Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyProbable ACP-binding domain of malonyl-CoA ACP transacylase8055841 4001289 SCOP2 (2022-06-29)
ASCOP2 FamilyThiolase-related8055837 4000245 SCOP2 (2022-06-29)
ASCOP2 FamilyKASAT domain-like8045095 4004293 SCOP2 (2022-06-29)
ASCOP2 FamilyPKS docking region-like8055909 4007409 SCOP2 (2022-06-29)
ASCOP2 FamilyFabD-like8055839 4003614 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyProbable ACP-binding domain of malonyl-CoA ACP transacylase8055842 3001224 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyThiolase-like8055838 3000122 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyKASAT domain-like8055836 3002319 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyPKS docking domain-like8055910 3002322 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyFabD/lysophospholipase-like8055840 3001121 SCOP2 (2022-06-29)
BSCOP2B SuperfamilyProbable ACP-binding domain of malonyl-CoA ACP transacylase8055842 3001224 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyKASAT domain-like8055836 3002319 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyThiolase-like8055838 3000122 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyKASAT domain-like8055836 3002319 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AAcyl_transf_1_2nd_1e4mz0A5 A: a+b two layersX: Alpha-beta plaitsH: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)T: Probable ACP-binding domain of malonyl-CoA ACP transacylaseF: Acyl_transf_1_2nd_1ECOD (1.6)
APksD_1e4mz0A3 A: a+b two layersX: KS-MAT linker domain in fatty acid synthase (From Topology)H: KS-MAT linker domain in fatty acid synthase (From Topology)T: KS-MAT linker domain in fatty acid synthaseF: PksD_1ECOD (1.6)
APksD,Acyl_transf_1_1ste4mz0A7 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: PksD,Acyl_transf_1_1stECOD (1.6)
Aketoacyl-synte4mz0A6 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: ketoacyl-syntECOD (1.6)
AKetoacyl-synt_Ce4mz0A4 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: Ketoacyl-synt_CECOD (1.6)
BAcyl_transf_1_2nd_1e4mz0B3 A: a+b two layersX: Alpha-beta plaitsH: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)T: Probable ACP-binding domain of malonyl-CoA ACP transacylaseF: Acyl_transf_1_2nd_1ECOD (1.6)
BPksD_1e4mz0B2 A: a+b two layersX: KS-MAT linker domain in fatty acid synthase (From Topology)H: KS-MAT linker domain in fatty acid synthase (From Topology)T: KS-MAT linker domain in fatty acid synthaseF: PksD_1ECOD (1.6)
BPksD,Acyl_transf_1_1ste4mz0B6 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: PksD,Acyl_transf_1_1stECOD (1.6)
Bketoacyl-synte4mz0B4 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: ketoacyl-syntECOD (1.6)
BKetoacyl-synt_Ce4mz0B5 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: Ketoacyl-synt_CECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.40.47.10 Alpha Beta 3-Layer(aba) Sandwich Peroxisomal Thiolase Chain A, domain 1CATH (utative)
B3.30.70.250 Alpha Beta 2-Layer Sandwich Alpha-Beta Plaits Malonyl-CoA ACP transacylase, ACP-bindingCATH (utative)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
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
A, B
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
A, B
PF16197Ketoacyl-synthetase C-terminal extension (KAsynt_C_assoc)Ketoacyl-synthetase C-terminal extension- Family
A, B
PF00698Acyl transferase domain (Acyl_transf_1)Acyl transferase domain- Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
CurL -