Annotations: 6L2G

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6l2ga1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	(Aspergillus fumigatus A1163 ) [TaxId: 451804 ],	SCOPe (2.08)
B	d6l2gb1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	(Aspergillus fumigatus A1163 ) [TaxId: 451804 ],	SCOPe (2.08)
C	d6l2gc1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	(Aspergillus fumigatus A1163 ) [TaxId: 451804 ],	SCOPe (2.08)
D	d6l2gd1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	(Aspergillus fumigatus A1163 ) [TaxId: 451804 ],	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	e6l2gA2	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	e6l2gA1	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	e6l2gB1	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	e6l2gB2	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	e6l2gC1	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	e6l2gC2	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	e6l2gD1	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	e6l2gD2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF02803	ECOD (1.6)

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, putative	acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity acetyl-CoA C-acyltransferase activity C-acyltransferase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	-	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity 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	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

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.