Annotations: 2IIK

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2iika1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d2iikb1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d2iikb3	Artifacts	Tags	Tags	Tags	N-terminal Tags	human (Homo sapiens ) [TaxId: 9606 ],	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	Thiolase_C	e2iikA2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: Thiolase_C	ECOD (1.6)
A	Thiolase_N	e2iikA1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: Thiolase_N	ECOD (1.6)
B	Thiolase_C	e2iikB2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: Thiolase_C	ECOD (1.6)
B	Thiolase_N	e2iikB1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: Thiolase_N	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	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	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	3-ketoacyl-CoA thiolase, peroxisomal	acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity acetyl-CoA C-acyltransferase activity C-acyltransferase activity catalytic activity acetate CoA-transferase activity transferase activity, transferring sulphur-containing groups CoA-transferase activity acetyl-CoA C-acetyltransferase activity acetyltransferase activity C-acetyltransferase activity oxidoreductase activity acyl-CoA oxidase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity acetyl-CoA C-acyltransferase activity C-acyltransferase activity catalytic activity acetate CoA-transferase activity transferase activity, transferring sulphur-containing groups CoA-transferase activity acetyl-CoA C-acetyltransferase activity acetyltransferase activity C-acetyltransferase activity oxidoreductase activity acyl-CoA oxidase activity palmitoyl-CoA oxidase activity oxidoreductase activity, acting on the CH-CH group of donors oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor myristoyltransferase activity acetyl-CoA C-myristoyltransferase activity	cellular response to stimulus catabolic process response to stimulus oxoacid metabolic process organic acid catabolic process organic acid metabolic process response to xenobiotic stimulus cellular catabolic process organic substance metabolic process monocarboxylic acid catabolic process carboxylic acid catabolic process small molecule metabolic process benzene-containing compound metabolic process cellular response to xenobiotic stimulus cellular response to stimulus catabolic process response to stimulus oxoacid metabolic process organic acid catabolic process organic acid metabolic process response to xenobiotic stimulus cellular catabolic process organic substance metabolic process monocarboxylic acid catabolic process carboxylic acid catabolic process small molecule metabolic process benzene-containing compound metabolic process cellular response to xenobiotic stimulus cellular metabolic process carboxylic acid metabolic process xenobiotic catabolic process organic cyclic compound catabolic process xenobiotic metabolic process organic cyclic compound metabolic process cellular response to chemical stimulus response to chemical phenylacetate catabolic process metabolic process cellular process monocarboxylic acid metabolic process small molecule catabolic process organic substance catabolic process cellular lipid catabolic process fatty acid beta-oxidation using acyl-CoA oxidase fatty acid oxidation fatty acid beta-oxidation lipid oxidation fatty acid metabolic process lipid catabolic process primary metabolic process lipid modification fatty acid catabolic process cellular lipid metabolic process lipid metabolic process steroid metabolic process organic hydroxy compound metabolic process bile acid metabolic process very long-chain fatty acid metabolic process long-chain fatty acid metabolic process unsaturated fatty acid metabolic process olefinic compound metabolic process alpha-linolenic acid metabolic process	membrane cellular anatomical entity extracellular region membrane-bounded organelle intracellular organelle intracellular anatomical structure organelle peroxisome microbody cytoplasm intracellular membrane-bounded organelle cytosol vesicle lumen intracellular vesicle membrane cellular anatomical entity extracellular region membrane-bounded organelle intracellular organelle intracellular anatomical structure organelle peroxisome microbody cytoplasm intracellular membrane-bounded organelle cytosol vesicle lumen intracellular vesicle membrane-enclosed lumen cytoplasmic vesicle lumen secretory granule lumen endomembrane system intracellular organelle lumen cytoplasmic vesicle organelle lumen specific granule lumen secretory granule secretory vesicle vesicle specific granule peroxisomal matrix microbody lumen

InterPro: Protein Family Classification InterPro Database Homepage

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

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: P09110	astrocytic tumor medulloblastoma pancreatic ductal adenocarcinoma ulcerative colitis large cell medulloblastoma osteosarcoma plasma cell myeloma malignant mesothelioma ovarian cancer psoriasis

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.