5XYJ

Purification,crystallization and structural analysis of cytoplastic acetoacetyl-CoA thiolase from Saccharomyces cerevisiae

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth B]	d5xyjb1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	Baker's yeast (Saccharomyces cerevisiae S288C ) [TaxId: 559292 ],	SCOPe (2.08)
B [auth A]	d5xyja1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	Baker's yeast (Saccharomyces cerevisiae S288C ) [TaxId: 559292 ],	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 [auth B]	Thiolase_C	e5xyjB2	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 [auth B]	Thiolase_N	e5xyjB1	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 [auth A]	Thiolase_C	e5xyjA2	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 [auth A]	Thiolase_N	e5xyjA1	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 [auth B]	3.40.47.10	Alpha Beta	3-Layer(aba) Sandwich	Peroxisomal Thiolase	Chain A, domain 1	CATH (4.3.0)
B [auth A]	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 [auth B], B [auth A]	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 [auth B], B [auth A]	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 [auth B], B [auth A]	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 cation binding ion binding binding metal ion binding small molecule binding	catabolic process oxoacid metabolic process organic acid catabolic process organic acid metabolic process cellular lipid catabolic process cellular catabolic process organic substance metabolic process monocarboxylic acid catabolic process fatty acid oxidation carboxylic acid catabolic process fatty acid beta-oxidation small molecule metabolic process lipid oxidation fatty acid metabolic process catabolic process oxoacid metabolic process organic acid catabolic process organic acid metabolic process cellular lipid catabolic process cellular catabolic process organic substance metabolic process monocarboxylic acid catabolic process fatty acid oxidation carboxylic acid catabolic process fatty acid beta-oxidation small molecule metabolic process lipid oxidation fatty acid metabolic process lipid catabolic process cellular metabolic process carboxylic acid metabolic process primary metabolic process lipid modification fatty acid catabolic process cellular lipid metabolic process metabolic process cellular process monocarboxylic acid metabolic process small molecule catabolic process organic substance catabolic process lipid metabolic process organic hydroxy compound metabolic process steroid metabolic process sterol metabolic process lipid biosynthetic process alcohol metabolic process ergosterol biosynthetic process cellular lipid biosynthetic process organic substance biosynthetic process ergosterol metabolic process steroid biosynthetic process phytosteroid metabolic process secondary alcohol biosynthetic process small molecule biosynthetic process organic cyclic compound metabolic process phytosteroid biosynthetic process secondary alcohol metabolic process biosynthetic process sterol biosynthetic process organic hydroxy compound biosynthetic process organic cyclic compound biosynthetic process alcohol biosynthetic process	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle cytosol nucleus vacuole

InterPro: Protein Family Classification InterPro Database Homepage

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

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.