Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyKASAT domain-like8055913 3002319 SCOP2B (2022-06-29)
ASCOP2B SuperfamilySDR-like8055928 3000038 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyThioesterase/thiol ester dehydrase-isomerase-like8055921 3000149 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyKASAT domain-like8055913 3002319 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyThioesterase/thiol ester dehydrase-isomerase-like8055920 3000149 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyThiolase-like8055915 3000122 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyProbable ACP-binding domain of malonyl-CoA ACP transacylase8055919 3001224 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyZinc-containing alcohol dehydrogenase-like8055926 3000040 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyGroES-like8055925 3000002 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyFabD/lysophospholipase-like8055917 3001121 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyFabD/lysophospholipase-like8055917 3001121 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyS-adenosyl-L-methionine-dependent methyltransferases8055923 3000118 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyGroES-like8055925 3000002 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyThioesterase/thiol ester dehydrase-isomerase-like8055921 3000149 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyProbable ACP-binding domain of malonyl-CoA ACP transacylase8055919 3001224 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyS-adenosyl-L-methionine-dependent methyltransferases8055923 3000118 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyFabD/lysophospholipase-like8055917 3001121 SCOP2B (2022-06-29)
BSCOP2B SuperfamilySDR-like8055928 3000038 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyFabD/lysophospholipase-like8055917 3001121 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyKASAT domain-like8055913 3002319 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyThiolase-like8055915 3000122 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyThioesterase/thiol ester dehydrase-isomerase-like8055920 3000149 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyZinc-containing alcohol dehydrogenase-like8055926 3000040 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyKASAT domain-like8055913 3002319 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AKOG1202_2nde2vz9A18 A: beta barrelsX: GroES-likeH: GroES-relatedT: Alcohol dehydrogenase-like, N-terminal domainF: KOG1202_2ndECOD (1.6)
APS-DH_Ne2vz9A11 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: PS-DH_NECOD (1.6)
APS-DH_C_2e2vz9A14 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: PS-DH_C_2ECOD (1.6)
AAcyl_transf_1_2nde2vz9A20 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_2ndECOD (1.6)
AKAsynt_C_assoce2vz9A15 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: KAsynt_C_assocECOD (1.6)
AADH_zinc_Ne2vz9A16 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: ADH_zinc_NECOD (1.6)
AKOG1202_1ste2vz9A17 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: KOG1202_1stECOD (1.6)
Aadh_short_C2_1e2vz9A8 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: adh_short_C2_1ECOD (1.6)
AMethyltransf_11_3e2vz9A13 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: Methyltransf_11_3ECOD (1.6)
AAcyl_transf_1_1ste2vz9A12 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: Acyl_transf_1_1stECOD (1.6)
Aketoacyl-synte2vz9A10 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: ketoacyl-syntECOD (1.6)
AKetoacyl-synt_Ce2vz9A19 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: Ketoacyl-synt_CECOD (1.6)
BKOG1202_2nde2vz9B9 A: beta barrelsX: GroES-likeH: GroES-relatedT: Alcohol dehydrogenase-like, N-terminal domainF: KOG1202_2ndECOD (1.6)
BPS-DH_Ne2vz9B5 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: PS-DH_NECOD (1.6)
BPS-DH_C_2e2vz9B6 A: a+b two layersX: Thioesterase/thiol ester dehydrase-isomerase-likeH: Thioesterase/thiol ester dehydrase-isomerase (From Topology)T: Thioesterase/thiol ester dehydrase-isomeraseF: PS-DH_C_2ECOD (1.6)
BAcyl_transf_1_2nde2vz9B4 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_2ndECOD (1.6)
BKAsynt_C_assoce2vz9B12 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: KAsynt_C_assocECOD (1.6)
BADH_zinc_Ne2vz9B10 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: ADH_zinc_NECOD (1.6)
BKOG1202_1ste2vz9B8 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: KOG1202_1stECOD (1.6)
Badh_short_C2_1e2vz9B11 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: adh_short_C2_1ECOD (1.6)
BMethyltransf_11_3e2vz9B7 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: Methyltransf_11_3ECOD (1.6)
BAcyl_transf_1_1ste2vz9B3 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: Acyl_transf_1_1stECOD (1.6)
Bketoacyl-synte2vz9B1 A: a/b three-layered sandwichesX: Thiolase-like (From Topology)H: Thiolase-like (From Topology)T: Thiolase-likeF: ketoacyl-syntECOD (1.6)
BKetoacyl-synt_Ce2vz9B2 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

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
PF13602Zinc-binding dehydrogenase (ADH_zinc_N_2)Zinc-binding dehydrogenase- Domain
A, B
PF21089Polyketide synthase dehydratase domain (PKS_DH_N)Polyketide synthase dehydratase domainThis domain is part of a dehydratase domain found in diverse PKS enzymes. This domain adopts a HotDog fold.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
PF08242Methyltransferase domain (Methyltransf_12)Methyltransferase domainMembers of this family are SAM dependent methyltransferases.Domain
A, B
PF08659KR domain (KR)KR domain- Family
A, B
PF21149Fatty acid synthase, pseudo-KR domain (FAS_pseudo-KR)Fatty acid synthase, pseudo-KR domainFatty acid synthase is a multifunctional enzyme that catalyses the de novo biosynthesis of long-chain saturated fatty acids, starting from acetyl-CoA and malonyl-CoA in the presence of NADPH [1-3]. This entry represents the pseudo-ketoreductase (pseu ...Fatty acid synthase is a multifunctional enzyme that catalyses the de novo biosynthesis of long-chain saturated fatty acids, starting from acetyl-CoA and malonyl-CoA in the presence of NADPH [1-3]. This entry represents the pseudo-ketoreductase (pseudo-KR) domain which is catalytically inactive and supports the integrity of the active KR domain [1,3].
Domain
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
FATTY ACID SYNTHASE -

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A, B
IPR016035Acyl transferase/acyl hydrolase/lysophospholipaseHomologous Superfamily
A, B
IPR014031Beta-ketoacyl synthase, C-terminalDomain
A, B
IPR006162Phosphopantetheine attachment sitePTM
A, B
IPR013217Methyltransferase type 12Domain
A, B
IPR020807Polyketide synthase, dehydratase domainDomain
A, B
IPR014030Beta-ketoacyl synthase, N-terminalDomain
A, B
IPR049552Polyketide synthase, dehydratase domain, N-terminalDomain
A, B
IPR049391Fatty acid synthase, pseudo-KR domainDomain
A, B
IPR020843Polyketide synthase, enoylreductase domainDomain
A, B
IPR013968Polyketide synthase, ketoreductase domainDomain
A, B
IPR016036Malonyl-CoA ACP transacylase, ACP-bindingHomologous Superfamily
A, B
IPR020806Polyketide synthase, phosphopantetheine-binding domainDomain
A, B
IPR014043Acyl transferaseDomain
A, B
IPR020841Polyketide synthase, beta-ketoacyl synthase domainDomain
A, B
IPR036736ACP-like superfamilyHomologous Superfamily
A, B
IPR032821Polyketide synthase, C-terminal extensionDomain
A, B
IPR011032GroES-like superfamilyHomologous Superfamily
A, B
IPR009081Phosphopantetheine binding ACP domainDomain
A, B
IPR029063S-adenosyl-L-methionine-dependent methyltransferase superfamilyHomologous Superfamily
A, B
IPR029058Alpha/Beta hydrolase foldHomologous Superfamily
A, B
IPR016039Thiolase-likeHomologous Superfamily
A, B
IPR001227Acyl transferase domain superfamilyHomologous Superfamily
A, B
IPR036291NAD(P)-binding domain superfamilyHomologous Superfamily
A, B
IPR018201Beta-ketoacyl synthase, active siteActive Site
A, B
IPR042104Polyketide synthase, dehydratase domain superfamilyHomologous Superfamily
A, B
IPR001031ThioesteraseDomain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase  M-CSA #972

The mammalian fatty acid synthase (mFAS) is a multidomain protein with seven different active sites working together for the de novo synthesis of lipids, specifically palmitic acid. The dehydratase (DH) domain of mFAS catalyses the dehydration of the β-hydroxyacyl (HAC) to an α,β-unsaturated acyl intermediate.

Defined by 6 residues: HIS:A-878LEU:A-885GLY:A-888TYR:A-1003ASP:A-1033HIS:A-1037
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