step type query desc file sequence aapJ curated TCDB::Q52812 AapJ, component of General L-amino acid porter; transports basic and acidic amino acids preferentially, but also transports aliphatic amino acids (catalyzes both uptake and efflux) MKNKLLSAAIGAAVLAVGASAASATTLSDVKAKGFVQCGVNTGLTGFAAPDASGNWAGFDVDFCKAVASAVFGDPTKVKYTPTNAKERFTALQSGEIDVLSRNTTWTINRDTALGFNFRPVTYYDGQGFMVRKGLNVKSALELSGAAICVQSGTTTELNLADYFKTNNLQYNPVVFENLPEVNAAYDAGRCDVYTTDQSGLYSLRLTLKNPDEHIILPEIISKEPLGPAVRQGDDQWFDIVSWTAYALINAEEFGITQANVDEMKNSPNPDIKRFLGSETDTKIGTDLGLTNDWAANVIKGVGNYGEIFERNIGQGSPLKIARGLNALWNKGGIQYAPPVR aapJ ignore reanno::Smeli:SMc02118 ABC transporter for L-Glutamine, L-Histidine, and other L-amino acids, periplasmic substrate-binding component MARRILTALVGAAVVGIGTHAASAATLDDVKAKGFVQCGVNTGLAGFAAPDASGNWSGFDVDYCKAIAAAIFGDGSKVKYTPLSAKERFPALQSGEVDVLARNTTWSINRDTALGFNFRPVNYYDGQGFMVRKELDVKSALELSGAAVCVQTGTTTELNLADYFKANNLQYNPVVFEKLEEVNAAYDAGRCDVYTTDQSGLYSLRLTLSKPDDHIVLPEIISKEPLAPAVRQGDDQWFDIVSWVHYALVQAEEFGVTQANLEEMKKSTNPDVQRFLGVEADSKIGTDLGLTNEWAVNIVKAVGNYGEVFDRNIGAGSPLKIERGLNALWNKGGLQYAPPVR aapM curated TCDB::Q52814 AapM, component of General L-amino acid porter; transports basic and acidic amino acids preferentially, but also transports aliphatic amino acids (catalyzes both uptake and efflux) MSVADKPFVRTSILAAEPPPPGERGAVAWIRRNLLATPKDVILTILALALIAWAVPHLVNWLFIQAVWSGPDRTFCATTLQGGIQPDGWSGACWAFISAKYDQFIFGRYPLGERWRPAIVGILFILLLVPMLIPSAPRKGLNAILLFAVLPVIAFWLLHGGFGLEVVETPLWGGLMVTLVLSFVGIAVSLPVGILLALGRRSRMPVIRMLCVTFIEVIRGVPLITVLFMASVMLPLFLPTGWNVDKLLRALIGVSIFTSAYMAEVIRGGLQAIPKGQFEGADSLGLGYWQKTRLIIMPQAIKLVIPSIVNTFIGTFKDTSLVTIIGMFDLLGIVKLNFSDANWASAVTPITGLIFAGFIFWLFCFGMSRYSGFMERHLDTGHKR aapM ignore reanno::Smeli:SMc02120 ABC transporter for L-Glutamine, L-Histidine, and other L-amino acids, permease component 2 MSTNQASFVRASMIEASPAPSLESGAVSWLRKNLFATPKDTALTIISLLILAWLVPPAIQWLFIDAAWSGGGRGVCATLSQGGSQPEGWSGACWAFVNAKFAQFLFGRYPLDERWRPALVGILFVLLLVPMLIPRIPYKGLNALLLLVALPILSAILLPGGWFGLTYVETPLWGGLMVTLVLSFVGIAVSLPLGILLALGRRSNMPVIKMLCTVFIEVIRGVPLITVLFMASVMLPLFLPQGVTFDKFLRALIGVSLFASAYMAEVVRGGLQAIPKGQYEGADSLGLSFWQKMGFIVLPQALKLVIPGIVNTFIGLFKDTSLVSIIGMFDLLGIVRLNFSDTNWATAVTPLTGLIFAGFVFWLFCFGMSRYSGFMERLLDRSQR aapP curated TCDB::Q52815 AapP, component of General L-amino acid porter; transports basic and acidic amino acids preferentially, but also transports aliphatic amino acids (catalyzes both uptake and efflux) MAEAPAKKLTVSATEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDEVRREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNEPAAFFDNPQHERTKLFLSQILH aapP ignore reanno::Smeli:SMc02121 ABC transporter for L-Glutamine, L-Histidine, and other L-amino acids, ATPase component MANTATAPKLAVSTTDVAIEITNMNKWYGDFHVLRDINLRVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEVRREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKEAEQVAMHFLERVKIPEQALKYPGQLSGGQQQRVAIARSLCMRPKILLFDEPTSALDPEMVKEVLDTMVGLAEEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFLSQILH aapQ curated TCDB::Q52813 AapQ, component of General L-amino acid porter; transports basic and acidic amino acids preferentially, but also transports aliphatic amino acids (catalyzes both uptake and efflux) MTHEAVDTTPLHGTGWSFRSAMYDPKYRSIFYQILTIVILVGFVWWVAHNTAVNLARSNTASGFGFLRGRAGFEIGQSLITFSSDSTYARALLVGILNTLLVAVTGIFTATIIGFLIGIGRLSRNWLIAKLCTVYVEVFRNIPPLLVIFFWYLGVLSVLPQPRESVGLPFSMYLNNRGLAFPKPIFDTGMIAVGIALVIAIVASIIIARWAHKRQAATGQPFHTVWTAIALIVGLPLLVFVVSGFPLTFDVPVAGKFNLTGGSVVGPEFMSLFLALSFYTASFIAEIVRGGIRGVPKGQSEAAGALGLHPSSVTRLVVVPQALRIIIPPLTSQYLNLTKNSSLAIAIGFSDLVAVGGTILNQSGQAIEIVCIWGIVYLSLSILTSLFMNWFNAKMALVER aapQ ignore reanno::Smeli:SMc02119 ABC transporter for L-Glutamine, L-Histidine, and other L-amino acids, permease component 1 MAIGVTNAPERSRSSGSIINDPQVRGIFYQAITIIILAALIYWIVDNTVDNLRRANIASGYDFVRSRAGFDVGQSLISFTSDSTYGRALLVGFINTLLVAITGIITATIIGFIVGIGRLSHNWIIAKLSLAYVEVFRNIPPLLVIFFWYSGVLSILPQARDALALPFDIFLSNRGVAFPRPIAEEGAEYTLLAFVIAVAASVFFARYARKRQLATGERLPVLWTVLGLIIGLPLVTFLVTGAPITFDIPVAGKFNLTGGSVVGPEFMSLFLALSFYTAAFIAEIVRAGIRGVSKGQTEAAHALGIRPALTTRLVVVPQAMRIIIPPLTSQYLNLTKNSSLAVAIGYADLVAVGGTILNQTGQSIEIVSIWLIVYLSLSLATSLFMNWYNARMALVER acaP curated SwissProt::A2RL65 Aspartate/glutamate permease AcaP MDTKKIRWFTVAFIAFNMVWGMGNVVNNFAQQGITVVTSWLLILALYFIPYALIVGQLCSTFKDSKGGVSSWVENTSTKRLAYYAAWTYWVVHIPYLAQKPQAILIAFGWVGQGNGNLVSQMSMTAVALISLAIFLAFLWLSTKGLNTLKVIGGLAGTAMFVMSLLFIVMAIGAPFIAKDFHIATPDMGNIKTYIPKFDFSYFTTISMLVFAVGGAEKISPYVNQTKNPAKEFPRGMFLLAGMVGICAVLGSIAMGMIFSSGNLPKDLMANGAYAAFQILGQHFGVGNFLMIVYALTNGVGQIAALAFSIDAPLRILLADADPEYVPAWLRKKTNKGTLKNGYTLTGILVSIIILLPLLGIGDMNELVKWLTNLNSVVMPMRYLWVFFAFIMLNRAVKHFQSEYKFIKQKRLAMIAGAWCFLFTLIACVLGMVPKLDYAANPSAWWFQLASNILTPIVLILLGMLLPFIARREQRKATSLDLDTIVTPD acaP curated TCDB::F2HJG8 Aspartate/Glutamate transporter of 488 aas and 12 TMSs, AcaP MDTKKIRWFTVAFIAFNMVWGMGNVVNNFAQQGITVVTSWLLILALYFIPYALIVGQLGSTFKDSKGGVSSWVENTSTKRLAYYAAWTYWVVHIPYLAQKPQAILIAFGWVGQGNGNLVSQMSMTAVALISLAIFLAFLWLSTKGLSTLKVIGGLAGTAMFVMSLLFIVMAIGAPFIAKDFHIATPDMGNIKTYIPKFDFSYFTTISMLVFAVGGAEKISPYVNQTKNPAKEFPRGMFLLAGMVGICAVLGSIAMGMIFSSGNLPNDLMANGAYAAFQILGQHFGVGNFLMIVYALTNGVGQIAALAFSIDAPLLILLADADPEFVSAWLRKKTNKGTLKNGYTLTGILVSIIILLPLLGIGDMNELVKWLTNLNSVVMPMRYLWVFFAFIMLNRAVKHFQSEYKFIKQKRLAMIAGAWCFLFTLIACVLGMVPKLDYAANPSAWWFQLASNILTPIVLILLGMLLPFIARREQRKTNGLDLNSLNVE acaP ignore TCDB::P75835 The GadC homologue MAGNVQEKQLRWYNIALMSFITVWGFGNVVNNYANQGLVVVFSWVFIFALYFTPYALIVGQLGSTFKDGKGGVSTWIKHTMGPGLAYLAAWTYWVVHIPYLAQKPQAILIALGWAMKGDGSLIKEYSVVALQGLTLVLFIFFMWVASRGMKSLKIVGSVAGIAMFVMSLLYVAMAVTAPAITEVHIATTNITWETFIPHIDFTYITTISMLVFAVGGAEKISPYVNQTRNPGKEFPKGMLCLAVMVAVCAILGSLAMGMMFDSRNIPDDLMTNGQYYAFQKLGEYYNMGNTLMVIYAIANTLGQVAALVFSIDAPLKVLLGDADSKYIPASLCRTNASGTPVNGYFLTLVLVAILIMLPTLGIGDMNNLYKWLLNLNSVVMPLRYLWVFVAFIAVVRLAQKYKPEYVFIRNKPLAMTVGIWCFAFTAFACLTGIFPKMEAFTAEWTFQLALNVATPFVLVGLGLIFPLLARKANSK aspA hmm TIGR00839 aspA: aspartate ammonia-lyase (EC 4.3.1.1) TIGR00839.hmm aspA curated BRENDA::P0AC38,CharProtDB::CH_024464,SwissProt::P0AC38,ecocyc::ASPARTASE-MONOMER,metacyc::ASPARTASE-MONOMER aspartate ammonia-lyase (EC 4.3.1.1);; aspartate ammonia-lyase;; Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1;; aspartate ammonia-lyase (EC 4.3.1.1);; aspartate ammonia-lyase (EC 4.3.1.1) MSNNIRIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISDIPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEVLNNGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYSSLIKLVDAINQLREGFERKAVEFQDILKMGRTQLQDAVPMTLGQEFRAFSILLKEEVKNIQRTAELLLEVNLGATAIGTGLNTPKEYSPLAVKKLAEVTGFPCVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMPAKVNPVVPEVVNQVCFKVIGNDTTVTMAAEAGQLQLNVMEPVIGQAMFESVHILTNACYNLLEKCINGITANKEVCEGYVYNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTEAELDDIFSVQNLMHPAYKAKRYTDESEQ aspA curated BRENDA::Q0PC50 aspartate ammonia-lyase (EC 4.3.1.1) MGTRKEHDFIGELEISDEVYYGVQTFRAVENFDISHDRLKDFPRFVRALARVKKAAAMANHELGLLDKNIQDAIIKACDKILEGGYYDQFVVDMIQGGAGTSTNMNANEVIANIGLELMGHKKGEYQYLHPNDHVNLSQSTNDAYPTALHLALHDYLSDLAKAMEHLKKAYERKAEEFKDVLKMGRTQLQDAVPMTLGREFKTFAVMIGEDIQRVLEARKLILEINLGGTAIGTGINSHPDYPKVVERKIREVTGFEYTVAEDLIEATQDTGAYVQISGVLKRVATKLSKVCNDLRLLSSGPKCGLNEINLPKMQPGSSIMPGKVNPVIPEVVNQVCYFVIGADVTVTFACEGGQLQLNVFEPVVAYSLFNSVVMLEKAMYTLADKCIDGITANEKICSDFVYNSVGIVTALNPYIGYENSASIAKEAMNTGKRVADIALERGLLSKEQIDEILTPSNMLNPHMEAKK aspA curated BRENDA::Q9HTD7 aspartate ammonia-lyase (EC 4.3.1.1) MSPVASSRIEKDLLGTLEVPADAYYGIQTLRAVNNFRLSGVPLSHYPKLVVALAMVKQAAADANRQLGHLPEDKHAAISEACARLIRGDFHEQFVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLAPELLTEVNLGGTAIGTGINADPGYQKLAVERLAAISGQPLKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPRQPGSSIMPGKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLREHCITGITANVERCHELVEHSIGLVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADILLPENMIAPRLIPLRA aspA curated BRENDA::Q9LCC6 aspartate ammonia-lyase (EC 4.3.1.1) MNTDVRIEKDFLGEKEIPKDAYYGVQTIRATENFPITGYRIHPELIKSLGIVKKSAALANMEVGLLDKEVGQYIVKAADEVIEGKWNDQFIVDPIQGGAGTSINMNANEVIANRALELMGEEKGNYSKISPNSHVNMSQSTNDAFPTATHIAVLSLLNQLIETTKYMQQEFMKKADEFAGVIKMGRTHLQDAVPILLGQEFEAYARVIARDIERIANTRNNLYDINMGATAVGTGLNADPEYISIVTEHLAKFSGHPLRSAQHLVDATQNTDCYTEVSSALKVCMINMSKIANDLRLMASGPRAGLSEIVLPARQPGSSIMPGKVNPVMPEVMNQVAFQVFGNDLTITSASEAGQFELNVMEPVLFFNLIQSISIMTNVFKSFTENCLKGIKANEERMKEYVEKSIGIITAINPHVGYETAAKLAREAYLTGESIRELCIKYGVLTEEQLNEILNPYEMTHPGIAGRK aspA curated2 P26899 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 MLNGQKEYRVEKDFLGEKQIEADVYYGIQTLRASENFPITGYKIHEEMINALAIVKKAAALANMDVKRLYEGIGQAIVQAADEILEGKWHDQFIVDPIQGGAGTSMNMNANEVIGNRALEIMGHKKGDYIHLSPNTHVNMSQSTNDVFPTAIHISTLKLLEKLLKTMEDMHSVFKQKAQEFDSVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYEVNMGATAVGTGLNADPEYIKQVVKHLADISGLPLVGADHLVDATQNTDAYTEVSASLKVCMMNMSKIANDLRLMASGPRAGLAEISLPARQPGSSIMPGKVNPVMAELINQIAFQVIGNDNTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRSFTDNCLKGIEANEKRMKQYVEKSAGVITAVNPHLGYEAAARIAREAIMTGQSVRDLCLQHDVLTEEELDIILNPYEMTKPGIAGKELLEK aspA curated2 P56149 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 MRIEHDFIGQMEISDEVYYGIQTLRASENFFITNDKLCSYPVFIKSFAQVKKAATLANVQLGLIDEKLKIAICHACDLLIDGKYHDQFIVDMIQGGAGTSTNMNMNEVIANLALEYMGHQKGEYQFCHPNDHVNRSQSTNDAYPSALKIAIYERLSNLVAPMKALRDAFAQKAKEFAHVIKMGRTQLQDAVPMTLGQEFETYALMVDRDIEQVLDARNWVRELNLGGTAIGTGINSHPDYRSLIEKKIQEVTGRPFVMANNLIEATQSTGAYVQVSGVLKRIAVKLSKVCNDLRLLSSGPRAGLNEINLPKMQPGSSIMPGKVNPVIPEVVNQVCFAVIGNDLSVALAAEGGQLQLNVFEPVIAYKLFHSFVILGRAIETLTTKCVEGITANEKICHDYVFNSIGIVTALNPHIGYEKSAMIAKEALKSDRSIYDIALEKKILTKEQLDDIFKPENMLSPHAFKKHKD aspA curated2 Q59200 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 MSKTSNKSSADSKNDAKAEDIVNGENQIATNESQSSDSAAVSERVVEPKTTVQKKFRIESDLLGELQIPSHAYYGVHTLRAVDNFQISRTTINHVPDFIRGMVQVKKAAALANRRLHTLPAQKAEAIVWACDQILIEERCMDQFPIDVFQGGAGTSLNMNTNEVVANLALEFLGHEKGEYHILHPMDDVNMSQSTNDSYPTGFRLGIYAGLQTLIAEIDELQVAFRHKGNEFVDIIKMGRTQLQDAVPMSLGEEFRAFAHNLAEEQTVLREAANRLLEVNLGATAIGTGVNTPAGYRHQVVAALSEVTGLELKSARDLIEATSDTGAYVHAHSAIKRAAMKLSKICNDLRLLSSGPRAGLNEINLPPRQAGSSIMPAKVNPVIPEVVNQVCFKVFGNDLTVTMAAEAGQLQLNVMEPVIGESLFQSLRILGNAAKTLREKCVVGITANADVCRAYVDNSIGIITYLNPFLGHDIGDQIGKEAAETGRPVRELILEKKLMDEKTLEAVLSKENLMHPMFRGRLYLEN aspA curated2 Q9HTD7 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 MSPVASSRIEKDLLGTLEVPADAYYGIQTLRAVNNFRLSGVPLSHYPKLVVALAMVKQAAADANRQLGHLPEDKHAAISEACARLIRGDFHEQFVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLAPELLTEVNLGGTAIGTGINADPGYQKLAVERLAAISGQPLKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPRQPGSSIMPGKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLREHCITGITANVERCHELVEHSIGLVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADILLPENMIAPRLIPLRA braC curated TCDB::Q9L3M3 BraC, component of General L- (and D-)amino acid uptake porter (transports acidic, basic, polar, semipolar and hydrophobic amino acids). The amino and carboxyl groups do not need to be α since γ-aminobutyric acid (GABA) is a substrate. The system may function with additional binding proteins since L-alanine uptake is not dependent on BraC MKKSLLSAVALTAMLAFSGNAWADVLIAVAGPLTGPNAAFGAQLQKGAEQAAADINAAGGINGEQIKIELGDDVSDPKQGISVANKFAADGVKFVIGHFNSGVSIPASEVYAENGILRNHPGRDEPDLHGTGLWNTFRTCGRDDQQGAIAGKYLADHFKDAKIAVVHDKTPYGQGLADETKKAMNAAGVTEVIYEGINVGDKDFSALIAKMKEAGVSIIYWGGLHTEAGLIIRQAADQGLKATLVSGDGIVSNELASIAGDAVAGTLNTFGPDPTANPANKELVEKFKAAGFNPEAYTLYSYAAMQTIAGAAKAAGSLDPEAVAKAMKEKGPFPTVLGDISFDEKGDPKIPGYIMYEWKKVRTASTATSRRHVSFAPLYGT braD uniprot Q1MCU0 SubName: Full=Transmembrane component of a broad range amino acid ABC transporter {ECO:0000313|EMBL:CAK09240.1}; MEYFVQQLLNGLTLGSIYGLVAIGYTMVYGIIGMINFAHGDIFMLGGFAALIVFLVLTSIFAGLPVAVLLLVMLVVAMLMTSLWNWTIERVAYRPLRGSFRLAPLITAIGMSITLSNFIQVTQGPRNKPIPPMVSSVYQFGNISVSLKQIIIIVITAVLLTIFWYIVNRTALGRAQRATEQDRKMAALLGVNVDQTISITFVMGAALAAVAGTMYLMYYGVASFNDGFTPGVKAFTAAVLGGIGSLPGAVFGGLLIGLIESLWSAYFTIAYKDVATFAILAFVLIFKPTGILGRPEVEKV braE uniprot Q1MCU1 SubName: Full=Transmembrane component of a broad range amino acid ABC transporter {ECO:0000313|EMBL:CAK09239.1}; MANIENSAGKPDAGLVRKGLTEALFAAVLSFGMFVLYVGLKTDQNISNELIIVQRWGLLAIFVAVAAIGRFAMVVFIRPNIDRRKLSKAREGELDISTEKSFFHRHFLKIALIALLLYPMVVVAIKGPQGSLTYVDNFGIQILIYVMLAWGLNIVVGLAGLLDLGYVAFYAVGAYSYALLSSYFGLSFWVLLPLSGIFAALWGVILGFPVLRLRGDYLAIVTLAFGEIIRLVLINWTDVTKGTFGISSIPKATLFGIPFDATAGGFAKLFHLPISSAYYKIFLFYLILALCMLTAYVTIRLRRMPIGRAWEALREDEIACRSLGINTVTTKLTAFATGAMFAGFAGSFFAARQGFVSPESFVFLESAVILAIVVLGGMGSLTGIAIAAIVMVGGTELLREMSFLKLIFGPDFTPELYRMLIFGLAMVVVMLFKPRGFVGSREPTAFLRERKAISGSFIKEGHG braF uniprot Q1MCU2 SubName: Full=ATP-binding component of a broad range amino acid ABC transporter {ECO:0000313|EMBL:CAK09238.1}; MMSPVTNTMSDDTLLKVEHLSMKFGGLMAINDFSFEAKRGDITALIGPNGAGKTTVFNCITGFYKPTMGMITFNQKSGKQYLLERLPDFRITKEARVARTFQNIRLFSGLTVLENLLVAQHNKLMKASGYTILGLIGVGPYKREAAEAIELARFWLEKADLIDRADDPAGDLPYGAQRRLEIARAMCTGPELLCLDEPAAGLNPRESATLNALLKSIRAETGTSILLIEHDMSVVMEISDHVVVLEYGQKISDGTPDHVKNDPRVIAAYLGVEDEEVEEVIAAVEQLEGGAN braG uniprot Q1MCU3 SubName: Full=ATP-binding component of a broad range amino acid ABC transporter {ECO:0000313|EMBL:CAK09237.1}; MGDEVMTGQPLLQVNGVETYYGNIRALAGVDVHVNKGEIVSLIGANGAGKSTLMMTICGSPQARTGSVVFEGRDITRMPTHEIARLRIAQSPEGRRIFPRMTVLENLQMGAGLDNLKHFAEDVEKIFTLFPRLKERHAQRGGTLSGGEQQMLSIGRALMARPKLLLLDEPSLGLAPLIVKGIFEAIRKLNEAEGLTVFLVEQNAFAALRLSHRAYVMVNGKVTMSGSGKELLANPEVRAAYLEGGRH bztA curated TCDB::Q52663 BztA, component of Glutamate/glutamine/aspartate/asparagine porter MKKSVFFGSVALAALVAGAASASTLDDVKARGQLICGSNPGLTGFAAPDANGVYQGFDVAVCKAVAAAVLGDPMKVKYVPLTGETRFTALASGEVDVLVRNSTWTFSRDTELALDFVAVNYYDGQGFMVNKSLGVSSAKELDGATICVQTGTTTEMNLADFFKANNMTYTPVNIADDAEGQQKFAAGACDSYTTDASGLASSRATLPNAADIVILPEIISKEPLGPVVRHGDNNWGDIVRWSFYALVAAEEYGITKANLEEVAASTQNPEIRRLLGLEGDMGKKIGLDNDFAKRAILASGNYGEVFEANIGASTSIGLARGLNAQWTQGGLMYAPPFR bztB curated CharProtDB::CH_011913,TCDB::Q52664 glutamate/glutamine/aspartate/asparagine transport system permease protein BztB;; BztB, component of Glutamate/glutamine/aspartate/asparagine porter MALASDPPKAGFRLSMLIYDTRFRSITIQIVVLLLFLAGLVWLLNNAYVNLEAKGKDFNFSFLWTRAGYDLAQTLIPYSNDDTHFRALIEGLLNTLLVSVLGCILATILGTIIGVLRLSQNWLVARIMTVYVETFRNIPLLLWILLMGTILAETRPVPKDFRLTEAMKAAGEEPKASMWFFDSVAVTNRGTNLPAPAFDHSLGVVDLGWNLPVSLNALAILAVMSASFWGWRRFMARAKAVQEATGTRPTTWWPSLLILFAPISALLYGLGFHLDYPQITKFDFTGGFQMLHSFTALLIALTLYTAAFIAEIVRAGIQAISRGQTEAAYALGLRPGRTMSLVILPQALRVIVPPLISQFLNLTKNSSLAIAVSYMDLRGTLGGITLNQTGRELECMLLMMLIYLTISLTISSLMNLYNKSIKLKER bztC curated TCDB::Q52665 BztC, component of Glutamate/glutamine/aspartate/asparagine porter MSDTSFVRTEMLAPRPAPVSQVGAIKWMRENLFSGPLNTALTVFGLLATVWLVQAAAPWLLHGVWNANSLTECRAIIAERWGPEATGACWAVIRVRWNQFLFGFYPVDQYWRLFVTFAGLFLALAPVLFDALPRKLIWGTLLYPLAAFWLLWGGPIWGPVSVLAGFAILGLLFTALAPKLGVPVSAGIGLVVAALFWLYAAAPIEAALQSALPLALPEVDSDQFGGFLLALVIGVTAIVVSLPLGILLALGRQSDMLIVKSLSVGIIEFVRGVPLITLLFTASLLLQYFLPPGTNFDLILRVVILVTLFAAAYIAEVIRGGLAALPRGQYEAADALGLDYWQAQRLIIMPQALKISIPGIVSSFIGLFKDTTLVAFVGLFDPLKGISNVVRSDMAWKGTYWEPYIFVALIFFLFNFSMSRYSMYLERKLKRDHR dmeA curated TCDB::Q31PG5 Possible transporter of polar amino acids including glutamate, glutamine and aspartate, DmeA. It complements a sepJ mutation in Anabaena (TC# 2.A.7.23.2), and SepJ complements a dmeA mutation. Alternatively, and less likely, it could be an activator of an ABC transporter catalyzing uptake of these amino acids MGDDQSDRLRCAGLPLKFPVSLQLAIATALWGGTFTAGRIAVQQLSPLAVACGRYLLATTVLLLILWQREGWPPLNRRQQLLLFGLGVSGIALYNWLFFIGLSLIPASRAALIIALNPTAIALGAAIWTGDRLRSWQWAGVGLSLIGAILLLGSRQAGALTLPGWGDLALVGCVLCWTVYSLLARQALRSLSPLTVTTGACCWGSVLLIGLWLGQGAQLPVNVSFSTGSAIAFLGLGGTALAFCLYANGIERLGAARAGLFINLVPVFGSAIGALLLQEPLSGLTLLGGLLVLAGVGLGTLQRLQPVPISTTEPVGGDRSPGPPALGHDR fumD curated BRENDA::P0AC33,CharProtDB::CH_021646,SwissProt::P0AC33,ecocyc::FUMA-MONOMER,metacyc::FUMA-MONOMER fumarate hydratase (EC 4.2.1.2); (S)-2-methylmalate dehydratase (EC 4.2.1.34);; fumarate hydratase class I, aerobic; EC 4.2.1.2;; Fumarate hydratase class I, aerobic; Fumarase A; Oxaloacetate keto--enol-isomerase; OAAKE isomerase; Oxaloacetate tautomerase; EC 4.2.1.2; EC 5.3.2.2;; fumarase A (EC 4.2.1.2; EC 5.3.2.2);; fumarase A (EC 4.2.1.2; EC 5.3.2.2) MSNKPFHYQAPFPLKKDDTEYYLLTSEHVSVSEFEGQEILKVAPEALTLLARQAFHDASFMLRPAHQQQVADILRDPEASENDKYVALQFLRNSDIAAKGVLPTCQDTGTAIIVGKKGQRVWTGGGDEAALARGVYNTYIEDNLRYSQNAPLDMYKEVNTGTNLPAQIDLYAVDGDEYKFLCIAKGGGSANKTYLYQETKALLTPGKLKNYLVEKMRTLGTAACPPYHIAFVIGGTSAETNLKTVKLASAKYYDELPTEGNEHGQAFRDVELEKELLIEAQNLGLGAQFGGKYFAHDIRVIRLPRHGASCPVGMGVSCSADRNIKAKINRQGIWIEKLEHNPGKYIPEELRKAGEGEAVRVDLNRPMKEILAQLSQYPVSTRLSLNGTIIVGRDIAHAKLKERMDNGEGLPQYIKDHPIYYAGPAKTPEGYASGSLGPTTAGRMDSYVDQLQAQGGSMIMLAKGNRSQQVTDACKKHGGFYLGSIGGPAAVLAQGSIKSLECVEYPELGMEAIWKIEVEDFPAFILVDDKGNDFFQQIQLTQCTRCVK fumD curated BRENDA::P14407,CharProtDB::CH_004085,CharProtDB::CH_024650,SwissProt::P14407,ecocyc::FUMB-MONOMER,metacyc::FUMB-MONOMER fumarate hydratase (EC 4.2.1.2); (S)-2-methylmalate dehydratase (EC 4.2.1.34);; fumarate hydratase class I, anaerobic; EC 4.2.1.2;; anaerobic class I fumarate hydratase (fumarase B);; Fumarate hydratase class I, anaerobic; D-tartrate dehydratase; Fumarase B; EC 4.2.1.2; EC 4.2.1.81;; fumarase B (EC 4.2.1.2; EC 4.2.1.81);; fumarase B (EC 4.2.1.2; EC 4.2.1.81) MSNKPFIYQAPFPMGKDNTEYYLLTSDYVSVADFDGETILKVEPEALTLLAQQAFHDASFMLRPAHQKQVAAILHDPEASENDKYVALQFLRNSEIAAKGVLPTCQDTGTAIIVGKKGQRVWTGGGDEETLSKGVYNTYIEDNLRYSQNAALDMYKEVNTGTNLPAQIDLYAVDGDEYKFLCVAKGGGSANKTYLYQETKALLTPGKLKNFLVEKMRTLGTAACPPYHIAFVIGGTSAETNLKTVKLASAHYYDELPTEGNEHGQAFRDVQLEQELLEEAQKLGLGAQFGGKYFAHDIRVIRLPRHGASCPVGMGVSCSADRNIKAKINREGIWIEKLEHNPGQYIPQELRQAGEGEAVKVDLNRPMKEILAQLSQYPVSTRLSLTGTIIVGRDIAHAKLKELIDAGKELPQYIKDHPIYYAGPAKTPAGYPSGSLGPTTAGRMDSYVDLLQSHGGSMIMLAKGNRSQQVTDACHKHGGFYLGSIGGPAAVLAQQSIKHLECVAYPELGMEAIWKIEVEDFPAFILVDDKGNDFFQQIVNKQCANCTK fumD curated BRENDA::Q141Z6 fumarate hydratase (EC 4.2.1.2); (S)-2-methylmalate dehydratase (EC 4.2.1.34) MSDNKRPVSTELAMTVIKQEDLIQSIADSLQYISYYHPLDYIQALGRAYELEQSPAAKDAIAQILTNSRMCAEGKRPICQDTGIVTVFVKVGMDVRWDGATMGVTDMINEGVRRGYLNPDNVLRASIVSPPEGGRKNTKDNTPAVIHYEIVPGNTVDVQVAAKGGGSENKSKFAMLNPSDSIVDWILKTVPTMGAGWCPPGMLGIGIGGTAEKAMVMAKESLMDPIDIQDVIARGPKDWIEELRVELHEKVNALGIGAQGLGGLATVLDVKIMAAPTHAASKPVAIIPNCAATRHAHFTLDGSGAARLEAPSLDAWPKVHWQPDTEKSKRVDLNTLTPEEVAAWTPGQTLLLSGKMLTGRDAAHKRIADMLAKGEKLPVDFTNRVIYYVGPVDPVRDEAVGPAGPTTATRMDKFTEMMLAQTGLISMIGKAERGPVAIEAIRKHKAAYLMAVGGAAYLVSKAIRSAKVLAFEDLGMEAIYEFDVQDMPVTVAVDSNGTSVHQTGPKEWQARIGKIPVATV fumD ignore BRENDA::A0A251UH44 fumarate hydratase (EC 4.2.1.2) MAMVQAYRRISGGSVVCADSLRLTTCWRYFSTGFREERDTFGPIQVPSDKLWGAQTQRSLQNFEIGGDRERMPEPIIRSFGILKKCAAKVNMEYGLDPSIGKAIMEAAQEVAEGKLNDHFPLVVWQTGSGTQSNMNANEVIANRAAEILGHKRGDKFVHPNDHVNRSQSSNDTFPTVMHIAAATEINSRLIPKLKQLHTSLQAKTNEFSDIVKIGRTHTQDATPLTLGQEFSGYTTQVKYGIDRVICTLPRMYQLAQGGTAVGTGLNTKKGFDVKIAAAVADETRLPFVTAENKFEALAAHDAFVEASGALNTIAASLMKIANDIRFLGSGPRCSLGELILPENEPGSSIMPGKVNPTQCEALTMVCAQAIGNHVALTVGGSNGHFELNVFKPMIASSLLHSIRLLADASASFEKNCVRGIQANKDRISKLLHESLMLVTSLNPKIGYDNAAAVAKTAHKQGCTLKEAALQLGVLTSEEFEQLVVPEKMIGPTD fumD ignore BRENDA::A0A251UZF1 fumarate hydratase (EC 4.2.1.2) MVQAFRRTPGGSAIVADSVRFITCWRHFSTAFREERDTFGPIQVPSDKLWGAQTQRSLQNFEIGGDRERMPEPIIRSFGILKKCAAKVNMEYGLDPSIGKAIMEAAQEVAEGKLNDHFPLVIWQTGSGTQSNMNANEVIANRAAEILGHKRGDKFVHPNDHVNRSQSSNDTFPTVMHIAAATEINSRLIPKLKQLHTALQAKTNEFSDIVKIGRTHTQDATPLTLGQEFSGYTTQVKYGIDRVMCTLPRLYQLAQGGTAVGTGLNTKKGFDVKIAAAVADETRLPFITAENKFEALAAHDAFVEASGALNTIATSLMKIANDIRFLGSGPRCGLGELILPENEPGSSIMPGKVNPTQCEALTMVCAQAIGNHVALTVGGSNGHFELNVFKPMIASTLLHSIRLLADASASFEKNCVSGIQANRERISKLLHESLMLVTSLNPKIGYDNAAAVAKTAHKQGCTLKEAALKLGVLNSEEFDQLVVPEKMIGPSD fumD ignore BRENDA::A5Y6J1 fumarate hydratase (EC 4.2.1.2) MSEYRIERDSMGEVRVPVHAKWRAQTQRALENFPVSGQRIERAHIAALARIKGAAAKVNAELGVLDRDVAEAIQEAAAEVAEGKWDEHFPVDVFQTGSGTSSNMNANEVIATLASERLGRDVHPNDHVNASQSSNDVFPSSLHIAATAAVLHDLIPALDHLARALARKSEEFADVVKSGRTHLMDATPVTLGQEFAGYAAQVRYGIERLNASLPRLAELPLGGTAVGTGINTPPGFSAAVIREVARVTGLPLTEARDHFEAQGARDGIVETSGQLRTIAVGLTKIANDLRWMASGPRTGLAEISLPDLQPGSSIMPGKVNPVVPEAVLMVCAQVIGNDTTVTVAGASGNFELNVMLPVIARNVLESVRLLANASRLLADRTVDGIVAHRERAREYAESSPSIVTPLNRYIGYEEAAKVAKKALAEQKTIRQAVLESGYVERGQLTLEQLDEALDVLRMTRP fumD ignore BRENDA::B1Y931 fumarate hydratase (subunit 2/2) (EC 4.2.1.2) MATYSLKTPLSSEDVAKLRVGDTLYISGVVVSARDSAHKRMLEHIGRGEALPVDLRGGVIYHAGPVVRKTERGWEVISMGPTTSARMEAFEADVIERLGVKLVVGKGGMGRRTAEAMKKYTAAYAIFTGGAGVLAAKAIKRVVDVYWLDLGVAEAMWVLEVENFGPLTVMIDPTGRNYYDELREEAKRRIPEILKSLEWPH fumD ignore BRENDA::B1Y932 fumarate hydratase (subunit 1/2) (EC 4.2.1.2) MLEHVILKAAKEAIIRASVGPALDVASALKRAKEEEEAEAARIQLSAILKNIDLSTDKKAAVCQDTGFPNFYVKLGDRFPVRSKIYDILTQALREVTRELPLRPNTVQPFTEKNPGDNTGVGAPWFEVELFDGDYLEFYYVPKGGGTELPSKAFTLPPGVAMKELPRLVLEAVVDAGPMPCPPVIVGVGIGPSVDIAAKLAKKAAALRPVGSRHPEPEVAKMEEELLRAINKLGIGAHGVGGRITALDVHIEYIYRHPAAFSIGIVFSCWATRRAGARIYPDGRYEIL fumD ignore BRENDA::P05042,SwissProt::P05042,ecocyc::FUMC-MONOMER,metacyc::FUMC-MONOMER fumarate hydratase (EC 4.2.1.2);; Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2;; fumarase C (EC 4.2.1.2);; fumarase C (EC 4.2.1.2) MNTVRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVLAGQHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQLIPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYARRVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGKVNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQMVGSMKAGR fumD ignore BRENDA::P07954,SwissProt::P07954,metacyc::ENSG00000091483-MONOMER fumarate hydratase (EC 4.2.1.2);; Fumarate hydratase, mitochondrial; Fumarase; HsFH; EC 4.2.1.2;; fumarate hydratase monomer (EC 4.2.1.2) MYRALRLLARSRPLVRAPAAALASAPGLGGAAVPSFWPPNAARMASQNSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYGLDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK fumD ignore BRENDA::P08417,SwissProt::P08417 fumarate hydratase (EC 4.2.1.2);; Fumarate hydratase, mitochondrial; Fumarase; EC 4.2.1.2 MLRFTNCSCKTFVKSSYKLNIRRMNSSFRTETDAFGEIHVPADKYWGAQTQRSFQNFKIGGARERMPLPLVHAFGVLKKSAAIVNESLGGLDPKISKAIQQAADEVASGKLDDHFPLVVFQTGSGTQSNMNANEVISNRAIEILGGKIGSKQVHPNNHCNQSQSSNDTFPTVMHIAASLQIQNELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTAVGTGLNTKPGFDVKIAEQISKETGLKFQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPRCGYHELMLPENEPGSSIMPGKVNPTQNEALTQVCVQVMGNNAAITFAGSQGQFELNVFKPVMIANLLNSIRLITDAAYSFRVHCVEGIKANEPRIHELLTKSLMLVTALNPKIGYDAASKVAKNAHKKGITLKESALELGVLTEKEFDEWVVPEHMLGPK fumD ignore BRENDA::P14408,SwissProt::P14408 fumarate hydratase (EC 4.2.1.2);; Fumarate hydratase, mitochondrial; Fumarase; EC 4.2.1.2 MNRAFCLLARSRRFPRVPSAGAVLSGEAATLPRCAPNVVRMASQNSFRIEYDTFGELKVPTDKYYGAQTVRSTMNFKIGGATERMPIPVIKAFGILKRAAAEVNQEYGLDPKIASAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAALEVHQVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMERIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK fumD ignore BRENDA::P55250 fumarate hydratase (EC 4.2.1.2) MLRASATRFLSQAKNMNNSPRLFSSASAALQKFRAERDTFGDLQVPADRYWGAQTQRSLQNFDIGGPTERMPEPLIRAFGVLKKAAATVNMTYGLDPKVGEAIQKAADEVIDGSLIDHFPLVVWQTGSGTQTKMNVNEVISNRAIELLGGELGSKAPVHPNDHVNMSQSSNDTFPTAMHVAAVVEIHGRLIPALTTLRDALQAKSAEFEHIIKIGRTHLQDATPLTLGQEFSGYTQQLTYGIARVQGTLERLYNLAQGGTAVGTGLNTRKGFDAKVAEAIASITGLPFKTAPNKFEALAAHDALVEAHGALNTVACSLMKIANDIRYLGSGPRCGLGELSLPENEPGSSIMPGKVNPTQCEAMTMVCAQVMGNNTAISVAGSNGQFELNVFKPVMIKNLIQSIRLISDASISFTKNCVVGIEANEKKISSIMNESLMLVTALNPHIGYDKAAKCAKKAHKEGTTLKEAALSLGYLTSEEFDQWVRPEDMISAKD fumD ignore BRENDA::P93033,SwissProt::P93033 fumarate hydratase (EC 4.2.1.2);; Fumarate hydratase 1, mitochondrial; AtFUM1; Fumarase 1; EC 4.2.1.2 MSIYVASRRLSGGTTVTALRYATSLRSYSTSFREERDTFGPIQVPSDKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGVLKKCAAKVNMEYGLDPTIGKAIMQAAQEVAEGKLNDHFPLVVWQTGSGTQSNMNANEVIANRAAEILGRKRGEKCVHPNDHVNRSQSSNDTFPTVMHIAAATEINSRLIPSLKTLHSTLESKSFEFKDIVKIGRTHTQDATPLTLGQEFGGYATQVKYGLNRVTCTLPRLYQLAQGGTAVGTGLNTKKGFDVKIAAAVAEETNLPFVTAENKFEALAAHDACVETSGSLNTIATSLMKIANDIRFLGSGPRCGLGELVLPENEPGSSIMPGKVNPTQCEALTMVCAQVMGNHVAVTVGGSNGHFELNVFKPVIASALLHSVRLIADASASFEKNCVRGIEANRERISKLLHESLMLVTSLNPKIGYDNAAAVAKKAHKEGCTLKEAALNLGVLTAEEFDTLVVPEKMIGPSD fumD ignore BRENDA::P9WN93,SwissProt::P9WN93 fumarate hydratase (EC 4.2.1.2);; Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2 MAVDADSANYRIEHDTMGEVRVPAKALWRAQTQRAVENFPISGRGLERTQIRALGLLKGACAQVNSDLGLLAPEKADAIIAAAAEIADGQHDDQFPIDVFQTGSGTSSNMNTNEVIASIAAKGGVTLHPNDDVNMSQSSNDTFPTATHIAATEAAVAHLIPALQQLHDALAAKALDWHTVVKSGRTHLMDAVPVTLGQEFSGYARQIEAGIERVRACLPRLGELAIGGTAVGTGLNAPDDFGVRVVAVLVAQTGLSELRTAANSFEAQAARDGLVEASGALRTIAVSLTKIANDIRWMGSGPLTGLAEIQLPDLQPGSSIMPGKVNPVLPEAVTQVAAQVIGNDAAIAWGGANGAFELNVYIPMMARNILESFKLLTNVSRLFAQRCIAGLTANVEHLRRLAESSPSIVTPLNSAIGYEEAAAVAKQALKERKTIRQTVIDRGLIGDRLSIEDLDRRLDVLAMAKAEQLDSDRL fumD ignore BRENDA::Q13VI0 fumarate hydratase (EC 4.2.1.2) MTEDVRMERDTFGEIAVPNARLWGAQTQRSLQNFRISTEKQSPELITALAVIKRAAAEVNLGLGVLDESKAKAIIEAADEIIAGKHPDEFPLAVWQTGSGTQTNMNLNEVIANRASELLGGERGEARKVHPNDDVNRGQSSNDVFPTAMHVAAAYAIVKHLLPALKTLRDTLDGKAKAFVDIVKIGRTHLQDATPLTLGQEFSGYVAQLDQGIRHVESALPHLYELAQGGTAVGTGLNAHPQFAGKVAAAIGKLTGLPFVSAPNKFEVMAAADALVFAHGALKTVAASLNKIANDIRWLASGPRCGLGELSIPENEPGSSIMPGKVNPTQSEALTMLCAQVFGNDVAVNIGGASGNFELNVFRPMIAHNVLQSVRLLADGAHSFNDNCAVGIEANHERIDTLLNESLMLVTALNPHIGYDKAAKIAKKAHKEGTTLKASALALGFVTEQQFDEWVRPKDMVGHPAA fumD ignore BRENDA::Q5SKT5 fumarate hydratase (EC 4.2.1.2) MEYRIERDTMGEVRVPADKYWGAQTQRSLENFRIGTDRFRMPLEIIRAYGMLKKAAARANLELGELPEEIAKAIIQAAEEVVQGKWDDHFPLVVFQTGSGTQTNMNVNEVIANRASEILGKPLGSKYVHPNDHVNRGQSSNDTFPTAMYVAVALALHQRLYPAVEGLIRTFTAKAQAFDQIVKVGRTHLMDAVPITLGQEIGSWAAQLKTTLAAVKEMEKGLYNLAIGGTAVGTGLNAHPRFGELVAKYLAEETGLPFRVAENRFAALAAHDELVNVMGAIRTLAGALMKIGNDVRWLASGPYAGIGEITIPANEPGSSIMPGKVNPTQVEALTMVVVRVYGNDHTVAFAGSQGNFQLNVYKPVMAYSTLESINLLADAVASFDAHLAQGIEPNLERIEEHLQKNPMLATALNKAIGYDKAAEIVKKALKEKKTLKQAALELGYLTEEEFDRIVVPMRLAKPHEGA fumD ignore BRENDA::Q8NRN8 fumarate hydratase (EC 4.2.1.2) MSDFMTEQEFRIEHDTMGEVKVPAKALWQAQTQRAVENFPISGRGLESAQIRAMGLLKAACAQVNKDSGALDAEKADAIIAAGKEIASGKHDAEFPIDVFQTGSGTSSNMNTNEVIASIAKANGVEVHPNDHVNMGQSSNDTFPTATHVAATEAAVNDLIPGLKVLHESLAKKANEWSEVVKSGRTHLMDAVPVTLGQEFGGYARQIQLGIERVEATLPRLGELAIGGTAAGTGINTSADFGGKVVAELINLTDVKELKEAENHFEAQAARDALVEFSGAMRVIAVSLYKIANDIRLMGSGPLTGLGEIRLPDLQPGSSIMPGKVNPVLCETATQVSAQVIGNDAAVAFSGTQGQFELNVFIPVMARNVLESARLLANTSRVFATRLVDGIEPNEAHMKELAESSPSIVTPLNSAIGYEAAAKVAKTALAEGKTIRQTVIDLGLVDGEKLTEEELDKRLDVLAMAHTERENKF fumD ignore BRENDA::Q8U062 fumarate hydratase (subunit 2/2) (EC 4.2.1.2) MEDIVEALKLAVTNLPEDVALALKNAYEREDYEIAKYNLEIMLRAVKTSKKEKVPLCQDTGTPIFFVETDGTWNVKEIYETIAEAVKRATDEIPLRPNAICLLSGKVVGNVPEIHIEPGKRNRISILIKGGGSENCSALFPLTPGDWFEGVKKKIIDHIRSCGGKPCPPIIVGIGIASPAERAITLAKKSLFRKIGERHEKLGWLEEEILEEINFLDIGPMGLGGKTTALDVKIEVGERHPASFIVGIAIQCWAHRRAFIEEKEDGEVVIWQ fumD ignore BRENDA::Q8U063 fumarate hydratase (subunit 1/2) (EC 4.2.1.2) MAVRLKTPLTWEDIRDLEIGDRVLLSGIVYTARDLAHRRFLEEGFPFNPEGAVIYHCGPLIKNGIVVSAGPTTSARMEKYLDFLFNRGVRGVIGKGGMNHEKFKGRAVYFSYPGGAGSLAREFIVKVRDVYWEDLGMTDAVWELEVRDMPLLVSIDSKGRSLYRKN fumD ignore BRENDA::Q8X999 fumarate hydratase (EC 4.2.1.2) MSKPFIWQEPFLQNKDGTEYTLISDQHITVTELDGEEVIKIAPEALTLLARQAFYEASFFLRSAHLQQVASILNDQQASSNDKYVALQLLRNAEVSAKGVLPNCQDTGTATIVASKGQQIWTGGNDAEALSKGIYSTFQENNLRFSQNAPLDMYTEVNTQTNLPAQIDISAVAGDEYHFLCVNKGGGSANKAALYQETKSLLQPEKLTAFLIEKMKSLGTAACPPYHIAFVVGGLSADQTLKIAKLASTKYYDNLPTSGNEQGQAFRDIELEKVLLEASQQFGIGAQFGGKYFAHDIRVIRLPRHGGSCPIAMALSCSADRNIKAKINKHGIWLEKLEHNPGQYIPASLREENHAQHVQLDLNRPLRDVMQDLARLPVGTRVSLSGPIVVARDIAHAKIKARLDSGEPMPEYLKHHIVYYAGPAKTPENMACGSLGPTTGGRMDGYIDTFQAAGGSLVMLSKGNRSQQVTDACHKHGGFNLGSIGGAAALLAQEYVKSLRCLEYPELGMEAVWMMEVENLPAFILVDDKGNNFFSQFEQQHRCASCPAGH fumD ignore BRENDA::Q9FI53,SwissProt::Q9FI53,metacyc::AT5G50950-MONOMER fumarate hydratase (EC 4.2.1.2);; Fumarate hydratase 2; AtFUM2; Fumarase 2; EC 4.2.1.2;; fumarase (EC 4.2.1.2) MAALTMQFEGEKKNVSEVADVTLKQEDEQQERRSYSTPFREERDTFGPIQVPSDKLWGAQTQRSLQNFEIGGDRERMPEPIVRAFGVLKKCAAKVNMEYGLDPMIGEAIMEAAQEVAEGKLNDHFPLVVWQTGSGTQSNMNANEVIANRAAEILGHKRGEKIVHPNDHVNRSQSSNDTFPTVMHIAAATEITSRLIPSLKNLHSSLESKSFEFKDIVKIGRTHTQDATPLTLGQEFGGYATQVEYGLNRVACTLPRIYQLAQGGTAVGTGLNTKKGFDVKIAAAVAEETNLPFVTAENKFEALAAHDACVETSGSLNTIATSLMKIANDIRFLGSGPRCGLGELSLPENEPGSSIMPGKVNPTQCEALTMVCAQVMGNHVAVTIGGSNGHFELNVFKPVIASALLHSIRLIADASASFEKNCVRGIEANRERISKLLHESLMLVTSLNPKIGYDNAAAVAKRAHKEGCTLKHAAMKLGVLTSEEFDTLVVPEKMIGPSD fumD ignore BRENDA::Q9ZCQ4,SwissProt::Q9ZCQ4 fumarate hydratase (EC 4.2.1.2);; Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2 MKNYRIESDSFGEIQIEEKFYWGAQTQRSLNNFKISKQKMPKILIRALAILKKCAAQVNYEFGDLEYKIATSIDKAIDRILAGEFEDNFPLVVWQTGSGTQTNMNMNEVIASIANEELTGKKGGKFPVHPNDHVNKGQSSNDSFPTAMHIATVLATKQQLIPALNNLLTYLQDKSKDWDKIIKIGRTHLQDATPLTLKQEFSGYITQIEYALERIEDALKKVYLLAQGGTAVGTGINSKIGFDIKFAQKVAEFTQQPFKTAPNKFESLAAHDALVEFSGTLNTIAVSLMKIANDIRLLGSGPRCGLGELHLPENEPGSSIMPGKVNPTQVEALTMVCTQVMGNHVTVTIAGSNGHLELNVFKPVIIYNILQSIELLSDSVNSFVTHCVKGLEPNIARINTLRDKSLMLVTVLNPHIGYDNAAKIAKEAHKYGITLKEAAKKLNFLSEEEFDKIVVPEKMIS fumD ignore SwissProt::E9AE57 Fumarate hydratase 2; Fumarase 2; LmFH-2; EC 4.2.1.2 MSLCDQCEIGCRRVGIKDIEDASAVNADFHFSAIFQPTDPHHHQTEFAKVEGSEKYVEEVEVFGRQALKVNPEALTILAHRAFSDVHHFFRKDHLEGWRRAIEDPEASDNDRYVATTLLKNACIAAGRVLPSCQDTGTAIVLGKRGELCWTGGEDEKYLSKGIWNAYRYHNLRYSQTAALDMFKECNTGDNLPAQLDLLAVPGSDYEFLFIAKGGGSANKAYLYQETKALLNPKSLRAFIEEKLKTLGTAACPPYHIALVIGGTSAEMTMKTVKLASCRYYDSLPTTGDKYGRAFRDPEWEKIVMEVAQKSGIGAQFGGKYFAHQARVIRLPRHGASCPVGLAVSCSADRQILAHINKSGIYIEQLEQNPAQYLPDIPEVHLSTTSVKVDLKRPIDKVRQQLSQYPVGTRVMLNGTLIVARDIAHAKIKEMMDNGEPLPEYMKTSPIYYAGPAKTPEGYASGSFGPTTAGRMDSYVDLFQSHGGSYITLAKGNRSKQVTDACKKHGGFYLGSIGGPAAILAKDSIKQVTCLAFPELGMEAVWKIEVEDFPAFIVVDDKGNDMYSKTLA fumD ignore SwissProt::P0ACX5,ecocyc::G6903-MONOMER,metacyc::G6903-MONOMER Fumarase D; EC 4.2.1.2;; fumarase D (EC 4.2.1.2);; fumarase D (EC 4.2.1.2) MGNRTKEDELYREMCRVVGKVVLEMRDLGQEPKHIVIAGVLRTALANKRIQRSELEKQAMETVINALVK fumD ignore SwissProt::P10173 Fumarate hydratase, mitochondrial; Fumarase; EC 4.2.1.2 MDRALRLLARSRCLSRVPASAPGPGPGSSPSGVSRLLLRPPNAARMASQNSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPIPVIKAFGILKRAAAEVNQDYGLDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHEALLPGLQKLHDALDAKSREFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAITRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEALTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDAAVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKATAVELGYLTAEQFDEWVKPKDMLGPK fumD ignore SwissProt::P11663,ecocyc::EG11162-MONOMER,metacyc::EG11162-MONOMER Fumarase E; EC 4.2.1.2;; fumarase E (EC 4.2.1.2);; fumarase E (EC 4.2.1.2) MATLTEDDVLEQLDAQDNLFSFMKTAHTILLQGIRQFLPSLFVDNDEEIVEYAVKPLLAQSGPLDDIDVALRLIYALGKMDKWLYADITHFSQFWHYLNEQDETPGFADDMTWDFISNVNSITRNAMLYDALKAMKFADFSVWSEARFSGMVKTALTLAVTTTLKELTP fumD ignore SwissProt::P39461,BRENDA::P39461 Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2;; fumarate hydratase (EC 4.2.1.2) MKYTDTAPKLFMNTGTKFPRRIIWSMGVLKKSCAKVNADLGLLDKKIADSIIKASDDLIDGKLDDKIVLDVFQTGSGTGLNMNVNEVIAEVASSYSNLKVHPNDHVNFGQSSNDTVPTAIRIAAVAEVTNRLLPALQQIISSLNKKAEEYKDVIKAGRTHLRDALPVTLGQELSAYADAFQHEHEQVMNILEYVKELPIGGTATGTGLNSHPEFQERVINEINRITGLGFKPANRFRAMRLLTDLLLLSGALRNIAVDLYRLGQDIRLMFSGPLTGLNEIDLPTQEEIAGSSIMPGKTNPVTVEATLLISAQVVGLDHANQFASMLGEFELSMGIPLVGYNIVTQVNFISEALEKMSRLVIDGMVANVEKMKRYAESSPSLITIVSPVIGYDKATEIGKKLNKGMSIREALRELGYSDNEINKILDLSKLVKPGFTAK fumD ignore SwissProt::P97807 Fumarate hydratase, mitochondrial; Fumarase; EF-3; EC 4.2.1.2 MYRALRLLARSRRLLRVPSAGAAVSGEATTLPRCAPNVARMASQNSFRVEFDTFGELKVPTDKYYGAQTVRSTMNFKIGGATERMPIPVIQAFGILKRAAAEVNQEYGLDPKIASAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK fumD ignore SwissProt::Q4QAU9 Fumarate hydratase 1, mitochondrial; Fumarase 1; LmFH-1; EC 4.2.1.2 MLRRLAPLLAEFNFVPLVSKVSHKETKYRLLTKDYVSVVQPGAGLPEMLRVDPAALTLLSSTAFDDVEHLLRSSHLMSLRKIFDDPEASDNDKFVALQLLKNANISSARLLPGCQDTGTAIIAGYRGDQVFVPGNDEEALSRGVYDIFQKRNFRYSQNVPLSMYDEKNTGTNLPAQIDLYASKGMEYSFMFVAKGGGSANKSFLLQETKSVLNPKSLRNFLKEKLAMFGTSACPPYHVAVVIGGTSAEMTMKVLKYASCHYYDDLITKPDMKTGYTFRDLELEEEVLKVCQNIGMGAQFGGKYYAHDVRVIRMPRHGASCPIGIGVSCSADRQALGKINKDGVWLEELEMEPSQYLPDLKEDELLKTPAVMVNLNRPMPEVLQELSKHPVRTRLSLTGTIIVARDSAHARMREMLEAGKPLPQYMKEHPVYYAGPAKQPDGLPSGSFGPTTAGRMDPFVDLFQSHGGSMVMLAKGNRSKQVTKACHKYGGFYLGSIGGPAAVLAQNAIKKVECLDMKDLGMEAVWRIEVENFPAFIVVDDKGNDFFEQL fumD ignore SwissProt::Q83Q96 Fumarase E; EC 4.2.1.2 MATLTEDDVLEQLDAQDNLFSFMKTAHSILLQGIRQFLPSLFVDNDEEIVEYAVKPLLAQSGPLDDIDVALRLIYALGKMDKWLYADITHFSQYWHYLNEQDETPGFADDITWDFISNVNSITRNATLYDALKAMKFADFAVWSEARFSGMVKTALTLAVTTTLKELTP fumD ignore SwissProt::Q92PB6 Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2 MTSTRTETDTFGPIEVASDRYWGAQAQRSLGNFKIGWEKQPLAIVRALGIVKQAAARANMALGRLDPAIGDAIVKAAQEVIDGKLDEHFPLVVWQTGSGTQSNMNANEVVSNRAIELLGGVMGSKKPVHPNDHVNMSQSSNDTYPTAMHIACAERVIHDLLPALKHLHKALEEKVKAFDHIIKIGRTHTQDATPLTLGQEFSGYAAQVASSIKRIEMTLPGLCELAQGGTAVGTGLNAPVGFAEKVAEEIAAITGIGFTSAPNKFEALAAHDSMVFSHGAINATAAALFKIANDIRFLGSGPRSGLGELSLPENEPGSSIMPGKVNPTQCEALTQVCVQVFGNHAALTFAGSQGHFELNVYNPLMAYNFLQSVQLLADAAISFTDNCVVGIEAREDNIKAALDRSLMLVTALAPKIGYDNAAKIAKTAHKNGTTLREEAVGGGYVTDEEFDAVVRPETMIGPA fumD ignore metacyc::HP1325-MONOMER fumarase (EC 4.2.1.2) MQFRIEHDTMGEIKVNDSQYWGAQTQRSLENFKIGTEKMPKELIGAFAKLKRSLAVVNHKLGKLSLEKSQAIIKACDCILKGELCGEFPLAIWQTGSGTQTNMNLNEVIANKATEILGGNFREKKLIHPNDDVNMSQSSNDTFPTAMHIVSVLEITHRLLPSLENLLKTFKEKSQQFKEIVKIGRTHLQDATPLTLGQEFSGYASMLEHSKQQILESLEHLRELAIGGTAVGTGLNAHKELSEKVAEELSQFSGVKFVSAPNKFHALTSHDAIAYAHGAFKALAANLMKIANDIRWLASGPRCGLGELNIPENEPGSSIMPGKVNPTQCEAMTMVAVQVMGNDTAIGIAASQGNFELNVFKPVIIYNFLQSLRLLSDSMESFNIHCASGIEPNREKIDYYLHHSLMLVTALNPHVGYENAAKIAKNAHKKGISLKESALELKLLSAEDFDKFVVPEKMIGPKA gdhA uniprot G8AE86 RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896}; EC=1.4.1.2 {ECO:0000256|ARBA:ARBA00012896}; MALRAEQLKDELTEEVVRQVRERLGRSRAAPAERFVRQFYDNVPPDDIIQAPAEQLYGAALAMWQWGQQREATDRAKVRVYNPRVEEHGWQSHRTVVEIVNDDMPFLVDSVTAELNRQGLTVHLVIHPVVRVKRDADGQLAELYEPAAAPTDAAPESFMHVEVGAVTGAAALDQAREGLERVLADVRAAVADWRAMRQQVRAAIVEADCARAAVPAIIPDDEVDEAKAFLSWADDDHFTFLGYREYRFESGADGADSSLGLVAGSGLGILRDDSVTVFDGLRNYATLPPDVRDFLRNPRVLMVTKGNRPSPVHRAVPMDAFLIKRFDAEGRIIGERLVAGLFTSVAYNRSPREIPYLRRKVAEVMELAGFDPQGHDGKALLHILETYPRDELFQIQVPELLDIAVGILHLQERQRLALFVRKDPFERFASCLVYVPRDRYDTTLRRRIQSILEAAYDGTCTGFTTQLTESVLARLHFIIRTEPGRVPTVDATDLEARLVQASRGWDDHLRDALVEAHGEEQGRTLFRRYADAFPTAYREEFNAEAAVFDIERIEKATAQGTLGINLYRPLEAEGDELHVKIYHEGRPVPLSDVLPMLEHMDLKVITEAPFEIAIAGHAAPVWIHDFTARSQNGLPIDCAMVKEKFQDAFAAVWDGRMEDDGFNRLVLRAGLTAREVTVLRAYAKYLRQARIPYGQDVVESTLAGHPAIARKLVALFHSRFDPARRSQNDPGLAAEIERALDGVKNLDEDRILRRFLNLLCNTLRTNAYQNGADGRPKTYLSFKIDSRNIDDLPLPRPMVEVFVYSPRMEGVHLRGGKVARGGIRWSDRREDFRTEILGLMKAQMVKNTVIVPVGSKGGFVVKRPPPPSAGREAQLAEGIECYKTLMRGLLDITDNLDAQGAVVPPPEVVRHDGDDPYLVVAADKGTATFSDIANSVSVDHGFWLGDAFASGGSAGYDHKKMGITARGAWESVKRHFRELGHDTQTQDFTVVGVGDMSGDVFGNGMLLSKHIRLLAAFDHRHIFIDPDPDAARSWEERQRLFDLPRSSWADYDASLLSAGGRVFDRSAKSLELTPEIRQRFGIAKDHVTPLELMQTLLKAEVDLLWFGGIGTYLKAAEETNAEVGDKANDALRIDGRDVRAKVIGEGANLGVTQRGRIEAAQHGVRLNTDAIDNSAGVDTSDHEVNIKILLNDVVVRGDMTLKQRDQLLAAMTDEVAGLVLADNYLQSQALTVARAQGPDALEAQARLIRSLEKAGRLNRAIEYLPDEEELSARMANREGLTRPELAVLLAYAKITLYDDLLASDLPDDPFMADDLTRYFPKPLRKAHAEAVGRHRLRREIIATSVTNSLVNRTGPTFVKEMMEKTGMGPADVARAYTIVRDAFGLRSLWTGIEDLDTVVPAALQTSMILETVRHMERAAAWFLASCQQPLDIARETEAFRPGIETLLAGLDNVLDAEETARLTARVASYQEQGVPAELARRMAALPVLAAAPDLVRIAGRTGRGVADVAAVYFMLGRRFGLEWLRDKAAAAKAENHWQKQAVAALVDDLFAHQTALTTRVLEAVDQLPAEAPVEAWIAHRRPVVERVEQLLSELRTQPNVDLSMLAVANRQLRGLTAG gdhA curated BRENDA::A0A0H3C571 glutamate dehydrogenase (EC 1.4.1.2) MSGVKIDPSNSLTAAYALTRGKTVQELALEERDFLAQVGADWAIEDAPVLSAKAAAASLAEFFDFARTLKGDQPTVRLRSAGEAGAARDLLEIVQPDRPFLVDSVMGEITESGFRVRAMFHPVVEIDGIARSFIQVHLDPVGEDRVESLLEQIRETLFDVRRAVGDFKAMRDLMHRAVAELAATPGVTSEEGRQEDLAFLRWLEDDNFVFLGARVYEYPRSSDGGYAAEEPLYEAEASLGVLRDSSRSVLRRAYEPAILSKQLQRQLETGAPVVVAKSNLRSRVHRRGFMDYVGVRRYGDDGKPSGEVRFVGLFTAEAYETPAVEVPLIRHRVARIMRRAAKAPGSHNEKRLRNILETWPRDELFQTSEDTLLSMALGVLHLIDRPRVRLFARLDPFDRFASVLVYIPRERFDTEVCARAGAILADAYDGKVLEYYPEISDAPLARAHFIIEVTPGDHPDPDLSQVEARIADTALTWEDRFEAVVRAGGAPTGGVRTLLDKYGYAFPPGYRDQYDALEALADIDIIETLTEGALPRVRAFRRFEDGPRTFRFKLYLRGAAAPLAEVLPILERMGLKALIEDGFRLSIHEKDGPHSVWVHEFVLDDPAGEHIVFDEVRQVFEEAFIAIWTGATENDGFNRIVLEMAVGWREAALLRALARYRQQSGLDPSQQVQEAALRDHPMVARLILDLFRVKFDPAIRADLRTRREQAEAVQFSIVEALQAVESLDADRVLRRLAALVGAIQRTNFYQLGADGEPKSYISFKIASRELEDLPAPKPYREIYVSAPHVEGVHLRFGPVARGGLRWSDRRDDFRTEVLGLVKAQQVKNAVIVPVGSKGGFYPKQLPRGGDRDAIQAEAIRAYKTFLSGLLDLTDNIDSDNQVVPPPSVIAHDAQDPYLVVAADKGTATFSDIANGVAESYGFWLGDAFASGGSVGYDHKVMGITARGAWEAVKRHFRELGKDIQTEAFTVVGVGDMSGDVFGNGMLLSKQTKLLAAFDHRHIFLDPNPDPAVSWAERDRMFKLPRSSWEDYDKSKISAGGGVFARSLKSIPLSAEVRAMLEIKAEAVSPAELMTAILKSKAELLYLGGIGTYVKAKGETNADAGDKANDAIRINGSDLRVKVVGEGANLGLTQAGRIEFAQAGGHINTDAIDNSAGVDSSDHEVNIKILTGILERGGQLDRESRNTLLASMTDDVAHHVLEHNYDQTLALTLLESDAVSEVDAQIRYMVNLEQRGRLDRRVEGLPTNTTLLERKAAGRGLTRPELAVLLAYGKLDLFDEIVASQSPDDPWFERTLRGYFPRALDQYADAMQKHRLKREIIATVVGNQMVNMCGPTFVSRLKAAAGADVNAVVVGFTAAREILGIDGLWDQVNGLDNKASAEGQTALYKALAYALRSLTFWLARRAQRDAANVQTLVEAYGPSVAALKALAPAILSPFEQKAVSKRVKAYVADGAPEALALSVAALQPLTTAADLVDLANASSWSVENVARLYHQVGAAFGFDRLRGAAGSFVGGDAFERLAVRRLIEDMLTEQTSITQQVLKFAANAQAGEDEAAAKAAISSWAALRGDRPRAVKRTIEDIEQAGGGWTFAKLTIANAALRELSSAA gdhA curated BRENDA::A0R1C2,SwissProt::A0R1C2 glutamate dehydrogenase (EC 1.4.1.2);; NAD-specific glutamate dehydrogenase; NAD-GDH; NAD(+)-dependent glutamate dehydrogenase; EC 1.4.1.2 MIRRLSVAFLSTYRGPQADAPGVTSTGPLAVAAHDDLVSDDLVAAHYRLASMRAPGETKAAVYPGDAGSGAALQIVTDQAPMLVDSVTVLLHRHGIAYTAIMNPVFRVRRGLDGELLDVRPAAEAAPGDGADECWILVPITAAADGEALTEATRLVPGILAEARQIGLDSGAMIAALHGLANDLATDLEGHFPNAERKEVAALLRWLADGHFVLLGYQQCVVGDGNAEVDPASRLGVLRLRNDVLPPLTDSDDLLVLAQATMPSYLRYGAYPYIVVVRESPGASRVIEHRFVGLFTVAAMNANALEIPLISRRVEEALAMAHRDPSHPGQLLRDIIQTIPRPELFALSSKQLLEMALAVVDLGSRRRTLLFLRADHLAHFVSCLVYLPRDRYTTAVRLEMQDILVRELGGAGIDYSARVSESPWAVVHFTVRLPEGTAADSVDTSLENESRIQDLLTEATRNWGDRMISAAAAASISPAALEHYAHAFPEDYKQAFAPQDAIADISLIEALQDDSVKLVLADTAEDRVWKLTWYLGGHSASLSELLPMLQSMGVVVLEERPFTLRRTDGLPVWIYQFKISPHPSIPHAPDAEAQRDTAQRFADAVTAIWHGRVEIDRFNELVMRAGLTWQQVVVLRAYAKYLRQAGFPYSQSHIESVLNENPHTTRSLIDLFEALFDPSQETDGRRDAQGAAAAVAADIDALVSLDTDRVLRAFANLIEATLRTNYFVARPDSARARNVLAFKLNPLVIKELPLPRPKFEIFVYSPRVEGVHLRFGFVARGGLRWSDRREDFRTEILGLVKAQAVKNAVIVPVGAKGGFVVKRPPTLTGDAAADREATRAEGVECYRLFISGLLDVTDNVDKATGAVVTPPEVVRRDGEDAYLVVAADKGTATFSDIANEVAKSYGFWLGDAFASGGSIGYDHKAMGITAKGAWESVKRHFREMGVDTQTQDFTVVGIGDMSGDVFGNGMLLSKHIRLVAAFDHRDIFLDPNPDAGRSWDERKRLFDLPRSSWADYDKSLISEGGGVYSRQQKSIPISPQVRTALGLDADVEELTPPALIKAILKAPVDLLWNGGIGTYIKAETEADADVGDRANDQIRVCGNQVRAKVIGEGGNLGVTALGRIEFDLAGGRINTDALDNSAGVDCSDHEVNIKILIDSAVTAGKVTPEERTELLLSMTDEVGELVLADNRDQNDLMGTSRANAASLLSVHARMIKDLVDNRGLNRELEALPSEKEIRRRADAGIGLTSPELATLMAHVKLALKDDVLASDLPDQEVFASRLPYYFPTRLREELHGEIRSHQLRREIITTMLVNDLVDTAGISYAYRITEDVGVGPVDAVRSYVAINAIFGIGDVWRRIRAAGDAGVPTSVTDRMTLDLRRLVDRAGRWLLNYRPQPLAVGAEINRFGAKVAALTPRMSEWLRGDDKAIVSKEAGDFASHGVPEDLAYHIATGLYQYSLLDVIDIADIVDREPDEVADTYFALMDHLGADALLTAVSRLSRDDRWHSLARLAIRDDIYGSLRALCFDVLAVGEPDENGEEKIAEWETTNSSRVTRARRTLTEIYKDGEQDLATLSVAARQIRSMTRTSGTGTTG gdhA curated BRENDA::A3MUY9,SwissProt::A3MUY9 glutamate dehydrogenase (EC 1.4.1.2);; NAD(+)-dependent glutamate dehydrogenase; NAD-GDH; NAD-specific glutamate dehydrogenase; EC 1.4.1.2 MSTTYIVSDFLINTLLTIKRGVELAGLPPEFYEALEKPKRILVVNIPVKMDDGKIKYFEGYRVQHNDALGPFKGGIRFHPEVTLADDIALAMLMTLKNSLAGLPYGGAKGAVRVDPRRLSRRELEELARGYARAVAPLIGEQLDIPAPDVGTDSQVMAWMVDEYSRLVGRNAPAVFTSKPPELWGNPVREYSTGFGVAVAAREVAKRLWGGIVGKTAAVQGLGNVGRWAAYWLEKMGAKVVAVSDVNGVVYRERGLDVDLIRETKAKGPQLLEMISQKNGVEIVKNPDQIFSLDVDILVPAAIENVVREDNVDGVRARLVVEGANGPTTPGAERRLYERGVVVVPDILANAGGVIMSYLEWVENLQWLFWDEEETRRRLEAIMSNNVARVYARWEKEKSWTMRDAAVVTALERIYNAMKTRGWI gdhA curated BRENDA::P00366,SwissProt::P00366 glutamate dehydrogenase (EC 1.4.1.2);; Glutamate dehydrogenase 1, mitochondrial; GDH 1; EC 1.4.1.3 MYRYLGEALLLSRAGPAALGSASADSAALLGWARGQPAAAPQPGLVPPARRHYSEAAADREDDPNFFKMVEGFFDRGASIVEDKLVEDLKTRETEEQKRNRVRSILRIIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGVDVPAPDMSTGEREMSWIADTYASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFGDKTFVVQGFGNVGLHSMRYLHRFGAKCITVGESDGSIWNPDGIDPKELEDFKLQHGTILGFPKAKIYEGSILEVDCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNIMVIPDLYLNAGGVTVSYFEWLNNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGKHGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYVNAIEKVFRVYNEAGVTFT gdhA curated BRENDA::P24295,SwissProt::P24295 glutamate dehydrogenase (EC 1.4.1.2);; NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 MSKYVDRVIAEVEKKYADEPEFVQTVEEVLSSLGPVVDAHPEYEEVALLERMVIPERVIEFRVPWEDDNGKVHVNTGYRVQFNGAIGPYKGGLRFAPSVNLSIMKFLGFEQAFKDSLTTLPMGGAKGGSDFDPNGKSDREVMRFCQAFMTELYRHIGPDIDVPAGDLGVGAREIGYMYGQYRKIVGGFYNGVLTGKARSFGGSLVRPEATGYGSVYYVEAVMKHENDTLVGKTVALAGFGNVAWGAAKKLAELGAKAVTLSGPDGYIYDPEGITTEEKINYMLEMRASGRNKVQDYADKFGVQFFPGEKPWGQKVDIIMPCATQNDVDLEQAKKIVANNVKYYIEVANMPTTNEALRFLMQQPNMVVAPSKAVNAGGVLVSGFEMSQNSERLSWTAEEVDSKLHQVMTDIHDGSAAAAERYGLGYNLVAGANIVGFQKIADAMMAQGIAW gdhA curated BRENDA::P27346,CharProtDB::CH_015452 glutamate dehydrogenase (EC 1.4.1.2);; NAD-specific glutamate dehydrogenase; EC 1.4.1.2 MSGKDVNVFEMAQSQVKNACDKLGMEPAVYELLKEPMRVIEVSIPVKMDDGSIKTFKGFRSQHNDAVGPTKGGIRFHQNVSRDEVKALSIWMTFKCSVTGIPYGGGKGGIIVDPSTLSQGELERLSRGYIDGIYKLIGEKVDVPAPDVNTNGQIMSWMVDEYNKLTGQSSIGVITGKPVEFGGSLGRTAATGFGVAVTAREAAAKLGIDMKKAKIAVQGIGNVGSYTVLNCEKLGGTVVAMAEWCKSEGSYAIYNENGLDGQAMLDYMKEHGNLLNFPGAKRISLEEFWASDVDIVIPAALENSITKEVAESIKAKLVCEAANGPTTPEADEVFAERGIVLTPDILTNAGGVTVSYFEWVQNLYGYYWSEEEVEQKEEIAMVKAFESIWKIKEEYNVTMREAAYMHSIKKVAEAMKLRGWY gdhA curated BRENDA::P33327,SwissProt::P33327 glutamate dehydrogenase (EC 1.4.1.2);; NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 MLFDNKNRGALNSLNTPDIASLSISSMSDYHVFDFPGKDLQREEVIDLLDQQGFIPDDLIEQEVDWFYNSLGIDDLFFSRESPQLISNIIHSLYASKLDFFAKSKFNGIQPRLFSIKNKIITNDNHAIFMESNTGVSISDSQQKNFKFASDAVGNDTLEHGKDTIKKNRIEMDDSCPPYELDSEIDDLFLDNKSQKNCRLVSFWAPESELKLTFVYESVYPNDDPAGVDISSQDLLKGDIESISDKTMYKVSSNENKKLYGLLLKLVKEREGPVIKTTRSVENKDEIRLLVAYKRFTTKRYYSALNSLFHYYKLKPSKFYLESFNVKDDDIIIFSVYLNENQQLEDVLLHDVEAALKQVEREASLLYAIPNNSFHEVYQRRQFSPKEAIYAHIGAIFINHFVNRLGSDYQNLLSQITIKRNDTTLLEIVENLKRKLRNETLTQQTIINIMSKHYTIISKLYKNFAQIHYYHNSTKDMEKTLSFQRLEKVEPFKNDQEFEAYLNKFIPNDSPDLLILKTLNIFNKSILKTNFFITRKVAISFRLDPSLVMTKFEYPETPYGIFFVVGNTFKGFHIRFRDIARGGIRIVCSRNQDIYDLNSKNVIDENYQLASTQQRKNKDIPEGGSKGVILLNPGLVEHDQTFVAFSQYVDAMIDILINDPLKENYVNLLPKEEILFFGPDEGTAGFVDWATNHARVRNCPWWKSFLTGKSPSLGGIPHDEYGMTSLGVRAYVNKIYETLNLTNSTVYKFQTGGPDGDLGSNEILLSSPNECYLAILDGSGVLCDPKGLDKDELCRLAHERKMISDFDTSKLSNNGFFVSVDAMDIMLPNGTIVANGTTFRNTFHTQIFKFVDHVDIFVPCGGRPNSITLNNLHYFVDEKTGKCKIPYIVEGANLFITQPAKNALEEHGCILFKDASANKGGVTSSSMEVLASLALNDNDFVHKFIGDVSGERSALYKSYVVEVQSRIQKNAELEFGQLWNLNQLNGTHISEISNQLSFTINKLNDDLVASQELWLNDLKLRNYLLLDKIIPKILIDVAGPQSVLENIPESYLKVLLSSYLSSTFVYQNGIDVNIGKFLEFIGGLKREAEASA gdhA curated BRENDA::Q0E5H9 glutamate dehydrogenase (EC 1.4.1.2) MQKQQTIIEESLKALMEDESFLPDLQAQTREQAFKSLVALLSTPNHIHKSFLRVTLDDNTIVRIPAFRVQHSDTVGPYKGGVRFHESVNEGEVSNLAKLMTLKNALHELPFGGGKGGVVIKPKEYNIKELNLICKKYVQYFDDILGPDKDIPAPDVGTGEREMDWMMGEFKNIHPGEPYRNSFTGKSVVNGGSLGRREATGKGVYFTFRYMMHNFLNENRKWLSDTDNIFANTALNHHDQKLSMAIQGFGNLGSVAALEAYQCDYLQNKIVAVSDHNVMLYNNDGLDVPALIKFTEESDGDLPTTEEELEEHEIKAEIRERDELLEMDCDVLLLAALEDQIHEDNMERIQASMIIEGANGPITEDADRYLADKGVLIVPDILANAGGVIVSYYEWIQGREAQFMTEDQVFERLFDKMKYTMDTILPQFFGDPFPLRQNCYIHSVMKLSTIMYRQGKLY gdhA curated BRENDA::Q0E5I0 glutamate dehydrogenase (EC 1.4.1.2) MVADKPTDAANENNDKLDVLKSTQTVVKKALDKLGYPNEVYELLKEPVRMMTVRIPVRMDNDHIKIFTGYRSQHNDAVGPTKGGVRFHPNVSEKEVKALSIWMSLKAGIVDLPYGGGKGGIVCDPREMSFRELEGVSRGYVRAISQIVGPTKDIPAPDVFTNSQIMAWMMDEYSRIDEFNNPGFITGKPLVLGGSHGRETATAKGVTICIEEAAKKKGISVEGARVVVQGFGNAGSFLAKFMHDRGAKVIGISDAYGGLHDPDGLDIDYLLDRRDSFGTVTNLFKNTISNEELLELDCDILVPAAIENQIREENAHNIKASIVVEAANGPTTLDATRILSERGILLVPDVLASSGGVTVSYFEWVQNNQGYYWTEEEVEEKLHKVIVKGFDNVYKTAETRRVDMRLAAYMVGVRKMAEASRFRGWI gdhA curated BRENDA::Q38946,SwissProt::Q38946,metacyc::AT5G07440-MONOMER glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3);; Glutamate dehydrogenase 2; GDH 2; EC 1.4.1.3;; glutamate dehydrogenase β subunit (EC 1.4.1.2) MNALAATNRNFRHASRILGLDSKIERSLMIPFREIKVECTIPKDDGTLVSYIGFRVQHDNARGPMKGGIRYHPEVDPDEVNALAQLMTWKTAVADIPYGGAKGGIGCSPRDLSLSELERLTRVFTQKIHDLIGIHTDVPAPDMGTNAQTMAWILDEYSKFHGHSPAVVTGKPIDLGGSLGREAATGRGVVFATEALLAEYGKSIQGLTFVIQGFGNVGTWAAKLIHEKGGKVVAVSDITGAIRNPEGIDINALIKHKDATGSLNDFNGGDAMNSDELLIHECDVLIPCALGGVLNKENAGDVKAKFIVEAANHPTDPDADEILSKKGVIILPDIYANAGGVTVSYFEWVQNIQGFMWEEEKVNLELQKYMTRAFHNIKTMCHTHSCNLRMGAFTLGVNRVARATQLRGWEA gdhA curated BRENDA::Q5QDM6 glutamate dehydrogenase (EC 1.4.1.2) MNALAATNRNFKLASRLLRLDSKLEKSLLIPFREIKVECSIPKDDGTLATYVGFRIQHDNARGPMKGGIRYHPEVNTDEVNALAQLMTWKTAVANIPYGGAKGGIGCDPAELSNSELERLTRVFTQKIHDLIGVQIDVPAPDMGTGPQTMAWILDEYSKFHGHSPAVVTGKPIELGGSLGRDAATGRGVLFATETLLNEHGKSISGQRFVIQGFGNVGSWAAQLISEKGGIVVAVSDITGAIKNSKGLDIPSLIKHSKEHKGVKGFHGGDPIDPKSIFSEDCDVLVPAALGGVINRENANDIKAKFIVEAANHPTDPEADEILKKKGVVILPDIFANSGGVTVSYFEWVQNIQGFMWDEEKVNNELKRYMTKGFKDVKEMCKTHDCDLRMGAFTLAVNRVARATVLRGWEA gdhA curated BRENDA::Q8CJY0 glutamate dehydrogenase (EC 1.4.1.2) MQTKLDEAKAELLERAARVAENSPVGGHLPTGTTGEGTPGTPDGPDGAPDYASVFAFLQRYYRHTAPEDLADRDPVDIFGAAVSHYRLAENRPQGTANVRVHTPTVEENGWTCSHSVVEVVTDDMPFLVDSVTNELTRQGRGIHVVVHPQIVVRRDIAGKLVEVLAGPPAADLPHDAHVESWIHVEIDRETDRGDLKQITADLLRVLNDVRETVEDWGKMRDAAVRIADQLSTEATPEDLPARELEEARELLRWLADDHFTFLGYREYQLREDDSLAAVAGTGLGILRSDPHHAADESHPVSPSFERLPADARAKAREHRLLVLTKANSRATVHRPSYLDYVGVKKFDENGNVVGERRFLGLFSSAAYTESVRRVPVVRRKVEEVLERAGFSPNSHDGRDLLQILETYPRDEMFQTSVEELEPIVTSVLYLQERRRLRLYLRQDEYGRYYSALVYLPRDRYTTGVRLRIIDILKEELGGTSVDFTAWNTESILSRLHFVVRVPQGTELPHLSDADKERVEARLVEAARSWADGFGEALTAEFGEERAAELLRLYGSAFPEGYKADHGPRSAVADLGHLEQLDEETTFALSLYEPVGAAPEERRFKIYQKGGSVSLSAVLPVLSRLGVEVTDERPYELRCADRTTAWIYDFGLRMPKAPSGGADYLGDDARERVQDAFAATWTGKAENDGFNALVLSAGLTWREAMVLRAYAKYLRQAGSTFSQDYMEDTLRNNVHTTRLLINLFEARMAPERQRAGREIVDALLEEVDAALDQVASLDEDRILRSFLTVIKATLRTNFFQEASGGVPHDYVSMKFDPQAIPDLPAPRPAFEIWVYSPRVEGVHLRFGKVARGGLRWSDRREDFRTEILGLVKAQMVKNTVIVPVGAKGGFVAKQLPDPGVDRDAWLAEGIASYKTFISALLDITDNMVAGEVVHPADVVRHDEDDTYLVVAADKGTAKFSDIANEVAESYNFWLGDAFASGGSAGYDHKGMGITARGAWESVKRHFRELGVDTQTQDFTVVGIGDMSGDVFGNGMLLSEHIRLVAAFDHRHIFIDPTPDAATSYAERRRLFELPRSSWEDYNTELLSAGGGIFPRTAKSIPVNAHVREALGIEPGVTKMTPAELMKAILSSPVDLLWNGGIGTYVKASTESNADVGDKGNDAIRVDGKDLRVQVVGEGGNLGLTQLGRIEFALQGGRINTDAIDNSAGVDTSDHEVNIKILLNGLVKDGDMTVKQRNKLLAQMTDEVGALVLRNNYAQNTAIANALAQSRDMLHAQQRFMRHLVREGHLNRALEFLPTDRQIRERLSSGHGLTGPETAVLLAYTKITVAEELLHTSLPDDPYLKGLLHAYFPTALREQFAEQVDGHPLRREITTTVLVNDTVNTGGTTYLHRMREETGASLEEIVRAQTVARAIFRSSPVWDAVEELDTKADAAVQTRIRLHSRRLVERGTRWLLNNRPQPLELAETVDFFAERVEQVWSQLPKLLRGADAEWYQHIYDELTGAGVPDEPATLVAGFSSVFAALDIVSVADRMGKEPLDVAEVYYDLADRLGVTQLMDRISDLPRDDRWQSMARAAIREDLYAAHAALTADVLAVGNGSSTPEQRFKAWEEKNAAILGRARTTLEEIRQSDAFDLSNLSVAMRTMRTLLRTHS gdhA curated BRENDA::Q977U6 glutamate dehydrogenase (EC 1.4.1.2) MQTSEPEGSSPNTAEAASQSSEPKPASESALETARRQLYRAADHLDIDPNVVERLKHPEAVHEVTVPIERDDGSVSVYTGYRAQHDSVRGPYKGGLRYHPGVTRDECVGLRMWMTWKTEVRRDGPIFGGAKGGIAVNPKDLTLDEKERLTRRFTQEIRTIIGPMKDIPAPDMGTDPQTMAWVMDAYSMQEGETVPGVVTGKPPIVGGSEGRDTAPGRSVAIIAREAIDYLSWDIEDTTVAVQGFGSVGAPAARLLDDYGANVVAVSDVNGAIYDPDGLDTHAIPTHEEEPEAVMTHDAPETFSNEELLELDVDVLIPAAVGNVLTAENADDVQANLIVEGANGPTTSAADANFAERGVPVIPDILANAGGVTVSYFEWLQDINRRTWSLERVHDELETEMLNAWSVVRDEYESRDVPWRDAAYIVALSRIAAAHDARGLWP gdhA curated BRENDA::Q9TVN3 glutamate dehydrogenase (EC 1.4.1.2) MKDLEARNPAQPEFIQASREVIESIIDVVNSNPKYLENKILERITEPNLIHEFKVEWENDKHEIMVNKGYRIQFNNAIGPYKGGLRFHRAVTLGTLKFLGFEQIFKNSLTGLPMGGGKGGSDFDPRGKSDAEILRFCRSFMTSLFKYIGPEIDVPAGDIGVGGREIGYLFGQYKRLTQQHEGVLTGKGLNWGGSLVRPEATGFGTMYFANEVLHAHGDDIKGKTIAISGFGNVAFGAVLKAKQLGAKVVTISGPDGYIYDENGINTDEKINYMLELRASNNDVVAPFAEKFGAKFIPGKKPWEVPVDMAFPCAIQNELNAEDAATLHKNGVKYVIETSNMGCTADAVQYFIKNRIVFAPGKAANAGGVAVSGLEMSQNSMKLNWTAEEVDAKLKNIMTNIHASCVKEGKESDGYINYVKGANIAGFKKVADAMVDLGY gdhA curated BRENDA::Q9Y8I4 glutamate dehydrogenase (EC 1.4.1.2) MERTGFLEYVLNYVKKGVELGGFPEDFYKILSRPRRVLIVNIPVRLDGGGFEVFEGYRVQHCDVLGPYKGGVRFHPEVTLADDVALAILMTLKNSLAGLPYGGAKGAVRVDPKKLSQRELEELSRGYARAIAPLIGDVVDIPAPDVGTNAQIMAWMVDEYSKIKGYNVPGVFTSKPPELWGNPVREYATGFGVAVATREMAKKLWGGIEGKTVAIQGMGNVGRWTAYWLEKMGAKVIAVSDINGVAYRKEGLNVELIQKNKGLTGPALVELFTTKDNAEFVKNPDAIFKLDVDIFVPAAIENVIRGDNAGLVKARLVVEGANGPTTPEAERILYERGVVVVPDILANAGGVIMSYLEWVENLQWYIWDEEETRKRLENIMVNNVERVYKRWQREKGWTMRDAAIVTALERIYNAMKIRGWI gdhA curated CharProtDB::CH_122231 NAD dependent glutamate dehydrogenase; EC 1.4.1.2 MVSPASSLQSLPDVHVNGNEPNKLPVRSAPKLYGSNDGASSGTGTPIGFQRQPHNKILDSVAGSNVRMPSPQPTHLAIPGSPHRVLSEEDPGYIAAKFEGKEHQMEEVMDQLEKKGFIPPEFIVGETEWFYNQLGIDDTYFQTETVEAIVTQILSLYAAKVAAYARDDKKLEIRLDKEAEDHAVYIDTSKPGFSSVNGPGYEQRIDKKYIDGSTHDHSYRIETFRSPTPVPGDDGQQLRCYFVYKCQFANPNPGPQETNIDIIGEKRFLQKATPNTKAIYQEIISNAVARAGPVIEMFEIEGSREKRLVIAYRQGSAMGLFSALSDLYHYYRLTSSRKYLENFSNGITVISLYLRPLKNAEVAAKFPPIEAAVHQIIKEISLLYCIPQNRFQHHFASGRLSLQETIYAHCAWVFVQQFLNRLGSEYTSLTDLLDSNNSTHAELLAKIKKRLRTETFTSDYIAEIVNKYPDLIHKLYLDFANTHYVQTQGPTEDDFLPTLSYLRLQVDQVLDSRQLKQLVSSTAANEHDEMVMSAFRVFNASILKTNFFTPTKVALSFRLDPHFLPEHEYPQRLYGMFLVISSEFRGFHLRFRDIARGGIRIVKSRNKEAYSINARSLFDENYNLANTQQRKNKDIPEGGAKGVILLDVNHQDKARVAFEKYIDSILDLLLPPASPGIKDPIVDLYGKDEILFMGPDENTAELVDWATEHARNRGAPWWKSFFTGKSPRLGGIPHDTYGMTTLSVRQYVLGIYRKLKIDPSTIRKLQTGGPDGDLGSNEILLANEKYTAIVDGSGVIVDPQGLNREELVRLAKKRATISEFDVSKLSPNGYRVLVDESNVHLPSGELVHNGMVFRNMFHLRKELTYDTFVPCGGRPESIDLSNVGKLIENGKSTIPYIVEGANLFITQDSKLRLEKAGCILFKDASANKGGVTSSSLEVLASLSFDDQGFVQNMCVGDDDSVPEFYREYVKQVQEVIKENATLEFEAIWREHEQTGIPRSVLSDRLSVAITQLDEELQKTELWDNVELRRSVLNDALPKLLLDKIGLDTILQRVPENYLRAIFGSHLASRFVYEYGSSPSQFSFFNL gdhA curated SwissProt::E1V4J5 NAD-specific glutamate dehydrogenase; NAD-GDH; NAD(+)-dependent glutamate dehydrogenase; EC 1.4.1.2 MLHVAQEEARLDLLKQLKERLQSRLDKDKAAEVDTFAHLFYAAVPLEDLADRRLDDLYGATLSVWHFIQQFDPEAPKVRVLNPDFEEHGWQSTHTFIAVLHEDMPFLVDSVRVELNRRGMTVHAIHNAVLAVGRDDEHRLQRVASPEETDAPEARESLIAIEVDRHSNPAELEEIEASLLEVLREVRTAVSDFDPMRAQARAAIEELEATRPAQVDPADHREAIEFLQWLLQDNFTFLGYDEYEVREDQGRQRLDKVQNSELGVFRLDQPRYRERIRTDLGVEGDHYVPMPQLMSFAKSAHHARIHRPTYPDYISIDRYDDQGRVIGERRFLGMFTATVYNESPRNVPILRRKLQAVMDIAGFSPKGHNGKQLLQILEVYPRDDLFQIDIEELAQTALGILDIRERRRVRLFIREDTFGKFYSCLVFVPRDVFSTELRVRLQELLCEELDATFGDFNTYLSESVLARIQFILRFNGEKPVEYDIKRLEEKLVKLARNWRDDLLNASIEGFGEESANLLMSRFRDAFPASYREDFSARTAVYDLQHIGELDEGAPLALSLYRLIEEEGSGVNLKLFHRGAPIPLSDVLPMMENLGLRVIGERPYEVQASDASYWIHDFNLEHHTSVEMNLQEMRGPFIEAFQRIWAGEADNDAFNRLIIGANLDWREVAMLRAYARYLKQIRFGMSQDYIATTLGSHPEITRELVSLFELRFDPAERPGEGDIEECESRILTLLDEVPSLNDDQLLRRYMELIKATLRTNYYQRTEEGRYKDYLAFKLDPSQVSGIPKPCPAYEIFVCSPRVEGVHLRGGKVARGGLRWSDRHEDFRTEVLGLVKAQQVKNAVIVPMGAKGGFVCKRMPEGADREATQKEGIACYQIFIRALLDVTDNLVGGEVVPPRDVVRHDDNDPYLVVAADKGTATFSDIANEISTEYGHWLGDAFASGGANGYDHKKMAITAKGAWESVKRHFRGLGVNTQEDEFSVVGIGDMAGDVFGNGMLLSDKIRLVGAFNHLHIFVDPTPDAAASFAERQRLFDMPRSSWEDYNTELISEGGGIFPRSAKSITITPQMKKVFGIREDKLSPNELIRAMLVSKVDLVWNGGIGTYVKSSEETDAEVGDKANDALRIDGRELNCRVVGEGGNLGLTQRGRMEAAAKGVRVNTDFIDNAGGVNCSDHEVNIKILIDEVVSRGDLTEKQRNQLLADMTDEVSELVLLDNYRQTQALDLAELLSRQGIGPYRRFISELEAAGQIDRELEFLPSDEELLERTQHNQGMTLPELSVLISYAKSVLKGDLIASDVPDDPTIMRFVERVFPSMLAERYRDEMYEHRLKREIVATQVANDLVDYMGVVFVRRLMDSTGADRADIARAYVIARDSFQLPRLWEQIEALDNKVPSQVQYSMMLDLMRMLRRSTRWFLRQRTGMSTRDTIDYFAPRLAQLQENIGKRLRGEEQEQWSARRQELVKAGVPEALASTVAAAGSLYAALGIIQTARQTDEKPQRVAEIFYEVGARLELPWIIQQVTRLEVRDGWQAKARDTFRDDIDRQQLALTASVLGMDGGPRDSAERVDRWLSLHEGMHQRWRHLLEEVGSGSQGGFPLFAVAVRELVDLAESNSEA gdhA curated SwissProt::O53203 NAD-specific glutamate dehydrogenase; NAD-GDH; NAD(+)-dependent glutamate dehydrogenase; EC 1.4.1.2 MTIDPGAKQDVEAWTTFTASADIPDWISKAYIDSYRGPRDDSSEATKAAEASWLPASLLTPAMLGAHYRLGRHRAAGESCVAVYRADDPAGFGPALQVVAEHGGMLMDSVTVLLHRLGIAYAAILTPVFDVHRSPTGELLRIEPKAEGTSPHLGEAWMHVALSPAVDHKGLAEVERLLPKVLADVQRVATDATALIATLSELAGEVESNAGGRFSAPDRQDVGELLRWLGDGNFLLLGYQRCRVADGMVYGEGSSGMGVLRGRTGSRPRLTDDDKLLVLAQARVGSYLRYGAYPYAIAVREYVDGSVVEHRFVGLFSVAAMNADVLEIPTISRRVREALAMAESDPSHPGQLLLDVIQTVPRPELFTLSAQRLLTMARAVVDLGSQRQALLFLRADRLQYFVSCLVYMPRDRYTTAVRMQFEDILVREFGGTRLEFTARVSESPWALMHFMVRLPEVGVAGEGAAAPPVDVSEANRIRIQGLLTEAARTWADRLIGAAAAAGSVGQADAMHYAAAFSEAYKQAVTPADAIGDIAVITELTDDSVKLVFSERDEQGVAQLTWFLGGRTASLSQLLPMLQSMGVVVLEERPFSVTRPDGLPVWIYQFKISPHPTIPLAPTVAERAATAHRFAEAVTAIWHGRVEIDRFNELVMRAGLTWQQVVLLRAYAKYLRQAGFPYSQSYIESVLNEHPATVRSLVDLFEALFVPVPSGSASNRDAQAAAAAVAADIDALVSLDTDRILRAFASLVQATLRTNYFVTRQGSARCRDVLALKLNAQLIDELPLPRPRYEIFVYSPRVEGVHLRFGPVARGGLRWSDRRDDFRTEILGLVKAQAVKNAVIVPVGAKGGFVVKRPPLPTGDPAADRDATRAEGVACYQLFISGLLDVTDNVDHATASVNPPPEVVRRDGDDAYLVVAADKGTATFSDIANDVAKSYGFWLGDAFASGGSVGYDHKAMGITARGAWEAVKRHFREIGIDTQTQDFTVVGIGDMSGDVFGNGMLLSKHIRLIAAFDHRHIFLDPNPDAAVSWAERRRMFELPRSSWSDYDRSLISEGGGVYSREQKAIPLSAQVRAVLGIDGSVDGGAAEMAPPNLIRAILRAPVDLLFNGGIGTYIKAESESDADVGDRANDPVRVNANQVRAKVIGEGGNLGVTALGRVEFDLSGGRINTDALDNSAGVDCSDHEVNIKILIDSLVSAGTVKADERTQLLESMTDEVAQLVLADNEDQNDLMGTSRANAASLLPVHAMQIKYLVAERGVNRELEALPSEKEIARRSEAGIGLTSPELATLMAHVKLGLKEEVLATELPDQDVFASRLPRYFPTALRERFTPEIRSHQLRREIVTTMLINDLVDTAGITYAFRIAEDVGVTPIDAVRTYVATDAIFGVGHIWRRIRAANLPIALSDRLTLDTRRLIDRAGRWLLNYRPQPLAVGAEINRFAAMVKALTPRMSEWLRGDDKAIVEKTAAEFASQGVPEDLAYRVSTGLYRYSLLDIIDIADIADIDAAEVADTYFALMDRLGTDGLLTAVSQLPRHDRWHSLARLAIRDDIYGALRSLCFDVLAVGEPGESSEQKIAEWEHLSASRVARARRTLDDIRASGQKDLATLSVAARQIRRMTRTSGRGISG gdhA curated SwissProt::P28997,BRENDA::P28997,metacyc::MONOMER-1161 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2;; glutamate dehydrogenase (EC 1.4.1.2);; NAD-glutamate dehydrogenase subunit (EC 1.4.1.2) MTDTLNPLVAAQEKVRIACEKLGCDPAVYELLKEPQRVIEISIPVKMDDGTVKVFKGWRSAHSSAVGPSKGGVRFHPNVNMDEVKALSLWMTFKGGALGLPYGGGKGGICVDPAELSERELEQLSRGWVRGLYKYLGDRIDIPAPDVNTNGQIMSWFVDEYVKLNGERMDIGTFTGKPVAFGGSEGRNEATGFGVAVVVRESAKRFGIKMEDAKIAVQGFGNVGTFTVKNIERQGGKVCAIAEWDRNEGNYALYNENGIDFKELLAYKEANKTLIGFPGAERITDEEFWTKEYDIIVPAALENVITGERAKTINAKLVCEAANGPTTPEGDKVLTERGINLTPDILTNSGGVLVSYYEWVQNQYGYYWTEAEVEEKQEADMMKAIKGVFAVADEYNVTLREAVYMYAIKSIDVAMKLRGWY gdhA curated SwissProt::P29051,BRENDA::P29051,CharProtDB::CH_015467,metacyc::MONOMER-741 NAD-specific glutamate dehydrogenase A; NAD-GDH A; EC 1.4.1.2;; glutamate dehydrogenase (EC 1.4.1.2);; glutamate dehydrogenase; EC 1.4.1.2;; GdhA (EC 1.4.1.4) MTMASKSDSTHDESGDEAADSTEPESALETARRQLYHAASYLDIDQNIVERLKYPKKVHEVTIPIERDDGTVEVFTGYRAQHDSVRGPYKGGLRYHPDVTRDECVGLGMWMTWKCAVMDLPFGGAKGGVAVNPKELSPEEKERLTRRFTQEIRDVIGPNQDIPAPDMGTDPQTMAWLMDAYSMQEGETTPGVVTGKPPVVGGSEGREEAPGRSVAIITQLVCEYYDQPLDETTVAVQGYGSVGANAARLLDKWGATIVAISDVNGAMYEPDGIDTASVPSHDEEPEAVTTYADTVISNEELLTLDVDVLIPAALGNVITKENAEAIAADLVVEGANGPTTSTADSILADRDVAVIPDILANAGGVTVSYFEWLQDINRRAWSLERVNDELEAEMQAAWRAVKDEYENRDVTWRDAAYIVALSRIAEAHEARGLWP gdhA curated SwissProt::P39633 Catabolic NAD-specific glutamate dehydrogenase RocG; NAD-GDH; Glutamate dehydrogenase; GlutDH; Trigger enzyme RocG; EC 1.4.1.2 MSAKQVSKDEEKEALNLFLSTQTIIKEALRKLGYPGDMYELMKEPQRMLTVRIPVKMDNGSVKVFTGYRSQHNDAVGPTKGGVRFHPEVNEEEVKALSIWMTLKCGIANLPYGGGKGGIICDPRTMSFGELERLSRGYVRAISQIVGPTKDIPAPDVYTNSQIMAWMMDEYSRLREFDSPGFITGKPLVLGGSQGRETATAQGVTICIEEAVKKKGIKLQNARIIIQGFGNAGSFLAKFMHDAGAKVIGISDANGGLYNPDGLDIPYLLDKRDSFGMVTNLFTDVITNEELLEKDCDILVPAAISNQITAKNAHNIQASIVVEAANGPTTIDATKILNERGVLLVPDILASAGGVTVSYFEWVQNNQGYYWSEEEVAEKLRSVMVSSFETIYQTAATHKVDMRLAAYMTGIRKSAEASRFRGWV gdhA curated SwissProt::P50735 Cryptic catabolic NAD-specific glutamate dehydrogenase GudB; NAD-GDH; EC 1.4.1.2 MAADRNTGHTEEDKLDVLKSTQTVIHKALEKLGYPEEVYELLKEPMRLLTVKIPVRMDDGSVKIFTGYRAQHNDSVGPTKGGIRFHPNVTEKEVKAVKALSIWMSLKCGIIDLPYGGGKGGIVCDPRDMSFRELERLSRGYVRAISQIVGPTKDVPAPDVFTNSQIMAWMMDEYSRIDEFNSPGFITGKPLVLGGSHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAGSYLAKFMHDAGAKVVGISDAYGGLYDPEGLDIDYLLDRRDSFGTVTKLFNDTITNQELLELDCDILVPAAIENQITEENAHNIRAKIVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVSYFEWVQNNQGFYWSEEEVEEKLEKMMVKSFNNIYEMANNRRIDMRLAAYMVGVRKMAEASRFRGWI gdhA curated SwissProt::Q54VI3 Glutamate dehydrogenase 2; NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 MLNQNLTISQEIAAQPKTQYFTKEDGDALANLLESNPYKEQAVEVKSLLKSERLIESSRVEPEVDWFYCKLGLDSNYFDSTPSIVIARHILSLYAAKMVSHATGAKLEVHLHSKNEGSATFITPSNPGKRDSPAMMIEHAIESHYFGEGYHQDQQLLSPQQVAVAPFPVSPKPPTGTNLPPHGFRLACYRTTGTVSNSSPVHLRLYYLTKPVFPQATNDLSASKNDEILATETDLFKIGDISFIEKSSELTKKIYQEVMNEVVGKQGPVIKHYPYQTNGARLVIAYRRGSTHSYWSAIGELYHFHQMYATHKYVEQFSNGITIYSIYLRPLHPDVDINTKISKIAEQASLVYVLPRTSLTPLFLSHQLSFPEVTYAYVCWKFAYQFLNRYATEYSALAAAIGDDSTKQSMLAQLKTRLSKDTFTEGRVRDAVLQYPELIKILYQDFEKFHFSGSNSNNTQKYDVQHGSEILASIKKTVNNELDSQIFSAILSFNRHLLKTNFYKQTKTALSFRLDPGFLSTKEYVSTPYAVFFVVGSEFRGFHIRFRDISRGGIRIIRSGNSTQYDHNSSSLFDENYNLANTQQSKNKDIAEGGSKGTILLSADHQSKAEVAFHKYIDGLLDLLLPNHEIVDHFAKPEILFLGPDEGTADFMNWASSHAKDRGAHFWKAFTTGKSLSRGGIPHDLYGMTTRSIHQYVLGTLAKLGRNEADCTKFQTGGPDGDLGSNEIKISKDKTIGIVDGSGVLLDPQGLNRDEIGRLASKRQMARYFDKSKLSPQGFFVDVAENDVKLPNGDIVESGLIFRNNFHLNPLCNADIFVPCGGRPESVQLTNVDKMFTATGESRFPIIVEGANLFFTQKARLMIEEKGAIIFKDASANKGGVTSSSLEVLAALALNDEEFDRHMCVKDNVVPEFYENYIKDVHHTIESNARLEFECIWSEHESTKTPRSILSDLLSNKINSLNDSIQTSSLWTDQSLRRKIISAACPKVLLNLLGVDKIMERVPEPYVKAIFGSYLASRFVYKYGLNSNEFAFYTYMETLKQQ gdhA curated SwissProt::Q852M0,BRENDA::Q852M0 Glutamate dehydrogenase 1, mitochondrial; OsGDH1; EC 1.4.1.3;; glutamate dehydrogenase (EC 1.4.1.2) MNALAATSRNFKQAAKLLGLDSKLEKSLLIPFREIKVECTIPKDDGTLASYVGFRVQHDNARGPMKGGIRYHHEVDPDEVNALAQLMTWKTAVANIPYGGAKGGIGCSPGDLSISELERLTRVFTQKIHDLIGIHTDVPAPDMGTNSQTMAWILDEYSKFHGYSPAVVTGKPVDLGGSLGRDAATGRGVLFATEALLAEHGKGIAGQRFVIQGFGNVGSWAAQLISEAGGKVIAISDVTGAVKNSNGLDIAKLMKHSSENRGIKGFDGGDAIDPRSLLTEECDVLIPAALGGVINKDNANEIKAKYIIEAANHPTDPEADEILSKKGVLILPDILANSGGVTVSYFEWVQNIQGFMWDEEKVNNELKTYMTRGFRDVKEMCRSHHCDLRMGAFTLGVNRVARATVLRGWEA gdhA curated SwissProt::Q9HZE0 NAD-specific glutamate dehydrogenase; NAD-GDH; NAD(+)-dependent glutamate dehydrogenase; EC 1.4.1.2 MAFFTAASKADFQHQLQTALAQHLGDKALPQVTLFAEQFFSLISLDELTQRRLSDLVGCTLSAWRLLERFDRDQPEVRVYNPDYEKHGWQSTHTAVEVLHPDLPFLVDSVRMELNRRGYSIHTLQTNVLSVRRSAKGELKEILPKGSQGKDVSQESLMYLEIDRCAHAGELRALEKAILEVLGEVRVTVADFEPMKAKARELLTWLGKAKLKVPAEELKEVRSYLEWLLDNHFTFLGYEEFSVADEADGGRMVYDEKSFLGLTRLLRAGLSKDDLHIEDYAVAYLREPVLLSFAKAAHPSRVHRPAYPDYVSIRELDGKGRVIRECRFMGLFTSSVYNESVNDIPFIRGKVAEVMRRSGFDTKAHLGKELAQVLEVLPRDDLFQTPVDELFSTALAIVRIQERNKIRVFLRKDPYGRFCYCLAYVPRDVYSTETRLKIQQVLMERLQASDCEFWTFFSESVLARVQFILRVDPKSRIDIDPARLEEEVIQACRSWQDDYSSLVVENLGEAKGTNVLADFPKGFPAGYRERFAPHFAVVDLQHLLSLSEQRPLVMSFYQPLAQGEQQLHCKLYHADTPLALSDVLPILENLGLRVLGEFPYRLRHQNGREYWIHDFAFTYAEGLDVDIQQLNEILQDAFVHIVSGDAENDAFNRLVLTANLPWRDVALLRAYARYLKQIRLGFDLGYIASALNAHTDIARELVRLFKTRFYLARKLTAEDLEDKQQKLEQAILGALDEVQVLNEDRILRRYLDLIKATLRTNFYQPDGNGQNKSYFSFKFNPKAIPELPRPVPKYEIFVYSPRVEGVHLRGGKVARGGLRWSDREEDFRTEVLGLVKAQQVKNAVIVPVGAKGGFVPRRLPLGGSRDEIQAEAIACYRIFISGLLDITDNLKEGEVVPPANVVRHDEDDPYLVVAADKGTATFSDIANGIAAEYGFWLGDAFASGGSAGYDHKGMGITAKGAWVSVQRHFRERGIDVQKDNISVIGIGDMAGDVFGNGLLMSDKLQLVAAFNHMHIFIDPNPDAASSFVERQRLFNLPRSSWADYDAKLISAGGGIFLRSAKSIAITPEMKARFDIQADRLAPTELIHALLKAPVDLLWNGGIGTYVKSSKETHADVGDKANDGLRVDGRELRAKVVGEGGNLGMTQLARVEFGLHGGANNTDFIDNAGGVDCSDHEVNIKILLNEVVQAGDMTEKQRNALLVKMTDAVGALVLGNNYKQTQALSLAQRRARERIAEYKRLMGDLEARGKLDRALEFLPSDEELAERISAGQGLTRAELSVLISYSKIDLKESLLKSLVPDDDYLTRDMETAFPALLAEKFGDAMRRHRLKREIVSTQIANDLVNHMGITFVQRLKESTGMSAANVAGAYVIVRDVFHLPHWFRQIENLDYQVPADIQLTLMDELMRLGRRATRWFLRSRRNELDAARDVAHFGPRIAALGLKLNELLEGPTRELWQARYQTYVDAGVPELLARMVAGTSHLYTLLPIIEASDVTGQDTAEVAKAYFAVGSALDLTWYLQQITNLPVENNWQALAREAFRDDLDWQQRAITVSVLQMQDGPKEVEARVGLWLEQHLPLVERWRAMLVELRAASGTDYAMYAVANRELMDLAQSSQHGVCIP gdhA curated SwissProt::Q9USN5 Probable NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 MYLTKQIPHYSRIHTTQLLTVVNHRTIPFKIRGSFSNCRRYSNFATVPLLERPFKNKSKHNTARASRPFSTQKMLLTKSHPPNMYKDSVFFGYRPIVFSGKQDQKSKVIQCLRTERKTIPDDLVEDEVDRFYNKLGLDDYYFQMEPVSIIADHIEIIYAAKIAAHASHAKEELNIHVKNENEDLAIYLDSSPVTQPELDQSSAVEESISTRYLDPFKLTDPTAYRVESFTSVTNIDRTSTENSNIYTYFVTKCDFVDNPKKDASPDVPTDIASVSDKTFLEKASDNTIEMYQDVMNSVLTRFGPVVRLFDYQGRSEIRLVVGYRRGSIFQYFPSLSKLFRYYGLHSTRTYVEQFSNGVTIISYNFKPELFKNAAVTSINELFSQITREASLLYCLPSTDFQPLFVSEKLSIQEVTYAHCVRIFCEHVMNKLGPEYSSLSAILDHSNNIHAEILETIKRRLSTLAFTRTKIHDTIMQYPGLVHTLFEQFYLEHAINHNSTPHLHRAKSATSLADEASTYSITPMSATALMDLIQKTCTNEEDVSVMEMFVKFNTHLLKTNFFQTTKVALSFRFDPSFLDSTQYKDPLYAMIMSIGNEFRGFHLRFRDVARGGIRLIKSANPEAFGLNARGLFDENYNLAKTQMLKNKDIPEGGAKGVILLGKDCQDKPELAFMKYIDSIIDLLIVNKSQPLVDKLGKPEILFMGPDENTADLVNWATIHAHRRNAPWWKSFFTGKKPTMGGIPHDKYGMTSLSVRCYVEGIYKKLNITDPSKLTKVQTGGPDGDLGSNEIKLSNEKYIAVIDGSGVLYDPAGLDRTELLRLADERKTIDHFDAGKLSPEGYRVLVKDTNLKLPNGEIVRNGTIFRNTAHLRYKADTFVPCGGRPNAININNVEQLIDDHGRPAFKYLVEGANLFITQDAKSVLEKAGVIVIRDASANKGGVTSSSLEVLASLSFDDASFKENMCVHDGKVPTFYADYVNEVKRIIQRNANLEFEAIWKGHSENKIPYTSLSNHLSTEIVKLDHDIYNYEKLWADVGFRNAVLRASIPKTLQAKIGLEKMLERIPESYLRAIFSTYLASRFVYQHVVSSDPFAFFDYISTEMKMLKDA gdhA curated metacyc::MONOMER-15559,BRENDA::P93541 glutamate dehydrogenase (EC 1.4.1.3);; glutamate dehydrogenase (EC 1.4.1.2) MNALAATNRNFKLAARLLGLDSKLELSLLIPFREIKVECTIPKDDGTLASFVGFRVQHDNARGPMKGGIRYHPEVDPDEVNALAQLMTWKTAVANIPYGGAKGGIGCSPSDLSISELERLTRVFTQKIHDLIGIHTDVPAPDMGTNPQTMAWILDEYSKFHGYSPAVVTGKPVDLGGSLGRDAATGRGALFATEALLNEHGKSVAGQRFVIQGFGNVGSWAAKLIHEQGGKVVAVSDITGAIKNEKGIDIESLFKHVKETRGVKGFHDAHPIDANSILVEDCDVLIPAALGGVINKDNHKLKIKAKYIIEAANHPTDPEADEILSKKGVTILPDIYANSGGVTVSYFEWVQNIQGFMWDEKKVNDELKTYMTRGFKDVKDMCKTHNCDLRMGAFTLGVNRVARATVLRGWEA gdhA curated reanno::psRCH2:GFF1903 NAD-specific glutamate dehydrogenase (EC 1.4.1.2), large form MAFFSAASKADFQQQLQTALAQHVDSKILPQLNLFAEQFFGIVALPELTERRMSDLVGSTLASWRLLERFEPSTPEVQVFNPDFEKHGWQSTHSVVEVLHPDMPFLVDSVRMELTRRGYSIHTLQTSVLQVRRAADGSLLELLPKDERAADSHAESLIFVEIDRCASPSALRELEQSLLGVLADVRQVVGDFAAMKGKAVELQGRLEQVNLSIDGDELDEIRDFMRWLADDHFTFLGYEEFSVQEQADGGRIFYDESSLLGLSRTMRTGLSEEEQSLTAQSMSYLREPLLLSFAKAAMPSRVHRPAYPDFVSVREFDEAGRVVRECRFLGLFTSSVYTQSVRRIPFIRRKVETVVQRANFGSSAHLAKELVQVLEVLPRDELFQAPIDELFENAIAIVQIQERNRLRLFLRFDPYRRFCYCLVYVPRDSYSTETRLKIQQVLQERLEASDCEFSTYFSESVLTRVQFILRLDPSRAVQVDPVRLEQEVLQACRTWQDDYQSLVVERFGEAKGTHLLSEFPKGFPAGYRERFSPQSATVDMQHVLDLSEERPLVMSFYQPITAEENRLHCKLYHLNTPLPLSDILPIMENLGLRVLGEFPFRLRNRSGREYWIHDFAFTYAEGLEIDLLEINEALQDAFIHIYGGAAENDAFNRLVLTAGLAWREVALLRAYARYLKQIRMGFDLGYIASALLNHTDIARELVRLFKMRFYLARKLGDEDLADKQQRLEQAILSALDDVAVLNEDRILRRYLALIQATLRTNFYQPDANGRPKPYFSFKLDPRAIPEMPRPAPMYEIFVYSPRVEGVHLRGGKVARGGLRWSDREEDYRTEVLGLVKAQQVKNAVIVPGGAKGGFVPRRLPTTGTRDDIQAEAIACYRIFISGLLDITDNLREGQVAPPANVLRYDGDDPYLVVAADKGTASFSDIANGIAAEYDFWLGDAFASGGSAGYDHKKMGITARGAWVSVQRHFRERGINVQSDVISVIGIGDMAGDVFGNGLLMSETLQLVAAFNHLHIFIDPNPDPARSFLERKRLFDLPRSSWTDYDASLISEGGGIFPRSAKRVQISPQMKERFAIEADQLTPAELINALLKAPVDLLWNGGIGTYVKSSSESHAEVGDKANDAVRVNGAELRAKVVGEGGNLGMTQLGRVEYALHGGSSNTDFIDNAGGVDCSDHEVNIKILLNEVVSAGDMTAKQRNQLLFEMTDAVAELVLQNNYKQTQALSQAQHRSRERAAEYVRLINALEAAGQLDRALEFLPSDEALAERASIGKGLTRPELSVLISYSKIELKKALLDSRVPDDDYLAREMDSAFPQQLAEHFRAAMLQHRLKREIVATQIANDLVNNMGITFVQRLNEATGMSAANVAGAYVIVRDIFHLPHWFRQIEALDHKVPAELQLSLMDELMRLGRRATRWFLRNRRSELDAARDVAHFGPRVAALGLKLDELLQGSTRDHWQERYRRYTEAGVPELLARMVAGTNHLYTLLPILEAADETGQVPAQVAAAYFAVGGALELPWYLHQLTNMPVGNNWQALAREGFRDDLDSQQRSITVSVLQMENGAESISERVDAWLAQRPVPLARWRSMLAELRNASGNDYAIYAVASRELQGLAQSARHG gdhA curated2 A3MUY9 NAD(+)-dependent glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2; NAD-specific glutamate dehydrogenase MSTTYIVSDFLINTLLTIKRGVELAGLPPEFYEALEKPKRILVVNIPVKMDDGKIKYFEGYRVQHNDALGPFKGGIRFHPEVTLADDIALAMLMTLKNSLAGLPYGGAKGAVRVDPRRLSRRELEELARGYARAVAPLIGEQLDIPAPDVGTDSQVMAWMVDEYSRLVGRNAPAVFTSKPPELWGNPVREYSTGFGVAVAAREVAKRLWGGIVGKTAAVQGLGNVGRWAAYWLEKMGAKVVAVSDVNGVVYRERGLDVDLIRETKAKGPQLLEMISQKNGVEIVKNPDQIFSLDVDILVPAAIENVVREDNVDGVRARLVVEGANGPTTPGAERRLYERGVVVVPDILANAGGVIMSYLEWVENLQWLFWDEEETRRRLEAIMSNNVARVYARWEKEKSWTMRDAAVVTALERIYNAMKTRGWI gdhA curated2 B2RKJ1 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2; Surface-associated protein PGAG1 MKTQEIMTMLEAKHPGESEFLQAVKEVLLSVEEVYNQHPEFEKNGIIERIVEPDRVFTFRVPWVDDQGKVQVNIGYRVQFNNAIGPYKGGIRFHPSVNLSILKFLGFEQMFKNALTTLPMGGGKGGADFSPKGKSEAEIMRFCQSFMTELWRNIGPDTDIPAGDIGVGGREVGYMFGMYKKLAREHTGTLTGKGFEFGGSRLRPESTGFGAVYFVQNMCKQNGVDYKGKTLAISGFGNVAWGVAQKATELGIKVVTISGPDGYVYDPDGINTPEKFRCMLDLRDSGNDVVSDYVKRFPNAQFFPGKKPWEQKVDFAMPCATQNEMNLEDAKTLHKNGVTLVAETSNMGCTAEASEYYVANKMLFAPGKAVNAGGVSCSGLEMTQNAMHLVWTNEEVDKWLHQIMQDIHEQCVTYGKDGNYIDYVKGANIAGFMKVAKAMVAQGVC gdhA curated2 E1V4J5 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2; NAD(+)-dependent glutamate dehydrogenase MLHVAQEEARLDLLKQLKERLQSRLDKDKAAEVDTFAHLFYAAVPLEDLADRRLDDLYGATLSVWHFIQQFDPEAPKVRVLNPDFEEHGWQSTHTFIAVLHEDMPFLVDSVRVELNRRGMTVHAIHNAVLAVGRDDEHRLQRVASPEETDAPEARESLIAIEVDRHSNPAELEEIEASLLEVLREVRTAVSDFDPMRAQARAAIEELEATRPAQVDPADHREAIEFLQWLLQDNFTFLGYDEYEVREDQGRQRLDKVQNSELGVFRLDQPRYRERIRTDLGVEGDHYVPMPQLMSFAKSAHHARIHRPTYPDYISIDRYDDQGRVIGERRFLGMFTATVYNESPRNVPILRRKLQAVMDIAGFSPKGHNGKQLLQILEVYPRDDLFQIDIEELAQTALGILDIRERRRVRLFIREDTFGKFYSCLVFVPRDVFSTELRVRLQELLCEELDATFGDFNTYLSESVLARIQFILRFNGEKPVEYDIKRLEEKLVKLARNWRDDLLNASIEGFGEESANLLMSRFRDAFPASYREDFSARTAVYDLQHIGELDEGAPLALSLYRLIEEEGSGVNLKLFHRGAPIPLSDVLPMMENLGLRVIGERPYEVQASDASYWIHDFNLEHHTSVEMNLQEMRGPFIEAFQRIWAGEADNDAFNRLIIGANLDWREVAMLRAYARYLKQIRFGMSQDYIATTLGSHPEITRELVSLFELRFDPAERPGEGDIEECESRILTLLDEVPSLNDDQLLRRYMELIKATLRTNYYQRTEEGRYKDYLAFKLDPSQVSGIPKPCPAYEIFVCSPRVEGVHLRGGKVARGGLRWSDRHEDFRTEVLGLVKAQQVKNAVIVPMGAKGGFVCKRMPEGADREATQKEGIACYQIFIRALLDVTDNLVGGEVVPPRDVVRHDDNDPYLVVAADKGTATFSDIANEISTEYGHWLGDAFASGGANGYDHKKMAITAKGAWESVKRHFRGLGVNTQEDEFSVVGIGDMAGDVFGNGMLLSDKIRLVGAFNHLHIFVDPTPDAAASFAERQRLFDMPRSSWEDYNTELISEGGGIFPRSAKSITITPQMKKVFGIREDKLSPNELIRAMLVSKVDLVWNGGIGTYVKSSEETDAEVGDKANDALRIDGRELNCRVVGEGGNLGLTQRGRMEAAAKGVRVNTDFIDNAGGVNCSDHEVNIKILIDEVVSRGDLTEKQRNQLLADMTDEVSELVLLDNYRQTQALDLAELLSRQGIGPYRRFISELEAAGQIDRELEFLPSDEELLERTQHNQGMTLPELSVLISYAKSVLKGDLIASDVPDDPTIMRFVERVFPSMLAERYRDEMYEHRLKREIVATQVANDLVDYMGVVFVRRLMDSTGADRADIARAYVIARDSFQLPRLWEQIEALDNKVPSQVQYSMMLDLMRMLRRSTRWFLRQRTGMSTRDTIDYFAPRLAQLQENIGKRLRGEEQEQWSARRQELVKAGVPEALASTVAAAGSLYAALGIIQTARQTDEKPQRVAEIFYEVGARLELPWIIQQVTRLEVRDGWQAKARDTFRDDIDRQQLALTASVLGMDGGPRDSAERVDRWLSLHEGMHQRWRHLLEEVGSGSQGGFPLFAVAVRELVDLAESNSEA gdhA curated2 O53203 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2; NAD(+)-dependent glutamate dehydrogenase MTIDPGAKQDVEAWTTFTASADIPDWISKAYIDSYRGPRDDSSEATKAAEASWLPASLLTPAMLGAHYRLGRHRAAGESCVAVYRADDPAGFGPALQVVAEHGGMLMDSVTVLLHRLGIAYAAILTPVFDVHRSPTGELLRIEPKAEGTSPHLGEAWMHVALSPAVDHKGLAEVERLLPKVLADVQRVATDATALIATLSELAGEVESNAGGRFSAPDRQDVGELLRWLGDGNFLLLGYQRCRVADGMVYGEGSSGMGVLRGRTGSRPRLTDDDKLLVLAQARVGSYLRYGAYPYAIAVREYVDGSVVEHRFVGLFSVAAMNADVLEIPTISRRVREALAMAESDPSHPGQLLLDVIQTVPRPELFTLSAQRLLTMARAVVDLGSQRQALLFLRADRLQYFVSCLVYMPRDRYTTAVRMQFEDILVREFGGTRLEFTARVSESPWALMHFMVRLPEVGVAGEGAAAPPVDVSEANRIRIQGLLTEAARTWADRLIGAAAAAGSVGQADAMHYAAAFSEAYKQAVTPADAIGDIAVITELTDDSVKLVFSERDEQGVAQLTWFLGGRTASLSQLLPMLQSMGVVVLEERPFSVTRPDGLPVWIYQFKISPHPTIPLAPTVAERAATAHRFAEAVTAIWHGRVEIDRFNELVMRAGLTWQQVVLLRAYAKYLRQAGFPYSQSYIESVLNEHPATVRSLVDLFEALFVPVPSGSASNRDAQAAAAAVAADIDALVSLDTDRILRAFASLVQATLRTNYFVTRQGSARCRDVLALKLNAQLIDELPLPRPRYEIFVYSPRVEGVHLRFGPVARGGLRWSDRRDDFRTEILGLVKAQAVKNAVIVPVGAKGGFVVKRPPLPTGDPAADRDATRAEGVACYQLFISGLLDVTDNVDHATASVNPPPEVVRRDGDDAYLVVAADKGTATFSDIANDVAKSYGFWLGDAFASGGSVGYDHKAMGITARGAWEAVKRHFREIGIDTQTQDFTVVGIGDMSGDVFGNGMLLSKHIRLIAAFDHRHIFLDPNPDAAVSWAERRRMFELPRSSWSDYDRSLISEGGGVYSREQKAIPLSAQVRAVLGIDGSVDGGAAEMAPPNLIRAILRAPVDLLFNGGIGTYIKAESESDADVGDRANDPVRVNANQVRAKVIGEGGNLGVTALGRVEFDLSGGRINTDALDNSAGVDCSDHEVNIKILIDSLVSAGTVKADERTQLLESMTDEVAQLVLADNEDQNDLMGTSRANAASLLPVHAMQIKYLVAERGVNRELEALPSEKEIARRSEAGIGLTSPELATLMAHVKLGLKEEVLATELPDQDVFASRLPRYFPTALRERFTPEIRSHQLRREIVTTMLINDLVDTAGITYAFRIAEDVGVTPIDAVRTYVATDAIFGVGHIWRRIRAANLPIALSDRLTLDTRRLIDRAGRWLLNYRPQPLAVGAEINRFAAMVKALTPRMSEWLRGDDKAIVEKTAAEFASQGVPEDLAYRVSTGLYRYSLLDIIDIADIADIDAAEVADTYFALMDRLGTDGLLTAVSQLPRHDRWHSLARLAIRDDIYGALRSLCFDVLAVGEPGESSEQKIAEWEHLSASRVARARRTLDDIRASGQKDLATLSVAARQIRRMTRTSGRGISG gdhA curated2 P24295 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 MSKYVDRVIAEVEKKYADEPEFVQTVEEVLSSLGPVVDAHPEYEEVALLERMVIPERVIEFRVPWEDDNGKVHVNTGYRVQFNGAIGPYKGGLRFAPSVNLSIMKFLGFEQAFKDSLTTLPMGGAKGGSDFDPNGKSDREVMRFCQAFMTELYRHIGPDIDVPAGDLGVGAREIGYMYGQYRKIVGGFYNGVLTGKARSFGGSLVRPEATGYGSVYYVEAVMKHENDTLVGKTVALAGFGNVAWGAAKKLAELGAKAVTLSGPDGYIYDPEGITTEEKINYMLEMRASGRNKVQDYADKFGVQFFPGEKPWGQKVDIIMPCATQNDVDLEQAKKIVANNVKYYIEVANMPTTNEALRFLMQQPNMVVAPSKAVNAGGVLVSGFEMSQNSERLSWTAEEVDSKLHQVMTDIHDGSAAAAERYGLGYNLVAGANIVGFQKIADAMMAQGIAW gdhA curated2 P27346 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 MSGKDVNVFEMAQSQVKNACDKLGMEPAVYELLKEPMRVIEVSIPVKMDDGSIKTFKGFRSQHNDAVGPTKGGIRFHQNVSRDEVKALSIWMTFKCSVTGIPYGGGKGGIIVDPSTLSQGELERLSRGYIDGIYKLIGEKVDVPAPDVNTNGQIMSWMVDEYNKLTGQSSIGVITGKPVEFGGSLGRTAATGFGVAVTAREAAAKLGIDMKKAKIAVQGIGNVGSYTVLNCEKLGGTVVAMAEWCKSEGSYAIYNENGLDGQAMLDYMKEHGNLLNFPGAKRISLEEFWASDVDIVIPAALENSITKEVAESIKAKLVCEAANGPTTPEADEVFAERGIVLTPDILTNAGGVTVSYFEWVQNLYGYYWSEEEVEQKEEIAMVKAFESIWKIKEEYNVTMREAAYMHSIKKVAEAMKLRGWY gdhA curated2 Q5HHC7 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 MTENNNLVTSTQGIIKEALHKLGFDEGMYDLIKEPLRMLQVRIPVRMDDGTVKTFTGYRAQHNDAVGPTKGGVRFHPDVDEEEVKALSMWMTLKCGIVNLPYGGGKGGIVCDPRQMSIHEVERLSRGYVRAISQFVGPNKDIPAPDVFTNSQIMAWMMDEYSALDKFNSPGFITGKPIVLGGSHGRDRSTALGVVIAIEQAAKRRNMQIEGAKVVIQGFGNAGSFLAKFLYDLGAKIVGISDAYGALHDPNGLDIDYLLDRRDSFGTVTNLFEETISNKELFELDCDILVPAAISNQITEDNAHDIKASIVVEAANGPTTPEATRILTERGILLVPDVLASAGGVTVSYFEWVQNNQGYYWSEEEVNEKLREKLEAAFDTIYELSQNRKIDMRLAAYIIGIKRTAEAARYRGWA gdhA curated2 Q9HZE0 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2; NAD(+)-dependent glutamate dehydrogenase MAFFTAASKADFQHQLQTALAQHLGDKALPQVTLFAEQFFSLISLDELTQRRLSDLVGCTLSAWRLLERFDRDQPEVRVYNPDYEKHGWQSTHTAVEVLHPDLPFLVDSVRMELNRRGYSIHTLQTNVLSVRRSAKGELKEILPKGSQGKDVSQESLMYLEIDRCAHAGELRALEKAILEVLGEVRVTVADFEPMKAKARELLTWLGKAKLKVPAEELKEVRSYLEWLLDNHFTFLGYEEFSVADEADGGRMVYDEKSFLGLTRLLRAGLSKDDLHIEDYAVAYLREPVLLSFAKAAHPSRVHRPAYPDYVSIRELDGKGRVIRECRFMGLFTSSVYNESVNDIPFIRGKVAEVMRRSGFDTKAHLGKELAQVLEVLPRDDLFQTPVDELFSTALAIVRIQERNKIRVFLRKDPYGRFCYCLAYVPRDVYSTETRLKIQQVLMERLQASDCEFWTFFSESVLARVQFILRVDPKSRIDIDPARLEEEVIQACRSWQDDYSSLVVENLGEAKGTNVLADFPKGFPAGYRERFAPHFAVVDLQHLLSLSEQRPLVMSFYQPLAQGEQQLHCKLYHADTPLALSDVLPILENLGLRVLGEFPYRLRHQNGREYWIHDFAFTYAEGLDVDIQQLNEILQDAFVHIVSGDAENDAFNRLVLTANLPWRDVALLRAYARYLKQIRLGFDLGYIASALNAHTDIARELVRLFKTRFYLARKLTAEDLEDKQQKLEQAILGALDEVQVLNEDRILRRYLDLIKATLRTNFYQPDGNGQNKSYFSFKFNPKAIPELPRPVPKYEIFVYSPRVEGVHLRGGKVARGGLRWSDREEDFRTEVLGLVKAQQVKNAVIVPVGAKGGFVPRRLPLGGSRDEIQAEAIACYRIFISGLLDITDNLKEGEVVPPANVVRHDEDDPYLVVAADKGTATFSDIANGIAAEYGFWLGDAFASGGSAGYDHKGMGITAKGAWVSVQRHFRERGIDVQKDNISVIGIGDMAGDVFGNGLLMSDKLQLVAAFNHMHIFIDPNPDAASSFVERQRLFNLPRSSWADYDAKLISAGGGIFLRSAKSIAITPEMKARFDIQADRLAPTELIHALLKAPVDLLWNGGIGTYVKSSKETHADVGDKANDGLRVDGRELRAKVVGEGGNLGMTQLARVEFGLHGGANNTDFIDNAGGVDCSDHEVNIKILLNEVVQAGDMTEKQRNALLVKMTDAVGALVLGNNYKQTQALSLAQRRARERIAEYKRLMGDLEARGKLDRALEFLPSDEELAERISAGQGLTRAELSVLISYSKIDLKESLLKSLVPDDDYLTRDMETAFPALLAEKFGDAMRRHRLKREIVSTQIANDLVNHMGITFVQRLKESTGMSAANVAGAYVIVRDVFHLPHWFRQIENLDYQVPADIQLTLMDELMRLGRRATRWFLRSRRNELDAARDVAHFGPRIAALGLKLNELLEGPTRELWQARYQTYVDAGVPELLARMVAGTSHLYTLLPIIEASDVTGQDTAEVAKAYFAVGSALDLTWYLQQITNLPVENNWQALAREAFRDDLDWQQRAITVSVLQMQDGPKEVEARVGLWLEQHLPLVERWRAMLVELRAASGTDYAMYAVANRELMDLAQSSQHGVCIP gdhA ignore BRENDA::A0A1V1FMC4 glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3) MTTGKEYVAGVFEKVKAQNAHEPEFLQAVEEVFESLVPVFDKYPKYIEENLLERLVEPERIITFRVPWVDDKGQVQVNRGFRVQFSSAIGPYKGGLRFHPSVNQSIIKFLGFEQIFKNSLTGQPIGGGKGGSNFDPKGKSDNEIMRFCQSFMTELSKHIGADTDVPAGDIGVGGREIGYLYGQYKRLRNEYTGVLTGKGLTYGGSLARTEATGYGAVYFAEQMLKARGEDFAGKVAVVSGSGNVAIYATEKLQTLGAKVVAVSDSSGFVYDPEGIDVPLLKQLKEVERARIVKYAEARPSATFTPASEGSIWNIKADLAFPCATQNEINEEHAKALVANGVIAVTEGANMPSTLEAIEVFQKAGVSFGPAKAANAGGVAVSALEMAQNSQRTPWTFEEVDAKLYNIMKGIYENAASAAKEFGAEGNLVVGANVAGFLKVAEAMSAQGIV gdhA ignore BRENDA::O04937 glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3) MNALAATNRNFRQAARILGLDSKLEKSLLIPFREIKVECTIPKDDGTLVSYVGFRVQHDNARGPMKGGIRYHPEVDLDEVNALAQLMTWKTAVADIPYGGAKGGIGCKPKDLSKSELERLTRVFTQKIHDLIGINTDVPAPDMGTNAQTMAWILDEYSKFHGHSPAIVTGKPIDLGGSLGREAATGRGVVYATEALLAEYGKNIKDLTFAIQGFGNVGAWAAKLIHERGGKVIAVSDITGAVKNPNGLDIPALLNHKEATGKLIDFSGGDVMNSDEVLTHECDVLIPCALGGVLNRENADNVKAKFIIEAANHPTDPEADEILCKKGIVILPDIYANAGGVTVSYFEWVQNIQGFMWDEEKVNRELRKYMTKAFHNLKNMCQSHNCSLRMGAFTLGVNRVARATTLRGWEA gdhA ignore BRENDA::O59650,CharProtDB::CH_015459 glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3);; glutamate dehydrogenase (NAD(P)(+)); EC 1.4.1.3 MVEIDPFEMAVQQLERAAQFMDISEEALEWLKRPMRIVEVSVPVEMDDGSVKVFTGFRVQHNWARGPTKGGIRWHPAETLSTVKALATWMTWKVAVVDLPYGGGKGGIIVDPKKLSEREQERLARSYIRAVYDVIGPWTDIPAPDVYTNPKIMAWMMDEYETIMRRKGPAFGVITGKPPGVGGIVARMDATARGAAFTIREAAKALGWDDLKGKTIAIQGYGNAGYYLHKIMSEEFGMKVVAVSDSKGGIYNPDGLPPADEVLKWKKEHGSVKDMPGTQNITNEELLELEVDILAPSAIEGVITKENADNVKAKIVAEVANGPVTPEADEILHEKGILQIPDFLCNAGGVTVSYFEWVQNINGFYWTVEETRKRLDDKMTKAFWDVFNTHKEKNIHMRDAAYVVAVSRVYEAMKHRGWVKK gdhA ignore BRENDA::O74024 glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3) MVEIDPFEMAVKQLERAAQYMDISEEALEWLKKPMRIVEVSVPIEMDDGSVKVFTGFRVQHNWARGPTKGGIRWHPAETLSTVKALATWMTWKVAVVDLPYGGGKGGIIVNPKELSEREQERLARAYIRAVYDVIGPWTDIPAPDVYTNPKIMGWMMDEYETIMRRKGPAFGVITGKPLSIGGSLGRGTATAQGAIFTIREAAKALGIDLKGKKIAVQGYGNAGYYTAKLAKEQLGMTVVAVSDSRGGIYNPDGLDPDEVLKWKREHGSVKDFPGATNITNEELLELEVDVLAPAAIEEVITEKNADNIKAKIVAEVANGPVTPEADDILREKGILQIPDFLCNAGGVTVSYFEWVQNINGYYWTEEEVREKLDKKMTKAFWEVYNTHKDKNIHMRDAAYVVAVSRVYQAMKDRGWVKK gdhA ignore BRENDA::P00367,SwissProt::P00367,metacyc::HS07548-MONOMER glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3);; Glutamate dehydrogenase 1, mitochondrial; GDH 1; EC 1.4.1.3;; Glutamate dehydrogenase 1, mitochondrial (EC 1.4.1.3) MYRYLGEALLLSRAGPAALGSASADSAALLGWARGQPAAAPQPGLALAARRHYSEAVADREDDPNFFKMVEGFFDRGASIVEDKLVEDLRTRESEEQKRNRVRGILRIIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTYASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFGDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILGFPKAKPYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGKHGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYVNAIEKVFKVYNEAGVTFT gdhA ignore BRENDA::P10860,SwissProt::P10860 glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3);; Glutamate dehydrogenase 1, mitochondrial; GDH 1; Memory-related gene 2 protein; MRG-2; EC 1.4.1.3 MYRRLGEVLLLSRAGPAALGSAAADSAALLGWARGQPSAVPQPGLTPVARRHYSEAATDREDDPNFFKMVEGFFDRGASIVEDKLVEDLKTRENEEQKRNRVRGILRIIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTYASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGLGDKTFVVQGFGNVGLHSMRYLHRFGAKCVGVGESDGSIWNPDGIDPKELEDFKLQHGSILGFPKAKVYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGKHGGTIPVVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYVNAIEKVFKVYNEAGVTFT gdhA ignore BRENDA::P26443,SwissProt::P26443 glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3);; Glutamate dehydrogenase 1, mitochondrial; GDH 1; EC 1.4.1.3 MYRRLGEALLLSRAGPAALGSAAADSAALLGWARGQPSAAPQPGLTPVARRHYSEAAADREDDPNFFKMVEGFFDRGASIVEDKLVEDLKTRESEEQKRNRVRGILRIIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTYASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFGDKTFVVQGFGNVGLHSMRYLHRFGAKCVGVGESDGSIWNPDGIDPKELEDFKLQHGSILGFPKAKVYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGKHGGTIPVVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYVNAIEKVFKVYNEAGVTFT gdhA ignore BRENDA::P49448,SwissProt::P49448,metacyc::HS00018-MONOMER glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3);; Glutamate dehydrogenase 2, mitochondrial; GDH 2; EC 1.4.1.3;; Glutamate dehydrogenase 2, mitochondrial (EC 1.4.1.3) MYRYLAKALLPSRAGPAALGSAANHSAALLGRGRGQPAAASQPGLALAARRHYSELVADREDDPNFFKMVEGFFDRGASIVEDKLVKDLRTQESEEQKRNRVRGILRIIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTENELEKITRRFTMELAKKGFIGPGVDVPAPDMNTGEREMSWIADTYASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFRDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILGFPKAKPYEGSILEVDCDILIPAATEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNILVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLLSVQESLERKFGKHGGTIPIVPTAEFQDSISGASEKDIVHSALAYTMERSARQIMHTAMKYNLGLDLRTAAYVNAIEKVFKVYSEAGVTFT gdhA ignore BRENDA::P80053 glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3) MMEEVLSSSLYTQQVKKLYKVGELLGLDNETLETLSQPERIIQVKIQIRGSDGKLKTFMGWRSQHNSALGPYKGGVRYHPNVTQDEVEALSMIMTWKNSLLLLPYGGGKGGVRVDPKKLTREELEQLSRKYIQAIYKYLGSELDIPAPDVNTDSQTMAWFLDEYIKITGKVDFAVFTGKPVELGGIGVRLYSTGLGVATIAKEAANKFIGGVEEARVIIQGFGNVGYYAGKFLSEMGAKIVGVSDSKGGVINEKGIDVGKAIEIKEKTGSVINYPEGRKVTNEELLISDCDILIPAALENVINKFNAPKVKAKLIVEGANGPLTADADEIMRQRGIAVVPDILANAGGVVGSYVEWANNKMGEIISDEEAKKLIVDRMNNAFNTLYDYHQKKLEDHDLRTAAMALAVDRVVRAMKARGIL gdhA ignore BRENDA::P80319 glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3) MVEQDPYEIVIKQLERAAQYMEISEEALEFLKRPQRIVEVTIPVEMDDGSVKVFTGFRVQHNWARGPTKGGIRWHPEETLSTVKALAAWMTWKTAVMDLPYGGGKGGIIVDPKKLSDREKERLARGYIRAIYDVISPYEDIPAPDVYTNPQIMAWMMDEYETISRRKTPAFGIITGKPLSIGGSLGRIEATARGASYTIREAAKVLGWDTLKGKTIAIQGYGNAGYYLAKIMSEDFGMKVVAVSDSKGGIYNPDGLNADEVLKWKNEHGSVKDFPGATNITNEELLELEVDVLAPAAIEEVITKKNADNIKAKIVAEVANGPVTPEADEILFEKGILQIPDFLCNAGGVTVSYFEWVQNITGYYWTIEEVRERLDKKMTKAFYDVYNIAKEKNIHMRDAAYVVAVQRVYQAMLDRGWVKH gdhA ignore BRENDA::Q43314 glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3) MNALAATNRNFKLAARLLGLDSKLEKSLLIPFREIKVECTIPKDDGTLASFVGFRVQHDNARGPMKGGIRYHPEVDPDEVNALAQLMTWKTAVAKIPYGGAKGGIGCDPSKLSISELERLTRVFTQKIHDLIGIHTDVPAPDMGTGPQTMAWILDEYSKFHGYSPAVVTGKPIDLGGSLGRDAATGRGVMFGTEALLNEHGKTISGQRFVIQGFGNVGSWAAKLISEKGGKIVAVSDITGAIKNKDGIDIPALLKHTKEHRGVKGFDGADPIDPNSILVEDCDILVPAALGGVINRENANEIKAKFIIEAANHPTDPDADEILSKKGVVILPDIYANSGGVTVSYFEWVQNIQGFMWEEEKVNDELKTYMTRSFKDLKEMCKTHSCDLRMGAFTLGVNRVAQATILRGWGA gdhA ignore BRENDA::Q9LEC8 glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3) MNALAATNRNFKLASRLLGLDSKLEQCLLIPFREIKVECTIPKDDGSLATFIGFRVQHDNARGPMKGGIRYHPEVDPDEVNALAQLMTWKTAVANIPYGGAKGGIGCSPSDLSISELERLTRVFTQKIHDLIGVHTDVPAPDMGTNPQTMAWILDEYSKFHGYSPAVVTGKPIDLGGSLGRDAATGRGVLFAAEALLRDHGKSIAGQRFVVQGFGNVGSWAAQLITEQGGKIVAVSDITGAIKNKNGIDIASLLKHVKENRGVKGFHGADSIDPNSILVEDCDVLIPAALGGVINRDNAKDIKAKFIVEAANHPTDPEADEILAKKGVVILPDIYANSGGVTVSYFEWVQNIQGFMWDEERVNTELKAYMNRGFKDVKDMCKTHNCDLRMGAFTLGVNRVARATTLRGWEA gdhA ignore BRENDA::Q9S7A0 glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3) MNALAATNRNFKLASRLLGLDSKLEKSLLIPFREIKVECTIPKDDGTLASFVGFRVQHDNARGPMKGGIRYHPEVEPDEVNALAQLMTWKTAVAKIPYGGAKGGIGCDPSELSLSELERLTRVFTQKIHDLIGIHTDVPAPDMGTGPQTMAWILDEYSKFHGHSPAVVTGKPIDLGGSLGRDAATGRGVLFATEALLNEHGKTISGQRFAIQGFGNVGSWAAKLISDKGGKIVAVSDVTGAIKNNNGIDILSLLEHAEENRGIKGFDGADSIDPDSILVEDCDILVPAALGGVINRENANEIKAKFIIEGANHPTDPEADEILKKKGVMILPDIYANSGGVTVSYFEWVQNIQGFMWDEEKVNRELKTYMTRGFKDLKEMCQTHSCDLRMGAFTLGINRVAQATTIRGWGS gdhA ignore CharProtDB::CH_015456 glutamate dehydrogenase (NAD(P)(+)); EC 1.4.1.3 MVEQDPFEIAVKQLERAAQYMKISEEALEFLKRPQRIVEVTIPVEMDDGTVKVFTGFRVQYNWARGPTKGGIRWHPEETLSTVKALAAWMTWKTAVMDLPYGGGKGGIIVDPKKLSDREKERLARGYIRAIYDVISPYEDIPAPDVYTNPQIMAWMMDEYEAISRRKTPAFGIITGKPLSIGGSLGRNEATARGASYTIREARKVLGWGDLKGKTIAIQGYGNAGYYLAKIMSEDYGMKVVAVSDSKGGIYNPDGLNADEVLKWKQEHGSVKDFPGATNITNEELLELEVDVLAPAAIEEVITKKNADNIKAKIVAEVANGPVTPEADEILFEKGILQIPDFLCNAGGVTVSYFEWVQNITGYYWTLEEVREKLDKKMTKAFYDVYNTAKEKNIHMRDADYVVAVQRVYQAMLDRGWVKH gdhA ignore CharProtDB::CH_015463,BRENDA::P96110 glutamate dehydrogenase; EC 1.4.1.3;; glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3) MPEKSLYEMAVEQFNRAASLMDLESDLAEVLRRPKRVLIVEFPVRMDDGHVEVFTGYRVQHNVARGPAKGGIRYHPDVTLDEVKALAFWMTWKTAVMNLPFGGGKGGVRVDPKKLSRNELERLSRRFFSEIQVIIGPYNDIPAPDVNTNADVMAWYMDTYSMNVGHTVLGIVTGKPVELGGSKGREEATGRGVKVCAGLAMDVLGIDPKKATVAVQGFGNVGQFAALLISQELGSKVVAVSDSRGGIYNPEGFDVEELIRYKKEHGTVVTYPKGERITNEELLELDVDILVPAALEGAIHAGNAERIKAKAVVEGANGPTTPEADEILSRRGILVVPDILANAGGVTVSYFEWVQDLQSFFWDLDQVRNALEKMMKGAFNDVMKVKEKYNVDMRTAAYILAIDRVAYATKKRGIYP gdhA ignore SwissProt::P54385 Glutamate dehydrogenase, mitochondrial; GDH; EC 1.4.1.3 MYHLKSLARQGARRQQELATLAKALPTAVMQSSRGYATEHQIPDRLKDVPTAKDPRFFDMVEYFFHRGCQIAEESLVDDMKGKLTRDEKKQKVKGILMLMQPCDHIIEIAFPLRRDAGNYEMITGYRAQHSTHKTPTKGGIRFSLDVSRDEVKALSALMTFKCACVDVPFGGAKAGLKINPKEYSEHELEKITRRFTLELAKKGFIGPGVDVPAPDMGTGEREMSWIADTYAKTIGHLDINAHACVTGKPINQGGIHGRVSATGRGVFHGLENFINEANYMSQIGTTPGWGGKTFIVQGFGNVGLHTTRYLTRAGATCIGVIEHDGTLYNPEGIDPKLLEDYKNEHGTIVGYQNAKPYEGENLMFEKCDIFIPAAVEKVITSENANRIQAKIIAEAANGPTTPAADKILIDRNILVIPDLYINAGGVTVSFFEWLKNLNHVSYGRLTFKYERESNYHLLASVQQSIERIINDESVQESLERRFGRVGGRIPVTPSESFQKRISGASEKDIVHSGLDYTMERSARAIMKTAMKYNLGLDLRTAAYVNSIEKIFTTYRDAGLAF gdhA ignore SwissProt::P95544 NAD(P)-specific glutamate dehydrogenase; NAD(P)-GDH; NAD(P)H-dependent glutamate dehydrogenase; EC 1.4.1.3 MKATEVIEKLKAKFPGQPEYIQAVSQVLGTIEEEYNKHPEFEKANLIERLCVPDRILQFRVSWVDDNGNVQTNLGYRVQHNNAIGPYKGGLRFHKSVNASILKFLAFEQTFKNSLTTLPMGGAKGGSDFDPHGKSDMEVMRFCQAFMNELYRLIGPDEDVPAGDIGVGGREVGYMFGQYKKLTHQFQGILTGKGLEFGGSLIRPEATGYGNVYFLEDMLKTRGESLEGKTVLVSGSGNVAQYTIEKLLQLGAKPVTCSDSNGYIYDPDGIDAEKLAFIMELKNVKRGRIKEYAEKYGVKYVENARPWGEKADIATPCATQDEINEAEAKTLIANGVFAVSEGANMPTEPAAIKVFQDAKILYCPGKASNAGGVATSGLEMSQNSERLSWTREEVDTKLHNIMDEIHANCVKYGTEPDGYINYVKGANVAGFMKVAKAMMAQGIY gdhA ignore SwissProt::Q33E23 Glutamate dehydrogenase 2, mitochondrial; OsGDH2; EC 1.4.1.3 MNALAATSRNFRQAARLLGLDSKLEKSLLIPFREIKVECTIPKDDGTLASFIGFRVQHDNARGPMKGGIRYHPEVDPDEVNALAQLMTWKTAVAAIPYGGAKGGIGCAPGELSTSELERLTRVFTQKIHDLIGAHTDVPAPDMGTNSQTMAWILDEYSKFHGHSPAVVTGKPIDLGGSLGRDAATGRGVMYATEALLAEHGKSISGSTFVIQGFGNVGSWAARIIHEKGGKVIALGDVTGSIRNKNGLDIPALMKHRNEGGALKDFHDAEVMDSSELLVHECDVLIPCALGGVLNRENAPDVKAKFIIEAANHPTDPEADEILAKKGVTILPDIYANSGGVIVSYFEWVQNIQGFMWDEEKVNMELHKYMNNSFQHIKAMCKSHDCNLRMGAFTLGVNRVARATLLRGWEA gdhA ignore SwissProt::Q54KB7 Glutamate dehydrogenase, mitochondrial; GDH; EC 1.4.1.3 MQSLARLSRTSLVQKGLVPQTIKNYSSVSQAEIDNEPRFLECFKTFFDKAAGLTNLKPGVLNNMKECNVALRVEFPIKNEHGDVDIIAGYRAQHSHHRLPCKGGIRFSEEVDLQEVMALASLMTYKCAVVDVPFGGAKGGVRIDPKKYTVAQREKITRAYTLLLCQKNFIGPGVDVPAPDMGTGEQEMAWIRDTYQAFNTNDVDSMACVTGKPISSGGIRGRTEATGLGVFYGIREFLSYEEVLKKTGLTPGIKGKSIVIQGFGNVGYFAAKFFEQAGAKVIAVAEHNGAVYNADGLNIDALNKYKLQHGTFIDFPGATNIVDSVKALEIPCDILIPAALEKQIHIGNVADIQAKLIGEAANGPMTPRADQILLNRGHVIIPDLLLNAGGVTVSYFEWLKNLSHVRFGRLNKKWEESSKKLLLEFVESTVNKKLSEAERSLIIHGADEIDIVRSGLEDTMQNACAETRKTANEKNTDYRSAALYNAIMKIKAVYESSGNVFS gdhA ignore SwissProt::Q56304,BRENDA::Q56304 Glutamate dehydrogenase; GDH; EC 1.4.1.3;; glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3); glutamate dehydrogenase (NADP+) (EC 1.4.1.4) MVEQDPFEIAVKQLERAAQYMDISEEALEFLKRPQRIVEVSIPVEMDDGSVKVFTGFRVQYNWARGPTKGGIRWHPEETLSTVKALAAWMTWKTAVMDLPYGGGKGGVICNPKEMSDREKERLARGYVRAIYDVISPYTDIPAPDVYTNPQIMAWMMDEYETISRRKDPSFGVITGKPPSVGGIVARMDATARGASYTVREAAKALGMDLKGKTIAIQGYGNAGYYMAKIMSEEYGMKVVAVSDSKGGIYNPDGLNADEVLAWKKKTGSVKDFPGATNITNEELLELEVDVLAPSAIEEVITKKNADNIKAKIVAELANGPTTPEADEILYEKGILIIPDFLCNAGGVTVSYFEWVQNITGDYWTVEETRAKLDKKMTKAFWDVYNTHKEKNINMRDAAYVVAVSRVYQAMKDRGWIKK gdhA ignore SwissProt::Q6H3Y7 Glutamate dehydrogenase 3, mitochondrial; OsGDH3; EC 1.4.1.3 MNALAATSRNFRQAARLLGLDSKLQKSLLIPLREIKVECTIPKDDGTLATFVGFRVQHDNSRGPMKGGIRYHPEVDPDEVNALAQLMTWKTAVAAVPYGGAKGGIGCTPGELSRSELERLTRVFTQKIHDLIGINTDVPAPDMGTNAQTMAWILDEYSKFHGHSPAVVTGKPIDLGGSLGRDAATGRGVMYATEALLTEYSESISGSTFVIQGLGNVGSWAAKLIHQKGGKIVAVGDVTGAIRNKSGIDIPALLKHRSEGGSLEDFYGAEVMDAAELLVHECDVLVPCALGGVLNRENAAEVKARFIIEGANHPTDTEADEILAKKGVIVLPDIYANSGGVVVSYFEWVQNIQGFMWDEEKVNRELQKYMKNAFQNIKDMCKSQNCNLRMGAFTLGVNRVAKATLLRGWEA glmE curated SwissProt::P80077,metacyc::MONOMER-1101 Glutamate mutase epsilon subunit; Glutamate mutase E chain; Glutamate mutase large subunit; Methylaspartate mutase; EC 5.4.99.1;; GlmE MELKNKKWTDEEFHKQREEVLQQWPTGKEVDLQEAVDYLKKIPAEKNFAEKLVLAKKKGITMAQPRAGVALLDEHIELLRYLQDEGGADFLPSTIDAYTRQNRYDECENGIKESEKAGRSLLNGFPGVNYGVKGCRKVLEAVNLPLQARHGTPDSRLLAEIIHAGGWTSNEGGGISYNVPYAKNVTIEKSLLDWQYCDRLVGFYEEQGVHINREPFGPLTGTLVPPSMSNAVGITEALLAAEQGVKNITVGYGECGNMIQDIAALRCLEEQTNEYLKAYGYNDVFVTTVFHQWMGGFPQDESKAFGVIVTATTIAALAGATKVIVKTPHEAIGIPTKEANAAGIKATKMALNMLEGQRMPMSKELETEMAVIKAETKCILDKMFELGKGDLAIGTVKAFETGVMDIPFGPSKYNAGKMMPVRDNLGCVRYLEFGNVPFTEEIKNYNRERLQERAKFEGRDVSFQMVIDDIFAVGKGRLIGRPE glmE curated SwissProt::Q05509,BRENDA::Q05509 Glutamate mutase epsilon subunit; Glutamate mutase E chain; Glutamate mutase large subunit; Methylaspartate mutase; EC 5.4.99.1;; methylaspartate mutase (subunit 1/2) (EC 5.4.99.1) MELKNKKWTDEEFFKQREEVLKQWPTGKEVDLQEAVDYLKKVPTEKNFADKLVRAKEAGITLAQPRAGVALLDEHINLLRYLQDEGGADLLPSTIDAYTRQNRYEECEIGIKESEKAGRSLLNGFPGVNHGVKGCRKVLESVNLPLQARHGTPDSRLLAEIIHAGGWTSNEGGGISYNIPYAKSVPIDKCLKDWQYCDRLVGFYEEQGVHINREPFGPLTGTLVPPSMSNAVGITEALLAAEQGVKNITVGYGECGNMLQDIAALRCLEEQTNEYLKAYGYNDVFVTTVFHQWMGGFPQDESKAFGVIVTATTIASLAGATKVIVKTPHEAIGIPTKEANASGIKATKMALNMLEGQRMPMSKELETEMAIIKAETKCILDKMFELGKGDLAVGTVKAFETGVMDIPFGPSKYNAGKMMPVRDNLGCVRYLEFGNVPFTEELKNYNRERLAERAKFEGREVSFQMVIDDIFAVGKGRLIGRPENK glmE curated metacyc::MONOMER-16254 glutamate mutase β subunit (EC 5.4.99.1) MPTDERLSDDQLQRIANDLRDNWHTGREVDFEEAIAFHESLPASKQFAQVLESADQPLLQPRAGVPCLEEQIDLLRYLQDEGGADLLPTTIDSYTRDNEYEKAEEGLAASRGSDENELNGFPAVNHGVEDCRRLIRALDAPVEVRHGTPDARLLAMVTLAGGFQSFEGGPISYNIPYTKRHDLATTIEHWQFVDRLCGAYTERGVTINREPFGPLTGTLVPPSIAIAVMLVEGELAATQGVRSLTLGYGQVGNLVQDVAALRALRKLGNEYLRDEVTVTTVFHEWMGGFPPDEARANGVISLGGATAAVAQPDKVITKSAQEFQGVPTKEANAAGLRTTRQLIDMMIEQDIDLGGIDEEQALIERETRALMDAIYEAGDGDVAQGVINAFDSGALDVPFAPSDAAKGAVLPARDDDGRVRIFEFADLALPDDIKEIHAARLGERAETEGRDQSFRMVADDVDAISDGKLIGRPGGDNSPAGGASDAD glmS curated SwissProt::P80078,BRENDA::P80078 Glutamate mutase sigma subunit; Glutamate mutase S chain; Glutamate mutase small subunit; Methylaspartate mutase; EC 5.4.99.1;; methylaspartate mutase (EC 5.4.99.1) MEKKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQEVFIKAAIETKADAILLSSLYGQGEIDCKGLRQKCDEAGLEGILLYVGGNIVVGKQHWPDVEKRFKDMGYDRVYAPGTPPEVGIADLKKDLNIE glmS curated SwissProt::Q05488,BRENDA::Q05488 Glutamate mutase sigma subunit; Glutamate mutase S chain; Glutamate mutase small subunit; Methylaspartate mutase; EC 5.4.99.1;; methylaspartate mutase (subunit 2/2) (EC 5.4.99.1) MEKKTIVLGVIGSDCHAVGNKILDHSFTNAGFNVVNIGVLSSQEDFINAAIETKADLICVSSLYGQGEIDCKGLREKCDEAGLKGIKLFVGGNIVVGKQNWPDVEQRFKAMGFDRVYPPGTSPETTIADMKEVLGVE glmS curated metacyc::MONOMER-16253 glutamate mutase α subunit (EC 5.4.99.1) MTGKYMPRTVILGVIGSDAHVVGITILEQALSAAGFEVINLGVQTAQDEFVSAAKSHDAEAVLVSSLYGHARQDCEGLHDELDDAGLDVLTYVGGNLAVGQSDFEETQATFRQMGFDRVFDAETDPEEAIEMLREDLQLTTTEAEQIRVDG glnP curated TCDB::Q9CES5 Glutamine ABC transporter permease and substrate binding protein protein, component of Glutamine transporter, GlnQP. Takes up glutamine, asparagine and glutamate which compete for each other for binding both substrate and the transmembrane protein constituent of the system (Fulyani et al. 2015). Tandem substrate binding domains (SBDs) differ in substrate specificity and affinity, allowing cells to efficiently accumulate different amino acids via a single ABC transporter. Analysis revealed the roles of individual residues in determining the substrate affinity MKKLFFALAMMLATVTAFLVAPSVKAETTVKIASDSSYAPFEFQNGQKKWVGIDVDIMQEVAKINDWKLEMSYPGFDAALQNLKAGQVDGIIAGMTITDERKETFDFSNPYYTSALTIATTKDSKLSDYSDLKGKAVGAKNGTAAQTWLQENQKKYGYTIKTYSDGVHMFAALSSGNIAGAMDEVPVISYAMKQGQDLAMNFPSISLPGGYGFAVMKGKNSTLVDGFNKALAEMKSNGDYDKILKKYGITATKKATPKKDVYTIASDNSFAPFEFQNDDKQFTGIDVDLLNAIAKNQGFKLKWNFIGFQAAVDSVQSGHADGMMSGMSITDARKQVFDYGSPYYSSNLTIATSSTDDSIKSWKDLKGKTLGAKNGTASFDYLNAHAKEYGYTVKTFTDATTMYSSLNNGSINALMDDEPVIKYAIKQGQKFATPIKPIPDGQYGFAVKKGSNPELIEMFNNGLANLRANGEYDKIIDKYLESDAKTIQSSAKENTFFGILQNNWEQIGRGLLVTLELAILSFILAMIVGIIFGLFSVAPSKILRTIARIYVDLNRSIPLLVLTIFIFYGIPNLLQIITGHQSPLNEFTAGVIALTLNSSAYIAEIVRSGVQAVPSGQMEASRSLGVTYLTSMRKVILPQAIKITIPSLINQFIITLKDTTLVSVIGLVELLQTGQIIVARNFQAFRVYGLIGLVYMIVLLFLMWIGRRVEKRMK gltI curated CharProtDB::CH_002441,SwissProt::P37902,TCDB::P37902,ecocyc::G6359-MONOMER,metacyc::G6359-MONOMER glutamate-aspartate periplasmic-binding protein;; Glutamate/aspartate import solute-binding protein;; YBEJ aka GltI aka B0655, component of Glutamate/aspartate porter;; glutamate/aspartate ABC transporter periplasmic binding protein (EC 7.4.2.1);; glutamate/aspartate ABC transporter periplasmic binding protein (EC 7.4.2.1) MQLRKPATAILALALSAGLAQADDAAPAAGSTLDKIAKNGVIVVGHRESSVPFSYYDNQQKVVGYSQDYSNAIVEAVKKKLNKPDLQVKLIPITSQNRIPLLQNGTFDFECGSTTNNVERQKQAAFSDTIFVVGTRLLTKKGGDIKDFANLKDKAVVVTSGTTSEVLLNKLNEEQKMNMRIISAKDHGDSFRTLESGRAVAFMMDDALLAGERAKAKKPDNWEIVGKPQSQEAYGCMLRKDDPQFKKLMDDTIAQVQTSGEAEKWFDKWFKNPIPPKNLNMNFELSDEMKALFKEPNDKALN gltI curated TCDB::Q88NY2 PP1071, component of Acidic amino acid uptake porter, AatJMQP MMRIVRQLLGAAIAAAVIASPAMAEELTGTLKKIKESGTITLGHRDSSIPFSYLAGKPEPVGYSHDIQLAVVDALKKQLGTDIKVRYNLVTSQTRIPLVQNGTVDLECGSTTNNVERQQQVGFSVGIFEVGTRLLTKVKDGQPAYKDFPDLAGKNVVTTAGTTSERILKAMNADKQMKMNVISAKDHGEAFNMLESGRAVAFMMDDALLAGEMAKARKPADWVITGTPQSYEIYGCMVRKDDAAFKKAVDDAIVAYFKSGEVNKSYEKWFMQPIPPKGLNLNFQMSEELKKLIAEPTDKAADEKKS gltI curated TCDB::Q9I402 Probable binding protein component of ABC transporter, component of Amino acid transporter, AatJMQP. Probably transports L-glutamic acid, D-glutamine acid, L-glutamine and N-acetyl L-glutamic acid (Johnson et al. 2008). Very similar to 3.A.1.3.19 of P. putida MRIAPSLLSTAIVAALLSAPVVADELTGTLKKIKETGTITLGHRDASIPFSYLGTEPGKPIGYSHDLQLKVVEAVKKELNLPELKVRYNLVTSQTRIPLVQNGTVDIECGSTTNNEERQKQVDFSVGIFEVGTRLLSKKTANIKDFDDLKGKNVVTTAGTTSERLLKAMNADKKMGMNIISAKDHGESFMMLESGRAVAFMMDDALLYGEMAKAKKPDDWVVGGTPQSFEIYGCMVRKGDAAFKKVVDKAITDTYASGEVNKIYDKWFTQPIPPKGLNLNFPMSEELKKLIASPTDKAAEQM gltI curated reanno::pseudo1_N1B4:Pf1N1B4_771 ABC transporter for L-asparagine and L-glutamate, periplasmic substrate-binding component MRIVPHILGAAIAAALISTPVFAAELTGTLKKIKESGTITLGHRDASIPFSYIADASGKPVGYSHDIQLKIVEAIKKDLDMPNLQVKYNLVTSQTRIPLVQNGTVDVECGSTTNNVERQQQVDFSVGIFEIGTKLLSKKDSAYKDFADLKGKNVVTTAGTTSERILKSMNADKQMGMNVISAKDHGESFQMLETGRAVAFMMDDALLAGEMAKAKKPTDWAVTGTAQSNEIYGCMVRKGDAPFKKAVDDAIIATYKSGEINKIYEKWFMQPIPPKGLNLMFPMSEELKALIANPTDKAADEKKS gltI curated reanno::pseudo3_N2E3:AO353_16290 ABC transporter for L-aspartate, L-asparagine, L-glutamate, and L-glutamine, periplasmic substrate-binding component MRIVPHILGAAITAALISTPVFAAELTGTLKKIKESGTITLGHRDASIPFSYIADASGVPVGYSHDIQLKIVEAIKKDLDMPNLKVKYNLVTSQTRIPLVQNGTVDVECGSTTNNTERQQQVDFSVGIFEIGTKLLSKKDSTYKDFADLKGKNVVTTAGTTSERILKSMNADKQMGMNVISAKDHGESFQMLESGRAVAFMMDDALLAGEMAKAKSPTDWAVTGTAQSYEIYGCMVRKGDAPFKKAVDDAIVATYKSGEINTIYGKWFTQPIPPKNLNLMFPMSDELKALISNPTDKAAEEKKS gltI ignore reanno::pseudo13_GW456_L13:PfGW456L13_4770 ABC transporter for L-Asparagine and possibly other L-amino acids, periplasmic substrate-binding component MRIVPHILGAAIAAALISTPVFAAELTGTLKKIKESGTITLGHRDASIPFSYIADASGKPVGYSHDIQLKVVEALKKDLDMPNLQVKYNLVTSQTRIPLVQNGTVDLECGSTTNNVERQQQVDFSVGIFEIGTRLLSKADSKYKDFPDLAGKNVVTTAGTTSERILKAMNADKQMGMNVISAKDHGESFQMLETGRAVAFMMDDALLAGEAAKAKKASDWAVTGTPQSYEIYGCMVRKGDEPFKKAVDDAIKATYASGEINKIYEKWFMQPIPPKGLNLNFPMSDELKALIAKPTDKAADDKKS gltJ curated SwissProt::P0AER3,TCDB::P0AER3,ecocyc::GLTJ-MONOMER,metacyc::GLTJ-MONOMER Glutamate/aspartate import permease protein GltJ;; Glutamate/aspartate transport system permease protein GltJ aka B0654, component of Glutamate/aspartate porter;; glutamate/aspartate ABC transporter membrane subunit GltJ (EC 7.4.2.1);; glutamate/aspartate ABC transporter membrane subunit GltJ (EC 7.4.2.1) MSIDWNWGIFLQQAPFGNTTYLGWIWSGFQVTIALSICAWIIAFLVGSFFGILRTVPNRFLSGLGTLYVELFRNVPLIVQFFTWYLVIPELLPEKIGMWFKAELDPNIQFFLSSMLCLGLFTAARVCEQVRAAIQSLPRGQKNAALAMGLTLPQAYRYVLLPNAYRVIVPPMTSEMMNLVKNSAIASTIGLVDMAAQAGKLLDYSAHAWESFTAITLAYVLINAFIMLVMTLVERKVRLPGNMGGK gltJ curated TCDB::Q88NY3 PP1070, component of Acidic amino acid uptake porter, AatJMQP MNYNWDWGVFFKSTGVGSETYLDWYITGLGWTIAIAITAWIIALLLGSLLGVMRTVPNRLVSGIATAYVELFRNVPLLVQLFIWYFLVPDLLPEGLQEWFKQDLNPTTSALISVVICLGLFTAARVCEQVRTGIQALPKGQEAAARAMGFSLPQIYNNVLLPQAYRIIIPPLTSEFLNVFKNSSVASLIGLMELLAQTKQTAEFSANLFEAFTLATLIYFTLNMGLMLLMRMVEKKVAVPGLISVGGK gltJ curated TCDB::Q9I403 Amino acid ABC transporter membrane protein, component of Amino acid transporter, AatJMQP. Probably transports L-glutamic acid, D-glutamine acid, L-glutamine and N-acetyl L-glutamic acid (Johnson et al. 2008). Very similar to 3.A.1.3.19 of P. putida MNYNWDWGVFFKSTGIGSETYLDWYIAGLGWTIAIALVGWIIALALGSLLGVMRTVPNRLVSGIATAYVEIFRNVPLLVQLFIWYFLVPDLLPEGLQTWFKQDLNPTTSAYLSVVVCLGLFTAARVCEQVRTGIQALPYGQTSAARAMGFRLPQIYRHVLLPQAFRIIIPPLTSEFLNIFKNSSVASLIGLMELLAQTKQTAEFSANLFEAFTLATLIYFTLNMSLMLIMRLVERKVAVPGLISVGGK gltJ curated reanno::pseudo1_N1B4:Pf1N1B4_772 ABC transporter for L-asparagine and L-glutamate, permease component 1 MNYNWDWGVFFKSTGVGSEIYFDWYLSGLGWTIAIAVAAWIIALLLGSILGVMRTVPNRIVSGIATCYVELFRNVPLLVQLFIWYFLVPDLLPADIQEWYKQDLNPTTSAFLSVVVCLGLFTTARVCEQVRTGIQALPRGQEAAARAMGFKLPQIYWNVLLPQAYRIIIPPLTSEFLNVFKNSSVASLIGLMELLAQTKQTAEFSANLFEAFTLATLIYFTLNMSLMLLMRSVEKKVAVPGLISVGGK gltJ curated reanno::pseudo3_N2E3:AO353_16285 ABC transporter for L-aspartate, L-asparagine, L-glutamate, and L-glutamine, permease component 2 MNYNWDWGVFFKSTGVGSETYLDWFITGLGWTIAIAIVAWIIALMLGSVLGVMRTVPNRLVSGIATCYVELFRNVPLLVQLFIWYFLVPDLLPQNLQDWYKQDLNPTTSAYLSVVVCLGLFTAARVCEQVRTGIQALPRGQESAARAMGFKLPQIYWNVLLPQAYRIVIPPLTSEFLNVFKNSSVASLIGLMELLAQTKQTAEFSANLFEAFTLATLIYFTLNMSLMLLMRMVEKKVAVPGLISVGGK gltJ ignore reanno::pseudo13_GW456_L13:PfGW456L13_4771 ABC transporter for L-Asparagine and possibly other L-amino acids, permease component 1 MNYNWDWGVFFKSTGVGSETYFDWYVTGLAWTIGIAIAAWIIALTLGSILGVMRTVPNRIVSGIATCYVELFRNVPLLVQLFIWYFLVPDLLPADLQEWYKQDLNPTTSAFLSVVVCLGLFTTARVCEQVRTGIQALPKGQESAARAMGFKLPQIYWNVLLPQAYRIIIPPLTSEFLNVFKNTSVASLIGLMELLAQTKQTAEFSANLFEAFTLATLIYFTLNMSLMLLMRVVEKKVAVPGLISVGGK gltK curated SwissProt::P0AER5,TCDB::P0AER5,ecocyc::GLTK-MONOMER,metacyc::GLTK-MONOMER Glutamate/aspartate import permease protein GltK;; Glutamate/aspartate transport system permease protein GltK aka B0653, component of Glutamate/aspartate porter;; glutamate/aspartate ABC transporter membrane subunit GltK (EC 7.4.2.1);; glutamate/aspartate ABC transporter membrane subunit GltK (EC 7.4.2.1) MYEFDWSSIVPSLPYLLDGLVITLKITVTAVVIGILWGTMLAVMRLSSFAPVAWFAKAYVNVFRSIPLVMVLLWFYLIVPGFLQNVLGLSPKNDIRLISAMVAFSMFEAAYYSEIIRAGIQSISRGQSSAALALGMTHWQSMKLIILPQAFRAMVPLLLTQGIVLFQDTSLVYVLSLADFFRTASTIGERDGTQVEMILFAGFVYFVISLSASLLVSYLKRRTA gltK curated TCDB::Q88NY4 PP1069, component of Acidic amino acid uptake porter, AatJMQP MEMDFSEIIPALPALWEGMVMTLKLMVMGVIGGIVLGTILALMRLSSSKLLSNLAGAYVNYFRSIPLLLVITWFYLAVPFVLRWITGEDTPVGAFTSCVVAFMMFEAAYFCEIVRAGVQSISKGQMGAAQALGMNYAQTMRLIILPQAFRKMTPLLLQQSIILFQDTSLVYTVGLVDFLNSARSNGDIIGRSHEFLIFAGVVYFLISFSASWLVKRLQKRISV gltK curated TCDB::Q9I404 Amino acid ABC transporter membrane protein, component of Amino acid transporter, AatJMQP. Probably transports L-glutamic acid, D-glutamine acid, L-glutamine and N-acetyl L-glutamic acid (Johnson et al. 2008). Very similar to 3.A.1.3.19 of P. putida MMDFSGIVPALPSLWEGMLMTLKLMVLGVLGGVALGTVLALMRLSHSKLLSNIAGFYVNYFRSIPLLLVITWFYFAVPFILRWITGEDTPVGAFTSCLVAFMMFEAAYYCEIVRAGIQAIPKGQMGAAQALGMTYGQTMRLVILPQAFRKMTPLLLQQSIILFQDTSLVYTVGLMDFLNSARSRGDIIGQANEFLIFAGLVYFVVSFTASFAVKRLQKRLTV gltK curated reanno::pseudo1_N1B4:Pf1N1B4_773 ABC transporter for L-asparagine and L-glutamate, permease subunit 2 MEFDFSGIIPSLPGLWNGMIMTLKLMALGVIGGIILGTILALMRLSHNKLLSNIAGAYVNYFRSIPLLLVITWFYLAVPFVLRWITGEDTPIGAFASCIVAFMMFEAAYFCEIVRAGVQSIPKGQMGAAQALGMEYGQMMRLIILPQAFRKMTPLLLQQSIILFQDTSLVYAVGLVDFLNASRASGDIIGRSNEFLIFAGLTYFTISFAASLLVKRLQKRFAV gltK curated reanno::pseudo3_N2E3:AO353_16280 ABC transporter for L-aspartate, L-asparagine, L-glutamate, and L-glutamine, permease component 1 MDLDFSGVVQAVPGMWNGMVMTLQLTVLGVVGGIILGTLLALMRLSHSKLLSNIAGAYVNYFRSIPLLLVITWFYLAVPFVLRWITGEDTPIGAFTSCIVAFMMFEAAYFCEIVRAGVQSIPKGQMGAAKALGMGYGQMMRLIILPQAFRKMTPLLLQQSIILFQDTSLVYTVGLVDFLNATRASGDIIGRANEFLIIAGLVYFTISFAASRLVKRLQKRFAV gltK ignore reanno::pseudo13_GW456_L13:PfGW456L13_4772 ABC transporter for L-Asparagine and possibly other L-amino acids, permease component 2 MEFDFSGIIPSLPGLWNGMIMTLKLMAMGVIGGIILGTILALMRLSHNKVLSNIAGAYVNYFRSIPLLLVITWFYLAVPFVLRWITGEDTPIGAFASCIVAFMMFEAAYFCEIVRAGVQSIPKGQMGAAQALGMSYGQMMRLIILPQAFRKMTPLLLQQSIILFQDTSLVYAVGLVDFLNASRASGDIIGRSNEFLIFAGLVYFIISFAASQLVKRLQKRFAV gltL curated TCDB::A3ZI83 PEB1C, component of Uptake system for glutamate and aspartate MIELKNVNKYYGTHHVLKNINLSVKEGEKLVIIGPSGSGKSTTIRCMNGLEEVSSGEVVVNNLVLNHKNKIEICRKYCAMVFQHFNLYPHMTVLQNLTLAPMKLQKKSKKEAEETAFKYLKVVGLLDKANVYPATLSGGQQQRVAIARSLCTKKPYILFDEPTSALDPETIQEVLDVMKEISHQSNTTMVVVTHEMGFAKEVADRIIFMEDGAIVEENIPSEFFSNPKTERARLFLGKILKN gltL curated TCDB::P0AAG3,ecocyc::GLTL-MONOMER,metacyc::GLTL-MONOMER Glutamate/aspartate transport ATP-binding protein GltL aka B0652, component of Glutamate/aspartate porter;; glutamate/aspartate ABC transporter ATP binding subunit (EC 7.4.2.1);; glutamate/aspartate ABC transporter ATP binding subunit (EC 7.4.2.1) MITLKNVSKWYGHFQVLTDCSTEVKKGEVVVVCGPSGSGKSTLIKTVNGLEPVQQGEITVDGIVVNDKKTDLAKLRSRVGMVFQHFELFPHLSIIENLTLAQVKVLKRDKAPAREKALKLLERVGLSAHANKFPAQLSGGQQQRVAIARALCMDPIAMLFDEPTSALDPEMINEVLDVMVELANEGMTMMVVTHEMGFARKVANRVIFMDEGKIVEDSPKDAFFDDPKSDRAKDFLAKILH gltL curated TCDB::P48243 GluA aka CGL1950, component of Glutamate porter MIKMTGVQKYFGDFHALTDIDLEIPRGQVVVVLGPSGSGKSTLCRTINRLETIEEGTIEIDGKVLPEEGKGLANLRADVGMVFQSFNLFPHLTIKDNVTLAPIKVRKMKKSEAEKLAMSLLERVGIANQADKYPAQLSGGQQQRVAIARALAMNPKIMLFDEPTSALDPEMVNEVLDVMASLAKEGMTMVCVTHEMGFARKAADRVLFMADGLIVEDTEPDSFFTNPKSDRAKDFLGKILAH gltL curated TCDB::Q52666 BztD, component of Glutamate/glutamine/aspartate/asparagine porter MSEPSYDHQVDRSHMQVSDEIAIQISQMNKWYGQFHVLRDINLTVHRGERIVIAGPSGSGKSTMIRCINRLEEHQSGKIIVDGIELTSDLKNIDKVRSEVGMVFQHFNLFPHLTILENLTLAPIWVRKVPKREAEETAMYYLEKVKIPEQAQKYPGQLSGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMIKEVLDTMIQLAEEGMTMLCVTHEMGFAQAVANRVIFMADGQIVEQNNPHDFFHNPQSERTKQFLSQILGH gltL curated TCDB::Q88NY5 PP1068, component of Acidic amino acid uptake porter, AatJMQP MAGQAPAKKDLRMISIKNVNKWYGDFQVLTDCSTEVKKGEVVVVCGPSGSGKSTLIKCVNALEPFQKGDIVVDGTSIADPKTNLPKLRSRVGMVFQHFELFPHLTITENLTIAQRKVLGRSEAEATKKGLALLDRVGLSAHAKKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVSEVLDVMVQLAQEGMTMMCVTHEMGFARKVANRVIFMDKGSIIEDCTKEEFFGDQSARDQRTQHLLSKILQH gltL curated TCDB::Q9CES4 Glutamine ABC transporter ATP-binding protein, component of Glutamine transporter, GlnQP. Takes up glutamine, asparagine and glutamate which compete for each other for binding both substrate and the transmembrane protein constituent of the system (Fulyani et al. 2015). Tandem substrate binding domains (SBDs) differ in substrate specificity and affinity, allowing cells to efficiently accumulate different amino acids via a single ABC transporter. Analysis revealed the roles of individual residues in determining the substrate affinity MGINTQIEVTDLHKSFGKNEVLKGITTKFEKGDVVCIIGPSGSGKSTFLRALNGLETATSGDIIIDGFNLTDKNTNLNLVRQNVGMVFQHFNLFPNMTVMQNITYAPVELKKMSKDDADKKAIQLLETVGLLDKKDAMPEMLSGGQKQRVAIARALAMNPDVMLFDEPTSALDPEMVGDVLAVMQKLAEEGMTMLIVTHEMGFARKVANRVIFTDGGVILEDGTPEELFDSPKHPRLQDFLSKVLNA gltL curated TCDB::Q9I405 Amino acid ABC transporter ATP binding protein, component of Amino acid transporter, AatJMQP. Probably transports L-glutamic acid, D-glutamine acid, L-glutamine and N-acetyl L-glutamic acid (Johnson et al. 2008). Very similar to 3.A.1.3.19 of P. putida MISIKNVSKWYGDFQVLTDCSTEVAKGEVVVVCGPSGSGKSTLIKCVNALEPFQKGDIVVDGTSIADPKTNLPKLRSRVGMVFQHFELFPHLSITENLTIAQIKVLGRSKEEATKKGLALLERVGLKEHAHKHPGQLSGGQQQRVAIARALAMDPVVMLFDEPTSALDPEMVNEVLDVMVQLAHEGMTMMCVTHEMGFARKVANRVIFMDRGQIVEDCEKEEFFGDVSARSERAQQFLAKILPH gltL curated reanno::pseudo1_N1B4:Pf1N1B4_774 ABC transporter for L-asparagine and L-glutamate, ATPase component MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLPKLRSRVGMVFQHFELFPHLSIMDNLTIAQVKVLGRSKEEASKKALQLLERVGLSAHAKKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAHEGMTMMCVTHEMGFARKVADRVIFMDQGKIIEDCKKEEFFGDITARSDRAQHFLEKILQH gltL curated reanno::pseudo3_N2E3:AO353_16275 ABC transporter for L-aspartate, L-asparagine, L-glutamate, and L-glutamine, ATPase component MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVVVDGTSIADPKTDLPKLRSRVGMVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLERVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLANEGMTMMCVTHEMGFARKVADRVIFMDQGKIIEDCKKEEFFGDINARSDRAQHFLDKILQH gltL ignore TCDB::Q52815 AapP, component of General L-amino acid porter; transports basic and acidic amino acids preferentially, but also transports aliphatic amino acids (catalyzes both uptake and efflux) MAEAPAKKLTVSATEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDEVRREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNEPAAFFDNPQHERTKLFLSQILH gltL ignore reanno::Smeli:SMc02121 ABC transporter for L-Glutamine, L-Histidine, and other L-amino acids, ATPase component MANTATAPKLAVSTTDVAIEITNMNKWYGDFHVLRDINLRVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEVRREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKEAEQVAMHFLERVKIPEQALKYPGQLSGGQQQRVAIARSLCMRPKILLFDEPTSALDPEMVKEVLDTMVGLAEEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFLSQILH gltL ignore reanno::pseudo13_GW456_L13:PfGW456L13_4773 ABC transporter for L-Asparagine and possibly other L-amino acids, putative ATPase component MISIKSINKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDIVVDGTSIADPKTNLPKLRSRVGMVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLERVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAHEGMTMMCVTHEMGFARKVADRVIFMDQGKIIEDCKKEEFFGDINARAERTQHFLNKILQH gltP uniprot A1S570 SubName: Full=Sodium:dicarboxylate symporter {ECO:0000313|EMBL:ABL99526.1}; MAAAQSSKIGLTGKILIGMGAGILIGLLLRNFFGGSEWVQDYITEGFFHVIGTIFINSLKMLVVPLVFISLVCGTCSLSEPSKLGRLGGKTLAFYLFTTAIALVVAISAAVLVQPGNASLASESMQYSAKEAPSLADVLINIVPSNPMKALSEGNMLQIIIFAVIFGFAISHIGERGRRVAALFDDLNEVIMRVVTLIMQLAPYGVFALMGKLALTLGMETLESVIKYFMLVLVVLLFHGFVVYPTLLKLFSGLSPLMFIRKMRDVQLFAFSTASSNATLPVTMEASEHRLGADNKVASFTLPLGATINMDGTAIMQGVATVFIAQVFGIDLTITDYAMVVMTATLASIGTAGVPGVGLVMLAMVLNQVGLPVEGIALILGVDRMLDMVRTAVNVTGDTVATVVIAKSEGALNEAVFNDPKAGKTAGSFDAEVHRGE gltP uniprot L0GT47 SubName: Full=Na+/H+ dicarboxylate symporter {ECO:0000313|EMBL:AGA88545.1}; MTQSTTLSAPLRLLVRLPLWQQILIGLALGVAAGMAFGADAQLLAPIGTLFLNAIKMLIVPLVFVSLVAGITSMQDSAKLGRISLKTIAIYLVTTAFAVSIGLLFGALFSPGEGMNMVASGNEQAKQAPSLVSILVGLVPANPVTAFAEGNILQIIVFAIALGVSINLIGERGAPAVRLFDALAETFYKLTDLVMRVAPIGVFALTAGVVGSHGAEVLLPLAGVIGVIYLASIAHVLLVYGGLLGLLARLNPLRFFQGIAPALAVAFSTSSSSGTLPVSIECARKNLGVSEGVAGFVLPVGATINMDGTAIYQGVLALFIAQAFGIDLSAGQYAMIILTATLASIGTAGIPGAGLIMLGLVLTAAGLPLEGVALIAGIDRILDMARTTVNVAGDLMTTTLVGRSEQELDRAIYDSSNKE gltP curated CharProtDB::CH_088342,SwissProt::P24944 proton/sodium-glutamate symport protein GltT;; Proton/sodium-glutamate symport protein; Glutamate-aspartate carrier protein MRKIGLAWQIFIGLILGIIVGAIFYGNPKVAAYLQPIGDIFLRLIKMIVIPIVISSLVVGVASVGDLKKLGKLGGKTIIYFEIITTIAIVVGLLAANIFQPGAGVNMKSLEKTDIQSYVDTTNEVQHHSMVETFVNIVPKNIFESLSTGDMLPIIFFSVMFGLGVAAIGEKGKPVLQFFQGTAEAMFYVTNQIMKFAPFGVFALIGVTVSKFGVESLIPLSKLVIVVYATMLFFIFAVLGGVAKLFGINIFHIIKILKDELILAYSTASSETVLPRIMDKMEKFGCPKAITSFVIPTGYSFNLDGSTLYQALAAIFIAQLYGIDMSVSQQISLLLVLMVTSKGIAGVPGVSFVVLLATLGTVGIPVEGLAFIAGIDRILDMARTAVNVIGNSLAAIIMSKWEGQYNEEKGKQYLAELQQSA gltP curated SwissProt::P21345,TCDB::P21345,ecocyc::GLTP-MONOMER Proton/glutamate-aspartate symporter; Glutamate-aspartate carrier protein; Proton-glutamate-aspartate transport protein;; Glutamate/aspartate:H+ symporter, GltP or GltT; has 8 TMSs with 2 re-entrant loops as for GltPh (TC# 2.A.23.1.5);; glutamate/aspartate : H+ symporter GltP MKNIKFSLAWQILFAMVLGILLGSYLHYHSDSRDWLVVNLLSPAGDIFIHLIKMIVVPIVISTLVVGIAGVGDAKQLGRIGAKTIIYFEVITTVAIILGITLANVFQPGAGVDMSQLATVDISKYQSTTEAVQSSSHGIMGTILSLVPTNIVASMAKGEMLPIIFFSVLFGLGLSSLPATHREPLVTVFRSISETMFKVTHMVMRYAPVGVFALIAVTVANFGFSSLWPLAKLVLLVHFAILFFALVVLGIVARLCGLSVWILIRILKDELILAYSTASSESVLPRIIEKMEAYGAPVSITSFVVPTGYSFNLDGSTLYQSIAAIFIAQLYGIDLSIWQEIILVLTLMVTSKGIAGVPGVSFVVLLATLGSVGIPLEGLAFIAGVDRILDMARTALNVVGNALAVLVIAKWEHKFDRKKALAYEREVLGKFDKTADQ gltP curated SwissProt::P24943,CharProtDB::CH_088341,TCDB::P24943 Proton/sodium-glutamate symport protein; Glutamate-aspartate carrier protein;; proton/sodium-glutamate symport protein GltT;; Glutamate/aspartate:Na+ + H+ symporter MRKIGLAWQIFIGLILGIIVGAIFYGNPKVATYLQPIGDIFLRLIKMIVIPIVISSLVVGVASVGDLKKLGKLGGKTIIYFEIITTIAIVVGLLAANIFQPGTGVNMKSLEKTDIQSYVDTTNEVQHHSMVETFVNIVPKNIFESLTKGDMLPIIFFSVMFGLGVAAIGEKGKPVLQFFQGTAEAMFYVTNQIMKFAPFGVFALIGVTVSKFGVESLIPLSKLVIVVYATMVFFIFVVLGGVAKLFGINIFHIIKILKDELILAYSTASSETVLPKIMEKMENFGCPKAITSFVIPTGYSFNLDGSTLYQALAAIFIAQLYGIDMPISQQISLLLVLMVTSKGIAGVPGVSFVVLLATLGTVGIPIEGLAFIAGIDRILDMARTAVNVIGNSLAAIIMSKWEGQYNEEKGKQYIAQLQQSA gltP curated SwissProt::P39817 Proton/glutamate-aspartate symporter; Proton/glutamate symport protein MKKLIAFQILIALAVGAVIGHFFPDFGMALRPVGDGFIRLIKMIVVPIVFSTIVIGAAGSGSMKKMGSLGIKTIIWFEVITTLVLGLGLLLANVLKPGVGLDLSHLAKKDIHELSGYTDKVVDFKQMILDIIPTNIIDVMARNDLLAVIFFAILFGVAAAGIGKASEPVMKFFESTAQIMFKLTQIVMVTAPIGVLALMAASVGQYGIELLLPMFKLVGTVFLGLFLILFVLFPLVGLIFQIKYFEVLKMIWDLFLIAFSTTSTETILPQLMDRMEKYGCPKRVVSFVVPSGLSLNCDGSSLYLSVSCIFLAQAFQVDMTLSQQLLMMLVLVMTSKGIAAVPSGSLVVLLATANAVGLPAEGVAIIAGVDRVMDMARTGVNVPGHAIACIVVSKWEKAFRQKEWVSANSQTESI gltP ignore SwissProt::O59010,TCDB::O59010 Glutamate transporter homolog; Glt(Ph); Sodium-aspartate symporter Glt(Ph); Sodium-dependent aspartate transporter;; Archaeal aspartate transporter, Gltph (GltPh) (3-D structure known; 3V8F and 3V8G) (Boudker et al., 2007; Yernool et al., 2004). Cotransports aspartate with 2 Na+ (Ryan et al., 2009) or 3 Na+ (Groeneveld and Slotboom, 2010) or 1Na+ plus 1 H+ plus 1 K+ MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYADAVKTYVKPFGDLFVRLLKMLVMPIVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQQFQPKQAPPLVKILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSAETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVKVVGELAKVTAAVYVGLTLQILLVYFVLLKIYGIDPISFIKKAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYSFTLPLGATINMDGTALYQGVCTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGAIMLAMVLESVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGELEKGVIA gltS curated SwissProt::P0AER8,TCDB::P0AER8,ecocyc::GLTS-MONOMER Sodium/glutamate symporter; Glutamate permease;; Glutamate:Na+ symporter (transports L- and D-glutamate, α-methylglutamate and homocysteate). Swapping the order of the two halves (repeat units) does not decrease activity;; glutamate:sodium symporter MFHLDTLATLVAATLTLLLGRKLVHSVSFLKKYTIPEPVAGGLLVALALLVLKKSMGWEVNFDMSLRDPLMLAFFATIGLNANIASLRAGGRVVGIFLIVVVGLLVMQNAIGIGMASLLGLDPLMGLLAGSITLSGGHGTGAAWSKLFIERYGFTNATEVAMACATFGLVLGGLIGGPVARYLVKHSTTPNGIPDDQEVPTAFEKPDVGRMITSLVLIETIALIAICLTVGKIVAQLLAGTAFELPTFVCVLFVGVILSNGLSIMGFYRVFERAVSVLGNVSLSLFLAMALMGLKLWELASLALPMLAILVVQTIFMALYAIFVTWRMMGKNYDAAVLAAGHCGFGLGATPTAIANMQAITERFGPSHMAFLVVPMVGAFFIDIVNALVIKLYLMLPIFAG gltS curated TCDB::P73275 Glutamate:Na+ symporter METIQFNIRQTIIVAILVLYIGKYLTKKIKFLQSFNIPDAVSGGVLASLFFGLIYGIFRTEVAFNFPIRDAFLIIFFTCIGLSSKLKVLLQGGKPLLILLATAVSFLVIQNFVGVGMASLLGQALPVGLLSGSISLSGGHGTAIAWSPVFYDNHGIRNASEIAIACATFGLVFGGIVGGPIAKFLIIRNKLEPDCDTKDLTIGIRRDQDNVQIDYNTMLHTILVIGVTIGLGYEINDLVAKLGLMLPAFVSCLLAGIVLTNTIPLAFKKFPWPAETPSLALISDVSLGLFLAISLMSLQLWTLADIGGVIALILLVQFMATVLYSIAVVFPLMGRDYNAAVVCSGYSGLTLGATPTAIANMTAVTEKFGAAPQAFIVVPLVGAFFIDIANAFVIQQFLNFLG gltS curated TCDB::Q9HZ58 Probable L-glutamate/N-acetylglutamate uptake porter, GltS.  Involved in N-acetylglutamate catabolism as a carbon and nitrogen source MPTLHLDALSTTALALLLLALGSQLKKRSRWLTRLCVPSPVIAGFGFAFLVWLLRDRGWLDIGLDTSLQTPLMVAFFTTVGLGGSLGLLRKGGKTLLVYLSACWALAILQNLIGVGSAGLLGLDPLLGIMAGAVSLEGGFGAAAAFGPVAEGLGAQGATTVALASATFGMVAGGLLGSPVARWLIERNRLPVQAESDNRLEALGQQERRQHAAATLDGNLLLRLLTCVLLVMVLGFWLGDALEERLGLVLPSYVGAMFIAIVLRNLDDRLGWLRIPDHAVGTLGDVCLGIFLTMAMMSLKFWELENLGLPLLGVLFIQVAVLLLLTIFVLFRLLGRNYDAAVLCAGFLGHGLGATPNAVANMGAVCEHYRVFSHKAFIIVPLCGAVLIDLVAIPAITWFINAFS gltS_Syn curated TCDB::B1XKD9 Glutamate:sodium symporter, GltS MFTLRDVFFAFILIALLVLAGRYVKQKVRWIQRLYLPESIVAGVLALLLGPQVLGAIATAISGGTSILSDGLFSEPIRAVWSQSPGIFINIVFAALFLGEAIPRPKDIWTKTAPQVVFGQTLAWGQYVVGILVTLLILMPLFGVNPIAACLIEIGFEGGHGTAGGMAETFTELGFEAGADLALGIATVGIVGGIVAGTALADWGRRKGHVTSFQKAVEDLDGVPELTETESPEVRRRRAQLMRNLLIDPLSINFGIVGAAIVIGWLILEALVWVESVTWGQTGFEVISYVPLFPMALIGGIIVQLVMERLGLAPLIIRSLMSNIAGLALDVVVVTALASISLSVIGSNLGVFTILSVVGITWNVVMFLYFAPRIFPSHWFEKGIGDMGQSMGVTATGILLLRMVDPENRTGAFESFAYKQLFFEPIVGGGLFTAAAPALVVRFGLVPVLLLTGGLLIFWLAMGFLIIRQNQQQRRRSPSL gluB curated TCDB::P48242 GluB aka CGL1951, component of Glutamate porter MSAKRTFTRIGAILGATALAGVTLTACGDSSGGDGFLAAIENGSVNVGTKYDQPGLGLRNPDNSMSGLDVDVAEYVVNSIADDKGWDHPTIEWRESPSAQRETLIQNGEVDMIAATYSINAGRSESVNFGGPYLLTHQALLVRQDDDRIETLEDLDNGLILCSVSGSTPAQKVKDVLPGVQLQEYDTYSSCVEALSQGNVDALTTDATILFGYSQQYEGDFRVVEMEKDGEPFTDEYYGIGLKKDDQEGTDAINAALERMYADGTFQRLLTENLGEDSVVVEEGTPGDLSFLDAS gluC curated TCDB::P48244 GluC aka CGL1952, component of Glutamate porter MSTLWADLGPSLLPAFWVTIKLTIYSAIGAMIFGTILTTMRVSPVKILRTLSTAYINTVRNTPLTLVVLFCSFGLYQNLGLTLAGRESSTFLVDNNFRLAVLGFILYTSTFVAESLRSGINTVHFGQAEAARSLGLGFGATFRSIIFPQAVRAAIVPLGNTLIALTKNTTIASVIGVGEASLLMKATIENHANMLFVVFAIFAVGFMILTLPMGLGLGKLSERLAVKK gluD curated TCDB::P48245 GluD aka CGL1953, component of Glutamate porter MLSGNGQLDANKWTPFINSQTWTTYILPGLWGTLKSAVFSVILALVMGTALGLGRISEIRILRWFCAVIIETFRAIPVLILMIFAYQMFAQYNIVPSSQLAFAAVVFGLTMYNGSVIAEILRSGIASLPKGQKEAAIALGMSSRQTTWSILLPQAVAAMLPALISQMVIALKDSALGYQIGYIEVVRSGIQSASVNRNYLAALFVVALIMIVLNFSLTALASRIERQLRAGRARKNIVAKVPEQPDQGLETKDNVNVDWQDPDYKDLKTPGVQ gtrA curated TCDB::P74225 GtrA aka SLL1102, component of Tripartite glutamate:Na+ symporter MDKLLKIAQLIDQFTAWIGKFTAWLVLAMVLTGGWNVVGRYLGRLVGQNLASNGLLEAQWYLFDLVFLLGAAYTLQTNDHVRVDIFYKSLGDRQRAWVNLLGTCLFLFPFCGLVIFYSWESVINSWHIWETSPDPGGLPRYPIKTMIIVGFVLLIFQGIAEVIKNLAIALGHVDTEARG gtrB curated TCDB::P74224 GtrB aka SLL1103, component of Tripartite glutamate:Na+ symporter MVDYDWLGPMMFVGALVFLGCGYPVAFSLGGVAILFAIIGAALGSFDPIFLSAMPQRIFGIMANGTLLAIPFFIFLGSMLERSGIAEQLLETMGIILGHLRGGLALAVILVGTMLAATTGVVAATVVAMGLISLPIMLRYGYSKELASGVIVASGTLGQIIPPSVVLIVLADQLGVSVGDLFIGSLLPGLMMAGSFALYVLIIAWLKPDLAPALPAEVRNIGGQELRRRIVQVMLPPLVLILLVLGSIFFGIASPTEAGAVGSIGAIALAHFNQRLNWKALWEVCDATLRITSMVMLILLGSTAFSLVFRGLEGDRFMFDLLANLPGGQIGFLAISMITIFILGFFIDFFEIAFIVLPLFKPVAEALNLDLIWYGVIVGANLQTSFLTPPFGFALFYLRGVAPASLTTGQIYRGAVPFIGLQVLVLLLIIIFPALINWLPSLSVQ gtrC curated TCDB::P74223 GtrC aka GLNH aka SLL1104, component of Tripartite glutamate:Na+ symporter MFNKVINFLPMGKFFCFFTYTTLSMRSLIVASCLLFLIPGLTVSATAQTMVLETNGIAMTSREVSLEAIRQRGKLRVGVKDNLRPLGFRDGQGELTGLEIALARRLALALLGDETAVELVPVQNQDRLPLLLNGDVDLIIAQMGQNPARDRLVDFSPPYYMDGVGLISKNSSLKNIDRNQAHTIAVLNNSGTIPVIKQAFPQATLVGVDSYDQAYQILEQGQAMAFAGDNSVLSGWAQSQSDYYHLPLQLTVNPLAIAMAKGLQHQALQREVNQTLLQLRASGWLRQQWQAWGLPF mal hmm TIGR01502 methylaspartate ammonia-lyase (EC 4.3.1.2) TIGR01502.hmm mal curated SwissProt::O66145 Methylaspartate ammonia-lyase; MAL; 3-methylaspartate ammonia-lyase; Beta-methylaspartase; EC 4.3.1.2 MKIKQALFTAGYSSFYFDDQQAIKNGAGHDGFIYTGDPVTPGFTSVRQAGECVSVQLILENGAVAVGDCAAVQYSGAGGRDPLFLAEHFIPFLNDHIKPLLEGRDVDAFLPNARFFDKLRIDGNLLHTAVRYGLSQALLDATALASGRLKTEVVCDEWQLPCVPEAIPLFGQSGDDRYIAVDKMILKGVDVLPHALINNVEEKLGFKGEKLREYVRWLSDRILSLRSSPRYHPTLHIDVYGTIGLIFDMDPVRCAEYIASLEKEAQGLPLYIEGPVDAGNKPDQIRMLTAITKELTRLGSGVKIVADEWCNTYQDIVDFTDAGSCHMVQIKTPDLGGIHNIVDAVLYCNKHGMEAYQGGTCNETEISARTCVHVALAARPMRMLIKPGMGFDEGLNIVFNEMNRTIALLQTKD mal curated SwissProt::Q05514,BRENDA::Q05514,metacyc::MONOMER-1103 Methylaspartate ammonia-lyase; MAL; 3-methylaspartase ammonia-lyase; Beta-methylaspartase; EC 4.3.1.2;; methylaspartate ammonia-lyase (EC 4.3.1.2);; methylaspartase subunit (EC 4.3.1.2) MKIVDVLCTPGLTGFYFDDQRAIKKGAGHDGFTYTGSTVTEGFTQVRQKGESISVLLVLEDGQVAHGDCAAVQYSGAGGRDPLFLAKDFIPVIEKEIAPKLIGREITNFKPMAEEFDKMTVNGNRLHTAIRYGITQAILDAVAKTRKVTMAEVIRDEYNPGAEINAVPVFAQSGDDRYDNVDKMIIKEADVLPHALINNVEEKLGLKGEKLLEYVKWLRDRIIKLRVREDYAPIFHIDVYGTIGAAFDVDIKAMADYIQTLAEAAKPFHLRIEGPMDVEDRQKQMEAMRDLRAELDGRGVDAELVADEWCNTVEDVKFFTDNKAGHMVQIKTPDLGGVNNIADAIMYCKANGMGAYCGGTCNETNRSAEVTTNIGMACGARQVLAKPGMGVDEGMMIVKNEMNRVLALVGRRK mal curated SwissProt::Q3AEU2,BRENDA::Q3AEU2 Methylaspartate ammonia-lyase 1; MAL; 3-methylaspartate ammonia-lyase 1; Beta-methylaspartase 1; EC 4.3.1.2;; methylaspartate ammonia-lyase (EC 4.3.1.2) MRIKDVLFVKGSSGFYFDDQKAIKSGAVTDGFTYKGKPLTPGFSRVRQGGEAVSIMLFLENGEIAVGDCVAVQYSGVDGRDPVFLADNFIEVLEEEIKPRLVGYNLVRFREAARYFTNLTDKRGKRYHTALRYGLTQALLDAVAKINRTTMAEVIAEEYGLDLTLNPVPLFAQSGDDRYINADKMILKRVDVLPHGLFNHPAKTGEEGKNLTEYALWLKQRIKTLGDHDYLPVFHFDVYGTLGTVFNDNLDRIADYLARLEEKVAPHPLQIEGPVDLGSKERQIEGLKYLQEKLITLGSKVIIVADEWCNNLSDIKEFVDAGAGGMVQIKSPDLGGVNDIIEAVLYAKEKGTGAYLGGSCNETDVSAKITVHVGLATGPAQLLVKPGMGVDEGLTIMRNEMMRTLAILQRNKVTFQKKVG mal curated metacyc::MONOMER-16255 methylaspartate ammonia-lyase (EC 4.3.1.2) MRIEDVRTVPGLSGFFFDDQQAIKDGATQTGFAYDGQPVTDGFDRIREAGEALIVEIELADGSIATGDCAAVQYSGAGGRDPLFRAEKYRPVVEGAVADALRGQDATQFGANATMLEEMSPQRSGGDQLHTAVRYGVSQALLNAAAQARGVTPTDVLADTYDTEPATSPVPVFGQSGDERRINAEKMLIKGVPVLPHGLFNSVEKVGENGEGLRDYLAWLSDRATALGPEPYSPRFHVDVYGILGKVFGPPYDRTEVTDYFETLREAAAPYPLQVEGPMDAGGRQAQITEMAELREGLADAGVDVDIVADEWCNTFEDVQAFVDAEAADLVQIKTPDLGGIQRSAEAVLYCDGTDTRAYVGGTCNETVTSARACAHVALATDAAQVLAKPGMGFDEGFMVVTNEMRRALARRDATQEVPADD mal curated2 O66145 Methylaspartate ammonia-lyase; MAL; EC 4.3.1.2; 3-methylaspartate ammonia-lyase; Beta-methylaspartase MKIKQALFTAGYSSFYFDDQQAIKNGAGHDGFIYTGDPVTPGFTSVRQAGECVSVQLILENGAVAVGDCAAVQYSGAGGRDPLFLAEHFIPFLNDHIKPLLEGRDVDAFLPNARFFDKLRIDGNLLHTAVRYGLSQALLDATALASGRLKTEVVCDEWQLPCVPEAIPLFGQSGDDRYIAVDKMILKGVDVLPHALINNVEEKLGFKGEKLREYVRWLSDRILSLRSSPRYHPTLHIDVYGTIGLIFDMDPVRCAEYIASLEKEAQGLPLYIEGPVDAGNKPDQIRMLTAITKELTRLGSGVKIVADEWCNTYQDIVDFTDAGSCHMVQIKTPDLGGIHNIVDAVLYCNKHGMEAYQGGTCNETEISARTCVHVALAARPMRMLIKPGMGFDEGLNIVFNEMNRTIALLQTKD mal curated2 Q3AEJ6 Methylaspartate ammonia-lyase 2; MAL; EC 4.3.1.2; 3-methylaspartate ammonia-lyase 2; Beta-methylaspartase 2 MKIIDALFAPGLTGFYFDDQEAIKKGAVHNGFWYEGNPQTPGYKRIRQKGEAILVMLVLENGEVAYGDCAAVQYSGTGGRDPLFTAEEFLPILENEIRPKLIGLELNSFRNLAHIFDRELTVNGKPLHTALRYGLTQALLDGVARAQKKLMAEVIAEEYQLPVIPEPVPIFVQTGDDLYTNADKAIIKRADVLPHALINNVEEKLGRQGEKLLAYIKWLKKRIFELAGDEYRPVIHIDVYGTVGLIFANDLEKIAGYLATLAHEAAPFKLRIEGPVDMGSLWGQIEALSKLREIIDRRGIPVEIVADEWCNTLEDIKLFADHKAGHMVQIKTPDLGGINNVVEAVLYAKMKGIGAYLGGTCNETDRSAQISVHLALATRPDQMLAKPGMGLDEGLMIVYNEMQRAIALLKRRGGK mal curated2 Q3AEU2 Methylaspartate ammonia-lyase 1; MAL; EC 4.3.1.2; 3-methylaspartate ammonia-lyase 1; Beta-methylaspartase 1 MRIKDVLFVKGSSGFYFDDQKAIKSGAVTDGFTYKGKPLTPGFSRVRQGGEAVSIMLFLENGEIAVGDCVAVQYSGVDGRDPVFLADNFIEVLEEEIKPRLVGYNLVRFREAARYFTNLTDKRGKRYHTALRYGLTQALLDAVAKINRTTMAEVIAEEYGLDLTLNPVPLFAQSGDDRYINADKMILKRVDVLPHGLFNHPAKTGEEGKNLTEYALWLKQRIKTLGDHDYLPVFHFDVYGTLGTVFNDNLDRIADYLARLEEKVAPHPLQIEGPVDLGSKERQIEGLKYLQEKLITLGSKVIIVADEWCNNLSDIKEFVDAGAGGMVQIKSPDLGGVNDIIEAVLYAKEKGTGAYLGGSCNETDVSAKITVHVGLATGPAQLLVKPGMGVDEGLTIMRNEMMRTLAILQRNKVTFQKKVG mal curated2 Q5V465 Methylaspartate ammonia-lyase; MAL; EC 4.3.1.2; 3-methylaspartate ammonia-lyase; Beta-methylaspartase MRIEDVRTVPGLSGFFFDDQQAIKDGATQTGFAYDGQPVTDGFDRIREAGEALIVEIELADGSIATGDCAAVQYSGAGGRDPLFRAEKYRPVVEGAVADALRGQDATQFGANATMLEEMSPQRSGGDQLHTAVRYGVSQALLNAAAQARGVTPTDVLADTYDTEPATSPVPVFGQSGDERRINAEKMLIKGVPVLPHGLFNSVEKVGENGEGLRDYLAWLSDRATALGPEPYSPRFHVDVYGILGKVFGPPYDRTEVTDYFETLREAAAPYPLQVEGPMDAGGRQAQITEMAELREGLADAGVDVDIVADEWCNTFEDVQAFVDAEAADLVQIKTPDLGGIQRSAEAVLYCDGTDTRAYVGGTCNETVTSARACAHVALATDAAQVLAKPGMGFDEGFMVVTNEMRRALARRDATQEVPADD mcl curated BRENDA::A0A172MLA1 (S)-citramalyl-CoA lyase (EC 4.1.3.25); (R)-citramalyl-CoA lyase (EC 4.1.3.46) MASRNTLRRALLYIPGSSQRFIDKSRTLTADCVAYDLEDSVTPHKKAEARSLVRRALDQPAPAGILERAVRINSVDSGLALADLTEVLQSPNLSTIVIPKVNSASDLTFVTDVITHTLSQLPLSQSASRPPISLLALVESAKSLTNLSQICAASPLLQGLIFAAEDFALDLSLTRTPALTEFLFARSAIATAARAANLPSTIDLVCTTYKSDKGDGSPPVVLQQECRDGKNLGFNGKQCIHPSQVSTVQQIFGPELEEVQWAVRVTIADDKASKAGRGAWTLDGKMIDIPVAEKARAIVKKADACGFNVQELREKWQHQEPE mcl curated BRENDA::Q3J5L6,SwissProt::Q3J5L6 malyl-CoA lyase (EC 4.1.3.24);; L-malyl-CoA/beta-methylmalyl-CoA lyase; (3S)-malyl-CoA/beta-methylmalyl-CoA lyase; (S)-citramalyl-CoA lyase; EC 4.1.3.24; EC 4.1.3.25 MSFRLQPAPPARPNRCQLFGPGSRPALFEKMAASAADVINLDLEDSVAPDDKAQARANIIEAINGLDWGRKYLSVRINGLDTPFWYRDVVDLLEQAGDRLDQIMIPKVGCAADVYAVDALVTAIERAKGRTKPLSFEVIIESAAGIAHVEEIAASSPRLQAMSLGAADFAASMGMQTTGIGGTQENYYMLHDGQKHWSDPWHWAQAAIVAACRTHGILPVDGPFGDFSDDEGFRAQARRSATLGMVGKWAIHPKQVALANEVFTPSETAVTEAREILAAMDAAKARGEGATVYKGRLVDIASIKQAEVIVRQAEMISA mcl curated BRENDA::Q8N0X4,SwissProt::Q8N0X4,metacyc::HS04862-MONOMER citrate (pro-3S)-lyase (EC 4.1.3.6);; Citramalyl-CoA lyase, mitochondrial; (3S)-malyl-CoA thioesterase; Beta-methylmalate synthase; Citrate lyase subunit beta-like protein; Citrate lyase beta-like; Malate synthase; EC 4.1.3.25; EC 3.1.2.30; EC 2.3.3.-; EC 2.3.3.9;; malate/β-methylmalate synthase (EC 2.3.3.9) MALRLLRRAARGAAAAALLRLKASLAADIPRLGYSSSSHHKYIPRRAVLYVPGNDEKKIKKIPSLNVDCAVLDCEDGVAANKKNEARLRIVKTLEDIDLGPTEKCVRVNSVSSGLAEEDLETLLQSRVLPSSLMLPKVESPEEIQWFADKFSFHLKGRKLEQPMNLIPFVETAMGLLNFKAVCEETLKVGPQVGLFLDAVVFGGEDFRASIGATSSKETLDILYARQKIVVIAKAFGLQAIDLVYIDFRDGAGLLRQSREGAAMGFTGKQVIHPNQIAVVQEQFSPSPEKIKWAEELIAAFKEHQQLGKGAFTFQGSMIDMPLLKQAQNTVTLATSIKEK mcl curated BRENDA::Q9I562 (S)-citramalyl-CoA lyase (EC 4.1.3.25) MNRQIVRSALFVPATRPERIPKALASGADRVIVDLEDAVEEGLKVEARANLRRFLVDTPEARVLVRINAAEHPGHADDLALCRDHAGVIGLLLPKVESAAQVRHAAVASGKPVWPIVESARGLAALGEIAAAAGVERLSFGSLDLALDLDLNSGSNAAEQILGHARYALLLQTRLAGLAPPLDGVYPAIQNRAGLVEAVRFARDMGFGGLLCIHPSQVEPIHQTLMPSPAELEWARRVAEAGASGAGVFVVDGEMVDAPVLGRARRLLERAGEGG mcl curated BRENDA::S5N020,SwissProt::S5N020,metacyc::MONOMER-13604 malyl-CoA lyase (EC 4.1.3.24); (S)-citramalyl-CoA lyase (EC 4.1.3.25);; Malyl-CoA/beta-methylmalyl-CoA/citramalyl-CoA lyase; (3S)-3-carboxy-3-hydroxypropanoyl-CoA glyoxylate-lyase; (3S)-citramalyl-CoA pyruvate-lyase; (S)-citramalyl-CoA lyase; Erythro-beta-methylmalyl-CoA; L-malyl-CoA lyase; EC 4.1.3.24; EC 4.1.3.25;; L-malyl CoA lyase subunit (EC 4.1.3.25; EC 4.1.3.24) MRKLAHNFYKPLAIGAPEPIRELPVRPERVVHFFPPHVEKIRARIPEVAKQVDVLCGNLEDAIPMDAKEAARNGFIEVVKATDFGDTALWVRVNALNSPWVLDDIAEIVAAVGNKLDVIMIPKVEGPWDIHFVDQYLALLEARHQIKKPILIHALLETAQGMVNLEEIAGASPRMHGFSLGPADLAASRGMKTTRVGGGHPFYGVLADPQEGQAERPFYQQDLWHYTIARMVDVAVAHGLRAFYGPFGDIKDEAACEAQFRNAFLLGCTGAWSLAPNQIPIAKRVFSPDVNEVLFAKRILEAMPDGSGVAMIDGKMQDDATWKQAKVIVDLARMIAKKDPDLAQAYGL mcl curated SwissProt::Q8R4N0,BRENDA::Q8R4N0 Citramalyl-CoA lyase, mitochondrial; (3S)-malyl-CoA thioesterase; Beta-methylmalate synthase; Citrate lyase subunit beta-like protein, mitochondrial; Citrate lyase beta-like; Malate synthase; EC 4.1.3.25; EC 3.1.2.30; EC 2.3.3.-; EC 2.3.3.9;; citrate (pro-3S)-lyase (EC 4.1.3.6) MALCVLRNTVRGAAALPRLKASHVVSVYKPRYSSLSNHKYVPRRAVLYVPGNDEKKIRKIPSLKVDCAVLDCEDGVAENKKNEARLRIAKTLEDFDLGTTEKCVRINSVSSGLAEVDLETFLQARVLPSSLMLPKVEGPEEIRWFSDKFSLHLKGRKLEQPMNLIPFVETAMGLLNFKAVCEETLKTGPQVGLCLDAVVFGGEDFRASIGATSNKDTQDILYARQKVVVTAKAFGLQAIDLVYIDFRDEDGLLRQSREAAAMGFTGKQVIHPNQIAVVQEQFTPTPEKIQWAEELIAAFKEHQQLGKGAFTFRGSMIDMPLLKQAQNIVTLATSIKEK mcl curated2 A9WC35 Malyl-CoA/beta-methylmalyl-CoA/citramalyl-CoA lyase; EC 4.1.3.24; EC 4.1.3.25; (3S)-3-carboxy-3-hydroxypropanoyl-CoA glyoxylate-lyase; (3S)-citramalyl-CoA pyruvate-lyase; (S)-citramalyl-CoA lyase; Erythro-beta-methylmalyl-CoA; L-malyl-CoA lyase MRKLAHNFYKPLAIGAPEPIRELPVRPERVVHFFPPHVEKIRARIPEVAKQVDVLCGNLEDAIPMDAKEAARNGFIEVVKATDFGDTALWVRVNALNSPWVLDDIAEIVAAVGNKLDVIMIPKVEGPWDIHFVDQYLALLEARHQIKKPILIHALLETAQGMVNLEEIAGASPRMHGFSLGPADLAASRGMKTTRVGGGHPFYGVLADPQEGQAERPFYQQDLWHYTIARMVDVAVAHGLRAFYGPFGDIKDEAACEAQFRNAFLLGCTGAWSLAPNQIPIAKRVFSPDVNEVLFAKRILEAMPDGSGVAMIDGKMQDDATWKQAKVIVDLARMIAKKDPDLAQAYGL mcl curated2 Q3J5L6 L-malyl-CoA/beta-methylmalyl-CoA lyase; EC 4.1.3.24; (3S)-malyl-CoA/beta-methylmalyl-CoA lyase; (S)-citramalyl-CoA lyase; EC 4.1.3.25 MSFRLQPAPPARPNRCQLFGPGSRPALFEKMAASAADVINLDLEDSVAPDDKAQARANIIEAINGLDWGRKYLSVRINGLDTPFWYRDVVDLLEQAGDRLDQIMIPKVGCAADVYAVDALVTAIERAKGRTKPLSFEVIIESAAGIAHVEEIAASSPRLQAMSLGAADFAASMGMQTTGIGGTQENYYMLHDGQKHWSDPWHWAQAAIVAACRTHGILPVDGPFGDFSDDEGFRAQARRSATLGMVGKWAIHPKQVALANEVFTPSETAVTEAREILAAMDAAKARGEGATVYKGRLVDIASIKQAEVIVRQAEMISA mcl ignore SwissProt::B6E2X2,metacyc::MONOMER-13588 L-malyl-CoA/beta-methylmalyl-CoA lyase; (3S)-malyl-CoA/beta-methylmalyl-CoA lyase; EC 4.1.3.24;; malyl-CoA lyase subunit (EC 4.1.3.24) MSFRTQPPAPARLNRCQLFGPGSRPAIFEKMAQSAADVINLDLEDSVAPDDKPQARRNIIEASHNIDWGNKYLSVRINGLDTPFWYRDVVELLEDGSERIDQIMIPKVGCAADVYAVDALVTAIEAAKGRKKRISLEVIIESAAGIAHVEEIAAASPRLQAMSLGAADFAASMGMATTGIGGTQENYYMLHAGVKHWSDPWHWAQAAIVAACRTHGILPVDGPFGDFSDDEGFRAQALRSATLGMVGKWAIHPKQVALANEVFTPSDAAVAEAREILAAMEKAKAEGAGATVYKGRLVDIASIRQAEVIVRQAEMAKV mcl ignore reanno::Phaeo:GFF3000 Malyl-CoA lyase (EC 4.1.3.24) MSFRIQPAAPARPNRCQLFGPGSNTKLFPKMAASAADVINLDLEDSVAPLDKDVARANVIEALNTVDWGNKYISVRINGLDTPYWYRDVVDLLEQAGDRLDQIMIPKVGCAEDVYAVDALVTAIERAKGRAKPISFEVIIESAAGIAHVEAIAAASPRLQAMSLGAADFAASMGMQTTGIGGTQEDYYMLRAGEKHWSDPWHWAQAAIVAACRTHGILPVDGPFGDFSDDDGYIAQAKRSATLGMVGKWAIHPKQIALANQVFTPSDEAVGEAREILAAMEQAKANGEGATVYKGRLVDIASIKQAEVIVAQSELIAQNG peb1A curated CharProtDB::CH_021449,TCDB::Q0P9X8 major cell-binding factor;; PEB1A, component of Uptake system for glutamate and aspartate MVFRKSLLKLAVFALGACVAFSNANAAEGKLESIKSKGQLIVGVKNDVPHYALLDQATGEIKGFEVDVAKLLAKSILGDDKKIKLVAVNAKTRGPLLDNGSVDAVIATFTITPERKRIYNFSEPYYQDAIGLLVLKEKKYKSLADMKGANIGVAQAATTKKAIGEAAKKIGIDVKFSEFPDYPSIKAALDAKRVDAFSVDKSILLGYVDDKSEILPDSFEPQSYGIVTKKDDPAFAKYVDDFVKEHKNEIDALAKKWGL peb1B curated TCDB::A1VZQ3 PEP1B, component of Uptake system for glutamate and aspartate MNESVGFVEHLRQILTSWGLYDENSISPFAVWKFLDALDNKDAFINGFIYTLEVSILALLIATIFGTIGGVMATSRFKIIRAYTRIYVELFQNVPLVIQIFFLFYALPVLGIRLDIFTIGVLGVGAYHGAYVSEVVRSGILAVPRGQFEASASQGFTYIQQMRYIIVPQTIRIILPPMTNQMVNLIKNTSVLLIVGGAELMHSADSYAADYGNYAPAYIFAAVLYFIICYPLAYFAKAYENKLKKAHLTR yveA curated SwissProt::O07002,TCDB::O07002 Aspartate-proton symporter; L-aspartate transporter;; The aspartate uptake permease, YveA MSKQGNFQKSMSLFDLILIGMGAIFGSAWLFAVSNVASKAGPSGAFSWILGGAIILLIGLVYAELGAALPRTGGIIRYPVYSHGHLVGYLISFVTIVAYTSLISIEVTAVRQYVAYWFPGLTIKGSDSPTISGWILQFALLCLFFLLNYWSVKTFAKANFIISIFKYIVPITIIIVLIFHFQPENLSVQGFAPFGFTGIQAAISTGGVMFAYLGLHPIVSVAGEVQNPKRNIPIALIICIIVSTIIYTVLQVTFIGAIPTETLKHGWPAIGREFSLPFKDIAVMLGLGWLATLVILDAILSPGGNGNIFMNTTSRLVYAWARNGTLFGIFSKVNKDTGTPRASLWLSFALSIFWTLPFPSWNALVNVCSVALILSYAIAPISSAALRVNAKDLNRPFYLKGMSIIGPLSFIFTAFIVYWSGWKTVSWLLGSQLVMFLIYLCFSKYTPKEDVSLAQQLKSAWWLIGFYIMMLIFSYIGSFGHGLGIISNPVDLILVAIGSLAIYYWAKYTGLPKAAIDYDK