>WP_039103118.1 NCBI__GCF_000807275.1:WP_039103118.1
MVVQTLTKDENKFLLLEGVHPSAIEILKNAGYSNIEYYKGALTEQELKEAIKDARFIGVRSRTQLTEDIINCAPKLAGIGCFCIGTNQVNLSAASKKGIPVFNAPFSNTRSVAELVLAEIILLLRRVPEANAQAHLGKWNKIAIGSHETRGKSLGIIGYGHIGSQLSVLAESLGMKVFFYDIETKLPLGNAKQMPSLAALFAESDVISLHVPENATTINMISKKELEMMKPRSILVNASRGKVVDIEALANALADKHIAGAAIDVFPSEPASNSEPFTSPLCQFDNVIITPHIGGSTIEAQENIGIEVATKLAKYSDTGSTLSAVNFPEVSLPIPSKGVSRFINIHKNQPGVLNAINNLLASRGLNIAGQYLQTSAEVGYVVIDIDSVDLKQSEQILAELKKVDGTIKARLLF
>ecocyc__PGLYCDEHYDROG-MONOMER phosphoglycerate dehydrogenase (EC 1.1.1.95; EC 1.1.1.399) (Escherichia coli K-12 substr. MG1655)
MAKVSLEKDKIKFLLVEGVHQKALESLRAAGYTNIEFHKGALDDEQLKESIRDAHFIGLRSRTHLTEDVINAAEKLVAIGCFCIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGELLLLLRGVPEANAKAHRGVWNKLAAGSFEARGKKLGIIGYGHIGTQLGILAESLGMYVYFYDIENKLPLGNATQVQHLSDLLNMSDVVSLHVPENPSTKNMMGAKEISLMKPGSLLINASRGTVVDIPALCDALASKHLAGAAIDVFPTEPATNSDPFTSPLCEFDNVLLTPHIGGSTQEAQENIGLEVAGKLIKYSDNGSTLSAVNFPEVSLPLHGGRRLMHIHENRPGVLTALNKIFAEQGVNIAAQYLQTSAQMGYVVIDIEADEDVAEKALQAMKAIPGTIRARLLY
>PDB_1yba_A The active form of phosphoglycerate dehydrogenase
SLEKDKIKFLLVEGVHQKALESLRAAGYTNIEFHKGALDDEQLKESIRDAHFIGLRSRTHLTEDVINAAEKLVAIGCFCI
GTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGELLLLLRGVPEANAKAHRGVWNKLAAGSFEARGKKLGIIGYGHIGT
QLGILAESLGMYVYFYDIENKLPLGNATQVQHLSDLLNMSDVVSLHVPENPSTKNMMGAKEISLMKPGSLLINASRGTVV
DIPALCDALASKHLAGAAIDVFPTEPATNSDPFTSPLCEFDNVLLTPHIGGSTQEAQENIGLEVAGKLIKYSDNGSTLSA
VNFPEVSLPLHGGRRLMHIHENRPGVLTALNKIFAEQGVNIAAQYLQTSAQMGYVVIDIEADEDVAEKALQAMKAIPGTI
RARLLY
>PDB_1psd_A The allosteric ligand site in the vmax-type cooperative enzyme phosphoglycerate dehydrogenase
EKDKIKFLLVEGVHQKALESLRAAGYTNIEFHKGALDDEQLKESIRDAHFIGLRSRTHLTEDVINAAEKLVAIGCFCIGT
NQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGELLLLLRGVPEANAKAHRGVWNKLAAGSFEARGKKLGIIGYGHIGTQL
GILAESLGMYVYFYDIENKLPLGNATQVQHLSDLLNMSDVVSLHVPENPSTKNMMGAKEISLMKPGSLLINASRGTVVDI
PALCDALASKHLAGAAIDVFPTEPATNSDPFTSPLCEFDNVLLTPHIGGSTQEAQENIGLEVAGKLIKYSDNGSTLSAVN
FPEVSLPLHGGRRLMHIHENRPGVLTALNKIFAEQGVNIAAQYLQTSAQMGYVVIDIEADEDVAEKALQAMKAIPGTIRA
RLLY
>biolip__2p9eA Crystal structure of g336v mutant of e.Coli phosphoglycerate dehydrogenase
SLEKDKIKFLLVEGVHQKALESLRAAGYTNIEFHKGALDDEQLKESIRDAHFIGLRSRTHLTEDVINAAEKLVAIGAFAIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGELLLLLRGVPEANAKAHRGVWNKLAAGSFEARGKKLGIIGYGHIGTQLGILAESLGMYVYFYDIENKLPLGNATQVQHLSDLLNMSDVVSLHVPENPSTKNMMGAKEISLMKPGSLLINASRGTVVDIPALADALASKHLAGAAIDVFPTEPATNSDPFTSPLAEFDNVLLTPHIGGSTQEAQENIGLEVAGKLIKYSDNGSTLSAVNFPEVSLPLHVGRRLMHIHENRPGVLTALNKIFAEQGVNIAAQYLQTSAQMGYVVIDIEADEDVAEKALQAMKAIPGTIRARLLY
>biolip__1sc6D Crystal structure of w139g d-3-phosphoglycerate dehydrogenase complexed with NAD+
EKDKIKFLLVEGVHQKALESLRAAGYTNIEFHKGALDDEQLKESIRDAHFIGLRSRTHLTEDVINAAEKLVAIGAFAIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGELLLLLRGVPEANAKAHRGVGSFEARGKKLGIIGYGHIGTQLGILAESLGMYVYFYDIENKLPLGNATQVQHLSDLLNMSDVVSLHVPENPSTKNMMGAKEISLMKPGSLLINASRGTVVDIPALADALASKHLAGAAIDVPFTSPLAEFDNVLLTPSTQEAQENIGLEVAGKLIKYSDNGSTLSAVNFPEVSLPLHGGRRLMHIHENRPGVLTALNKIFAEQGVNIAAQYLQTSAQMGYVVIDIEADEDVAEKALQAMKAIPGTIRARLLY
>BRENDA__Q9I6H5 phosphoglycerate dehydrogenase (EC 1.1.1.95) (Pseudomonas aeruginosa)
MSKTSLDKSKIKFLLLEGVHQNAVDTLKAAGYTNIEYLKTALSGDELKERIADAHFIGIRSRTQLTEEVFDCAKKLIAVGCFCIGTNQVDLNAARERGIAVFNAPYSNTRSVAELVLAEAILLLRGIPEKNASCHRGGWIKSAANSFEIRGKKLGIVGYGSIGTQLSVLAEALGMQVFFYDTVTKLPLGNAVQIGSLHELLGMSDIVSLHVPELPSTQWMIGEKEIRAMKKGGILINAARGTVVELDHLAAAIKDEHLIGAAIDVFPVEPKSNDEEFASPLRGLDRVILTPHIGGSTAEAQANIGLEVAEKLVKYSDNGTSVSSVNFPEVALPSHPGKHRLLHIHANIPGVMSEINKVFADNGINVSGQYLQTNEKVGYVVIDVDAEYSDLALEKLQQVNGTIRSRVLF
>BRENDA__A4VGK3 phosphoglycerate dehydrogenase (EC 1.1.1.95) (Pseudomonas stutzeri)
MVTLSTLQHRGGGVSRGSYASIRTPLKRASADSRHRHCRVGQPSLDTSVLSFGLKVLMQMSQTSLDKSKIKFLLLEGVHQNAVDTLKAAGYTNIEDLKTALSGDELKEKIADAHFIGIRSRTQLTEEVFDCAKKLIAVGCFCIGTNQVDLNAARERGIAVFNAPYSNTRSVAELVLAEAILLLRGIPEKNASCHRGGWIKSAANSFEIRGKKLGIIGYGSIGTQLSVLAEALGMQVFFYDVVTKLPLGNATQIGSLYELLGMCDIVSLHVPELPSTQWMIGEKEIRAMKKGAILINAARGTVVELDHLAAAIKDEHLIGAAIDVFPVEPKSNDEEFESPLRGLDRVILTPHIGGSTAEAQANIGLEVAEKLVKYSDNGTSVSSVNFPEVALPSHPGKHRLLHIHQNIPGVMSEINKVFADNGINICGQFLQTNEKVGYVVIDVDKEYSDLALEKLQHVNGTIRSRVLF
>reanno__Cola_Echvi_2777 fused D-3-phosphoglycerate dehydrogenase / phosphoserine phosphatase (EC 1.1.1.95; EC 3.1.3.3) (Echinicola vietnamensis KMM 6221, DSM 17526)
MTTDKKFIIDFDSTFTQVEALDILGEISLRNDPKRDEKLQAIKDITDLGMEGKLNLRESLERRIEILQANKSQIAELIDALKQKVSKSFQRNREFFQENAENIYILSNGFKDFITPVVAAYGLKEENVFANDFIYDEAGNIIDLNKENLLSNNNGKPATIKSLKLEGDVYVIGDGYTDYEIKASGLANKFYAFTENINRPKVSSKADHIAPSLDEILYVNKMNKKFSYPKSRINVLLLENVHPIGVEIMKQEGYNVEVVSSAMSEEELCEKIKNVSIIGIRSKTQITKKVLENANRLMAVGAFCIGTNQIDLETCQEKGIAVFNAPFSNTRSVVELAISEIIFLMRNLHDKTLKMHQGIWNKSASGSFEVRGKKLGIIGYGNIGAQLSVLAENMGMNVFYYDIVERLALGNATKIDSLDELLETCDIISLHVDGRTENKNILNKEKIFKMKKGAILVNLSRGHVVDVPALRDALESGHLAGAAVDVFPTEPKNNDEPFESELIGCPNTILTPHIGGSTLEAQENIAQFVPGKIIEYINSGNTFNSVNFPNIQLPFLKDAHRLIHIHQNAPGVLAKINQVLASYKINIVGQYLKTNEKIGYVITDIDKRYSNDVIDALKEIEGTIRFRILY
>SwissProt__P40054 D-3-phosphoglycerate dehydrogenase 1; 3-PGDH 1; 2-oxoglutarate reductase; EC 1.1.1.95; EC 1.1.1.399 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast))
MTSIDINNLQNTFQQAMNMSGSPGAVCTSPTQSFMNTVPQRLNAVKHPKILKPFSTGDMKILLLENVNQTAITIFEEQGYQVEFYKSSLPEEELIEKIKDVHAIGIRSKTRLTSNVLQHAKNLVCIGCFCIGTNQVDLDYATSRGIAVFNSPFSNSRSVAELVIAEIISLARQLGDRSIELHTGTWNKVAARCWEVRGKTLGIIGYGHIGSQLSVLAEAMGLHVLYYDIVTIMALGTARQVSTLDELLNKSDFVTLHVPATPETEKMLSAPQFAAMKDGAYVINASRGTVVDIPSLIQAVKANKIAGAALDVYPHEPAKNGEGSFNDELNSWTSELVSLPNIILTPHIGGSTEEAQSSIGIEVATALSKYINEGNSVGSVNFPEVALKSLSYDQENTVRVLYIHQNVPGVLKTVNDILSNHNIEKQFSDSNGEIAYLMADISSVDQSDIKDIYEQLNQTSAKISIRLLY
>BRENDA__U3RH61 phosphoglycerate dehydrogenase (EC 1.1.1.95) (Acanthamoeba castellanii)
MSNEGMFTMDDTGSPVTARSDATAGPEMCFSPPRQTVSYPKSKIKILLLEGVSDEAVNILKQEGFNVEAHRGKLPDDELAEKIRDAHCVGIRSGTKLTKELLALGQRLLCVGCFCIGSEQVDLQSAQSLGVPVFNSPFCNTRSVAELIVAAVISLARRLGDKNKELHSGHWNKSAKGCHEVRGKTLGIVGYGHIGSQLSVMAEALGMRVIFHDIVPKLPLGNSRQVADLNTLLEQSHFVTMHVPSTPQTKNMIGEEQIKLMRRGSFLLNASRGSVVIIPDLVKALKSGHLAGAYVDVYPHDMEPGSVSDNWECDLRGCPNTLLTPHIGGSTEEAQAAIGVDVANKIVNYINAGASIGAVNFPQIGLPYGGPQTHRILSIHRNRPGVLRDINLILADFNVTRQVLGTQGDVGYLVVEVDRAASKPIKDAIIKLEASIKTRILF
>SwissProt__P40510 D-3-phosphoglycerate dehydrogenase 2; 3-PGDH 2; 2-oxoglutarate reductase; EC 1.1.1.95; EC 1.1.1.399 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast))
MSYSAADNLQDSFQRAMNFSGSPGAVSTSPTQSFMNTLPRRVSITKQPKALKPFSTGDMNILLLENVNATAIKIFKDQGYQVEFHKSSLPEDELIEKIKDVHAIGIRSKTRLTEKILQHARNLVCIGCFCIGTNQVDLKYAASKGIAVFNSPFSNSRSVAELVIGEIISLARQLGDRSIELHTGTWNKVAARCWEVRGKTLGIIGYGHIGSQLSVLAEAMGLHVLYYDIVTIMALGTARQVSTLDELLNKSDFVTLHVPATPETEKMLSAPQFAAMKDGAYVINASRGTVVDIPSLIQAVKANKIAGAALDVYPHEPAKNGEGSFNDELNSWTSELVSLPNIILTPHIGGSTEEAQSSIGIEVATALSKYINEGNSVGSVNFPEVSLKSLDYDQENTVRVLYIHRNVPGVLKTVNDILSDHNIEKQFSDSHGEIAYLMADISSVNQSEIKDIYEKLNQTSAKVSIRLLY
>SwissProt_P87228 Putative D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase; EC 1.1.1.95; EC 1.1.1.399 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
MDIKGGRRGNVEDSLNKLSLSPPDNNSSFLSNHFQVRKSYSQAPARTLKPFASEDIKILLLENVNQSALSNLKDEGYQVE
FLKTSMSEDDLVEKIKGVHAIGIRSKTRLTRRVLEAADSLIVIGCFCIGTNQVDLDFAAERGIAVFNSPYANSRSVAELV
IGYIISLARQVGDRSLELHRGEWNKVSSGCWEIRGKTLGIIGYGHIGSQLSVLAEAMGLHVVYYDILPIMPLGSAKQLSS
LPELLHRADFVSLHVPASPETKNMISSKEFAAMKEGSYLINASRGTVVDIPALVDASKSGKIAGAAIDVYPSEPAGNGKD
KFVDSLNSWTSELTHCKNIILTPHIGGSTEEAQYNIGIEVSEALTRYINEGNSIGAVNFPEVSLRSLTEADRNAARVLFV
HRNVPGVLRQVNELFIDHNIKSQFSDSRGDIAYLVADISDCTPGSLEALHQKLESLPCKINTRLLY
>biolip__1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
MKVLVAAPLHEKAIQVLKDAGLEVIYEEYPDEDRLVELVKDVEAIIVRSKPKVTRRVIESAPKLKVIARAGVGLDNIDVEAAKEKGIEVVNAPAASSRSVAELAVGLMFSVARKIAFADRKMREGVWAKKEAMGIELEGKTIGIIGFGRIGYQVAKIANALGMNILLYDPYPNEERAKEVNGKFVDLETLLKESDVVTIHVPLVESTYHLINEERLKLMKKTAILINTSRGPVVDTNALVKALKEGWIAGAGLDVFEEEPLPKDHPLTKFDNVVLTPHIGASTVEAQERAGVEVAEKVVKILKG
>metacyc__SGL_RS08600-MONOMER glycerate dehydrogenase (EC 1.1.1.29) (Synechocystis sp. (strain PCC 6803 / Kazusa))
MNLAWLQGLSLGLLSPPAPALLIFRSFTMAKVLVSDSIDQVGIDILKQVAQVDVKTGLSEAEIIDIVPEYDAIMLRSATKVTEKIIQAGSQLKIIGRAGVGVDNIDVPAATRQGIVVVNSPEGNTIAAAEHALAMMMALARHIPDANKSVKESKWERKQFIGTEVYKKTLGVVGLGKIGSHVAGVAKAMGMKLLAYDPFISQERADQIGCTLVDLDLLFSEADFITLHIPKTPETANLINAETLAKMKPTARIINCSRGGIIDEEALVTAIETAQIGGAALDVFAQEPLGESRLREFSNVILTPHLGASTEEAQVNVAVDVAEQIRDVLLGLPARSAVNIPGLTPDVMEKLRPYLKLAETLGTLVGQLAGGRIDRLTVCLQGDLAEYTNSQPLVVAAIKGLLSQALRERVNYVNAAIEAKERGIRVIETKDASVRDYSGSLHLKATGTMGEHSATGALLSNGEIRITDVDEFPINVPPNNYMLFTLHRDMPGIIGKIGSLLGSFNVNIASMQVGRKIVRGDAIMALSLDDPLPDGLLSEITKVAGIRDAYTVKL
>SwissProt__Q61753 D-3-phosphoglycerate dehydrogenase; 3-PGDH; A10; EC 1.1.1.95 (Mus musculus (Mouse))
MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWDRKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTVGYDPIISPEVAASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDSTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEAMGTLMHAWAGSPKGTIQVVTQGTSLKNAGTCLSPAVIVGLLREASKQADVNLVNAKLLVKEAGLNVTTSHNPGVPGEQGSGECLLTVALAGAPYQAVGLVQGTTPMLQMLNGAVFRPEVPLRRGQPLLVFRAQPSDPGMLPTMIGLLAEAGVQLLSYQTSMVSDGEPWHVMGLSSLLPSLETWKQHVLEAFQFCF
>biolip__7dkmA Phgdh covalently linked to oridonin
NLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKLE
>metacyc__HS01776-MONOMER D-3-phosphoglycerate dehydrogenase (EC 1.1.1.95) (Homo sapiens)
MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEALGTLMRAWAGSPKGTIQVITQGTSLKNAGNCLSPAVIVGLLKEASKQADVNLVNAKLLVKEAGLNVTTSHSPAAPGEQGFGECLLAVALAGAPYQAVGLVQGTTPVLQGLNGAVFRPEVPLRRDLPLLLFRTQTSDPAMLPTMIGLLAEAGVRLLSYQTSLVSDGETWHVMGISSLLPSLEAWKQHVTEAFQFHF
>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_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
>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_6rj2_A Crystal structure of phgdh in complex with compound 40
VLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAA
TRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFG
MKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRA
LQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMV
>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
>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
>SwissProt__O04130 D-3-phosphoglycerate dehydrogenase 2, chloroplastic; PGDH; EC 1.1.1.95 (Arabidopsis thaliana (Mouse-ear cress))
MAFSSSCSSVKAVNSRWTSPSPSPSSRFAVLPAFLHRRYATSVKLTAISAALKTVEQTTLTEDNRFSTVGSDSDEYNPTLPKPRILVTEKLGEAGVNLLREFGDVDCSYDLSPEDLKKKVAESDALIVRSGTKVTREVFEAAKGRLKVVGRAGVGIDNVDLQAATEHGCLVVNAPTANTVAAAEHGIALLASMARNVAQADASIKAGKWERSKYVGVSLVGKTLAVMGFGKVGTEVARRAKGLGMTVISHDPYAPADRARALGVDLVSFDQAISTADFVSLHMPLTPATKKVFNDETFSKMKKGVRLINVARGGVIDEDALVRALDAGIVAQAALDVFCEEPPSKDSRLIQHENVTVTPHLGASTKEAQEGVAIEIAEAVAGALKGELSATAVNAPMVAPEVLSELTPYIVLAEKLGRLAVQLASGGKGVQSIRVVYRSARDRDDLDTRLLRAMITKGIIEPISDSYVNLVNADFIAKQKGLRISEERMVVDSSPEYPVDSIQVQILNVESNFAGAVSDAGDISIEGKVKYGVPHLTCVGSFGVDVSLEGNLILCRQVDQPGMIGQVGNILGEQNVNVNFMSVGRTVLRKQAIMAIGVDEEPDNKTLERIGGVSAIEEFVFLKL
>PDB_3ddn_B Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis
SLPVVLIADKLAPSTVAALGDQVEVRWVDGPDRDKLLAAVPEADALLVRSATTVDAEVLAAAPKLKIVARAGVGLDNVDV
DAATARGVLVVNAPTSNIHSAAEHALALLLAASRQIPAADASLREHTWKRSSFSGTEIFGKTVGVVGLGRIGQLVAQRIA
AFGAYVVAYDPYVSPARAAQLGIELLSLDDLLARADFISVHLPKTPETAGLIDKEALAKTKPGVIIVNAARGGLVDEAAL
ADAITGGHVRAAGLDVFATEPCTDSPLFELAQVVVTPHLGASTAEAQDRAGTDVAESVRLALAGEFVPDAVNVGGGVVNE
EVAPWLDLVRKLGVLAGVLSDELPVSLSVQVRGELAAEEVEVLRLSALRGLFSAVIEVTFVNAPALAAERGVTAEICKAS
ESPNHRSVVDVRAVGADGSVVTVSGTLYGPQLSQKIVQINGRHFDLRAQGINLIIHYVDRPGALGKIGTLLGTAGVNIQA
AQLSEDAEGPGATILLRLDQDVPDDVRTAIAAAVDAYKLEVVDLS
>SwissProt__Q9LT69 D-3-phosphoglycerate dehydrogenase 3, chloroplastic; EC 1.1.1.95 (Arabidopsis thaliana (Mouse-ear cress))
MATSLNLSSIFSSSSRLVTTPSSVFPIRQRRRIILVTSSSSGGGGKPTILVTEKLGQAGIDLLKKYANVDCSYDLSLEELCTKISLCDALIVRSGTKVGRDVFESSRGRLKVVGRAGVGIDNVDLAAATEYGCLVVNAPTANTVAAAEHGIALLTAMARNIAQADASIKAGKWTRNKYVGVSLVGKTLAVLGFGKVGSEVARRARGLGMHVITHDPYAPADRARAIGVELVSFEVAISTADFISLHLPLTAATSKMMNDVTFAMMKKGVRIVNVARGGVIDEEALLRALDSGIVAQAALDVFTVEPPVKDNKLVLHESVTATPHLGASTMEAQEGVSIEVAEAVIGALRGELAATAVNAPMVPLEVLRELKPYVVLAEKLGRLAVQLVTGGSGVNAVKVTYASSRAPDDLDTRLLRAMVIKGIIEPISSVFINLVNSDYIAKQRGVKISEERMVLDGSPENPIEYITVRIANVESRFASALSESGEIKVEGRVKQGVPSLTKVGLFGVDVSLEGSVILCRQVDQPGMIGKVASILGDENVNVSFMSVGRIAPGKQAVMAIGVDEQPSKETLKKIGDIPAIEEFVFLKL
>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
>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__A0A1Z4EAX4 phosphoglycerate dehydrogenase (EC 1.1.1.95) (Beta vulgaris)
MAVASSATTALISSSNPSLNSKPRNLHPKISPNSQLSLSSKLSITPSISLFSHTPHIRLTHFTTTTTHKKFAVFASLESKPTVLVAEKLGDAGLDLLKSFANVDCSYNLSPEELCTKISLCDALIVRSGTKVTRDVFDLLVGRLKVVGRAGVGIDNVDLGAATEHGCLVVNAPTANTVAAAEHGIALLTAMSRNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGSEVARRAKGLGMHVVAHDPYAPADRARAIGVELASFEEALATADFISLHMPLTSATAKVLNDDTFAKMKKGVMIVNVARGGVIDEDALVRALDSGIVAQAALDVFTQEPPAKDSKLVMHERVTATPHLGASTMEAQEGVAIEIAEAVIGALNGELAATAVNAPMVPAEVLNELKPYVQLAEKLGRLAIQLVAGGSGVKTVKVGYATSRAPDDLDTRLLRAMITKGLIEPISSTFVNLVNADFTAKQRGLRITEERILLDGSPESPLESIQIQIANVESKFASAISDSGEIRLQGRVKDGIPYLTKVGSFEVDVSLEGSIILCRQVDQPGMIGRVGSVLGEENVNVSFMSVGRLAPRTHAVMAIGVDEPPSSQVMKRIGEIPAIEELVFLKS
>BRENDA__A0A2R6X868 phosphoglycerate dehydrogenase (EC 1.1.1.95) (Marchantia polymorpha)
MAATSAVAAVVAGALGAVPQRTDLAAAAAVPSRACSVSSLASFQSLSASCKTARSARAVSKKVGGRQIVCSVAAPSTSPRSASTEIVGKPTVLVAEKLGEAGLELLKKIANVDCSYNLSQEELCAKISLCDALIVRSGTKVTREVFEASNGRLKVVGRAGVGIDNVDLQAATEVGCLVVNAPTANTIAAAEHGIALLTALARNVAQASASMKAGEWKRNKYVGVSLVDKTLAVMGFGKVGSEVARRAKGLGMQVIAHDPYAPADRARAIGVELVSFDEALQRADFISLHMPLTPSTDKCFNDESFAKCKKGVRIVNVARGGVIDEEALVRALDSGIVAQAALDVFTVEPPAKDDKLIQHENVVVTPHLGASTMEAQEGVAVEIAEAVVGALQGELAATAVNAPMVPAEVLAELSPYVTLAERLGRLAVQLVSGGAGVKDVKVTYTSSRADDDLDTRLLRAMITKGLIEPVSSAFINLVNADFIAKQRGLRISEERRPSDGAVEVPLESIEVRISKVDSRFNTAMSSGDITLVGTVKGGVPHLSKVGGFSVDVSLEGSIILCRQVDQPGMIGKVGNFLGEQNVNISFMSVGRDSPRKQAVMAIGVDDVPSKEVLTKIGQISAIEEFVFLKL
>BRENDA__H9JRZ9 phosphoglycerate dehydrogenase (EC 1.1.1.95) (Bombyx mori)
MIYAHSSFLIQLIFADSALSSSLFFNAQAIRLATYAQTGECRCQSLPDARRRRTPASSLTTIALPGLERICQNSDYWSIIIKGTFTKYKGGRDVLKQKKYKKITKMVVDIKSVLIVDGVGAKCAELLNAYGIATTTKAKISKEELLMEIPNHDALVVRSATQVTKEVLDAGVKLKVVGRAGAGVDNIDVDSAGKKGVGVINAPGANALSACELTCTLMLVLARHVVPASTALKAGRWDRALYTGSELAGKTLAILGLGRVGREVATRMYAFGMNIIGFDPFVSADQCAQFHCTKMELEDIWPLADYITLHTPLIESTRNFINADVLKQCKKGVKIINVGRGGLIQETDFLQALKSGKVGGAALDVFEQEPPTDPVTLEIIQQPAVIATPHLGASTKEAQVRVGQEIAEQLVNLVKPGTFPTLLAEVTRVLNK
>BRENDA__A0A1Z4EAX3 phosphoglycerate dehydrogenase (EC 1.1.1.95) (Beta vulgaris)
MASATSAKSSSIITSLNKSPKNPKITSPNNLFFLKTKSPRPLPKKNLAITNNALSSPVLTTRETYAPKEVNNGAGSLRTRPSILVSEKLGEAGLAVLRQFADVECLYDLSPDELCEKIVQFDALIVRSGTKVNRAVFEAAKGQLKVVGRAGVGIDNVDLQAATEFGSLVVNAPTANTIAAAEHGIALLTSMARNVAQADASMKAGKWLRSKYVGVSLVGKTLAVMGFGKVGSEVARRAKGLGMHVIAHDPYAPADRARAVGVELVSFDHAISTADFISIHMPLTQTTKKVFNDTTFSKMKKGVRIVNVARGGVIDEDALVRALDNGVVAQAALDVFTEEPPAKESKLVQHENVTVTPHLGASTKEAQEGVAIEIAEAVTGALRGELSATAVNAPMVSAEVLSELAPYVHLAEKLGRLAVQLVAGGSGIQTIKVSYRSARGQDDLDTRLLRAMITKGIIEPISDMHINLVNADFTAKQKGLRITEERVSVDSSPENPIDSIQVQIPNVESKFESTMSEKGDITIEGKVKDGIPHLTRVGSFGVDVSLEGNIILCRQVDQPGMIGKVGNILADHNVNVNFMSVGRTSKKQKAIMAIGVDEQPEEDALTKIGQVPAVEEFVFLNL
>SwissProt__C0CMQ8 Hydroxypyruvate reductase; EC 1.1.1.81 (Blautia hydrogenotrophica (strain DSM 10507 / JCM 14656 / S5a33) (Ruminococcus hydrogenotrophicus))
MKIVVLDGYCLNPGDLDWKGLEALGECIVYDRTSLTDMEEVISRIGDADIVYTNKTPMPREVFEKCPNIRFVGVLATGYNVVDVNTAKEKGIPVANIPTYGTASVGQFAIALLLEICHHVGHHNQVVHEGKWESNPDWCFWDYPLIELDGKNMGIIGYGRIGQATGKIAQALGMKVLAYDAYKNPALENENCRYVELDELLSQSDVIALHCPLFPETEGIVNKENIAKMKDGVIILNNSRGPLIVEQDLVDALNSGKVAAAGLDVVSTEPIKGDNPLLGAKNCIITPHISWAPKESRKRLMDIAVNNLEEFLKGSPVNVVNK