteroides thetaiotaomicron VPI-5482 Btheta 349801 BT0273 Outer membrane binding protein for (+)-arabinogalactan (SusD-like) # Important on (+)-Arabinogalactan along with SusC-like BT0272 hypothetical protein (NCBI ptt file) MKNIVLIMTLIVSCLFAGCDSLANKSEDKLSGDDFWAQGNETNAEAFLLSIYNSFRNATMSQRPFLTYSGDMRCAPITAYSTGDKYVAYLANNDMGELRNTYPDDARGGLIMQWDVFYTAIQDANILLAEIDKVPGMDELKRSRFKAEAIFMRSLSYFFIVRAFGDVPYYTNAYNEAPLPRTNMVIVLQNCLADLQPLLDDDPGAEVLPWSYSSYSSKGIRASRGSVIALMMHINLWLVQFDAQNKEQYYRNVVSLGEELERNNGAYSLLDINRSSVIFAGGSDEGLFEIAQNINFNEIFMMNAKFSDNVSYSCLNKSMPLFCYSGDYLMTLFPMYEDDARKELWFDEKIYSTSVSSSAPKEIKKFWNIDTYGNGTITSNSGNQIVFRYAGALLLYAEALAALGTNDTKACELLNRVRNRAHASEINTSGSELMDAIFWERCRELIGEGHYYYDLVRTGKVYNRNYCMNPMTRTNFNVGAWTWPIHRNALKNNTQIGLNLFWE Bacteroides thetaiotaomicron VPI-5482 Btheta 352617 BT3090 TonB-dependent receptor for dextran (SusC-like) # Specifically important in carbon source dextran; may also be important for utilization of red arabinan from sugar-beet; previously proposed to be involved in dextran utilization, see PMC3878776; part of the BT3087-BT3090 complex for uptake and hydrolysis (PMID:37286596) putative outer membrane protein, probably involved in nutrient binding (NCBI ptt file) MEQSIKSKGFEHRLLLIMWGLLLSLSAFAQQITVKGHVVDATGEPVIGASVIEGKSTNGTITDIDGNFSLNVSANSALTISFVGYKTQTVSVNGKTALKVTLQEDTEVLDEVVVVGYGTMKKSDLTGAVSSVGVKDIKDSPVANIGQAMQGKVSGVQIIDAGKPGDNVTIKIRGLGTINNSNPLVVIDGIPTDLGLSSLNMADVERVDVLKDASATAIYGSRGANGVVMITSKRGAEGAGKVTVNANWAIQNATKVPDMLNAAQYAALSNDMLSNNDDNTNPYWADPSSLGKGTNWLDEMLRTGVKQSYSVSYSGGTEKAHYYVSGGFLDQSGIVKSVNYRRFNFQANSDAQVNKWLKFTTNLTFSTDVKEGGTYSIGDAMKALPTQPVKNDDGSWSGPGQEAQWYGSIRNPIGTLHMMTNETKGYNFLANITGEITFTKWLKLKSTFGYDAKFWFADNFTPAYDWKPNPVEESSRYKSDNKSFTYLWDNYFVFDHTFAKKHRVGVMAGSSAQWNNYDYLNAQKNIFMFDNIHEMDNGEKMYSLGGSQSDWALLSLMARLNYSYEDKYLLTATVRRDGSSRFGKNNRWGTFPSVSLAWRVSQEDWFPKDNFLMNDLKLRVGYGVTGNQEIGNYGFVASYNTGVYPFGNNNSTALVSTTLSNPNIHWEEVRQANFGVDMSLFDSRVSLSLDAYIKNTNDMLVKASIPITSGFEDTTETFTNAGKMRNKGVEMTLRTINLKGIFSWESALTATYNKNEILDLNSETPMFINQIGNSYVTMLKAGYPINVFYGYVTDGLFQNWGEVNRHATQPGAAPGDIRFRDLNNDGVINDEDRTILGNPNPNWFFSLSNNLSYKGWELSVFLQGVAGNKIYNANNVDNEGMAAAYNQTTAVLNRWTGEGTSYSMPRAIWGDPNQNCRVSDRFVENGSYLRLKNITLSYTLPKKWLQKIQLENARISFSCENVATITRYSGFDPEVDVNGIDSSRYPISRTFSMGLNFNF Bacteroides thetaiotaomicron VPI-5482 Btheta 352616 BT3089 Outer membrane binding protein for dextran (SusD-like) # Specifically important in carbon source dextran; may also be important for utilization of red arabinan from sugar-beet; part of the BT3087-BT3090 complex for uptake and hydrolysis (PMID:37286596) putative outer membrane protein, probably involved in nutrient binding (NCBI ptt file) MKKKLTFIMILAVLALTSCSDFLDKYPKYGVDPESEVTNEIAVALTTACYKTLQSSNMYNQRLWSLDILAGNSEVGAGGGTDGLETVQAANFIAQSDNGFALYVWRSPWVGIGRCNIVLSNLPSAAISDEIKDRCMGEAYFLRAHYYYILVRLYGGVPLRLQPFEPGQSTDIARNTVDEVYAQILSDCKNAVDMLPPKSSYGENDKGRACKEAAMAMLADIYLTLAPNHRDYYNEVVTLCDQITAMGYDLSQCKYADNFDATINNGAESLFEVQYSGSTEYDFWGGDNQSSWLSTFMGPRNSGMVAGAYGWNLPTEEFIKEYEAGDLRKDVTVLYQGCPAFDGMEYRRSWSNTGYNVRKFLVSKTVSPEYNTNPNNFVVYRYADVLLKKAEALNELGHPDQAAAPLNIVRQRAGLADVPTTLNQETMREKIIHERRMELAFEGHRWFDMIRINNGNYAIEFLKSIGKNQVTKERLLLPIPQTEMDSNNLMTQNPGY Bacteroides thetaiotaomicron VPI-5482 Btheta 351608 BT2080 L-cysteine desulfidase cdsB # 44% identical to cdsB ADO66727.1 from Yersinia ruckeri (PMC3028680); important for fitness in minimal media with cysteine as a reductant, for cysteine detoxification conserved hypothetical protein, putative inner membrane protein (NCBI ptt file) MIESERKQIIDLIKKEVIPAIGCTEPIAVALCVAKAAETLGMKPEKIEVLLSANILKNAMGVGIPGTDMVGLPIAVALGALIGRSEYQLEVLRDCTPEAVEQGKLFIAEKRICISLKEDITEKLYIEVICTAGSQKATAVIAGGHTTFVYIATDEKVLLDKQQTANEEEEDASLELNLRKVYDFALTSPLDEIRFILDTARLNKAAAEQAFKGNYGHSLGKMLRGTYEHKVMGDSVFSHILSYTSAACDARMAGAMIPVMSNSGSGNQGISATLPVVVFAEENGKTEEELIRALMLSHLTVIYIKQSLGRLSALCGCVVAATGSSCGITWLMGGNYNQVAFAVQNMIANLTGMICDGAKPSCALKVTTGVSTAVLSAMMAMEDRCVTSVEGIIDEDVDQSIRNLTRIGSQAMNETDKMVLDIMTHKGGC Desulfovibrio vulgaris Hildenborough JW710 DvH 207383 DVU1914 (R)-citramalate synthase (EC 2.3.3.21) # Important for fitness in defined media, except when isoleucine is added. (Citramalate is a precursor to 2-oxobutanoate and isoleucine in some prokaryotes.) 2-isopropylmalate synthase/homocitrate synthase family protein (TIGR) MRRQIHLYDTTLRDGSQSEDINLNTPDKLKIALRLDELGIAYIEGGWPGSNPVDVAFFKEIRNYNLKQAKISAFGSTHHPSHTAENDPNLKAIAAARTDAAAIFGKSCERHAREALRLDGRRNLDIIHDSIAFLKKQVAEVFFDAEHFFDGYRHNAAYALEVLRRAHEAGGDVLVLCDTNGGTLPHEVHDIVTAVREQLPEAKLGIHAHNDCEVAVANSIAAVQAGAVQVQGTMNGVGERCGNANLSSVIPILELKSAGAYACLPEGRLQQLTAVSSYVSEVTNLPPFSRQPFVGRSAFAHKGGVHVSAVNRNATLYEHITPESVGNHQRVLITELAGRSNIVSLARRFGFHLDKDEPVVKGLMNELKKKASLGYDYAAAEASVELLLLRKLARRGVREFFKLIQFRVLESKQENDLEPMSEASVMVEVEGIIEHTAATGRGPVNALDNALRKALSSFYPRIREMRLLDFKVRVLTGTETDGGTASTVRVLIESGDADSRWVTVGVSYNIIEASWQALADSMTYKLYKDEHVQRGMTD Desulfovibrio vulgaris Hildenborough JW710 DvH 208495 DVU2982 leuC 3-isopropylmalate dehydratase / (R)-citramalate isomerase, large subunit LeuC (EC 4.2.1.33; EC 4.2.1.35) # Important for fitness in defined media, except when both leucine and isoleucine are provided. 3-isopropylmalate dehydratase, large subunit, putative (TIGR) MAHTLAQKILQRHTDEAITDAGQIVRCRVSMVLANDITAPLAIKSFRAMGAKRVFDKDRVALVMDHFTPQKDIEAAQQVKLTREFAREMGVTHYYEGGDCGVEHALLPELGLVGPGDVVVGADSHTCTYGGLGAFATGLGSTDVAGAMALGETWFKVPPTIRATFTGTLPAYVGAKDLILTLIGAIGVDGALYRALEFDGAAIEALDVEGRMTMANMAIEAGGKAGLFAADAKTLTYCTTAGRTGDTAFSADAGAVYERELSFDVTGMTPVVACPHLPDNVKPVSEVKDVTVQQVVIGSCTNGRIGDLREAAAVLRGRKVSRDVRCIVLPATPGIWRQALREGLIETFMEAGCIVGPATCGPCLGGHMGILADGERAIATTNRNFKGRMGSLESEVYLSGPATAAASAVTGVITDPSTL Desulfovibrio vulgaris Hildenborough JW710 DvH 208496 DVU2983 leuD 3-isopropylmalate dehydratase / (R)-citramalate isomerase, small subunit LeuD (EC 4.2.1.33; EC 4.2.1.35) # Important for fitness in defined media, except when both leucine and isoleucine are provided. 3-isopropylmalate dehydratase, small subunit (TIGR) MRYAGTAHKVGDHIDTDAIIPARFLVTTDAQKLGENCMEGLEHGWVARVKSGDIMVGGRNFGCGSSREHAPIAILGAGMPVVVAHSFARIFYRNGFNMGLLLLEVGDDVDKIADGDDIEVDAASGVITNRTTGATITCAPVPQSMRELLDTGGLVPYVRARLERENG Pseudomonas simiae WCS417 WCS417 GFF1318 PS417_06700 3-oxoadipate CoA-transferase subunit A (EC 2.8.3.6) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (2.8.3.6) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 3-oxoadipate:succinyl-CoA transferase MAEILALRDAVKQFVNDGDTVALEGFTHLIPTAAGHEIIRQGKKDLTLVRMTPDLIYDQLIGAGCARKLIFSWGGNPGVGSLHRLRDAVEKQWPQPLEIEEHSHADLANAYVAGASGLPFAVLRAYAGSDLPKVNPLIKTVTCPFTGEVLAAVPSVRPDVTVIHAQKADRKGNVLLWGILGVQKEAALAAKRCIVTVEEIVDDLNAPMNSCVLPTWALTAVCHVPGGAHPSYAHGYNERDNRFYQAWDPIARDRGTFTAWINEYIHGTADFTEFQAKLATAQEAK Pseudomonas simiae WCS417 WCS417 GFF1319 PS417_06705 3-oxoadipate CoA-transferase subunit B (EC 2.8.3.6) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (2.8.3.6) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 3-oxoadipate:succinyl-CoA transferase MAYSTNEMMTVAAARRLKNGSVCFVGIGLPSKAANLARLTSSPDVVLIYESGPIGAKPSVLPLSIGDGELAETADTVVPTGEIFRYWLQGGRIDVGFLGAAQVDRFGNINTTVVGDYHQPKVRLPGAGGAPEIAGSAKSVLIILKQSARSFVDKLDFITSVGHGEGGDSRKRLGLPGAGPVGIITDLCIMEPEAGTHEFVVTALHPGVTREQVVAATGWAIRFADQVDTTAEPTDVELTALRDLEARTAAAHGQAPGEA Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4591 3-oxoadipate CoA-transferase subunit B (EC 2.8.3.6) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (2.8.3.6) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 3-oxoadipate CoA-transferase subunit B (EC 2.8.3.6); Glutaconate CoA-transferase subunit B (EC 2.8.3.12) MTYTTNEMMTVAAARRLKNGSVCFVGIGLPSKAANLARLTSSPDVVLIYESGPIGAKPSVLPLSIGDGELAETADTVVPTGEIFRYWLQGGRIDVGFLGAAQVDRFGNINTTVVGDYHAPKVRLPGAGGAPEIAGSAKSVLIILKQSSRSFVDKLDFITSVGHGEGGDSRKRLGLPGAGPVGIITDLCIMEPEAGTHEFVVTALHPGVTREQVVDATGWAIRFADQVEQTAEPTEVELTALRDLEARTAAAHGQAPGEA Pseudomonas fluorescens GW456-L13 pseudo13_GW456_L13 PfGW456L13_4592 3-oxoadipate CoA-transferase subunit A (EC 2.8.3.6) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (2.8.3.6) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 3-oxoadipate CoA-transferase subunit A (EC 2.8.3.6); Glutaconate CoA-transferase subunit A (EC 2.8.3.12) MAEILSLHDAVKQFVNDGDTVALEGFTHLIPTAAGHEIIRQGKKDLTLVRMTPDLIYDQLIGAGCARKLIFSWGGNPGVGSLHRLRDAVEKQWPHALEIEEHSHADLANAYVAGASGLPFAVLRAYAGSDLPKVNPLIKSVTCPFTGEVLAAVPSVRPDITVIHAQKADRKGNVLLWGILGVQKEAALAAKRCIVTVEEIVDDLNAPMNSCVLPTWALSAVCHVPGGAHPSYAHGYNERDNRFYQAWDPIARDRETFTAWINEYIHGSADFSEFQAKLAAASEAK Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_17195 AO353_17195 3-oxoadipate CoA-transferase subunit A (EC 2.8.3.6) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (2.8.3.6) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 3-oxoadipate--succinyl-CoA transferase MAEILSLHDAVKQFVNDGDTVALEGFTHLIPTAAGHEIIRQGKKDLTLVRMTPDLVYDQLIGAGCARKLIFSWGGNPGVGSLHRLRDAVEKQWPHALEIEEHSHADLANAYVAGASGLPFAVLRAYAGSDLPKVNPLIKSVTCPFTGEVLAAVPSVRPDVTVIHAQKADRKGNVLLWGILGVQKEAALAAKRCIVTVEEIVDDLKAPMNACVLPTWALSAVCHVPGGAHPSYAHGYTERDNRFYQAWDPIARDRETFTAWINEYIHGSADFSEFQAKLAKASEAQ Pseudomonas fluorescens FW300-N2E3 pseudo3_N2E3 AO353_17200 AO353_17200 3-oxoadipate CoA-transferase subunit B (EC 2.8.3.6) Specifically important for utilizing L-Tryptophan. Automated validation from mutant phenotype: the predicted function (2.8.3.6) was linked to the condition via a SEED subsystem. This annotation was also checked manually. 3-oxoadipate--succinyl-CoA transferase MAYSTNEMMTVAAARRLKNGSVCFVGIGLPSKAANLARLTSSPDVVLIYESGPIGAKPTVLPLSIGDGELAETADTVVPTGEIFRYWLQGGRIDVGFLGAAQVDRFGNINTTVVGDYHQPKVRLPGAGGAPEIAGSAKSVLIILKQSARSFVDKLDFITSVGHGEGGDSRKRLGLPGAGPVGIITDLCIMEPEAGTNEFVVTALHPGVTREQVIAATGWAVRFADQLEHTAEPTAIELAALRDLEARTAAAHGQAPGEA Pseudomonas putida KT2440 Putida PP_3590 PP_3590 aromatic-amino-acid transaminase (EC 2.6.1.57) Required for utilization of phenylalanine or tyrosine as the sole nitrogen source (PMID:38323821). Has phenotypes on a variety of carbon sources, which probably indicates a (partly genetically-redundant) biosynthetic role as well. May also act on isoleucine or on 2-aminoadipate, as part of pipecolate degradation (PMC9004399). Was previously proposed to be D-lysine aminotransferase, but is not important for utilizing D-lysine (PMID:38323821). 71% identical to E. coli tyrB. D-lysine aminotransferase MFKHVDAYAGDPILSLMETFKADPRADKVNLSIGLYYDEAGVVPQLAAVDAVEKRIAGQDHEASLYLPMEGLASYRQAIQALLFGADHPAVTGGRVATVQTVGGSGALKVGADFLKRYFPQSEVWVSNPTWDNHRAIFEGAGFKVHTYPYFDQATRGVDFDGMLATLQSLPANSVVLLHPCCHNPTGADLQQHQWQQVVEVVKARQLIPFLDIAYQGFAEGLVEDAYAIREMARAGVPCLVSNSFSKIFSLYGERVGGLSVVCDDEATAQSVLGQLKATVRRNYSSPPNFGAQLVAGVLSDAGLNAQWAEEVEVMRKRILDMRQALVDALAVLLPGQDFQFFLRQRGMFSYTGFSVEQVRRLRDEFGVYLIDSGRVCMSGLRPANLQRVAEAFAAVQK