Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APK_2nde6nu1A2 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: PK beta-barrel domain-likeF: PK_2ndECOD (1.6)
APK_1ste6nu1A3 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PK_1stECOD (1.6)
APK_Ce6nu1A1 A: a/b three-layered sandwichesX: PK C-terminal domain-like (From Topology)H: PK C-terminal domain-like (From Topology)T: PK C-terminal domain-likeF: PK_CECOD (1.6)
BPK_2nde6nu1B1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: PK beta-barrel domain-likeF: PK_2ndECOD (1.6)
BPK_1ste6nu1B3 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PK_1stECOD (1.6)
BPK_Ce6nu1B2 A: a/b three-layered sandwichesX: PK C-terminal domain-like (From Topology)H: PK C-terminal domain-like (From Topology)T: PK C-terminal domain-likeF: PK_CECOD (1.6)
DPK_2nde6nu1D3 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: PK beta-barrel domain-likeF: PK_2ndECOD (1.6)
DPK_1ste6nu1D2 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PK_1stECOD (1.6)
DPK_Ce6nu1D1 A: a/b three-layered sandwichesX: PK C-terminal domain-like (From Topology)H: PK C-terminal domain-like (From Topology)T: PK C-terminal domain-likeF: PK_CECOD (1.6)
CPK_2nde6nu1C2 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: PK beta-barrel domain-likeF: PK_2ndECOD (1.6)
CPK_1ste6nu1C1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PK_1stECOD (1.6)
CPK_Ce6nu1C3 A: a/b three-layered sandwichesX: PK C-terminal domain-like (From Topology)H: PK C-terminal domain-like (From Topology)T: PK C-terminal domain-likeF: PK_CECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D
PF02887Pyruvate kinase, alpha/beta domain (PK_C)Pyruvate kinase, alpha/beta domainPyruvate kinase catalyses the final step in glycolysis, the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP [1,2]. The structure of several pyruvate kinases from various organisms have been determined [2, ...Pyruvate kinase catalyses the final step in glycolysis, the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP [1,2]. The structure of several pyruvate kinases from various organisms have been determined [2, 3,4]. The protein comprises three-four domains: a small N-terminal helical domain (absent in bacterial PK), a beta/alpha barrel domain, a beta-barrel domain (inserted within the beta/alpha-barrel domain), and a 3-layer alpha/beta/alpha sandwich domain (represented in this entry). This domain is at the C-terminal of pyruvate kinases and contains the FBP (fructose 1,6-bisphosphate) binding site [2,4,5].
Domain
A, B, C, D
PF00224Pyruvate kinase, barrel domain (PK)Pyruvate kinase, barrel domainThis is the barrel domain of pyruvate kinases. This domain represents the beta/alpha barrel and the small beta-barrel domain inserted within it. The active site is found in a cleft between the two domains [1,2,3,4].Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C, D
Pyruvate kinase PKM