Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1ygya1 Alpha and beta proteins (a/b) NAD(P)-binding Rossmann-fold domains NAD(P)-binding Rossmann-fold domains Formate/glycerate dehydrogenases, NAD-domain Phosphoglycerate dehydrogenase (Mycobacterium tuberculosis ) [TaxId: 1773 ], SCOPe (2.08)
Ad1ygya2 Alpha and beta proteins (a/b) Flavodoxin-like Formate/glycerate dehydrogenase catalytic domain-like Formate/glycerate dehydrogenases, substrate-binding domain Phosphoglycerate dehydrogenase (Mycobacterium tuberculosis ) [TaxId: 1773 ], SCOPe (2.08)
Ad1ygya3 Alpha and beta proteins (a+b) Ferredoxin-like ACT-like Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain (Mycobacterium tuberculosis ) [TaxId: 1773 ], SCOPe (2.08)
Ad1ygya4 Alpha and beta proteins (a+b) FwdE/GAPDH domain-like Serine metabolism enzymes domain SerA intervening domain-like D-3-phosphoglycerate dehydrogenase SerA (Mycobacterium tuberculosis ) [TaxId: 1773 ], SCOPe (2.08)
Bd1ygyb1 Alpha and beta proteins (a/b) NAD(P)-binding Rossmann-fold domains NAD(P)-binding Rossmann-fold domains Formate/glycerate dehydrogenases, NAD-domain Phosphoglycerate dehydrogenase (Mycobacterium tuberculosis ) [TaxId: 1773 ], SCOPe (2.08)
Bd1ygyb2 Alpha and beta proteins (a/b) Flavodoxin-like Formate/glycerate dehydrogenase catalytic domain-like Formate/glycerate dehydrogenases, substrate-binding domain Phosphoglycerate dehydrogenase (Mycobacterium tuberculosis ) [TaxId: 1773 ], SCOPe (2.08)
Bd1ygyb3 Alpha and beta proteins (a+b) Ferredoxin-like ACT-like Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain (Mycobacterium tuberculosis ) [TaxId: 1773 ], SCOPe (2.08)
Bd1ygyb4 Alpha and beta proteins (a+b) FwdE/GAPDH domain-like Serine metabolism enzymes domain SerA intervening domain-like D-3-phosphoglycerate dehydrogenase SerA (Mycobacterium tuberculosis ) [TaxId: 1773 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyD-lactate/D-glycerate dehydrogenase-like 8001025 4000099 SCOP2 (2022-06-29)
ASCOP2 FamilyPhosphoglycerate dehydrogenase, regulatory (C-terminal) domain 8001026 4000051 SCOP2 (2022-06-29)
ASCOP2 FamilySerA intervening domain-like 8001027 4000037 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyD-2-hydroxyacid dehydrogenase-like 8017543 3000044 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyACT-like 8017540 3000006 SCOP2 (2022-06-29)
ASCOP2 SuperfamilySerine metabolism enzymes domain 8001028 3000019 SCOP2 (2022-06-29)
BSCOP2B SuperfamilyACT-like 8017540 3000006 SCOP2B (2022-06-29)
BSCOP2B SuperfamilySerine metabolism enzymes domain 8001028 3000019 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyD-2-hydroxyacid dehydrogenase-like 8017543 3000044 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APRK13581e1ygyA2 A: a+b two layersX: FwdE/GAPDH domain-likeH: Serine dehydratase beta chain-like (From Topology)T: Serine dehydratase beta chain-likeF: PRK13581ECOD (1.6)
AACTe1ygyA1 A: a+b two layersX: Alpha-beta plaitsH: ACT-like (From Topology)T: ACT-likeF: ACTECOD (1.6)
A2-Hacid_dh_Ce1ygyA3 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: 2-Hacid_dh_CECOD (1.6)
A2-Hacid_dhe1ygyA4 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: Formate/glycerate dehydrogenase catalytic domain-likeF: 2-Hacid_dhECOD (1.6)
BPRK13581e1ygyB2 A: a+b two layersX: FwdE/GAPDH domain-likeH: Serine dehydratase beta chain-like (From Topology)T: Serine dehydratase beta chain-likeF: PRK13581ECOD (1.6)
BACTe1ygyB1 A: a+b two layersX: Alpha-beta plaitsH: ACT-like (From Topology)T: ACT-likeF: ACTECOD (1.6)
B2-Hacid_dh_Ce1ygyB3 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: 2-Hacid_dh_CECOD (1.6)
B2-Hacid_dhe1ygyB4 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: Formate/glycerate dehydrogenase catalytic domain-likeF: 2-Hacid_dhECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF02826D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (2-Hacid_dh_C)D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domainThis domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family Pfam:PF00389.Domain
A, B
PF19304D-3-phosphoglycerate dehydrogenase intervening domain (PGDH_inter)D-3-phosphoglycerate dehydrogenase intervening domainThis domain is found in the D-3-phosphoglycerate dehydrogenase enzyme. In the structure of the Mycobacterium tuberculosis enzyme this domain was described as the intervening domain, also known as the allosteric substrate binding domain (ASB) [1,2,3]. ...This domain is found in the D-3-phosphoglycerate dehydrogenase enzyme. In the structure of the Mycobacterium tuberculosis enzyme this domain was described as the intervening domain, also known as the allosteric substrate binding domain (ASB) [1,2,3]. The intervening domain between the substrate-binding and regulatory domains is not present in E. coli PGDH. This domain is closely related to Pfam:PF03315. It serves as an anion-binding site and may function as an allosteric site for the control of enzyme activity [3].
Domain
A, B
PF01842ACT domain (ACT)ACT domainThis family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulati ...This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95 Swiss:P08328, which is inhibited by serine [1]. Aspartokinase EC:2.7.2.4 Swiss:P53553, which is regulated by lysine. Acetolactate synthase small regulatory subunit Swiss:P00894, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1 Swiss:P00439, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51 Swiss:P21203. formyltetrahydrofolate deformylase EC:3.5.1.10, Swiss:P37051, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5 Swiss:P11585
Domain
A, B
PF00389D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain (2-Hacid_dh)D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domainThis family represents the largest portion of the catalytic domain of 2-hydroxyacid dehydrogenases as the NAD binding domain is inserted within the structural domain.Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
D-3-phosphoglycerate dehydrogenase