Annotations: 6PCA

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6pcaa1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	(Pseudomonas putida KT2440 ) [TaxId: 160488 ],	SCOPe (2.08)
A	d6pcaa3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Pseudomonas putida KT2440 ) [TaxId: 160488 ],	SCOPe (2.08)
B	d6pcab1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	(Pseudomonas putida KT2440 ) [TaxId: 160488 ],	SCOPe (2.08)
B	d6pcab3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Pseudomonas putida KT2440 ) [TaxId: 160488 ],	SCOPe (2.08)
C	d6pcac1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	(Pseudomonas putida KT2440 ) [TaxId: 160488 ],	SCOPe (2.08)
C	d6pcac3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Pseudomonas putida KT2440 ) [TaxId: 160488 ],	SCOPe (2.08)
D	d6pcad1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	(Pseudomonas putida KT2440 ) [TaxId: 160488 ],	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	e6pcaA1	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	e6pcaA2	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	e6pcaB1	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	e6pcaB2	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	e6pcaC1	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	e6pcaC2	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	e6pcaD2	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	e6pcaD1	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 (utative)
B	3.40.47.10	Alpha Beta	3-Layer(aba) Sandwich	Peroxisomal Thiolase	Chain A, domain 1	CATH (utative)
C	3.40.47.10	Alpha Beta	3-Layer(aba) Sandwich	Peroxisomal Thiolase	Chain A, domain 1	CATH (utative)
D	3.40.47.10	Alpha Beta	3-Layer(aba) Sandwich	Peroxisomal Thiolase	Chain A, domain 1	CATH (utative)

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	Beta-ketoadipyl-CoA thiolase	3-oxoadipyl-CoA thiolase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity 3'-N-debenzoyl-2'-deoxytaxol N-benzoyltransferase activity	catabolic process oxoacid metabolic process organic hydroxy compound metabolic process catechol-containing compound metabolic process organic acid metabolic process organic acid catabolic process cellular catabolic process organic substance metabolic process monocarboxylic acid catabolic process carboxylic acid catabolic process small molecule metabolic process 3,4-dihydroxybenzoate catabolic process 3,4-dihydroxybenzoate metabolic process benzene-containing compound metabolic process catabolic process oxoacid metabolic process organic hydroxy compound metabolic process catechol-containing compound metabolic process organic acid metabolic process organic acid catabolic process cellular catabolic process organic substance metabolic process monocarboxylic acid catabolic process carboxylic acid catabolic process small molecule metabolic process 3,4-dihydroxybenzoate catabolic process 3,4-dihydroxybenzoate metabolic process benzene-containing compound metabolic process catechol-containing compound catabolic process cellular metabolic process carboxylic acid metabolic process organic cyclic compound catabolic process phenol-containing compound catabolic process organic cyclic compound metabolic process organic hydroxy compound catabolic process phenol-containing compound metabolic process metabolic process cellular process monocarboxylic acid metabolic process small molecule catabolic process organic substance catabolic process	-

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	IPR012793	Beta-ketoadipyl CoA thiolase	Family
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 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.