1F91

BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE I IN COMPLEX WITH C10 FATTY ACID SUBSTRATE

External Resource: Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1f91a2	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, C-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1f91a1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, N-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d1f91d2	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, C-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d1f91d1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, N-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1f91b2	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, C-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1f91b1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, N-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1f91c2	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, C-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1f91c1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Beta-ketoacyl-ACP synthase I, N-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Thiolase-like	8037440	3000122	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Thiolase-like	8037437	3000122	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thiolase-like	8037437	3000122	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thiolase-like	8037440	3000122	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thiolase-like	8037440	3000122	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thiolase-like	8037437	3000122	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Thiolase-like	8037437	3000122	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Thiolase-like	8037440	3000122	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	ketoacyl-synt	e1f91A1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ketoacyl-synt	ECOD (1.6)
A	Ketoacyl-synt_C	e1f91A2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: Ketoacyl-synt_C	ECOD (1.6)
D	ketoacyl-synt	e1f91D1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ketoacyl-synt	ECOD (1.6)
D	Ketoacyl-synt_C	e1f91D2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: Ketoacyl-synt_C	ECOD (1.6)
B	ketoacyl-synt	e1f91B1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ketoacyl-synt	ECOD (1.6)
B	Ketoacyl-synt_C	e1f91B2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: Ketoacyl-synt_C	ECOD (1.6)
C	ketoacyl-synt	e1f91C1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ketoacyl-synt	ECOD (1.6)
C	Ketoacyl-synt_C	e1f91C2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: Ketoacyl-synt_C	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)
D	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)
C	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, C, D	PF02801	Beta-ketoacyl synthase, C-terminal domain (Ketoacyl-synt_C)	Beta-ketoacyl synthase, C-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.	Domain
A, B, C, D	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, C, D	BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE I	acyltransferase activity 3-oxoacyl-[acyl-carrier-protein] synthase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity	fatty acid metabolic process monocarboxylic acid biosynthetic process oxoacid metabolic process small molecule biosynthetic process cellular biosynthetic process cellular metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid metabolic process organic acid biosynthetic process fatty acid biosynthetic process monounsaturated fatty acid biosynthetic process carboxylic acid biosynthetic process biosynthetic process fatty acid metabolic process monocarboxylic acid biosynthetic process oxoacid metabolic process small molecule biosynthetic process cellular biosynthetic process cellular metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid metabolic process organic acid biosynthetic process fatty acid biosynthetic process monounsaturated fatty acid biosynthetic process carboxylic acid biosynthetic process biosynthetic process cellular lipid metabolic process monounsaturated fatty acid metabolic process metabolic process cellular process small molecule metabolic process monocarboxylic acid metabolic process lipid metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR016039	Thiolase-like	Homologous Superfamily
A, B, C, D	IPR014031	Beta-ketoacyl synthase, C-terminal	Domain
A, B, C, D	IPR000794	Beta-ketoacyl synthase	Family
A, B, C, D	IPR018201	Beta-ketoacyl synthase, active site	Active Site
A, B, C, D	IPR014030	Beta-ketoacyl synthase-like, N-terminal	Domain
A, B, C, D	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain	Domain

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 R01GM157729.