Annotations: 4WYS

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4wysa1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
B	d4wysb1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
C	d4wysc1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
D	d4wysd1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00108	e4wysA2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF00108	ECOD (1.6)
A	PF02803	e4wysA1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF02803	ECOD (1.6)
B	PF00108	e4wysB2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF00108	ECOD (1.6)
B	PF02803	e4wysB1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF02803	ECOD (1.6)
C	PF00108	e4wysC2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF00108	ECOD (1.6)
C	PF02803	e4wysC1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF02803	ECOD (1.6)
D	PF00108	e4wysD2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF00108	ECOD (1.6)
D	PF02803	e4wysD1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF02803	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)
C	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	PF02803	Thiolase, C-terminal domain (Thiolase_C)	Thiolase, C-terminal domain	Thiolase is reported to be structurally related to beta-ketoacyl synthase (Pfam:PF00109), and also chalcone synthase.	Domain
A, B, C, D	PF00108	Thiolase, N-terminal domain (Thiolase_N)	Thiolase, N-terminal domain	Thiolase is reported to be structurally related to beta-ketoacyl synthase (Pfam:PF00109), and also chalcone synthase.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Acetyl-CoA acetyltransferase	acetyl-CoA C-acetyltransferase activity acetyltransferase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity acetyl-CoA C-acyltransferase activity C-acyltransferase activity catalytic activity C-acetyltransferase activity identical protein binding protein binding binding	catabolic process oxoacid metabolic process short-chain fatty acid metabolic process ketone body catabolic process organic acid catabolic process organic acid metabolic process cellular lipid catabolic process fatty acid derivative catabolic process cellular catabolic process organic substance metabolic process monocarboxylic acid catabolic process carboxylic acid catabolic process small molecule metabolic process ketone body metabolic process catabolic process oxoacid metabolic process short-chain fatty acid metabolic process ketone body catabolic process organic acid catabolic process organic acid metabolic process cellular lipid catabolic process fatty acid derivative catabolic process cellular catabolic process organic substance metabolic process monocarboxylic acid catabolic process carboxylic acid catabolic process small molecule metabolic process ketone body metabolic process fatty acid metabolic process short-chain fatty acid catabolic process lipid catabolic process cellular metabolic process carboxylic acid metabolic process acetoacetic acid metabolic process primary metabolic process generation of precursor metabolites and energy fatty acid catabolic process fatty acid derivative metabolic process acetoacetic acid catabolic process cellular lipid metabolic process cellular ketone body metabolic process metabolic process cellular process monocarboxylic acid metabolic process small molecule catabolic process organic substance catabolic process lipid metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR016039	Thiolase-like	Homologous Superfamily
A, B, C, D	IPR020617	Thiolase, C-terminal	Domain
A, B, C, D	IPR020616	Thiolase, N-terminal	Domain
A, B, C, D	IPR020613	Thiolase, conserved site	Conserved Site
A, B, C, D	IPR020610	Thiolase, active site	Active Site
A, B, C, D	IPR020615	Thiolase, acyl-enzyme intermediate active site	Active Site
A, B, C, D	IPR002155	Thiolase	Family

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.