4DFE

Crystal structure of 3-oxoacyl-[acyl-carrier-protein] synthase III from Burkholderia xenovorans

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
C	d4dfec1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	(Paraburkholderia xenovorans LB400 ) [TaxId: 266265 ],	SCOPe (2.08)
A	d4dfea1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	(Paraburkholderia xenovorans LB400 ) [TaxId: 266265 ],	SCOPe (2.08)
B	d4dfeb1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	(Paraburkholderia xenovorans LB400 ) [TaxId: 266265 ],	SCOPe (2.08)
D	d4dfed1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	(Paraburkholderia xenovorans LB400 ) [TaxId: 266265 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
C	ACP_syn_III_C	e4dfeC2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ACP_syn_III_C	ECOD (1.6)
C	ACP_syn_III	e4dfeC1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ACP_syn_III	ECOD (1.6)
A	ACP_syn_III_C	e4dfeA2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ACP_syn_III_C	ECOD (1.6)
A	ACP_syn_III	e4dfeA1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ACP_syn_III	ECOD (1.6)
B	ACP_syn_III_C	e4dfeB2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ACP_syn_III_C	ECOD (1.6)
B	ACP_syn_III	e4dfeB1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ACP_syn_III	ECOD (1.6)
D	ACP_syn_III_C	e4dfeD2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ACP_syn_III_C	ECOD (1.6)
D	ACP_syn_III	e4dfeD1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ACP_syn_III	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	3.40.47.10	Alpha Beta	3-Layer(aba) Sandwich	Peroxisomal Thiolase	Chain A, domain 1	CATH (4.3.0)
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)
D	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	PF08541	3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal (ACP_syn_III_C)	3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal	This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.	Domain
A, B, C, D	PF08545	3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III (ACP_syn_III)	3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III	This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	3-oxoacyl-[acyl-carrier-protein] synthase 3	beta-ketoacyl-acyl-carrier-protein synthase III activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity 3-oxoacyl-[acyl-carrier-protein] synthase activity	fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid 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 biosynthetic process small molecule metabolic process metabolic process fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid 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 biosynthetic process small molecule metabolic process metabolic process cellular process monocarboxylic acid metabolic process lipid metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR016039	Thiolase-like	Homologous Superfamily
A, B, C, D	IPR004655	Beta-ketoacyl-[acyl-carrier-protein] synthase III	Family
A, B, C, D	IPR013751	Beta-ketoacyl-[acyl-carrier-protein] synthase III, N-terminal	Domain
A, B, C, D	IPR013747	Beta-ketoacyl-[acyl-carrier-protein] synthase III, C-terminal	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B, C, D	CSO	Parent Component: CYS RESID: AA0205 PSI-MOD : L-cysteine sulfenic acid MOD:00210

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.