Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
A [auth C]SCOP2B SuperfamilyKASAT domain-like8055844 3002319 SCOP2B (2022-06-29)
A [auth C]SCOP2B SuperfamilyThiolase-like8055846 3000122 SCOP2B (2022-06-29)
B [auth A]SCOP2B SuperfamilyThiolase-like8055846 3000122 SCOP2B (2022-06-29)
B [auth A]SCOP2B SuperfamilyKASAT domain-like8055844 3002319 SCOP2B (2022-06-29)
C [auth B]SCOP2B SuperfamilyThiolase-like8055846 3000122 SCOP2B (2022-06-29)
C [auth B]SCOP2B SuperfamilyKASAT domain-like8055844 3002319 SCOP2B (2022-06-29)
DSCOP2 FamilyThiolase-related8055845 4000245 SCOP2 (2022-06-29)
DSCOP2 FamilyKASAT domain-like8045096 4004293 SCOP2 (2022-06-29)
DSCOP2 SuperfamilyThiolase-like8055846 3000122 SCOP2 (2022-06-29)
DSCOP2 SuperfamilyKASAT domain-like8055844 3002319 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
A [auth C]PF22336e5elpC3 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: PF22336ECOD (1.6)
A [auth C]PF00109e5elpC2 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: PF00109ECOD (1.6)
A [auth C]PF02801e5elpC1 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: PF02801ECOD (1.6)
B [auth A]PF22336e5elpA3 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: PF22336ECOD (1.6)
B [auth A]PF00109e5elpA1 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: PF00109ECOD (1.6)
B [auth A]PF02801e5elpA2 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: PF02801ECOD (1.6)
C [auth B]PF22336e5elpB3 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: PF22336ECOD (1.6)
C [auth B]PF00109e5elpB2 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: PF00109ECOD (1.6)
C [auth B]PF02801e5elpB1 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: PF02801ECOD (1.6)
DPF22336e5elpD1 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: PF22336ECOD (1.6)
DPF00109e5elpD3 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: PF00109ECOD (1.6)
DPF02801e5elpD2 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: PF02801ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A [auth C],
B [auth A],
C [auth B],
D
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 [auth C],
B [auth A],
C [auth B],
D
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 [auth C],
B [auth A],
C [auth B],
D
PF16197Ketoacyl-synthetase C-terminal extension (KAsynt_C_assoc)Ketoacyl-synthetase C-terminal extension- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A [auth C],
B [auth A],
C [auth B],
D
NRPS/PKS protein -

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A [auth C],
B [auth A],
C [auth B],
D
IPR014031Beta-ketoacyl synthase, C-terminalDomain
A [auth C],
B [auth A],
C [auth B],
D
IPR006162Phosphopantetheine attachment sitePTM
A [auth C],
B [auth A],
C [auth B],
D
IPR020807Polyketide synthase, dehydratase domainDomain
A [auth C],
B [auth A],
C [auth B],
D
IPR014030Beta-ketoacyl synthase, N-terminalDomain
A [auth C],
B [auth A],
C [auth B],
D
IPR049552Polyketide synthase, dehydratase domain, N-terminalDomain
A [auth C],
B [auth A],
C [auth B],
D
IPR049551Polyketide synthase, dehydratase domain, C-terminalDomain
A [auth C],
B [auth A],
C [auth B],
D
IPR020845AMP-binding, conserved siteConserved Site
A [auth C],
B [auth A],
C [auth B],
D
IPR023213Chloramphenicol acetyltransferase-like domain superfamilyHomologous Superfamily
A [auth C],
B [auth A],
C [auth B],
D
IPR013968Polyketide synthase, ketoreductase domainDomain
A [auth C],
B [auth A],
C [auth B],
D
IPR020806Polyketide synthase, phosphopantetheine-binding domainDomain
A [auth C],
B [auth A],
C [auth B],
D
IPR020841Polyketide synthase, beta-ketoacyl synthase domainDomain
A [auth C],
B [auth A],
C [auth B],
D
IPR001242Condensation domainDomain
A [auth C],
B [auth A],
C [auth B],
D
IPR036736ACP-like superfamilyHomologous Superfamily
A [auth C],
B [auth A],
C [auth B],
D
IPR025110AMP-binding enzyme, C-terminal domainDomain
A [auth C],
B [auth A],
C [auth B],
D
IPR032821Polyketide synthase, C-terminal extensionDomain
A [auth C],
B [auth A],
C [auth B],
D
IPR009081Phosphopantetheine binding ACP domainDomain
A [auth C],
B [auth A],
C [auth B],
D
IPR010071Amino acid adenylation domainDomain
A [auth C],
B [auth A],
C [auth B],
D
IPR016039Thiolase-likeHomologous Superfamily
A [auth C],
B [auth A],
C [auth B],
D
IPR045851AMP-binding enzyme, C-terminal domain superfamilyHomologous Superfamily
A [auth C],
B [auth A],
C [auth B],
D
IPR042099ANL, N-terminal domainHomologous Superfamily
A [auth C],
B [auth A],
C [auth B],
D
IPR036291NAD(P)-binding domain superfamilyHomologous Superfamily
A [auth C],
B [auth A],
C [auth B],
D
IPR018201Beta-ketoacyl synthase, active siteActive Site
A [auth C],
B [auth A],
C [auth B],
D
IPR000873AMP-dependent synthetase/ligase domainDomain
A [auth C],
B [auth A],
C [auth B],
D
IPR042104Polyketide synthase, dehydratase domain superfamilyHomologous Superfamily