6YBP

Propionyl-CoA carboxylase of Methylorubrum extorquens with bound CoA


Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BPF01039e6ybpB2 A: a/b three-layered sandwichesX: ClpP/crotonase (From Topology)H: ClpP/crotonase (From Topology)T: ClpP/crotonaseF: PF01039ECOD (1.6)
CPF01039e6ybpC2 A: a/b three-layered sandwichesX: ClpP/crotonase (From Topology)H: ClpP/crotonase (From Topology)T: ClpP/crotonaseF: PF01039ECOD (1.6)
APF01039e6ybpA2 A: a/b three-layered sandwichesX: ClpP/crotonase (From Topology)H: ClpP/crotonase (From Topology)T: ClpP/crotonaseF: PF01039ECOD (1.6)
DPF01039e6ybpD2 A: a/b three-layered sandwichesX: ClpP/crotonase (From Topology)H: ClpP/crotonase (From Topology)T: ClpP/crotonaseF: PF01039ECOD (1.6)
EPF01039e6ybpE1 A: a/b three-layered sandwichesX: ClpP/crotonase (From Topology)H: ClpP/crotonase (From Topology)T: ClpP/crotonaseF: PF01039ECOD (1.6)
FPF01039e6ybpF2 A: a/b three-layered sandwichesX: ClpP/crotonase (From Topology)H: ClpP/crotonase (From Topology)T: ClpP/crotonaseF: PF01039ECOD (1.6)
HPF18140e6ybpH2 A: a+b two layersX: Methylcrotonyl-CoA carboxylase alpha-subunit BT domain-related (From Homology)H: Methylcrotonyl-CoA carboxylase alpha-subunit BT domain-relatedT: Barrel domain in methylcrotonyl-CoA carboxylase alpha-subunitF: PF18140ECOD (1.6)
HPF00364e6ybpH1 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: Single hybrid motifF: PF00364ECOD (1.6)
JPF18140e6ybpJ3 A: a+b two layersX: Methylcrotonyl-CoA carboxylase alpha-subunit BT domain-related (From Homology)H: Methylcrotonyl-CoA carboxylase alpha-subunit BT domain-relatedT: Barrel domain in methylcrotonyl-CoA carboxylase alpha-subunitF: PF18140ECOD (1.6)
JPF02785e6ybpJ1 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: CO dehydrogenase molybdoprotein N-domain-likeF: PF02785ECOD (1.6)
JPF00364e6ybpJ2 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: Single hybrid motifF: PF00364ECOD (1.6)
GPF18140e6ybpG3 A: a+b two layersX: Methylcrotonyl-CoA carboxylase alpha-subunit BT domain-related (From Homology)H: Methylcrotonyl-CoA carboxylase alpha-subunit BT domain-relatedT: Barrel domain in methylcrotonyl-CoA carboxylase alpha-subunitF: PF18140ECOD (1.6)
GPF02785e6ybpG1 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: CO dehydrogenase molybdoprotein N-domain-likeF: PF02785ECOD (1.6)
GPF00364e6ybpG2 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: Single hybrid motifF: PF00364ECOD (1.6)
IPF18140e6ybpI3 A: a+b two layersX: Methylcrotonyl-CoA carboxylase alpha-subunit BT domain-related (From Homology)H: Methylcrotonyl-CoA carboxylase alpha-subunit BT domain-relatedT: Barrel domain in methylcrotonyl-CoA carboxylase alpha-subunitF: PF18140ECOD (1.6)
IPF02785e6ybpI1 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: CO dehydrogenase molybdoprotein N-domain-likeF: PF02785ECOD (1.6)
IPF00364e6ybpI2 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: Single hybrid motifF: PF00364ECOD (1.6)
KPF18140e6ybpK3 A: a+b two layersX: Methylcrotonyl-CoA carboxylase alpha-subunit BT domain-related (From Homology)H: Methylcrotonyl-CoA carboxylase alpha-subunit BT domain-relatedT: Barrel domain in methylcrotonyl-CoA carboxylase alpha-subunitF: PF18140ECOD (1.6)
KPF02785e6ybpK1 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: CO dehydrogenase molybdoprotein N-domain-likeF: PF02785ECOD (1.6)
KPF00364e6ybpK2 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: Single hybrid motifF: PF00364ECOD (1.6)
LPF18140e6ybpL3 A: a+b two layersX: Methylcrotonyl-CoA carboxylase alpha-subunit BT domain-related (From Homology)H: Methylcrotonyl-CoA carboxylase alpha-subunit BT domain-relatedT: Barrel domain in methylcrotonyl-CoA carboxylase alpha-subunitF: PF18140ECOD (1.6)
LPF02785e6ybpL1 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: CO dehydrogenase molybdoprotein N-domain-likeF: PF02785ECOD (1.6)
LPF00364e6ybpL2 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: Single hybrid motifF: PF00364ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D, E
PF01039Carboxyl transferase domain (Carboxyl_trans)Carboxyl transferase domain- Family
G, H, I, J, K
PF18140Propionyl-coenzyme A carboxylase BT domain (PCC_BT)Propionyl-coenzyme A carboxylase BT domainThis domain is found in Propionyl-coenzyme A carboxylase (PCC), present in Roseobacter denitrificans. PCC is a mitochondrial biotin-dependent enzyme that is essential for the catabolism of certain amino acids, cholesterol, and fatty acids with an odd ...This domain is found in Propionyl-coenzyme A carboxylase (PCC), present in Roseobacter denitrificans. PCC is a mitochondrial biotin-dependent enzyme that is essential for the catabolism of certain amino acids, cholesterol, and fatty acids with an odd number of carbon atoms. Since this domain mediates biotin carboxylase-carboxyltransferase interactions it is referred to as the BT domain. The BT domain is located between biotin carboxylase and the biotin carboxyl carrier protein domains. The BT domain shares some structural similarity with the pyruvate carboxylase tetramerization domain of pyruvate carboxylase [1].
Domain
G, H, I, J, K
PF00364Biotin-requiring enzyme (Biotin_lipoyl)Biotin-requiring enzymeThis family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognise the Glycine cleavage system H proteins.Domain

InterPro: Protein Family Classification InterPro Database Homepage