Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad2cf2a2 Alpha and beta proteins (a/b) Thiolase-like Thiolase-like Thiolase-related Beta-ketoacyl-ACP synthase I, C-terminal domain (Sus scrofa ) [TaxId: 9823 ], SCOPe (2.08)
Ad2cf2a1 Alpha and beta proteins (a/b) Thiolase-like Thiolase-like Thiolase-related Beta-ketoacyl-ACP synthase I, N-terminal domain (Sus scrofa ) [TaxId: 9823 ], SCOPe (2.08)
F [auth J]d2cf2j2 Alpha and beta proteins (a/b) Thiolase-like Thiolase-like Thiolase-related Beta-ketoacyl-ACP synthase I, C-terminal domain (Sus scrofa ) [TaxId: 9823 ], SCOPe (2.08)
F [auth J]d2cf2j1 Alpha and beta proteins (a/b) Thiolase-like Thiolase-like Thiolase-related Beta-ketoacyl-ACP synthase I, N-terminal domain (Sus scrofa ) [TaxId: 9823 ], SCOPe (2.08)
Cd2cf2c1 Alpha and beta proteins (a+b) Thioesterase/thiol ester dehydrase-isomerase Thioesterase/thiol ester dehydrase-isomerase beta-Hydroxydecanol thiol ester dehydrase beta-Hydroxydecanol thiol ester dehydrase (Sus scrofa ) [TaxId: 9823 ], SCOPe (2.08)
H [auth L]d2cf2l1 Alpha and beta proteins (a+b) Thioesterase/thiol ester dehydrase-isomerase Thioesterase/thiol ester dehydrase-isomerase beta-Hydroxydecanol thiol ester dehydrase beta-Hydroxydecanol thiol ester dehydrase (Sus scrofa ) [TaxId: 9823 ], SCOPe (2.08)
Ed2cf2e1 Low resolution protein structures Fatty acid synthase Fatty acid synthase Fatty acid syntase mammalian fatty acid synthase (Sus scrofa ) [TaxId: 9823 ], SCOPe (2.08)
J [auth N]d2cf2n1 Low resolution protein structures Fatty acid synthase Fatty acid synthase Fatty acid syntase mammalian fatty acid synthase (Sus scrofa ) [TaxId: 9823 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyThiolase-like8037440 3000122 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyThiolase-like8037437 3000122 SCOP2B (2022-06-29)
F [auth J]SCOP2B SuperfamilyThiolase-like8037440 3000122 SCOP2B (2022-06-29)
F [auth J]SCOP2B SuperfamilyThiolase-like8037437 3000122 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF00109e2cf2A1 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: PF00109ECOD (1.6)
APF02801e2cf2A2 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: PF02801ECOD (1.6)
F [auth J]PF00109e2cf2J1 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: PF00109ECOD (1.6)
F [auth J]PF02801e2cf2J2 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: PF02801ECOD (1.6)
BF_UNCLASSIFIEDe2cf2B1 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: F_UNCLASSIFIEDECOD (1.6)
BPF00698e2cf2B2 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: PF00698ECOD (1.6)
G [auth K]F_UNCLASSIFIEDe2cf2K1 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: F_UNCLASSIFIEDECOD (1.6)
G [auth K]PF00698e2cf2K2 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: PF00698ECOD (1.6)
CPF07977e2cf2C1 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: PF07977ECOD (1.6)
H [auth L]PF07977e2cf2L1 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: PF07977ECOD (1.6)
DPF08240,PF13602e2cf2D1 A: beta barrelsX: GroES-likeH: GroES-relatedT: Alcohol dehydrogenase-like, N-terminal domainF: PF08240,PF13602ECOD (1.6)
DPF00107e2cf2D2 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: PF00107ECOD (1.6)
I [auth M]PF08240,PF13602e2cf2M1 A: beta barrelsX: GroES-likeH: GroES-relatedT: Alcohol dehydrogenase-like, N-terminal domainF: PF08240,PF13602ECOD (1.6)
I [auth M]PF00107e2cf2M2 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: PF00107ECOD (1.6)
EPF13561e2cf2E1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: PF13561ECOD (1.6)
J [auth N]PF13561e2cf2N1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: PF13561ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A,
F [auth J]
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,
F [auth J]
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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A,
F [auth J]
FATTY ACID SYNTHASE, KS DOMAIN
B,
G [auth K]
FATTY ACID SYNTHASE, MAT DOMAIN---
C,
H [auth L]
FATTY ACID SYNTHASE, DH DOMAIN---
D,
I [auth M]
FATTY ACID SYNTHASE, ER DOMAIN---
E,
J [auth N]
FATTY ACID SYNTHASE, KR DOMAIN---