gdh

NAD-specific glutamate dehydrogenase

1624 amino acids

Catalyzes the reversible conversion of L-glutamate to 2-oxoglutarate.

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

176.9 kDa

MTIDPGAKQDVEAWTTFTASADIPDWISKAYIDSYRGPRDDSSEATKAAEASWLPASLLTPAMLGAHYRLGRHRAAGESCVAVYRADDPAGFGPALQVVAEHGGMLMDSVTVLLHRLGIAYAAILTPVFDVHRSPTGELLRIEPKAEGTSPHLGEAWMHVALSPAVDHKGLAEVERLLPKVLADVQRVATDATALIATLSELAGEVESNAGGRFSAPDRQDVGELLRWLGDGNFLLLGYQRCRVADGMVYGEGSSGMGVLRGRTGSRPRLTDDDKLLVLAQARVGSYLRYGAYPYAIAVREYVDGSVVEHRFVGLFSVAAMNADVLEIPTISRRVREALAMAESDPSHPGQLLLDVIQTVPRPELFTLSAQRLLTMARAVVDLGSQRQALLFLRADRLQYFVSCLVYMPRDRYTTAVRMQFEDILVREFGGTRLEFTARVSESPWALMHFMVRLPEVGVAGEGAAAPPVDVSEANRIRIQGLLTEAARTWADRLIGAAAAAGSVGQADAMHYAAAFSEAYKQAVTPADAIGDIAVITELTDDSVKLVFSERDEQGVAQLTWFLGGRTASLSQLLPMLQSMGVVVLEERPFSVTRPDGLPVWIYQFKISPHPTIPLAPTVAERAATAHRFAEAVTAIWHGRVEIDRFNELVMRAGLTWQQVVLLRAYAKYLRQAGFPYSQSYIESVLNEHPATVRSLVDLFEALFVPVPSGSASNRDAQAAAAAVAADIDALVSLDTDRILRAFASLVQATLRTNYFVTRQGSARCRDVLALKLNAQLIDELPLPRPRYEIFVYSPRVEGVHLRFGPVARGGLRWSDRRDDFRTEILGLVKAQAVKNAVIVPVGAKGGFVVKRPPLPTGDPAADRDATRAEGVACYQLFISGLLDVTDNVDHATASVNPPPEVVRRDGDDAYLVVAADKGTATFSDIANDVAKSYGFWLGDAFASGGSVGYDHKAMGITARGAWEAVKRHFREIGIDTQTQDFTVVGIGDMSGDVFGNGMLLSKHIRLIAAFDHRHIFLDPNPDAAVSWAERRRMFELPRSSWSDYDRSLISEGGGVYSREQKAIPLSAQVRAVLGIDGSVDGGAAEMAPPNLIRAILRAPVDLLFNGGIGTYIKAESESDADVGDRANDPVRVNANQVRAKVIGEGGNLGVTALGRVEFDLSGGRINTDALDNSAGVDCSDHEVNIKILIDSLVSAGTVKADERTQLLESMTDEVAQLVLADNEDQNDLMGTSRANAASLLPVHAMQIKYLVAERGVNRELEALPSEKEIARRSEAGIGLTSPELATLMAHVKLGLKEEVLATELPDQDVFASRLPRYFPTALRERFTPEIRSHQLRREIVTTMLINDLVDTAGITYAFRIAEDVGVTPIDAVRTYVATDAIFGVGHIWRRIRAANLPIALSDRLTLDTRRLIDRAGRWLLNYRPQPLAVGAEINRFAAMVKALTPRMSEWLRGDDKAIVEKTAAEFASQGVPEDLAYRVSTGLYRYSLLDIIDIADIADIDAAEVADTYFALMDRLGTDGLLTAVSQLPRHDRWHSLARLAIRDDIYGALRSLCFDVLAVGEPGESSEQKIAEWEHLSASRVARARRTLDDIRASGQKDLATLSVAARQIRRMTRTSGRGISG

gdh

NAD-specific glutamate dehydrogenase

1613 amino acids

Involved in arginine catabolism by converting L-glutamate, into 2-oxoglutarate, which is then channeled into the tricarboxylic acid cycle.

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

183.519 kDa

MLHVAQEEARLDLLKQLKERLQSRLDKDKAAEVDTFAHLFYAAVPLEDLADRRLDDLYGATLSVWHFIQQFDPEAPKVRVLNPDFEEHGWQSTHTFIAVLHEDMPFLVDSVRVELNRRGMTVHAIHNAVLAVGRDDEHRLQRVASPEETDAPEARESLIAIEVDRHSNPAELEEIEASLLEVLREVRTAVSDFDPMRAQARAAIEELEATRPAQVDPADHREAIEFLQWLLQDNFTFLGYDEYEVREDQGRQRLDKVQNSELGVFRLDQPRYRERIRTDLGVEGDHYVPMPQLMSFAKSAHHARIHRPTYPDYISIDRYDDQGRVIGERRFLGMFTATVYNESPRNVPILRRKLQAVMDIAGFSPKGHNGKQLLQILEVYPRDDLFQIDIEELAQTALGILDIRERRRVRLFIREDTFGKFYSCLVFVPRDVFSTELRVRLQELLCEELDATFGDFNTYLSESVLARIQFILRFNGEKPVEYDIKRLEEKLVKLARNWRDDLLNASIEGFGEESANLLMSRFRDAFPASYREDFSARTAVYDLQHIGELDEGAPLALSLYRLIEEEGSGVNLKLFHRGAPIPLSDVLPMMENLGLRVIGERPYEVQASDASYWIHDFNLEHHTSVEMNLQEMRGPFIEAFQRIWAGEADNDAFNRLIIGANLDWREVAMLRAYARYLKQIRFGMSQDYIATTLGSHPEITRELVSLFELRFDPAERPGEGDIEECESRILTLLDEVPSLNDDQLLRRYMELIKATLRTNYYQRTEEGRYKDYLAFKLDPSQVSGIPKPCPAYEIFVCSPRVEGVHLRGGKVARGGLRWSDRHEDFRTEVLGLVKAQQVKNAVIVPMGAKGGFVCKRMPEGADREATQKEGIACYQIFIRALLDVTDNLVGGEVVPPRDVVRHDDNDPYLVVAADKGTATFSDIANEISTEYGHWLGDAFASGGANGYDHKKMAITAKGAWESVKRHFRGLGVNTQEDEFSVVGIGDMAGDVFGNGMLLSDKIRLVGAFNHLHIFVDPTPDAAASFAERQRLFDMPRSSWEDYNTELISEGGGIFPRSAKSITITPQMKKVFGIREDKLSPNELIRAMLVSKVDLVWNGGIGTYVKSSEETDAEVGDKANDALRIDGRELNCRVVGEGGNLGLTQRGRMEAAAKGVRVNTDFIDNAGGVNCSDHEVNIKILIDEVVSRGDLTEKQRNQLLADMTDEVSELVLLDNYRQTQALDLAELLSRQGIGPYRRFISELEAAGQIDRELEFLPSDEELLERTQHNQGMTLPELSVLISYAKSVLKGDLIASDVPDDPTIMRFVERVFPSMLAERYRDEMYEHRLKREIVATQVANDLVDYMGVVFVRRLMDSTGADRADIARAYVIARDSFQLPRLWEQIEALDNKVPSQVQYSMMLDLMRMLRRSTRWFLRQRTGMSTRDTIDYFAPRLAQLQENIGKRLRGEEQEQWSARRQELVKAGVPEALASTVAAAGSLYAALGIIQTARQTDEKPQRVAEIFYEVGARLELPWIIQQVTRLEVRDGWQAKARDTFRDDIDRQQLALTASVLGMDGGPRDSAERVDRWLSLHEGMHQRWRHLLEEVGSGSQGGFPLFAVAVRELVDLAESNSEA

gdh

NAD-specific glutamate dehydrogenase

1594 amino acids

Catalyzes the reversible conversion of L-glutamate to 2-oxoglutarate. Highly specific for NAD.

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

174.095 kDa

MIRRLSVAFLSTYRGPQADAPGVTSTGPLAVAAHDDLVSDDLVAAHYRLASMRAPGETKAAVYPGDAGSGAALQIVTDQAPMLVDSVTVLLHRHGIAYTAIMNPVFRVRRGLDGELLDVRPAAEAAPGDGADECWILVPITAAADGEALTEATRLVPGILAEARQIGLDSGAMIAALHGLANDLATDLEGHFPNAERKEVAALLRWLADGHFVLLGYQQCVVGDGNAEVDPASRLGVLRLRNDVLPPLTDSDDLLVLAQATMPSYLRYGAYPYIVVVRESPGASRVIEHRFVGLFTVAAMNANALEIPLISRRVEEALAMAHRDPSHPGQLLRDIIQTIPRPELFALSSKQLLEMALAVVDLGSRRRTLLFLRADHLAHFVSCLVYLPRDRYTTAVRLEMQDILVRELGGAGIDYSARVSESPWAVVHFTVRLPEGTAADSVDTSLENESRIQDLLTEATRNWGDRMISAAAAASISPAALEHYAHAFPEDYKQAFAPQDAIADISLIEALQDDSVKLVLADTAEDRVWKLTWYLGGHSASLSELLPMLQSMGVVVLEERPFTLRRTDGLPVWIYQFKISPHPSIPHAPDAEAQRDTAQRFADAVTAIWHGRVEIDRFNELVMRAGLTWQQVVVLRAYAKYLRQAGFPYSQSHIESVLNENPHTTRSLIDLFEALFDPSQETDGRRDAQGAAAAVAADIDALVSLDTDRVLRAFANLIEATLRTNYFVARPDSARARNVLAFKLNPLVIKELPLPRPKFEIFVYSPRVEGVHLRFGFVARGGLRWSDRREDFRTEILGLVKAQAVKNAVIVPVGAKGGFVVKRPPTLTGDAAADREATRAEGVECYRLFISGLLDVTDNVDKATGAVVTPPEVVRRDGEDAYLVVAADKGTATFSDIANEVAKSYGFWLGDAFASGGSIGYDHKAMGITAKGAWESVKRHFREMGVDTQTQDFTVVGIGDMSGDVFGNGMLLSKHIRLVAAFDHRDIFLDPNPDAGRSWDERKRLFDLPRSSWADYDKSLISEGGGVYSRQQKSIPISPQVRTALGLDADVEELTPPALIKAILKAPVDLLWNGGIGTYIKAETEADADVGDRANDQIRVCGNQVRAKVIGEGGNLGVTALGRIEFDLAGGRINTDALDNSAGVDCSDHEVNIKILIDSAVTAGKVTPEERTELLLSMTDEVGELVLADNRDQNDLMGTSRANAASLLSVHARMIKDLVDNRGLNRELEALPSEKEIRRRADAGIGLTSPELATLMAHVKLALKDDVLASDLPDQEVFASRLPYYFPTRLREELHGEIRSHQLRREIITTMLVNDLVDTAGISYAYRITEDVGVGPVDAVRSYVAINAIFGIGDVWRRIRAAGDAGVPTSVTDRMTLDLRRLVDRAGRWLLNYRPQPLAVGAEINRFGAKVAALTPRMSEWLRGDDKAIVSKEAGDFASHGVPEDLAYHIATGLYQYSLLDVIDIADIVDREPDEVADTYFALMDHLGADALLTAVSRLSRDDRWHSLARLAIRDDIYGSLRALCFDVLAVGEPDENGEEKIAEWETTNSSRVTRARRTLTEIYKDGEQDLATLSVAARQIRSMTRTSGTGTTG

gdh

Quinoprotein glucose dehydrogenase

808 amino acids

Belongs to the bacterial PQQ dehydrogenase family.

87.335 kDa

MSTTSRPGLWALITAAVFALCGAILTVGGAWVAAIGGPLYYVILGLALLATAFLSFRRNPAALYLFAVVVFGTVIWELTVVGLDIWALIPRSDIVIILGIWLLLPFVSRQIGGTRTTVLPLAGAVGVAVLALFASLFTDPHDISGDLPTQIANASPADPDNVPASEWHAYGRTQAGDRWSPLNQINASNVSNLKVAWHIHTKDMMNSNDPGEATNEATPIEFNNTLYMCSLHQKLFAVDGATGNVKWVYDPKLQINPGFQHLTCRGVSFHETPANATDSDGNPAPTDCAKRIILPVNDGRLVEVDADTGKTCSGFGNNGEIDLRVPNQPYTTPGQYEPTSPPVITDKLIIANSAITDNGSVKQASGATQAFDVYTGKRVWVFDASNPDPNQLPDDSHPVFHPNSPNSWIVSSYDRNLNLVYIPMGVGTPDQWGGDRTKDSERFAPGIVALNADTGKLAWFYQTVHHDLWDMDVPSQPSLVDVTQKDGTLVPAIYAPTKTGDIFVLDRRTGKEIVPAPETPVPQGAAPGDHTSPTQPMSQLTLRPKNPLNDSDIWGGTIFDQMFCSIYFHTLRYEGPFTPPSLKGSLIFPGDLGMFEWGGLAVDPQRQVAFANPISLPFVSQLVPRGPGNPLWPEKDAKGTGGETGLQHNYGIPYAVNLHPFLDPVLLPFGIKMPCRTPPWGYVAGIDLKTNKVVWQHRNGTLRDSMYGSSLPIPLPPIKIGVPSLGGPLSTAGNLGFLTASMDYYIRAYNLTTGKVLWQDRLPAGAQATPITYAINGKQYIVTYAGGHNSFPTRMGDDIIAYALPDQK

Gdh

Glutamate dehydrogenase, mitochondrial

562 amino acids

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

62.536 kDa

MYHLKSLARQGARRQQELATLAKALPTAVMQSSRGYATEHQIPDRLKDVPTAKDPRFFDMVEYFFHRGCQIAEESLVDDMKGKLTRDEKKQKVKGILMLMQPCDHIIEIAFPLRRDAGNYEMITGYRAQHSTHKTPTKGGIRFSLDVSRDEVKALSALMTFKCACVDVPFGGAKAGLKINPKEYSEHELEKITRRFTLELAKKGFIGPGVDVPAPDMGTGEREMSWIADTYAKTIGHLDINAHACVTGKPINQGGIHGRVSATGRGVFHGLENFINEANYMSQIGTTPGWGGKTFIVQGFGNVGLHTTRYLTRAGATCIGVIEHDGTLYNPEGIDPKLLEDYKNEHGTIVGYQNAKPYEGENLMFEKCDIFIPAAVEKVITSENANRIQAKIIAEAANGPTTPAADKILIDRNILVIPDLYINAGGVTVSFFEWLKNLNHVSYGRLTFKYERESNYHLLASVQQSIERIINDESVQESLERRFGRVGGRIPVTPSESFQKRISGASEKDIVHSGLDYTMERSARAIMKTAMKYNLGLDLRTAAYVNSIEKIFTTYRDAGLAF

GDH

NADP-specific glutamate dehydrogenase

461 amino acids

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

49.832 kDa

MMQNLPFEPEFEQAYKELASTLENSTLFQKKPEYRKALQVVSVPERVIQFRVVWEDDKGQVQINRGYRVQFNSALGPYKGGLRFHPTVNLSILKFLGFEQIFKNALTGLNMGGGKGGSDFDPKGKTDNEIRRFCVSFMTELCKHIGADTDVPAGDIGVTGREVGFMFGQYKKIRNQWEGVLTGKGGSWGGSLIRPEATGYGVVYYVEHMIQHASGGKESFAGKRVAISGSGNVAQYAALKVIELGGSVISLSDSQGALVLNGEEGSFTAEEINTIAEIKVQRKQIAELATQDAFSSKFKYIPGARPWTNIAGRIDVALPSATQNEVSGDEAKALIAAGCKFIAEGSNMGSTQEAIDVFEAHRDANPGAAAIWYAPGKAANAGGVAVSGLEMAQNSARVNWSREEVDSRLKKIMEDCFNNGLSTAKEYVTPAEGVLPSLVAGSNIAGFTKVAEAMKEHGDWW

gdh

NADP-specific glutamate dehydrogenase

454 amino acids

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

48.853 kDa

MSNLPSEPEFEQAYKELAYTLENSSLFQKHPEYRTALTVASIPERVIQFRVVWEDDNGNVQVNRGYRVQFNSALGPYKGGLRLHPSVNLSILKFLGFEQIFKNALTGLSMGGGKGGADFDPKGKSDAEIRRFCCAFMAELHKHIGADTDVPAGDIGVGGREIGYMFGAYRKAANRFEGVLTGKGLSWGGSLIRPEATGYGLVYYVGHMLEYSGAGSYAGKRVALSGSGNVAQYAALKLIELGATVVSLSDSKGALVATGESGITVEDINAVMAIKEARQSLTSFQHAGHLKWIEGARPWLHVGKVDIALPCATQNEVSKEEAEGLLAAGCKFVAEGSNMGCTLEAIEVFENNRKEKKGEAVWYAPGKAANCGGVAVSGLEMAQNSQRLNWTQAEVDEKLKDIMKNAFFNGLNTAKTYVEAAEGELPSLVAGSNIAGFVKVAQAMHDQGDWWSKN

GDH

NADP-specific glutamate dehydrogenase

454 amino acids

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

48.888 kDa

MSNLPSEPEFEQAYKELAYTLENSSLFQKHPEYRTALTVASIPERVIQFRVVWEDDNGNVQVNRGYRVQFNSALGPYKGGLRLHPSVNLSILKFLGFEQIFKNALTGLSMGGGKGGADFDPKGKSDAEIRRFCCAFMAELHKHIGADTDVPAGDIGVGGREIGYMFGAYRKAANRFEGVLTGKGLSWGGSLIRPEATGYGLVYYVGHMLEYSGAGSYAGKRVALSGSGNVAQYAALKLIELGATVVSLSDSKGALVATGESGITVEDINAVMAIKEARQSLTSFQHAGHLKWIEGARPWLHVGKVDIALPCATQNEVSKEEAEGLLAAGCKFVAEGSNMGCTLEAIEVFENHRKEKKGEAVWYAPGKAANCGGVAVSGLEMAQNSQRLNWTQAEVDEKLKDIMKNAFFNGLNTAKIYVEAAEGELPSLVAGSNIAGFVKVAQAMHDQGDWWSKN

GDH

NADP-specific glutamate dehydrogenase

454 amino acids

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

48.835 kDa

MSNLPSEPEFEQAYKELAYTLENSSLFQKHPEYRTALAVASIPERVIQFRVVWEDDNGNVQVNRGYRVQFNSALGPYKGGLRLHPSVNLSILKFLGFEQIFKNALTGLSMGGGKGGADFDPKGKSDAEIRRFCCAFMAELHKHIGADTDVPAGDIGVGGREIGYMFGAYRKAANRFEGVLTGKGLSWGGSLIRPEATGYGLVYYVGHMLEYSGAGSYAGKRVALSGSGNVAQYAALKLIELGATVVSLSDSKGALVATGESGITVEDINAIMAIKEARQSLTTFQHAGHVKWIEGARPWLHVGKVDIALPCATQNEVSKEEAEGLLAAGCKFVAEGSNMGCTLEAIEVFENNRKEKKGEAVWYAPGKAANCGGVAVSGLEMAQNSQRLNWTQAEVDEKLKDIMKNAFFNGLNTAKTYAEAAEGELPSLVAGSNIAGFVKVPQAMHDQGDWWSKN

gdh

NAD-specific glutamate dehydrogenase

450 amino acids

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

49.296 kDa

MSKYVDRVIAEVEKKYADEPEFVQTVEEVLSSLGPVVDAHPEYEEVALLERMVIPERVIEFRVPWEDDNGKVHVNTGYRVQFNGAIGPYKGGLRFAPSVNLSIMKFLGFEQAFKDSLTTLPMGGAKGGSDFDPNGKSDREVMRFCQAFMTELYRHIGPDIDVPAGDLGVGAREIGYMYGQYRKIVGGFYNGVLTGKARSFGGSLVRPEATGYGSVYYVEAVMKHENDTLVGKTVALAGFGNVAWGAAKKLAELGAKAVTLSGPDGYIYDPEGITTEEKINYMLEMRASGRNKVQDYADKFGVQFFPGEKPWGQKVDIIMPCATQNDVDLEQAKKIVANNVKYYIEVANMPTTNEALRFLMQQPNMVVAPSKAVNAGGVLVSGFEMSQNSERLSWTAEEVDSKLHQVMTDIHDGSAAAAERYGLGYNLVAGANIVGFQKIADAMMAQGIAW

gdh

NADP-specific glutamate dehydrogenase

447 amino acids

Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia.

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

48.962 kDa

MTVDEQVSNYYDMLLKRNAGEPEFHQAVAEVLESLKIVLEKDPHYADYGLIQRLCEPERQLIFRVPWVDDNGQVHVNRGFRVQFNSALGPYKGGLRFHPSVNLGIVKFLGFEQIFKNSLTGLPIGGGKGGSDFDPKGKSELEIMRFCQSFMTELHRHIGEYRDVPAGDIGVGGREIGYLFGHYRRLANQHESGVLTGKGLTWGGSLVRTEATGFGTVYFVQEMIKAEGETLEGKKVIVSGSGNVATYAIQKVQELGAVVVGFSDSSGWVSTPNGVDVAKLREIKEVRRARVSSYADEVEGAEYHTDGSIWDLTADIALPCATQNELDGDNARTLADNGCRFVAEGANMPSTPEAIDVFRERGVLFGPGKAANAGGVATSALEMQQNASRDSWSFEYTDERLHRIMKNIFKSCADTAKEYGHEKNYVVGANIAGFKKVADAMLAQGVI

gdh

NADP-specific glutamate dehydrogenase

447 amino acids

Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia.

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

48.988 kDa

MTVDEQVSNYYDMLLKRNAGEPEFHQAVAEVLESLKIVLEKDPHYADYGLIQRLCEPERQLIFRVPWVDDQGQVHVNRGFRVQFNSALGPYKGGLRFHPSVNLGIVKFLGFEQIFKNSLTGLPIGGGKGGSDFDPKGKSDLEIMRFCQSFMTELHRHIGEYRDVPAGDIGVGGREIGYLFGHYRRMANQHESGVLTGKGLTWGGSLVRTEATGYGCVYFVSEMIKAKGESISGQKIIVSGSGNVATYAIEKAQELGATVIGFSDSSGWVHTPNGVDVAKLREIKEVRRARVSVYADEVEGATYHTDGSIWDLKCDIALPCATQNELNGENAKTLADNGCRFVAEGANMPSTPEAVEVFRERDIRFGPGKAANAGGVATSALEMQQNASRDSWSFEYTDERLQVIMKNIFKTCAETAAEYGHENDYVVGANIAGFKKVADAMLAQGVI

gdh

NAD-specific glutamate dehydrogenase

445 amino acids

Probably involved in degradation rather than biosynthesis of glutamate.

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

49.199 kDa

MKTQEIMTMLEAKHPGESEFLQAVKEVLLSVEEVYNQHPEFEKNGIIERIVEPDRVFTFRVPWVDDQGKVQVNIGYRVQFNNAIGPYKGGIRFHPSVNLSILKFLGFEQMFKNALTTLPMGGGKGGADFSPKGKSEAEIMRFCQSFMTELWRNIGPDTDIPAGDIGVGGREVGYMFGMYKKLAREHTGTLTGKGFEFGGSRLRPESTGFGAVYFVQNMCKQNGVDYKGKTLAISGFGNVAWGVAQKATELGIKVVTISGPDGYVYDPDGINTPEKFRCMLDLRDSGNDVVSDYVKRFPNAQFFPGKKPWEQKVDFAMPCATQNEMNLEDAKTLHKNGVTLVAETSNMGCTAEASEYYVANKMLFAPGKAVNAGGVSCSGLEMTQNAMHLVWTNEEVDKWLHQIMQDIHEQCVTYGKDGNYIDYVKGANIAGFMKVAKAMVAQGVC

gdh

NAD-specific glutamate dehydrogenase

445 amino acids

Probably involved in degradation rather than biosynthesis of glutamate.

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

49.199 kDa

MKTQEIMTMLEAKHPGESEFLQAVKEVLLSVEEVYNQHPEFEKNGIIERIVEPDRVFTFRVPWVDDQGKVQVNIGYRVQFNNAIGPYKGGIRFHPSVNLSILKFLGFEQMFKNALTTLPMGGGKGGADFSPKGKSEAEIMRFCQSFMTELWRNIGPDTDIPAGDIGVGGREVGYMFGMYKKLAREHTGTLTGKGFEFGGSRLRPESTGFGAVYFVQNMCKQNGVDYKGKTLAISGFGNVAWGVAQKATELGIKVVTISGPDGYVYDPDGINTPEKFRCMLDLRDSGNDVVSDYVKRFPNAQFFPGKKPWEQKVDFAMPCATQNEMNLEDAKTLHKNGVTLVAETSNMGCTAEASEYYVANKMLFAPGKAVNAGGVSCSGLEMTQNAMHLVWTNEEVDKWLHQIMQDIHEQCVTYGKDGNYIDYVKGANIAGFMKVAKAMVAQGVC

GDH

Glutamate dehydrogenase

411 amino acids

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

44.546 kDa

MNALAATNRNFRHASRILGLDSKLEKSLLIPFREIKVECTIPKDDGSLATYVGFRVQHDNARGPMKGGIRYHPEVDPDEVNALAQLMTWKTAVVDIPYGGAKGGIGCTPKDLSMSELERLTRVFTQKIHDLIGTHTDVPAPDMGTNAQTMAWILDEYSKFHGHSPAVVTGKPIALGGSLGREAATGRGVVFATEALLAQHGKSIKGLTFVIQGFGNVGSWVARLIGERGGKIIAVSDVTGAVKNQNGLDIVDLLRHKEETGCLTNFSGGDHMDPNELLTHECDVLIPCALGGVLNKENAADVKAKFIIEAANHPTDPEADEILSKKGGVILPDIYANAGGVTVSYFEWVQNIQGFMWEEEKVNNELQKYMTKAFHNIKAMCQSHNCSLRMGAFTLAVNRVACATTLRGWEA

gdh

Glucose 1-dehydrogenase

366 amino acids

Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Displays broad substrate specificity since it is able to catalyze the oxidation of a number of alternative aldose sugars, such as D-galactose, D-xylose and L-arabinose, to the corresponding glyconate. Can utilize both NAD(+) and NADP(+) as electron acceptor. Physiologically, seems to be involved in the degradation of both glucose and galactose through a non-phosphorylative variant of the Entner-Doudoroff pathway.

Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.

40.891 kDa

MKAIIVKPPNAGVQVKDVDEKKLDSYGKIKIRTIYNGICGTDREIVNGKLTLSTLPKGKDFLVLGHEAIGVVEESYHGFSQGDLVMPVNRRGCGICRNCLVGRPDFCETGEFGEAGIHKMDGFMREWWYDDPKYLVKIPKSIEDIGILAQPLADIEKSIEEILEVQKRVPVWTCDDGTLNCRKVLVVGTGPIGVLFTLLFRTYGLEVWMANRREPTEVEQTVIEETKTNYYNSSNGYDKLKDSVGKFDVIIDATGADVNILGNVIPLLGRNGVLGLFGFSTSGSVPLDYKTLQEIVHTNKTIIGLVNGQKPHFQQAVVHLASWKTLYPKAAKMLITKTVSINDEKELLKVLREKEHGEIKIRILWE

gdh

Glucose 1-dehydrogenase

361 amino acids

Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Is also significantly active with galactose as substrate, but not with mannose or glucose 6-phosphate. Can utilize both NAD(+) and NADP(+) as electron acceptor, with a marked preference for NADP(+). Physiologically, may be involved in the degradation of both glucose and galactose through a non-phosphorylative variant of the Entner-Doudoroff pathway.

Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.

40.25 kDa

MTEQKAIVTDAPKGGVKYTTIDMPEPEHYDAKLSPVYIGICGTDRGEVAGALSFTYNPEGENFLVLGHEALLRVDDARDNGYIKKGDLVVPLVRRPGKCINCRIGRQDNCSIGDPDKHEAGITGLHGFMRDVIYDDIEYLVKVEDPELGRIAVLTEPLKNVMKAFEVFDVVSKRSIFFGDDSTLIGKRMVIIGSGSEAFLYSFAGVDRGFDVTMVNRHDETENKLKIMDEFGVKFANYLKDMPEKIDLLVDTSGDPTTTFKFLRKVNNNGVVILFGTNGKAPGYPVDGEDIDYIVERNITIAGSVDAAKIHYVQALQSLSNWNRRHPDAMKSIITYEAKPSETNIFFQKPHGEIKTVIKWQ

gdh

Glucose 1-dehydrogenase

359 amino acids

Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose through a non-phosphorylative variant of the Entner-Doudoroff pathway.

Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.

39.326 kDa

MKAAAITPGKKDSLRVIDVDRPRPGAGEVLVRMLEAGVCGTDEELNLGIIGEAPAGSDYLIIGHENLGVVEEAGKDVRAFRKGDLVVATVRRSCPGMCFACRTGQPDMCDSDDYLERGIKGMHGYMAEYYTERPENLIPVPQSLRKVAVLLEPLSIVEKGIEQAFKIQERMIWRPRRALVAGAGPIGLLAALILRDVGLEVSTFATRSRESLKARIAEAAGIEYFNVKETPIEQIAELQGPLDMIVEATGSSEIAFKAIGLTDSNGIVCLTGLSPEQRTHSVCTDCVNQDLVMHNKAVFGTVSSNRVHFERGIDRLTSIERRWPGLLERMFSRRVRLENVKEGLKGDKEDVKVLVEIGA

gdh

Glucose 1-dehydrogenase

358 amino acids

Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose through a non-phosphorylative variant of the Entner-Doudoroff pathway.

Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.

39.443 kDa

MKAVVCTPGQKDSVRVIDMERPRCGPGEVLVRVHSIGVDGTDEEINEGLYGEAPEGCDFLVIGHEAVGIVEESGAGVRCTRPGDVVVATVRRPCPERCLNCRNHQPDFCLTGDYLERGIKGLHGFMAEYYTESMDYVIQLPRELLDTGSLLEPLSVVEKGIRESLRVQQRMLWEPRRALVLGAGPLGLLATFILRDMGLDVYTLATRERTSPKARVAEVSGARYIDVGEEPLDTLPEKHGPFDIIVEATGYSPYAFRAMELVNRNGVVCLAGLSPKKKDHALCTDCINMSMVLDNKAALGTVSASRRDFEKGVDRMLSIRNKWPGLLESLFTKKESLDSAPRALRRTKEDIKAVVVAT

gdh

Glucose 1-dehydrogenase

358 amino acids

Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose through a non-phosphorylative variant of the Entner-Doudoroff pathway.

Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.

39.611 kDa

MKAIIVRPPNEGVEVKDITLRESTDGKIVVRTRLSGLCGTDRGLVTGRLTFARPPPGYDFLILGHETLGEVVKGNGEFSPGDLVVPVVRRGCGSCLNCMLGRQDFCETGRFTEIGIRGAHGTMREEFLEDPKYLVRVPRELGDEGVLLEPLSNVVKALTEMEYLQRRSWWRCDDSTYSCRTAVVLGSGPIGLLFSMALRSMGFRVIVANRRPPSQVESEITRDIGATFLNTSEHEDLEPDLIVDTSGHPSAVVPLLPRIRKNGAVILFGTTGLERYELTAEEITMLVENNILIFGSVNASKADFQAGVNLLVEWKARYPGVLQRMITKRVSVEEAPQVLKEKVPGEIKTVIDWTARES

gdh

Glucose 1-dehydrogenase

357 amino acids

Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate. Displays broad substrate specificity since it is able to catalyze the oxidation of a number of alternative aldose sugars, such as D-xylose, D-galactose, and D-fucose, to the corresponding glyconate. Can utilize both NAD(+) and NADP(+) as electron acceptor, with a preference for NADP(+). Physiologically, seems to be involved in the degradation of glucose through a modified Entner-Doudoroff pathway.

Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.

39.242 kDa

MKAIAVKRGEDRPVVIEKPRPEPESGEALVRTLRVGVDGTDHEVIAGGHGGFPEGEDHLVLGHEAVGVVVDPNDTELEEGDIVVPTVRRPPASGTNEYFERDQPDMAPDGMYFERGIVGAHGYMSEFFTSPEKYLVRIPRSQAELGFLIEPISITEKALEHAYASRSAFDWDPSSAFVLGNGSLGLLTLAMLKVDDKGYENLYCLGRRDRPDPTIDIIEELDATYVDSRQTPVEDVPDVYEQMDFIYEATGFPKHAIQSVQALAPNGVGALLGVPSDWAFEVDAGAFHREMVLHNKALVGSVNSHVEHFEAATVTFTKLPKWFLEDLVTGVHPLSEFEAAFDDDDTTIKTAIEFSTV

gdh

Glucose 1-dehydrogenase

356 amino acids

Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose through a modified Entner-Doudoroff pathway.

Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.

37.51 kDa

MDAIVVSKADRTPRLVDRPRPDPTPGSVLVRTLRVGVDGTDHEVIAGTHGGFPEDADELVLGHEAIGVVADPTDTRFSAGQLVAPTVRRPRGDPTPQFDRGQPDMAAPGTYVERGIDGADGFMADYFTSPADALVALPDSLAAHGFLTEPVSVAEKAIELALASRSAFDWRPDSALVLGNGSLGLLTLAILAARDDTETLYCLGRRSRPDPTIDIIERLGATYIDSRTTPVADIPAAHQPVDMVYEATGHAKHAFDAIDALAPAGVAALLGVPAAGWTFEVPGSDLHRSLVLENKAVVGSVNSNARHFRAAADTLAALPDWLCDAIVTGVHDTAAFADAFRDGETSIKTAVQFDTR

gdh

Glucose 1-dehydrogenase

354 amino acids

Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose through a modified Entner-Doudoroff pathway.

Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.

38.846 kDa

MKVIGVTRDDDGPQLLERERPSPDPGEALVRTLRVGVDGTDHEVLNGSHGGFPDGADHMILGHEAVGVVEEPNGTGLEAGQVVAPTVRRKPNGETNEYFRRGEPDMAPDGEYTERGIVGDHGFMAEYFTSPADFLVPVPKSVAEYGFLVEPLSITEKANEHAYATREPFDWRPDSACVLGNGSLGLLTLWMLDQEYDRTYCVGRRDRPDPTVDIIDEIGSTYVDSRETPVDELPGAYEAMDYIYEATGFAPHAFQTVKALDQNGVGVLLGIPEPWEFEVDGGSLHNEIVLHNKCLIGTVNSHVSHFEDAVETLQELPAWLLDDLVTTVTDPEHVEAAFEDGDDQIKAVVEFDSL

gdh

Glucose 1-dehydrogenase

347 amino acids

Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. To a lesser extent, is also active with xylose as substrate, but mannose, arabinose, galactose, fructose 6-phosphate, glucose 6-phosphate, glycerinaldehyde 3-phosphate, ribose, sorbitol, ethanol, erythritol, or lactose are not oxidized by the enzyme. Can utilize both NAD(+) and NADP(+) as electron acceptor, with a marked preference for NADP(+). Is involved in the degradation of glucose through a non-phosphorylative variant of the Entner-Doudoroff pathway.

Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.

37.072 kDa

MRAVTVTPGVPESLRLREVPEPKPGPGQVLLKPLLVGVCGTDKEIIEGRYGKAPEGSDYLILGHEALAEVAALGKGVDNVSEGDLVVPTVRRPLDCQLPVDYCPPGKYLEHGIWGLHGHAAELSITDAAYLVKVPKELRDIAVLTEPLSVVEKGVELGVESYKARLGSPPKTALVLGAGPVGLLASMVLRLMGVSITAVATRPHDSLKARLVEELGGRYIDAVHERLEGEFDLVIEATGAPSLAVQGLERLAPGGVEVLLGVYPPTGELKGLGSLLTDAVLKNKLVVGSVNAGLRHFERALAHLKEANDSLNGFPKRLITKVVPLERYQEAYVWTHDDIKVVLQVQT

gdh

Glucose 1-dehydrogenase

261 amino acids

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

28.09 kDa

MYPDLKGKVVAITGAASGLGKAMAIRFGKEQAKVVINYYSNKQDPNEVKEEVIKAGGEAVVVQGDVTKEEDVKNIVQTAIKEFGTLDIMINNAGLENPVPSHEMPLKDWDKVIGTNLTGAFLGSREAIKYFVENDIKGNVINMSSVHEVIPWPLFVHYAASKGGIKLMTETLALEYAPKGIRVNNIGPGAINTPINAEKFADPKQKADVESMIPMGYIGEPEEIAAVAAWLASKEASYVTGITLFADGGMTQYPSFQAGRG

gdh

Glucose 1-dehydrogenase

261 amino acids

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

28.09 kDa

MYPDLKGKVVAITGAASGLGKAMAIRFGKEQAKVVINYYSNKQDPNEVKEEVIKAGGEAVVVQGDVTKEEDVKNIVQTAIKEFGTLDIMINNAGLENPVPSHEMPLKDWDKVIGTNLTGAFLGSREAIKYFVENDIKGNVINMSSVHEVIPWPLFVHYAASKGGIKLMTETLALEYAPKGIRVNNIGPGAINTPINAEKFADPKQKADVESMIPMGYIGEPEEIAAVAAWLASKEASYVTGITLFADGGMTQYPSFQAGRG

gdh

Galactitol 2-dehydrogenase

257 amino acids

Catalyzes the oxidation of galactitol to D-tagatose. Also catalyzes the oxidation of a wide range of substrates, including polyvalent aliphatic alcohols and polyols, to the corresponding ketones and ketoses. Galactitol is the preferred substrate.

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

27.289 kDa

MSYQQKFRLDGERAVVTGGGRAIGLCCTEALAEAGAAVVVIERSEADAEQALALRNRGYDVEVRVGDVTDAARMDAIATELADGGRPATILVNNAGIGQSGIPAQDLTDADWLRMMDVNLNGVFWCSRAFGRSMISMKRGAIVNLGSMSGTICNRPQPQTAYNVSKAAVHHLTRSLAAEWAHHGIRVNAVAPTYIETPMVVAVEANRERIPLWLADTPMARMGTPEEVASAVLFLASGAASLMTGAIVNVDAGFTCW