5E6K

Ketosynthase from module 6 of the bacillaene synthase from Bacillus subtilis 168 (C167S mutant, crystal form 2)

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	KASAT domain-like	8055817	3002319	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Thiolase-like	8055819	3000122	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thiolase-like	8055819	3000122	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	KASAT domain-like	8055817	3002319	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF22336	e5e6kA2	A: a+b two layers	X: 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 synthase	F: PF22336	ECOD (1.6)
A	PF00109	e5e6kA1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF00109	ECOD (1.6)
A	PF02801,PF16197	e5e6kA3	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF02801,PF16197	ECOD (1.6)
B	PF22336	e5e6kB2	A: a+b two layers	X: 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 synthase	F: PF22336	ECOD (1.6)
B	PF00109	e5e6kB1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF00109	ECOD (1.6)
B	PF02801,PF16197	e5e6kB3	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF02801,PF16197	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.47.10	Alpha Beta	3-Layer(aba) Sandwich	Peroxisomal Thiolase	Chain A, domain 1	CATH (4.3.0)
B	3.40.47.10	Alpha Beta	3-Layer(aba) Sandwich	Peroxisomal Thiolase	Chain A, domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00109	Beta-ketoacyl synthase, N-terminal domain (ketoacyl-synt)	Beta-ketoacyl synthase, N-terminal domain	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 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

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Polyketide synthase PksL	oxidoreductase activity catalytic activity vitamin binding amide binding modified amino acid binding binding phosphopantetheine binding small molecule binding acyltransferase activity 3-oxoacyl-[acyl-carrier-protein] synthase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity fatty acid synthase activity	antibiotic metabolic process biosynthetic process metabolic process antibiotic biosynthetic process cellular component biogenesis cellular component organization peptidoglycan-based cell wall biogenesis cellular component assembly cell wall biogenesis DIM/DIP cell wall layer assembly cell wall organization or biogenesis cellular process Actinobacterium-type cell wall biogenesis cellular component organization or biogenesis antibiotic metabolic process biosynthetic process metabolic process antibiotic biosynthetic process cellular component biogenesis cellular component organization peptidoglycan-based cell wall biogenesis cellular component assembly cell wall biogenesis DIM/DIP cell wall layer assembly cell wall organization or biogenesis cellular process Actinobacterium-type cell wall biogenesis cellular component organization or biogenesis fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process cellular metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process cellular lipid metabolic process small molecule metabolic process monocarboxylic acid metabolic process lipid metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR014031	Beta-ketoacyl synthase, C-terminal	Domain
A, B	IPR006162	Phosphopantetheine attachment site	PTM
A, B	IPR020807	Polyketide synthase, dehydratase domain	Domain
A, B	IPR014030	Beta-ketoacyl synthase, N-terminal	Domain
A, B	IPR049552	Polyketide synthase, dehydratase domain, N-terminal	Domain
A, B	IPR049551	Polyketide synthase, dehydratase domain, C-terminal	Domain
A, B	IPR013968	Polyketide synthase, ketoreductase domain	Domain
A, B	IPR020806	Polyketide synthase, phosphopantetheine-binding domain	Domain
A, B	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain	Domain
A, B	IPR036736	ACP-like superfamily	Homologous Superfamily
A, B	IPR011254	Prismane-like superfamily	Homologous Superfamily
A, B	IPR032821	Polyketide synthase, C-terminal extension	Domain
A, B	IPR009081	Phosphopantetheine binding ACP domain	Domain
A, B	IPR016039	Thiolase-like	Homologous Superfamily
A, B	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR018201	Beta-ketoacyl synthase, active site	Active Site
A, B	IPR042104	Polyketide synthase, dehydratase domain superfamily	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.