Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyThiolase-like 8041846 3000122 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyThiolase-like 8041847 3000122 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyACP-like 8040084 3001805 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
Aketoacyl-synte7l4eA1 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: ketoacyl-syntECOD (1.6)
AKetoacyl-synt_C_1e7l4eA2 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: Ketoacyl-synt_C_1ECOD (1.6)
BPP-bindinge7l4eB1 A: alpha bundlesX: ACP-likeH: Acyl-carrier protein (ACP) (From Topology)T: Acyl-carrier protein (ACP)F: PP-bindingECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF02801Beta-ketoacyl synthase, C-terminal domain (Ketoacyl-synt_C)Beta-ketoacyl synthase, C-terminal domainThe structure of beta-ketoacyl synthase is similar to that of the thiolase family (Pfam:PF00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.Domain
PF00109Beta-ketoacyl synthase, N-terminal domain (ketoacyl-synt)Beta-ketoacyl synthase, N-terminal domainThe structure of beta-ketoacyl synthase is similar to that of the thiolase family (Pfam:PF00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains m ...The structure of beta-ketoacyl synthase is similar to that of the thiolase family (Pfam:PF00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine [1].
Domain
PF00550Phosphopantetheine attachment site (PP-binding)Phosphopantetheine attachment siteA 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes memb ...A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
3-oxoacyl-[acyl-carrier-protein] synthase 2
Acyl carrier protein