6AQP

Aspergillus fumigatus Cytosolic Thiolase: Acetylated enzyme in complex with CoA and potassium ions

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00108	e6aqpA2	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	e6aqpA1	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	e6aqpB2	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	e6aqpB1	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	e6aqpC2	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	e6aqpC1	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	e6aqpD1	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	e6aqpD2	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 cation binding ion binding binding metal ion binding small molecule binding	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 metabolic process organic substance biosynthetic process small molecule metabolic process ergosterol metabolic process steroid biosynthetic process phytosteroid metabolic process secondary alcohol biosynthetic 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 metabolic process organic substance biosynthetic process small molecule metabolic process ergosterol metabolic process steroid biosynthetic process phytosteroid metabolic process secondary alcohol biosynthetic process small molecule biosynthetic process cellular metabolic process primary metabolic 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 cellular lipid metabolic process metabolic process cellular process lipid metabolic process catabolic process oxoacid metabolic process organic acid catabolic process organic acid metabolic process cellular lipid catabolic process cellular catabolic process monocarboxylic acid catabolic process fatty acid oxidation carboxylic acid catabolic process fatty acid beta-oxidation lipid oxidation fatty acid metabolic process lipid catabolic process carboxylic acid metabolic process lipid modification fatty acid catabolic process monocarboxylic acid metabolic process small molecule catabolic process organic substance catabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol membrane-bounded organelle intracellular organelle mitochondrion organelle intracellular membrane-bounded organelle

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	IPR020615	Thiolase, acyl-enzyme intermediate active site	Active Site
A, B, C, D	IPR002155	Thiolase	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B, C, D	SCY	Parent Component: CYS RESID: AA0056 PSI-MOD : S-acetyl-L-cysteine MOD:00065

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.