>H281DRAFT_04746 FitnessBrowser__Burk376:H281DRAFT_04746
MRIILFSSRQYDIETFTGANSRHGYELHFQESHLDSETAVLAQGYEVVCPFVNDLVDAAVLERLYAGGTRMIALRSAGFNHVDLATAERLGIAVARVPAYSPHAVAEHAVGLILALNRRIPRAVARTREGDFSLHGLLGFDLHGKTVGVIGTGMIGRVFGRIMAGFGMRVLAHDPGTPASDLLALGARYVALDTLLAESDIVSLHCPLVPSTYHLIDAAALAKMKRGAMLINTGRGGLVESNALVGALKDGQLGHLGLDVYEEESGLFFEDHSNLPLQDDVLARLLMFPNVIVTAHQAFFTREAMNEIAQTTLDNVAAWQTGVPRNTVSATGTTSATGTAS
>BRENDA__Q9I530 D-lactate dehydrogenase (EC 1.1.1.28) (Pseudomonas aeruginosa)
MRILFFSSQAYDSESFQASNHRHGFELHFQQAHLQADTAVLAQGFEVVCAFVNDDLSRPVLERLAAGGTRLVALRSAGYNHVDLAAAEALGLPVVHVPAYSPHAVAEHAVGLILTLNRRLHRAYNRTREGDFSLHGLTGFDLHGKRVGVIGTGQIGETFARIMAGFGCELLAYDPYPNPRIQALGGRYLALDALLAESDIVSLHCPLTADTRHLIDAQRLATMKPGAMLINTGRGALVNAAALIEALKSGQLGYLGLDVYEEEADIFFEDRSDQPLQDDVLARLLSFPNVVVTAHQAFLTREALAAIADTTLDNIAAWQDGTPRNRVRA
>biolip__5z20F The ternary structure of d-lactate dehydrogenase from pseudomonas aeruginosa with nadh and oxamate
KVHHHHHMRILFFSSQAYDSESFQASNHRHGFELHFQQAHLQADTAVLAQGFEVVCAFVNDDLSRPVLERLAAGGTRLVALRSAGYNHVDLAAAEALGLPVVHVPAYSPHAVAEHAVGLILTLNRRLHRAYNRTREGDFSLHGLTGFDLHGKRVGVIGTGQIGETFARIMAGFGCELLAYDPYPNPRIQALGGRYLALDALLAESDIVSLHCPLTADTRHLIDAQRLATMKPGAMLINTGRGALVNAAALIEALKSGQLGYLGLDVYEEEADIFFEDRSDQPLQDDVLARLLSFPNVVVTAHQAFLTREALAAIADTTLDNIAAWQDGTPRNRVRA
>ecocyc__DLACTDEHYDROGNAD-MONOMER D-lactate dehydrogenase (EC 1.1.1.28) (Escherichia coli K-12 substr. MG1655)
MKLAVYSTKQYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSRPVLEELKKHGVKYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYPSAAALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFEQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNLEKGETCPNELV
>BRENDA__A0A140N893 D-lactate dehydrogenase (EC 1.1.1.28) (Escherichia coli)
MKLAVYSTKQYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSRPVLEELKKHGVKYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYPSAAALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNLEKGETCPNELV
>biolip__4cukA Structure of salmonella d-lactate dehydrogenase in complex with nadh
MKLAVYSTKQYDKKYLQQVNEAFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSRPVLEELKKHGVKYIALRCAGFNNVDLDAAKELGLQVVRVPAYSPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMHGKTAGVIGTGKIGVAALRILKGFGMRLLAFDPYPSTAALDLGVEYVDLQTLFAESDVISLHCPLTPENYHLLNHAAFDQMKNGVMIINTSRGALIDSQAAIEALKNQKIGSLGMDVYENERDLFFEDKSVDVIQDDVFRRLSACHNVLFTGHQAFLTAEALISISETTLQNLSQLEKGEACPNALFK
>SwissProt__A0A348AXY0 Probable dehydrogenase TR07; KK-1 biosynthesis cluster protein TR07; EC 1.1.1.- (Curvularia clavata)
MKLTVFSAKPYDIEYLGGIATNQNSSPAIEINFLHVPLSSETAAFANGADAVCVFVHDVLDANVLRELYAAGVRAILFRCSGYNNIDLREAERLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAYNRVRDGNFNLDGLLGRTLHGKTVGIVGSGRIGLAMAQIVQGFGCKLLAYDPRPTEAFKKYGEYVDLDTLLSQCDIVSLHCPLMDSTQHIINDTTVSKMKRGAMLVNTSRGGLIDTQSVMKALKSKRLGGLALDVYEGERALFYKDHSGDIIHDDLLMRLTTFHNVVVSGHQAYFTEEALTEIAECTLRNLDDWAKGVPTANALVQGRNSNGRRERGLARL
>BRENDA__Q8EI78 D-lactate dehydrogenase (EC 1.1.1.28) (Shewanella oneidensis)
MRIGFFSAKHYDMQHFNRTNAAFDAQIEYFDYRLCMQTVKLAEGFEVVCAFVNDSLCEEVLVELAKGGTKIIAMRCAGFNNVDLVAAKRLGMQVVNVPAYSPESVAEHTVALMLTLNRKIHKAYQRTRDANFSLEGLVGFNMFGKTVGVIGTGKIGVATIKVLLGFGCKVIAFDPYPNPAVEALDVEYQDLDTIYATSDIISLHCPLTPDNHHLLNKDSFAKMKPGVMVINTSRGGLLNAFDAMEALKLGQIGALGLDVYENEKELFFEDKSNQIIQDDVFRRLSACHNVIFTGHQAFLTEEALGAIANTTLSNVQAVLAGKRCGNELF
>SwissProt__Q2UH56 2-hydroxyacid dehydrogenase A; 2-HadhA; EC 1.1.1.272 (Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold))
MKLAVFSAKSYDKHYFDATLRKHHPALCEITYHSFALSSETVSLAQDSDAVCVFVNDQLDAPVLETLYANGVRAILLRCAGFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDPFGGEEFKKYGEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEEGALFYNDHSGEIIHDDVLMRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDFVLKRTCKNSLVREGHLVVPTDKEPVRL
>BRENDA__Q8RG11 D-lactate dehydrogenase (EC 1.1.1.28) (Fusobacterium nucleatum subsp. nucleatum)
MQKTKIIFFDIKDYDKEFFKKYGADYNFEMTFLKVRLTEETANLTKGYDVVCGFANDNINKETIDIMAENGIKLLAMRCAGFNNVSLKDVNERFKVVRVPAYSPHAIAEYTVGLILAVNRKINKAYVRTREGNFSINGLMGIDLYEKTAGIIGTGKIGQILIKILRGFDMKVIAYDLFPNQKVADELGFEYVSLDELYANSDIISLNCPLTKDTKYMINRRSMLKMKDGVILVNTGRGMLIDSADLVEALKDKKIGAVALDVYEEEENYFFEDKSTQVIEDDILGRLLSFYNVLITSHQAYFTKEAVGAITVTTLNNIKDFVEGRPLVNEVPQNQ
>biolip__5z21B The ternary structure of d-lactate dehydrogenase from fusobacterium nucleatum with nadh and oxamate
KTKIIFFDIKDYDKEFFKKYGADYNFEMTFLKVRLTEETANLTKGYDVVCGFANDNINKETIDIMAENGIKLLAMRCAGFNNVSLKDVNERFKVVRVPAYSPHAIAEYTVGLILAVNRKINKAYVRTREGNFSINGLMGIDLYEKTAGIIGTGKIGQILIKILRGFDMKVIAYDLFPNQKVADELGFEYVSLDELYANSDIISLNCPLTKDTKYMINRRSMLKMKDGVILVNTGRGMLIDSADLVEALKDKKIGAVALDVYEEEENYFFEDKSTQVIEDDILGRLLSFYNVLITSHQAYFTKEAVGAITVTTLNNIKDFVEGRPLVNEVPQ
>biolip__4zgsA Identification of the pyruvate reductase of chlamydomonas reinhardtii
TPQEAAKVATTRCICYSTTQYVKDFLAGPMQKVFTDTYFVEPPLDKDTAQLARGYDVAVLFVNDRADASVIKELAKAGVKLIALRCAGFDRVDLHACAEHGVRVVRVPTYSPESVAEHAVALIFALNRHLTDAYIRVRMGNYSLSGLVGVEMRHKVVGVVGTGAIGQQAARILKGIGCKVFAYDIKPNPAVEAMGIPYVSLDELLAMSDIVTLHCPLLPSTRQLINKESIQKMKKGVMLINVSRGGLIDSAALFDALESGQIGALGLDVYENEGGLFFVDHTKFDPSVRMQKWDRQFRTLLSYPQVLVTPHTAFLTEEALNNICTTTIQNIADYVLDRPLGNEVKA
>BRENDA__F8A9V0 D-lactate dehydrogenase (EC 1.1.1.28) (Thermodesulfatator indicus)
MKVIFFSMHPYEEEFLGPILPSDWDVEMTPDFLDETTVEKAKGAQVVSLFVSDKADGPVLEALHSYGVGLLALRSAGYDHIDIETAKRLGIKVVNVPAYSPHAIADHTLAIMLALIRRLHRAHDKVRLGDFDLDGLMGFDLNGKVAGVIGLGKIGRLVATRLKAFGCKVLGYDPYIQPEIVENVDLDTLITQADIISIHCPLTRENFHMFNEETFKRMKPGAILVNTARGGLIDTKALLEALKSGKLGGAALDVYEYERGLFFKNHQKEGIKDPYLAQLLGLANVVLTGHQAFLTREAVKNIEETTVENILEWQKNPQAKLKNEI
>biolip__8grvA Dictyostelium discoideum lactate dehydrogenase (dicldha)with NAD
ADMKITLFSSKPYWVKWFNELNKFSYEINYVTSACDIKSVNEAKGSEAVCCFVNDDLSKEVIETLHSNGTKVILMRCAGFNKVDLDTANKLGIPVLRVPAYSPNAVSEYALSLIMALNRKTHKAHDRVRDANFEINGMEGFNMVSKVYGIVGTGNIGEQLCRVLKLGFGAKVIAYDIIENKAVTDIGIEYVKTLDEIWKQCDVISLHTPLNSQTKYMVNSESIEKMRDGVMIINVSRGALVNASDAIVGLKSGKISSLGMDVYENETDYFYQDHNGSIIKDDNLSLLISYPNVMITSHQAWYTKEAISCICGTSLQNFVDFRSNQIKKSNLVNNPI
>metacyc__MONOMER-8131 aromatic 2-oxoacid reductase (EC 1.1.1.110) (Clostridium sporogenes (strain ATCC 7955 / DSM 767 / NBRC 16411 / NCIMB 8053 / NCTC 8594 / PA 3679))
MKILAYCVRPDEIDSFKNFSEKYGHTVDLIPDSFGPSVAHLAKGYDGISILGNDTCNREALEKIKDCGIKYLATRTAGVNNIDFDAAKEFGINVANVPAYSPNSVSEFTVGLALSLTRKIPFALKRVELNNFALGGLIGVELRNLTLGVIGTGRIGLKVIEGFSGFGMKKMIGYDIFENEKAKEYIEYKSLDEVYKEADIITLHAPLTDDNYHMIGKESIAKMKDGVFIINAARGALIDSEALIEGLKSGKIAGAALDSYEYEQGVFHNNKMNEIMKDDTLARLKSFPNVVITPHLGFYTDEAVSNMVEITLMNLQEFELKGTCKNQRVCK
>SwissProt__J7SHB8 Aromatic 2-oxoacid reductase; Indolelactate dehydrogenase; EC 1.1.1.110 (Clostridium sporogenes (strain ATCC 15579))
MKILAYCVRPDEIDSFKNFSEKYGHTVDLIPDSFGPNVAHLAKGYDGISILGNDTCNREALEKIKDCGIKYLATRTAGVNNIDFDAAKEFGINVANVPAYSPNSVSEFTVGLALSLTRKIPFALKRVELNNFALGGLIGVELRNLTLGVIGTGRIGLKVIEGFSGFGMKKMIGYDIFENEKAKEYIEYKSLDEVYKEADIITLHAPLTDDNYHMIGKESIAKMKDGVFIINAARGALIDSEALIEGLKSGKIAGAALDSYEYEQGVFHNNKMNEIMKDDTLERLKSFPNVVITPHLGFYTDEAVSNMVEITLMNLQEFELKGTCKNQRVCK
>metacyc__MONOMER-15467 D-lactate dehydrogenase (EC 1.1.1.28) (Enterococcus faecium)
MNNIGITVYGCEQDEADAFHALSPRFGVMATIINANVSESNAKSAPFNQCISVGHKSEISASILLALKRAGVKYISTRSIGCNHIDTTAAKRMGITVDNVAYSPDSVADYTMMLILMAVRNVKSIVRSVEKHDFRLDSDRGKVLSDMTVGVVGTGQIGKAVIERLRGFGCKVLAYSRSRSIEVNYVPFDELLQNSDIVTLHVPLNTDTHYIISHEQIQRMKQGAFLINTGRGPLVDTYELVKALENGKLGGAALDVLEGEEEFFYSDCTQKPIDNQFLLKLQRMPNVIITPHTAYYTEQALRDTVEKTIKNCLDFERRQEHE
>SwissProt__P17584 D-2-hydroxyisocaproate dehydrogenase; D-HICDH; EC 1.1.1.- (Lacticaseibacillus paracasei (Lactobacillus paracasei))
MKIIAYGARVDEIQYFKQWAKDTGNTLEYHTEFLDENTVEWAKGFDGINSLQTTPYAAGVFEKMHAYGIKFLTIRNVGTDNIDMTAMKQYGIRLSNVPAYSPAAIAEFALTDTLYLLRNMGKVQAQLQAGDYEKAGTFIGKELGQQTVGVMGTGHIGQVAIKLFKGFGAKVIAYDPYPMKGDHPDFDYVSLEDLFKQSDVIDLHVPGIEQNTHIINEAAFNLMKPGAIVINTARPNLIDTQAMLSNLKSGKLAGVGIDTYEYETEDLLNLAKHGSFKDPLWDELLGMPNVVLSPHIAYYTETAVHNMVYFSLQHLVDFLTKGETSTEVTGPAK
>biolip__1dxyA Structure of d-2-hydroxyisocaproate dehydrogenase
MKIIAYGARVDEIQYFKQWAKDTGNTLEYHTEFLDENTVEWAKGFDGINSLQTTPYAAGVFEKMHAYGIKFLTIRNVGTDNIDMTAMKQYGIRLSNVPAYSPAAIAEFALTDTLYLLRNMGKVQAQLQAGDYEKAGTFIGKELGQQTVGVMGTGHIGQVAIKLFKGFGAKVIAYDPYPMKGDHPDFDYVSLEDLFKQSDVIDLHVPGIEQNTHIINEAAFNLMKPGAIVINTARPNLIDTQAMLSNLKSGKLAGVGIDTYEYETEDLLNLAKHGSFKDPLWDELLGMPNVVLSPHIAYYTETAVHNMVYFSLQHLVDFLTKGETSTEVTG
>BRENDA__E0NDE9 D-lactate dehydrogenase (EC 1.1.1.28) (Pediococcus acidilactici)
MKIIAYGIRDDEKPYLDEWVTKNHIEVKAVPDLLDSSNIDLAKDYDGVVAYQQKPYTADLFDKMHEFGIHAFSLRNVGVDNVPADALKKNDIKISNVPAYSPRAIAELSVTQLLALLRKIPEFEYKMAHGDYRWEPDIGLELNQMTVGVIGTGRIGRAAIDIFKGFGAKVIAYDVFRNPALEKEGMYVDTLEELYQQANVITLHVPALKDNYHMLDEKAFGQMQDGTFILNFARGTLIDTPALLKALDSGKVAGAALDTYENEVGIFDVDHGDQPIDDPVFNDLMSRRNVMITPHAAFYTRPAVKNMVQIALDNNRDLIEKNSSKNEVKFD
>SwissProt__P26297 D-lactate dehydrogenase; D-LDH; D-specific 2-hydroxyacid dehydrogenase; EC 1.1.1.28 (Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14))
MTKIFAYAIREDEKPFLKEWEDAHKDVEVEYTDKLLTPETVALAKGADGVVVYQQLDYTAETLQALADNGITKMSLRNVGVDNIDMAKAKELGFQITNVPVYSPNAIAEHAAIQAARILRQDKAMDEKVARHDLRWAPTIGREVRDQVVGVIGTGHIGQVFMQIMEGFGAKVIAYDIFRNPELEKKGYYVDSLDDLYKQADVISLHVPDVPANVHMINDESIAKMKQDVVIVNVSRGPLVDTDAVIRGLDSGKIFGYAMDVYEGEVGIFNEDWEGKEFPDARLADLIARPNVLVTPHTAFYTTHAVRNMVVKAFDNNLELVEGKEAETPVKVG
>BRENDA__F8RPR8 D-lactate dehydrogenase (EC 1.1.1.28) (Weizmannia coagulans)
MRKVVAYETRADEFPLFQKFARKFDLDIKYIDDVLTPETAMEAKGAEAVTILGNYPVGSGTFKALRDVGVKYIGLRTAGNNHIDQEAAKAYGIRFSNVAYSPYCVADFATMLILMCVRKAKQILSRVEAQDFSVEGIQGREMRNLTIGIIGAGRIGSIVAKNLSGFGCNLIAHDTVERDELRGILKYVSLDELLEESDVITIHTPLFESTYHMINQERIAKIKDGVCIINCSRGAEVDTYALIAGIEAGKAGAAGIDVLEDEEGIFHYDRRTDILDHRQLAILRSFPNVIVTPHTAFYPNQAVSDMAEMALTSLVSFVETGKSRWEIKS
>SwissProt__Q59642 D-lactate/D-glycerate dehydrogenase; D-LDH/GDH; D-specific 2-hydroxyacid dehydrogenase; EC 1.1.1.28; EC 1.1.1.29 (Pediococcus acidilactici)
MKIIAYGIRDDEKPYLDEWVTKNHIEVKAVPDLLDSSNIDLAKDYDGVVAYQQKPYTADLFDKMHEFGIHAFSLRNVGLDNVPADALKKNDIKISNVPAYSPRAIAELSVTQLLALLRKIPEFEYKMAHGDYRWEPDIGLELNQMTVGVIGTGRIGRAAIDIFKPFGAKVIAYDVFRNPALEKEGMYVDTLEELYQQANVITLHVPALKDNYHMLDEKAFGQMQDGTFILNFARGTLVDTPALLKALDSGKVAGAALDTYENEVGIFDVDHGDQPIDDPVFNDLMSRRNVMITPHAAFYTRPAVKNMVQIALDNNRDLIEKNSSKNEVKFE
>BRENDA__O66939 D-lactate dehydrogenase (EC 1.1.1.28) (Aquifex aeolicus)
MNVLFTSVPQEDVPFYQEALKDLSLKIYTTDVSKVPENELKKAELISVFVYDKLTEELLSKMPRLKLIHTRSVGFDHIDLDYCKKKGILVTHIPAYSPESVAEHTFAMILTLVKRLKRIEDRVKKLNFSQDSEILARELNRLTLGVIGTGRIGSRVAMYGLAFGMKVLCYDVVKREDLKEKGCVYTSLDELLKESDVISLHVPYTKETHHMINEERISLMKDGVYLINTARGKVVDTDALYRAYQRGKFSGLGLDVFEDEEILILKKYTEGKATDKNLKILELACKDNVIITPHIAYYTDKSLERIREETVKVVKAFVKGDLEQIKGNFVVGPS
>biolip__1j49A Insights into domain closure, substrate specificity and catalysis of d-lactate dehydrogenase from lactobacillus bulgaricus
MTKIFAYAIREDEKPFLKEWEDAHKDVEVEYTDKLLTPETVALAKGADGVVVYQQLDYIAETLQALADNGITKMSLRNVGVDNIDMAKAKELGFQITNVPVYSPNAIAEHAAIQAARILRQDKAMDEKVARHDLRWAPTIGREVRDQVVGVVGTGHIGQVFMQIMEGFGAKVITYDIFRNPELEKKGYYVDSLDDLYKQADVISLHVPDVPANVHMINDESIAKMKQDVVIVNVSRGPLVDTDAVIRGLDSGKIFGYAMDVYEGEVGIFNEDWEGKEFPDARLADLIARPNVLVTPHTAFYTTHAVRNMVVKAFDNNLELVEGKEAETPVKV
>metacyc__G12WB-500-MONOMER 4-methyl-2-oxopentanoate reductase (EC 1.1.1.345) (Clostridioides difficile (strain 630))
MKILVFGARDYEEPVIKKWSEEHKDVQVDIYPENMTEENVVKAKGYDGISIQQTNYIDNPYIYETLKDAGVKVIASRTAGVDMIHFDLVNENGLIVTNVPSYSPNAIAELAVTQAMNLLRKTPLVKKKVCEGDYRWIAELLGTEVRSITVGVIGTGKIGATSAKLFKGLGANVIAFDQYPNSDLNDILTYKDSLEDLLKEADLITLHTPLLEGTKHMINKDTLAIMKDGAYIVNTGRGGLINTGDLIEALESGKIRAAALDTFETEGLFLNKKMNPGELTDPEINKLLSMEQVIFTHHLGFFTSTAIENIVYSSLSSAVEVIKTGTATNRVN
>BRENDA__P30901 D-lactate dehydrogenase (EC 1.1.1.28) (Lactobacillus helveticus)
MTKVFAYAIRKDEEPFLNEWKEAHKDIDVDYTDKLLTPETAKLAKGADGVVVYQQLDYTADTLQALADAGVTKMSLRNVGVDNIDMDKAKELGFQITNVPVYSPNAIAEHAAIQAARVLRQDKRMDEKMAKRDLRWAPTIGREVRDQVVGVVGTGHIGQVFMRIMEGFGAKVIAYDIFKNPELEKKGYYVDSLDDLYKQADVISLHVPDVPANVHMINDKSIAEMKDGVVIVNCSRGRLVDTDAVIRGLDSGKIFGFVMDTYEDEVGVFNKDWEGKEFPDKRLADLIDRPNVLVTPHTAFYTTHAVRNMVVKAFNNNLKLINGEKPDSPVALNKNKF
>SwissProt_P30901 D-lactate dehydrogenase; D-LDH; D-specific 2-hydroxyacid dehydrogenase; EC 1.1.1.28 from Lactobacillus helveticus (Lactobacillus suntoryeus)
MTKVFAYAIRKDEEPFLNEWKEAHKDIDVDYTDKLLTPETAKLAKGADGVVVYQQLDYTADTLQALADAGVTKMSLRNVG
VDNIDMDKAKELGFQITNVPVYSPNAIAEHAAIQAARVLRQDKRMDEKMAKRDLRWAPTIGREVRDQVVGVVGTGHIGQV
FMRIMEGFGAKVIAYDIFKNPELEKKGYYVDSLDDLYKQADVISLHVPDVPANVHMINDKSIAEMKDGVVIVNCSRGRLV
DTDAVIRGLDSGKIFGFVMDTYEDEVGVFNKDWEGKEFPDKRLADLIDRPNVLVTPHTAFYTTHAVRNMVVKAFNNNLKL
INGEKPDSPVALNKNKF
>BRENDA__A0A0M3KL04 D-lactate dehydrogenase (EC 1.1.1.28) (Sporolactobacillus inulinus)
MKIIMFSVRDDEEAAIREWEKKTGVQVDINRLELDAETAQLTKGYDGIVIQQRSHISNPAVYETLQKNGLRQLTSRTAGYDMIDLEQASERGLVVTNVPAYSPNSVAELALTQTMRLIRNLPLFDARGAEQDFRWAGLMAREIRSLTVGIIGAGRIGGTVARLFKALGATVIANDIVERVELKDIVTYVSKEELLQAADVVTLHVPLMDSTTQLIDADALALMKNDAVLINASRGPVVDTDALIAALQNKQIAGAALDTLNGEEHFFNQDLCGKELPSEQLKVLRTLPNVLITPHIGFYTNKAVQNMVEISLNDVLAILKTGTSEHQLNKVAVEN
>biolip__4xkjA A novel d-lactate dehydrogenase from sporolactobacillus sp
MKIIMFSVRDDEEAAIREWEKKTGVQVDINRLELDAETAQLTKGYDGIVIQQRSHISNPAVYETLQKNGLRQLTSRTAGYDMIDLEQASERGLVVTNVPAYSPNSVAELALTQTMRLIRNLPLFDARGAEQDFRWAGLMAREIRSLTVGIIGAGRIGGTVARLFKALGATVIANDIVERVELKDIVTYVSKEELLQAADVVTLHVPLMDSTTQLIDADALALMKNDAVLINASRGPVVDTDALIAALQNKQIAGAALDTLNGEEHFFNQDLCGKELPSEQLKVLRTLPNVLITPHIGFYTNKAVQNMVEISLNDVLAILKTGTSEHQLNKVA
>metacyc__MONOMER-8683 D-lactate dehydrogenase subunit (EC 1.1.1.28) (Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1))
MKIIAYAVRDDERPFFDTWMKENPDVEVKLVPELLTEDNVDLAKGFDGADVYQQKDYTAEVLNKLADEGVKNISLRNVGVDNLDVPTVKARGLNISNVPAYSPNAIAELSVTQLMQLLRQTPLFNKKLAKQDFRWAPDIAKELNTMTVGVIGTGRIGRAAIDIFKGFGAKVIGYDVYRNAELEKEGMYVDTLDELYAQADVITLHVPALKDNYHMLNADAFSKMKDGAYILNFARGTLIDSEDLIKALDSGKVAGAALDTYEYETKIFNKDLEGQTIDDKVFMNLFNRDNVLITPHTAFYTETAVHNMVHVSMNSNKQFIETGKADTQVKFD
>biolip__4prlA Crystal structure of d-lactate dehydrogenase with NAD+ from lactobacillus jensenii
MKIAVFSPSESERKLVAATEKKFGCELKLIDESLSAENVDQVADCDGVLLKPLGNLDDEIVYKKLADYGIKSIGLRIVGTNTIDFDLAKKYHLTVTNVPVYSPRAIAEMAVTQAMYLNRKIGEFKANMDKGDFTNPDSLISNEIYNKTIGLIGVGHIGSAVAQIFSAMGAKVLAYDVIYNPEVEPYLTYADFDTVLKEADIISLHTPLLKSTENMIGKKQFAEMKNDAILINAARGELVDTAALIEALEKHEIAAAGLDTLAHESSYFFKKVDDAQIPADYKKLAAMPNVIVTPHSAYFTKTSVRNMIEISLRDTIALANGERAHFVVSR
>metacyc__MONOMER-13061 D-lactate dehydrogenase subunit (EC 1.1.1.28) (Leuconostoc mesenteroides subsp. cremoris)
MKIFAYGIRDDEKPSLEEWKAANPEIEVDYTQELLTPETAKLAEGSDSAVVYQQLDYTRETLTALANVGVTNLSLRNVGTDNIDFDAAREFNFNISNVPVYSPNAIAEHSMLQLSRLLRRTKALDAKIAKRDLRWAPTTGREMRMQTVGVIGTGHIGRVAINILKGFGAKVIAYDKYPNAELQAEGLYVDTLDELYAQADAISLYVPGVPENHHLINADAIAKMKDGVVIMNAARGNLMDIDAIIDGLNSGKISDFGMDVYENEVACSMKIGLVKNSPDAKIADLIARENVMITPHTAFYTTKAVLEMVHQSFDAAVAFAKGEKPAIAVEY
>CharProtDB__CH_091795 D-lactate dehydrogenase; EC 1.1.1.28 (Lactobacillus pentosus)
MKIIAYAVRDDERPFFDTWMKENPDVEVKLVPELLTEDNVDLAKGFDGADVYQQKDYTAEVLNKLADEGVKNISLRNVGVDNLDVPTVKARGLNISNVPAYSPNAIAELSVTQLMQLLRQTPMFNKKLAKQDFRWAPDIAKELNTMTVGVIGTGRIGRAAIDIFKGFGAKVIGYDVYRNAELEKEGMYVDTLDELYAQADVITLHVPALKDNYHMLNADAFSKMKDGAYILNFARGTLIDSEDLIKALDSGKVAGAALVTYEYETKIFNKDLEGQTIDDKVFMNLFNRDNVLITPHTAFYTETAVHNMVHVSMNSNKQFIETGKADTQVKFD
>BRENDA__O83080 D-lactate dehydrogenase (EC 1.1.1.28) (Treponema pallidum)
MRCVVFNLREEEAPYVEKWKQSHPGVVVDTYEEPLTAKNKELLKGYEGLVVMQFLAMEDEVYDYMGACKLKVLSTRTAGFDMYNATLLKKHGIRLTNVPSYSPNAIGEYALAAALQLTRHAREIETFVRKRDFRWQKPILSKELRCSRVGILGTGRIGQAAARLFKGVGAQVVGFDPYPNDAAKEWLTYVSMDELLSTSDVISLHMPATKDSHHLINAKTIAQMKDGVYLVNTARGAVIDSQALLDSLDKGKIAGAALDAYEFEGPYIPKDNGNNPITDTVYARLVAHERIIYTPHIAFYTETAIENMVFNSLDACTTVLRGEPCAAEIKL
>BRENDA__A0A0R1RJ30 D-lactate dehydrogenase (EC 1.1.1.28) (Furfurilactobacillus rossiae)
MEVSALKIIAYGIRDDERPYVEEWSKDQNIEVKIVKDLLTDDTVDQAKGFDGAVVYQQKPYTASVLDRLAELGVKNLSLRNVGVDNVDADAVKRNDIKVTNVPAYSPAAIAEFTVTELMRLLRHTTQYEHRQAKGDLKWTPDIATELNSLTVGVIATGRIGRAAIQIYRGFGAKIVAYDVFHNPELEKEGIYVDSLDELYKQADVISLHAPATKENMHMLNADAFNKMKDGVYILNPARGDLVDTDDLIKALDSGKVAGAALDVYENEVGIFNTDFGSFDAIPDDRLKNLMKRENVLVSPHIAFYTTTAVRNMVQFALNNNKQLIETGKADNVVAFN
>metacyc__MONOMER-3821 hydroxypyruvate reductase subunit (EC 1.1.1.81) (Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1))
MTKKVVFLDRESLDATVREFNFPHEYKEYESTWTPEEIVERLQGAEIAMINKVPMRADTLKQLPDLKLIAVAATGTDVVDKAAAKAQGITVVNIRNYAFNTVPEHVVGLMFALRRAIVPYANSVRRGDWNKSKQFCYFDYPIYDIAGSTLGIIGYGALGKSIAKRAEALGMKVLAFDVFPQDGLVDLETILTQSDVITLHVPLTPDTKNMIGAEQLKKMKRSAILINTARGGLVDEAALLQALKDGTIGGAGFDVVAQEPPKDGNILCDADLPNLIVTPHVAWASKEAMQILADQLVDNVEAFVAGKPQNVVEA
>SwissProt__D2RJU7 (R)-2-hydroxyglutarate dehydrogenase; HGDH; EC 1.1.1.399 (Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4))
MKVLCYGVRDVELPIFEACNKEFGYDIKCVPDYLNTKETAEMAAGFDAVILRGNCFANKQNLDIYKKLGVKYILTRTAGTDHIDKEYAKELGFPMAFVPRYSPNAIAELAVTQAMMLLRHTAYTTSRTAKKNFKVDAFMFSKEVRNCTVGVVGLGRIGRVAAQIFHGMGATVIGEDVFEIKGIEDYCTQVSLDEVLEKSDIITIHAPYIKENGAVVTRDFLKKMKDGAILVNCARGQLVDTEAVIEAVESGKLGGYGCDVLDGEASVFGKDLEGQKLENPLFEKLVDLYPRVLITPHLGSYTDEAVKNMVEVSYQNLKDLAETGDCPNKIK
>SwissProt__Q9X1C1 Hydroxypyruvate reductase; HPR; EC 1.1.1.81 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
MARYRVHVNDPLDKEATQLLMNKEELEVTSEHLEKDELMKIIPEVDVLVVRSATKVTADIIEAGKNLKIIARAGIGLDNIDVQKAKEKGIKVLNTPGASAPSVAELAMGLMLACARHIARATVSLKEGKWEKKALKGKELLGKTLGLIGFGNIGQEVAKRALAFGMKIIAYDPAKPETDLPVEYVDLDTLFKESDFISLHVPLTESTRHIINRESIAKMKDGVIIVNTARGGTIDEEALYEEVVSGKVYAAGLDVFEVEPPTDEIRRKLLSLDNVVATPHIGASTAEAQRRVGIELVEKIFKELGI
>biolip__2yq5C Crystal structure of d-isomer specific 2-hydroxyacid dehydrogenase from lactobacillus delbrueckii ssp. Bulgaricus: NAD complexed form
TKIAMYNVSPIEVPYIEDWAKKNDVEIKTTDQALTSATVDLAEGCSSVSLKPLGPVDEEVVYQKLSEYGVKCIGLRIVGFNTINFDWTKKYNLLVTNVPVYSPRAIAEMTVTQAMYLLRKIGEFRYRMDHDHDFTWPSNLISNEIYNLTVGLIGVGHIGSAVAEIFSAMGAKVIAYDVAYNPEFEPFLTYTDFDTVLKEADIVSLHTPLFPSTENMIGEKQLKEMKKSAYLINCARGELVDTGALIKALQDGEIAGAGLDTLAGESSYFGHTGLTDSEIPEDYKTLAKMPNVVITPHSAFYTETSIRNMVQICLTDQLTIAKGGRPRSIVN
>BRENDA__Q1GAA2 D-lactate dehydrogenase (EC 1.1.1.28); D-2-hydroxyacid dehydrogenase (NAD+) (EC 1.1.1.345) (Lactobacillus delbrueckii subsp. bulgaricus)
MTKIAMYNVSPIEVPYIEDWAKKNDVEIKTTDQALTSATVDLAEGCSSVSLKPLGPVDEEVVYQKLSEYGVKCIGLRIVGFNTINFDWTKKYNLLVTNVPVYSPRAIAEMTVTQAMYLLRKIGEFRYRMDHDHDFTWPSNLISNEIYNLTVGLIGVGHIGSAVAEIFSAMGAKVIAYDVAYNPEFEPFLTYTDFDTVLKEADIVSLHTPLFPSTENMIGEKQLKEMKKSAYLINCARGELVDTGALIKALQDGEIAGAGLDTLAGESSYFGHTGLTDSEIPEDYKTLAKMPNVVITPHSAFYTETSIRNMVQICLTDQLTIAKGGRPRSIVNL
>BRENDA__Q48534 D-2-hydroxyacid dehydrogenase (NAD+) (EC 1.1.1.345) (Lactobacillus delbrueckii)
MTKIAMYNVSPIEVPYIEDWAKKNDVEIKTTDQALTSATVDLAEGCSSVSLKPLGPVDEEVVYQKLSEYGVKCIGLRIVGFNTINFDWTKKYNLLVTNVPVYSPRAIAEMTVTQAMYLLRKIGEFRYRMDHDHDFTWPSNLISNEIYNLTVGLIGVGHIGSGLAEIFSAMGAKVIAYDVAYNPEFEPFLTYTDFDTVLKEADIVSLHTPLFPSTENMIGEKQLKEMKKSAYLINCARGELVDTGALIKALQDGEIAGAGLDTLAGESSYFGHTGLTDSEIPEDYKTLAKMPNVVITPHSAFYTETSIRNMVQICLTDQLTIAKGRRPRSIVNL
>biolip__1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
MKVLVAAPLHEKAIQVLKDAGLEVIYEEYPDEDRLVELVKDVEAIIVRSKPKVTRRVIESAPKLKVIARAGVGLDNIDVEAAKEKGIEVVNAPAASSRSVAELAVGLMFSVARKIAFADRKMREGVWAKKEAMGIELEGKTIGIIGFGRIGYQVAKIANALGMNILLYDPYPNEERAKEVNGKFVDLETLLKESDVVTIHVPLVESTYHLINEERLKLMKKTAILINTSRGPVVDTNALVKALKEGWIAGAGLDVFEEEPLPKDHPLTKFDNVVLTPHIGASTVEAQERAGVEVAEKVVKILKG
>BRENDA__Q03V58 D-2-hydroxyacid dehydrogenase (NAD+) (EC 1.1.1.345) (Leuconostoc mesenteroides subsp. mesenteroides)
MNKILMTSVRSDEEQAIRHYAEKNNVEIVISRDDFHPETLPDLTEIDGLVIQQTAKIGGDQQFYHHIAKQITQIATRTAGYDMIEVDLAKKAGLKITNVPAYSPRSVAEMALMQILRLLRHTPEFDKRIANNDFRWTGLQAREIHSVTIGIVGVGRIGGTLAKLLNSIGVNVLGYDTDRDASLCDVITYVTKDELLAQSDVISLHVDLNETSIHLLSEADFLKMKKGVLLINASRGPVINTSDLITFLGNGQVGAVALDTVENESGVFNHDLHGQGVQDARIQKLLSMSNVIITPHVGFFTNIAVKNMVDISLDDTLMILNGQSSPHEV
>SwissProt__Q9C4M5 Glyoxylate reductase; EC 1.1.1.26 (Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C))
MKPKVFITRQIPENGIKMIEKFYEIELWKDPKAPPRGVLLEKVREVDALVTLVTDKVDKELLENAPKLKIIAQYAVGYDNIDIEEATKRGIYVTNTPGVLTDATADLAFALLLAVARRIVEADAFVRSGEWKKSEVGWHPLMFLGYGLKGKTLGIVGFGRIGQALAKRAKGFGMKIIYYSRTRKPEAEEEIGAEYVDFETLLKESDFISLHVPLTKETYHMIGEKELKLMKPNAILINTSRGAVVDTNALIKALKEGWIAGAGLDVFEEEPYYNEELFKLKNVVLAPHIGSATHEAREGMAELVAKNLIAFAKGEIPPNLVNKDVLTSSPP
>metacyc__SGL_RS08600-MONOMER glycerate dehydrogenase (EC 1.1.1.29) (Synechocystis sp. (strain PCC 6803 / Kazusa))
MNLAWLQGLSLGLLSPPAPALLIFRSFTMAKVLVSDSIDQVGIDILKQVAQVDVKTGLSEAEIIDIVPEYDAIMLRSATKVTEKIIQAGSQLKIIGRAGVGVDNIDVPAATRQGIVVVNSPEGNTIAAAEHALAMMMALARHIPDANKSVKESKWERKQFIGTEVYKKTLGVVGLGKIGSHVAGVAKAMGMKLLAYDPFISQERADQIGCTLVDLDLLFSEADFITLHIPKTPETANLINAETLAKMKPTARIINCSRGGIIDEEALVTAIETAQIGGAALDVFAQEPLGESRLREFSNVILTPHLGASTEEAQVNVAVDVAEQIRDVLLGLPARSAVNIPGLTPDVMEKLRPYLKLAETLGTLVGQLAGGRIDRLTVCLQGDLAEYTNSQPLVVAAIKGLLSQALRERVNYVNAAIEAKERGIRVIETKDASVRDYSGSLHLKATGTMGEHSATGALLSNGEIRITDVDEFPINVPPNNYMLFTLHRDMPGIIGKIGSLLGSFNVNIASMQVGRKIVRGDAIMALSLDDPLPDGLLSEITKVAGIRDAYTVKL
>biolip__5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate
MKPKVFITRAIPENGINMLEEEFEVEVWEEEREIPREKLLEKVKDVDALVTMLSERIDQEVFENAPRLRIVANYAVGYDNIDVEEATRRGIYVTNTPDVLTNATADHAFALLLATARHVVKGDKFVRSGEWKRKGIAWHPKWFLGYELYGKTIGIVGFGRIGQAIARRAKGFNMRILYYSRTRKSQAEKELGAEYRPLEEVLKESDFVILAVPLTKETMYMINEERLKLMKPTAILVNIARGKVVDTKALIKALKEGWIAGAGLDVFEEEPYYNEELFSLDNVVLTPHIGSATFEAREAMAELVARNLIAFKRGEIPPTLVNKEVIKIRKPGFN
>BRENDA__Q8U3Y2 glyoxylate reductase (NADP+) (EC 1.1.1.79); hydroxypyruvate reductase (EC 1.1.1.81) (Pyrococcus furiosus)
MKPKVFITRAIPENGINMLEEEFEVEVWEEEREIPREKLLEKVKDVDALVTMLSERIDQEVFENAPRLRIVANYAVGYDNIDVEEATRRGIYVTNTPDVLTNATADHAFALLLATARHVVKGDKFVRSGEWKRKGIAWHPKWFLGYELYGKTIGIVGFGRIGQAIARRAKGFNMRILYYSRTRKSQAEKELGAEYRPLEEVLKESDFVILAVPLTKETMYMINEERLKLMKPTAILVNIARGKVVDTKALIKALKEGWIAGAGLDVFEEEPYYNEELFSLDNVVLTPHIGSATFEAREAMAELVARNLIAFKRGEIPPTLVNKEVIKIRKPGFNEQ
>SwissProt__C0CMQ8 Hydroxypyruvate reductase; EC 1.1.1.81 (Blautia hydrogenotrophica (strain DSM 10507 / JCM 14656 / S5a33) (Ruminococcus hydrogenotrophicus))
MKIVVLDGYCLNPGDLDWKGLEALGECIVYDRTSLTDMEEVISRIGDADIVYTNKTPMPREVFEKCPNIRFVGVLATGYNVVDVNTAKEKGIPVANIPTYGTASVGQFAIALLLEICHHVGHHNQVVHEGKWESNPDWCFWDYPLIELDGKNMGIIGYGRIGQATGKIAQALGMKVLAYDAYKNPALENENCRYVELDELLSQSDVIALHCPLFPETEGIVNKENIAKMKDGVIILNNSRGPLIVEQDLVDALNSGKVAAAGLDVVSTEPIKGDNPLLGAKNCIITPHISWAPKESRKRLMDIAVNNLEEFLKGSPVNVVNK
>SwissProt__O49485 D-3-phosphoglycerate dehydrogenase 1, chloroplastic; Protein EMBRYO SAC DEVELOPMENT ARREST 9; EC 1.1.1.95 (Arabidopsis thaliana (Mouse-ear cress))
MSATAAASSSIAVATNSLRNVTLSSRSPLPSAISVAFPSRGRNTLQRRLVLVSCSTGDGSKPTILVAEKLGDAGIKLLEDVANVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESSHGRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGELAATAVNAPMVSAEVLTELKPYVVLAEKLGRLAVQLVAGGSGVKNAKITYASARATDDLDTRLLRAMITKGIIEPISDVYVNLVNADFTAKQRGLRLSEERVLLDGSPESPLETITVQLSNVESKFASSLSESGEVKVEGKVKDGVPHLTKVGSFEVDVTLEGSIILCRQVDQPGMIGTVGSILGESNVNVNFMSVGRIAPRKQAIMAIGVDDIPSKETLKKIGEIPAVEEFVFLKL
>BRENDA__A0A2R6X868 phosphoglycerate dehydrogenase (EC 1.1.1.95) (Marchantia polymorpha)
MAATSAVAAVVAGALGAVPQRTDLAAAAAVPSRACSVSSLASFQSLSASCKTARSARAVSKKVGGRQIVCSVAAPSTSPRSASTEIVGKPTVLVAEKLGEAGLELLKKIANVDCSYNLSQEELCAKISLCDALIVRSGTKVTREVFEASNGRLKVVGRAGVGIDNVDLQAATEVGCLVVNAPTANTIAAAEHGIALLTALARNVAQASASMKAGEWKRNKYVGVSLVDKTLAVMGFGKVGSEVARRAKGLGMQVIAHDPYAPADRARAIGVELVSFDEALQRADFISLHMPLTPSTDKCFNDESFAKCKKGVRIVNVARGGVIDEEALVRALDSGIVAQAALDVFTVEPPAKDDKLIQHENVVVTPHLGASTMEAQEGVAVEIAEAVVGALQGELAATAVNAPMVPAEVLAELSPYVTLAERLGRLAVQLVSGGAGVKDVKVTYTSSRADDDLDTRLLRAMITKGLIEPVSSAFINLVNADFIAKQRGLRISEERRPSDGAVEVPLESIEVRISKVDSRFNTAMSSGDITLVGTVKGGVPHLSKVGGFSVDVSLEGSIILCRQVDQPGMIGKVGNFLGEQNVNISFMSVGRDSPRKQAVMAIGVDDVPSKEVLTKIGQISAIEEFVFLKL
>SwissProt__O04130 D-3-phosphoglycerate dehydrogenase 2, chloroplastic; PGDH; EC 1.1.1.95 (Arabidopsis thaliana (Mouse-ear cress))
MAFSSSCSSVKAVNSRWTSPSPSPSSRFAVLPAFLHRRYATSVKLTAISAALKTVEQTTLTEDNRFSTVGSDSDEYNPTLPKPRILVTEKLGEAGVNLLREFGDVDCSYDLSPEDLKKKVAESDALIVRSGTKVTREVFEAAKGRLKVVGRAGVGIDNVDLQAATEHGCLVVNAPTANTVAAAEHGIALLASMARNVAQADASIKAGKWERSKYVGVSLVGKTLAVMGFGKVGTEVARRAKGLGMTVISHDPYAPADRARALGVDLVSFDQAISTADFVSLHMPLTPATKKVFNDETFSKMKKGVRLINVARGGVIDEDALVRALDAGIVAQAALDVFCEEPPSKDSRLIQHENVTVTPHLGASTKEAQEGVAIEIAEAVAGALKGELSATAVNAPMVAPEVLSELTPYIVLAEKLGRLAVQLASGGKGVQSIRVVYRSARDRDDLDTRLLRAMITKGIIEPISDSYVNLVNADFIAKQKGLRISEERMVVDSSPEYPVDSIQVQILNVESNFAGAVSDAGDISIEGKVKYGVPHLTCVGSFGVDVSLEGNLILCRQVDQPGMIGQVGNILGEQNVNVNFMSVGRTVLRKQAIMAIGVDEEPDNKTLERIGGVSAIEEFVFLKL
>BRENDA__A0A1Z4EAX4 phosphoglycerate dehydrogenase (EC 1.1.1.95) (Beta vulgaris)
MAVASSATTALISSSNPSLNSKPRNLHPKISPNSQLSLSSKLSITPSISLFSHTPHIRLTHFTTTTTHKKFAVFASLESKPTVLVAEKLGDAGLDLLKSFANVDCSYNLSPEELCTKISLCDALIVRSGTKVTRDVFDLLVGRLKVVGRAGVGIDNVDLGAATEHGCLVVNAPTANTVAAAEHGIALLTAMSRNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGSEVARRAKGLGMHVVAHDPYAPADRARAIGVELASFEEALATADFISLHMPLTSATAKVLNDDTFAKMKKGVMIVNVARGGVIDEDALVRALDSGIVAQAALDVFTQEPPAKDSKLVMHERVTATPHLGASTMEAQEGVAIEIAEAVIGALNGELAATAVNAPMVPAEVLNELKPYVQLAEKLGRLAIQLVAGGSGVKTVKVGYATSRAPDDLDTRLLRAMITKGLIEPISSTFVNLVNADFTAKQRGLRITEERILLDGSPESPLESIQIQIANVESKFASAISDSGEIRLQGRVKDGIPYLTKVGSFEVDVSLEGSIILCRQVDQPGMIGRVGSVLGEENVNVSFMSVGRLAPRTHAVMAIGVDEPPSSQVMKRIGEIPAIEELVFLKS
>BRENDA__A0A1Z4EAX3 phosphoglycerate dehydrogenase (EC 1.1.1.95) (Beta vulgaris)
MASATSAKSSSIITSLNKSPKNPKITSPNNLFFLKTKSPRPLPKKNLAITNNALSSPVLTTRETYAPKEVNNGAGSLRTRPSILVSEKLGEAGLAVLRQFADVECLYDLSPDELCEKIVQFDALIVRSGTKVNRAVFEAAKGQLKVVGRAGVGIDNVDLQAATEFGSLVVNAPTANTIAAAEHGIALLTSMARNVAQADASMKAGKWLRSKYVGVSLVGKTLAVMGFGKVGSEVARRAKGLGMHVIAHDPYAPADRARAVGVELVSFDHAISTADFISIHMPLTQTTKKVFNDTTFSKMKKGVRIVNVARGGVIDEDALVRALDNGVVAQAALDVFTEEPPAKESKLVQHENVTVTPHLGASTKEAQEGVAIEIAEAVTGALRGELSATAVNAPMVSAEVLSELAPYVHLAEKLGRLAVQLVAGGSGIQTIKVSYRSARGQDDLDTRLLRAMITKGIIEPISDMHINLVNADFTAKQKGLRITEERVSVDSSPENPIDSIQVQIPNVESKFESTMSEKGDITIEGKVKDGIPHLTRVGSFGVDVSLEGNIILCRQVDQPGMIGKVGNILADHNVNVNFMSVGRTSKKQKAIMAIGVDEQPEEDALTKIGQVPAVEEFVFLNL
>SwissProt__Q61753 D-3-phosphoglycerate dehydrogenase; 3-PGDH; A10; EC 1.1.1.95 (Mus musculus (Mouse))
MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWDRKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTVGYDPIISPEVAASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDSTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEAMGTLMHAWAGSPKGTIQVVTQGTSLKNAGTCLSPAVIVGLLREASKQADVNLVNAKLLVKEAGLNVTTSHNPGVPGEQGSGECLLTVALAGAPYQAVGLVQGTTPMLQMLNGAVFRPEVPLRRGQPLLVFRAQPSDPGMLPTMIGLLAEAGVQLLSYQTSMVSDGEPWHVMGLSSLLPSLETWKQHVLEAFQFCF
>metacyc__HS01776-MONOMER D-3-phosphoglycerate dehydrogenase (EC 1.1.1.95) (Homo sapiens)
MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEALGTLMRAWAGSPKGTIQVITQGTSLKNAGNCLSPAVIVGLLKEASKQADVNLVNAKLLVKEAGLNVTTSHSPAAPGEQGFGECLLAVALAGAPYQAVGLVQGTTPVLQGLNGAVFRPEVPLRRDLPLLLFRTQTSDPAMLPTMIGLLAEAGVRLLSYQTSLVSDGETWHVMGISSLLPSLEAWKQHVTEAFQFHF
>biolip__7dkmA Phgdh covalently linked to oridonin
NLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKLE
>PDB_6rj3_A Crystal structure of phgdh in complex with compound 15
RKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLE
AATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQS
FGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALL
RALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQF
>PDB_6cwa_A Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution
RKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLE
AATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQS
FGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALL
RALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVD
>PDB_7ewh_A Crystal structure of human phgdh in complex with homoharringtonine
LRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDL
EAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQ
SFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGAL
LRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMV
>PDB_6rih_A Crystal structure of phgdh in complex with compound 9
LRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDL
EAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQ
SFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGAL
LRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMV
>PDB_6rj5_A Crystal structure of phgdh in complex with compound 39
LRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDL
EAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQ
SFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGAL
LRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDM
>PDB_6rj2_A Crystal structure of phgdh in complex with compound 40
VLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAA
TRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFG
MKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRA
LQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMV
>PDB_6plg_A Crystal structure of human phgdh complexed with compound 15
LRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDL
EAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQ
SFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGAL
LRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVK
>PDB_6plf_A Crystal structure of human phgdh complexed with compound 1
NLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVD
LEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRM
QSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGA
LLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKG
>metacyc__MONOMER-10261 3-phosphoglycerate dehydrogenase subunit (EC 1.1.1.95) (Rattus norvegicus)
MAFANLRKILISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGVLVMNTPNGNSLSAAELTCGMLMCLARQIPQATASMKDGKWDRKKFMGTELNGKTLGILGLGRIGREVAARMQAFGMKTVGYDPIISPEVAASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDSTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEALGTLMHAWAGSPKGTIQVVTQGTSLKNAGTCLSPAVIVGLLREASKQADVNLVNAKLLVKEAGLNVTTSHSPGVPGEQGIGECLLTVALAGAPYQAVGLVQGTTPMLQMLNGAVFRPEVPLRRGQPLLLFRAQPSDPVMLPTMIGLLAEAGVQLLSYQTSKVSDGDTWHVMGLSSLLPSLDAWKQHVSEAFQFCF
>PDB_6plf_B Crystal structure of human phgdh complexed with compound 1
RKVLISDSLDPCCRKILQDGGLQVVEKQNLLIAELQDCEGLIVRSAADVINAAEKLQVVGRAGTGVDNVDLEAATRKGIL
VMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGY
DPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQC
AGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDM
>reanno__BFirm_BPHYT_RS11290 2-ketogluconate 6-phosphate reductase (EC 1.1.1.43) (Burkholderia phytofirmans PsJN)
MKKIVAWKSLPEDVLAYLQQHAQVVQVDATQHDAFVAALKDADGGIGSSVKITPAMLEGATRLKALSTISVGFDQFDVADLTRRGIVLANTPDVLTESTADTVFSLILASARRVVELAEWVKAGHWQHSIGPALFGVDVQGKTLGIVGLGRIGGAVARRAALGFNMKVLYTNRSANPQAEEAYGARRVELAELLATADFVCLQVPLTPETKHLIGAAELKSMKKSAILINASRGATVDEKALIEALQNGTIHGAGLDVFETEPLPSDSPLLKLANVVALPHIGSATHETRHAMARNAAENLVAALDGTLTSNIVNREVLSK
>BRENDA__Q608T2 hydroxypyruvate reductase (EC 1.1.1.81) (Methylococcus capsulatus)
MSKPKVLVTRRWPESCESRLRESFHVVFNADDHPMSRDELKAALRDYDAVLPTVTDAIDADVLSVEPLRCKILGNFGVGFNHIDLDTARQRGIAVTNTPDVLTDCTADIAMLLMLAVARRGGEGEREVRSGRWTGWRPTHMLGTKVTGKILGLVGFGRIARAMAKKAHFGFDMPVIFYDPFPPPQDLIDALGAEQCGTLEEVLERADFVALHCPGSKENRHLINADRLARMKPQSYLVNTARGDVVDNEALIQALRNRRIRGAGLDVYEGEPRLNPGFLELDNVVLFPHLGSATEETRIAMGMRVIDNITAFFEGRPPRDKVT
>metacyc__MONOMER-15867 <i>S</i>-sulfolactate dehydrogenase subunit (EC 1.1.1.310) (Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11))
MSDVLISEFMDEAAVADLERDCSVTFDATLVDDRARLLSSGAGVRALIVRNRTRVDRELLARFPDLRAVGRLGVGLDNIDVDACRESDIAVLPATGGNTVSVAEYVLTGIFMLRRGAYLSTPRVLAGEWPRQALMGHETQGATLGLVGFGGIARDLARRAQCLGMQVMAHDPFVPADDAAWQTVERAERLATLLEKADAVSLHVPLSEGTRHLIDGEALATMKPGSLLINTARGGIVDERALAASLRDRHLGGAMLDVFEEEPLTADSVLSGVEGLIATPHIAGVTHESNERISWITVDNVRRALGVRA
>ecocyc__MONOMER-43 glyoxylate reductase (EC 1.1.1.79; EC 1.1.1.215) (Escherichia coli K-12 substr. MG1655)
MKPSVILYKALPDDLLQRLQEHFTVHQVANLSPQTVEQNAAIFAEAEGLLGSNENVNAALLEKMPKLRATSTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLSTARRVVEVAERVKAGEWTASIGPDWYGTDVHHKTLGIVGMGRIGMALAQRAHFGFNMPILYNARRHHKEAEERFNARYCDLDTLLQESDFVCLILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQEPLSVDSPLLSMANVVAVPHIGSATHETRYGMAACAVDNLIDALQGKVEKNCVNPHVAD
>BRENDA__O58256 phosphoglycerate dehydrogenase (EC 1.1.1.95) (Pyrococcus horikoshii)
MRPKVGVLLKMKREALEELKKYADVEIILYPSGEELKGVIGRFDGIIVSPTTKITREVLENAERLKVISCHSAGYDNIDLEEATKRGIYVTKVSGLLSEAVAEFTVGLIINLMRKIHYADKFIRRGEWESHAKIWTGFKRIESLYGKKVGILGMGAIGKAIARRLIPFGVKLYYWSRHRKVNVEKELKARYMDIDELLEKSDIVILALPLTRDTYHIINEERVKKLEGKYLVNIGRGALVDEKAVTEAIKQGKLKGYATDVFEKEPVREHELFKYEWETVLTPHYAGLALEAQEDVGFRAVENLLKVLRGEVPEDLVNKEVLEVRPIENVKML
>SwissProt__Q9Z2F5 C-terminal-binding protein 1; CtBP1; 50 kDa BFA-dependent ADP-ribosylation substrate; BARS-50; C-terminal-binding protein 3; CtBP3; EC 1.1.1.- (Rattus norvegicus (Rat))
MSGVRPPIMNGPMHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGIERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYSRYPPGVVSVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHTTDQL
>SwissProt__O88712 C-terminal-binding protein 1; CtBP1; EC 1.1.1.- (Mus musculus (Mouse))
MGSSHLLNKGLPLGVRPPIMNGPMHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGIERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYSRYPPGVVSVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHTSDQL
>SwissProt__Q9LT69 D-3-phosphoglycerate dehydrogenase 3, chloroplastic; EC 1.1.1.95 (Arabidopsis thaliana (Mouse-ear cress))
MATSLNLSSIFSSSSRLVTTPSSVFPIRQRRRIILVTSSSSGGGGKPTILVTEKLGQAGIDLLKKYANVDCSYDLSLEELCTKISLCDALIVRSGTKVGRDVFESSRGRLKVVGRAGVGIDNVDLAAATEYGCLVVNAPTANTVAAAEHGIALLTAMARNIAQADASIKAGKWTRNKYVGVSLVGKTLAVLGFGKVGSEVARRARGLGMHVITHDPYAPADRARAIGVELVSFEVAISTADFISLHLPLTAATSKMMNDVTFAMMKKGVRIVNVARGGVIDEEALLRALDSGIVAQAALDVFTVEPPVKDNKLVLHESVTATPHLGASTMEAQEGVSIEVAEAVIGALRGELAATAVNAPMVPLEVLRELKPYVVLAEKLGRLAVQLVTGGSGVNAVKVTYASSRAPDDLDTRLLRAMVIKGIIEPISSVFINLVNSDYIAKQRGVKISEERMVLDGSPENPIEYITVRIANVESRFASALSESGEIKVEGRVKQGVPSLTKVGLFGVDVSLEGSVILCRQVDQPGMIGKVASILGDENVNVSFMSVGRIAPGKQAVMAIGVDEQPSKETLKKIGDIPAIEEFVFLKL
>metacyc__ENSG00000159692-MONOMER C-terminal-binding protein 1 (EC 1.1.1.428) (Homo sapiens)
MGSSHLLNKGLPLGVRPPIMNGPLHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYRYPPGVVGVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHASDQL
>BRENDA__F8AEA4 glyoxylate reductase (NADP+) (EC 1.1.1.79); hydroxypyruvate reductase (EC 1.1.1.81) (Pyrococcus yayanosii)
MKPKVLITRAIPENGIELLREHFEVEVWEHEHEIPREVLLEKVKDVDALVTMLSEKIDREVFDAAPRLRIVANYAVGYDNIDIEEATKRGIYVTNTPDVLTDATADLAWALLLAAARHVVKGDKFVRSGEWKRRGIAWHPKMFLGYDVYGKTIGIVGFGRIGQAIAKRAKGFGMRILYTARSRKPEAEKELGAEFKPLEELLRESDFVVLAVPLTKETYHMINEERLRLMKPTAVLVNVARGKVVDTKALIRALKEGWIAAAGLDVFEEEPYYDEELFALDNVVLTPHIGSATFGAREGMAELVAKNLIAFKNGEVPPTLVNREVLKVRRPGF
>biolip__6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow)
KPKVLITRAIPENGIELLREHFEVEVWEHEHEIPREVLLEKVKDVDALVTMLSEKIDREVFDAAPRLRIVANYAVGYDNIDIEEATKRGIYVTNTPDVLTDATADLAWALLLAAARHVVKGDKFVRSGEWKRRGIAWHPKMFLGYDVYGKTIGIVGFGRIGQAIAKRAKGFGMRILYTARSRKPEAEKELGAEFKPLEELLRESDFVVLAVPLTKETYHMINEERLRLMKPTAVLVNVARGKVVDTKALIRALKEGWIAAAGLDVFEEEPYYDEELFALDNVVLTPHIGSATFGAREGMAELVAKNLIAFKNGEVPPTLVNREVLKVRRPGF
>biolip__3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis
LPVVLIADKLAPSTVAALGDQVEVRWVDGPDRDKLLAAVPEADALLVRSATTVDAEVLAAAPKLKIVARAGVGLDNVDVDAATARGVLVVNAPTSNIHSAAEHALALLLAASRQIPAADASLREHTWKRSSFSGTEIFGKTVGVVGLGRIGQLVAQRIAAFGAYVVAYDPYVSPARAAQLGIELLSLDDLLARADFISVHLPKTPETAGLIDKEALAKTKPGVIIVNAARGGLVDEAALADAITGGHVRAAGLDVFATEPCTDSPLFELAQVVVTPHLGASTAEAQDRAGTDVAESVRLALAGEFVPDAVNVGGGVVNEEVAPWLDLVRKLGVLAGVLSDELPVSLSVQVRGELAAEEVEVLRLSALRGLFSAVIEDAVTFVNAPALAAERGVTAEICKASESPNHRSVVDVRAVGADGSVVTVSGTLYGPQLSQKIVQINGRHFDLRAQGINLIIHYVDRPGALGKIGTLLGTAGVNIQAAQLSEDAEGPGATILLRLDQDVPDDVRTAIAAAVDAYKLEVVDLS
>BRENDA__P9WNX3 phosphoglycerate dehydrogenase (EC 1.1.1.95) (Mycobacterium tuberculosis)
MSLPVVLIADKLAPSTVAALGDQVEVRWVDGPDRDKLLAAVPEADALLVRSATTVDAEVLAAAPKLKIVARAGVGLDNVDVDAATARGVLVVNAPTSNIHSAAEHALALLLAASRQIPAADASLREHTWKRSSFSGTEIFGKTVGVVGLGRIGQLVAQRIAAFGAYVVAYDPYVSPARAAQLGIELLSLDDLLARADFISVHLPKTPETAGLIDKEALAKTKPGVIIVNAARGGLVDEAALADAITGGHVRAAGLDVFATEPCTDSPLFELAQVVVTPHLGASTAEAQDRAGTDVAESVRLALAGEFVPDAVNVGGGVVNEEVAPWLDLVRKLGVLAGVLSDELPVSLSVQVRGELAAEEVEVLRLSALRGLFSAVIEDAVTFVNAPALAAERGVTAEICKASESPNHRSVVDVRAVGADGSVVTVSGTLYGPQLSQKIVQINGRHFDLRAQGINLIIHYVDRPGALGKIGTLLGTAGVNIQAAQLSEDAEGPGATILLRLDQDVPDDVRTAIAAAVDAYKLEVVDLS
>PDB_3ddn_B Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis
SLPVVLIADKLAPSTVAALGDQVEVRWVDGPDRDKLLAAVPEADALLVRSATTVDAEVLAAAPKLKIVARAGVGLDNVDV
DAATARGVLVVNAPTSNIHSAAEHALALLLAASRQIPAADASLREHTWKRSSFSGTEIFGKTVGVVGLGRIGQLVAQRIA
AFGAYVVAYDPYVSPARAAQLGIELLSLDDLLARADFISVHLPKTPETAGLIDKEALAKTKPGVIIVNAARGGLVDEAAL
ADAITGGHVRAAGLDVFATEPCTDSPLFELAQVVVTPHLGASTAEAQDRAGTDVAESVRLALAGEFVPDAVNVGGGVVNE
EVAPWLDLVRKLGVLAGVLSDELPVSLSVQVRGELAAEEVEVLRLSALRGLFSAVIEVTFVNAPALAAERGVTAEICKAS
ESPNHRSVVDVRAVGADGSVVTVSGTLYGPQLSQKIVQINGRHFDLRAQGINLIIHYVDRPGALGKIGTLLGTAGVNIQA
AQLSEDAEGPGATILLRLDQDVPDDVRTAIAAAVDAYKLEVVDLS
>biolip__6cdfA Human ctbp1 (28-378)
SHMPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLT
>PDB_1hl3_A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide
PRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNI
DIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRV
GQAVALRAKAFGFNVLFYDPYLSDGIERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTA
RGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPD
SLKNCVNKDHL
>PDB_1hku_A Ctbp/bars: a dual-function protein involved in transcription corepression and golgi membrane fission
PRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNI
DIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRV
GQAVALRAKAFGFNVLFYDPYLSDGIERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTA
RGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPD
SLKNCVNKDHL
>PDB_4lce_A Ctbp1 in complex with substrate mtob
MPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNID
IKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVG
QAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTAR
GGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDS
LKNCVNK
>PDB_4u6s_A Ctbp1 in complex with substrate phenylpyruvate
HMPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNI
DIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRV
GQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTA
RGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPD
SLKNCVNK
>PDB_4u6q_A Ctbp1 bound to inhibitor 2-(hydroxyimino)-3-phenylpropanoic acid
HMPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNI
DIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRV
GQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTA
RGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPD
SLKNCVNK
>PDB_6v89_A Human ctbp1 (28-375) in complex with amp
HMPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNI
DIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRV
GQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTA
RGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPD
SLKNCVNKDHLT
>biolip__8atiA Human ctbp2(31-364) in complex with rai2 peptide(315-322)
RPLVALLDGRDCTVEMPILKDLATVAFCDAQSTQEIHEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPESLRNCVNKEFF
>PDB_4lcj_A Ctbp2 in complex with substrate mtob
RPLVALLDGRDCTVEMPILKDLATVAFCDAQSTQEIHEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVD
IKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEQIREVASGAARIRGETLGLIGFGRTG
QAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAAR
GGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPES
LRNCVNKEFF
>SwissProt__P56545 C-terminal-binding protein 2; CtBP2 (Homo sapiens (Human))
MALVDKHKVKRQRLDRICEGIRPQIMNGPLHPRPLVALLDGRDCTVEMPILKDLATVAFCDAQSTQEIHEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPESLRNCVNKEFFVTSAPWSVIDQQAIHPELNGATYRYPPGIVGVAPGGLPAAMEGIIPGGIPVTHNLPTVAHPSQAPSPNQPTKHGDNREHPNEQ
>SwissProt_O58320 Glyoxylate reductase; EC 1.1.1.26 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
MKPKVFITREIPEVGIKMLEDEFEVEVWGDEKEIPREILLKKVKEVDALVTMLSERIDKEVFENAPKLRIVANYAVGYDN
IDIEEATKRGIYVTNTPDVLTDATADLAFALLLATARHVVKGDRFVRSGEWKKRGVAWHPKWFLGYDVYGKTIGIIGLGR
IGQAIAKRAKGFNMRILYYSRTRKEEVERELNAEFKPLEDLLRESDFVVLAVPLTRETYHLINEERLKLMKKTAILINIA
RGKVVDTNALVKALKEGWIAGAGLDVFEEEPYYNEELFKLDNVVLTPHIGSASFGAREGMAELVAKNLIAFKRGEIPPTL
VNREVIKIRKPGFE
>biolip__2dbqA Crystal structure of glyoxylate reductase (ph0597) from pyrococcus horikoshii ot3, complexed with NADP (i41)
MKPKVFITREIPEVGIKMLEDEFEVEVWGDEKEIPREILLKKVKEVDALVTMLSERIDKEVFENAPKLRIVANYAVGYDNIDIEEATKRGIYVTNTPDVLTDATADLAFALLLATARHVVKGDRFVRSGEWKKRGVAWHPKWFLGYDVYGKTIGIIGLGRIGQAIAKRAKGFNMRILYYSRTRKEEVERELNAEFKPLEDLLRESDFVVLAVPLTRETYHLINEERLKLMKKTAILINIARGKVVDTNALVKALKEGWIAGAGLDVFEEEPYYNEELFKLDNVVLTPHIGSASFGAREGMAELVAKNLIAFKRGEIPPTLVNREVIKIRKPGF