Annotations: 1M1T

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1m1ta2	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Biosynthetic thiolase, C-terminal domain	(Zoogloea ramigera ) [TaxId: 350 ],	SCOPe (2.08)
A	d1m1ta1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Biosynthetic thiolase, N-terminal domain	(Zoogloea ramigera ) [TaxId: 350 ],	SCOPe (2.08)
B	d1m1tb2	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Biosynthetic thiolase, C-terminal domain	(Zoogloea ramigera ) [TaxId: 350 ],	SCOPe (2.08)
B	d1m1tb1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Biosynthetic thiolase, N-terminal domain	(Zoogloea ramigera ) [TaxId: 350 ],	SCOPe (2.08)
C	d1m1tc2	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Biosynthetic thiolase, C-terminal domain	(Zoogloea ramigera ) [TaxId: 350 ],	SCOPe (2.08)
C	d1m1tc1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Biosynthetic thiolase, N-terminal domain	(Zoogloea ramigera ) [TaxId: 350 ],	SCOPe (2.08)
D	d1m1td2	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Biosynthetic thiolase, C-terminal domain	(Zoogloea ramigera ) [TaxId: 350 ],	SCOPe (2.08)
D	d1m1td1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Thiolase-related	Biosynthetic thiolase, N-terminal domain	(Zoogloea ramigera ) [TaxId: 350 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Thiolase-like	8043264	3000122	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Thiolase-like	8043265	3000122	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thiolase-like	8043264	3000122	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thiolase-like	8043265	3000122	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Thiolase-like	8043265	3000122	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Thiolase-like	8043264	3000122	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thiolase-like	8043265	3000122	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thiolase-like	8043264	3000122	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Thiolase_C	e1m1tA2	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	e1m1tA1	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	e1m1tB2	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	e1m1tB1	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)
C	Thiolase_C	e1m1tC2	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)
C	Thiolase_N	e1m1tC1	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)
D	Thiolase_C	e1m1tD2	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)
D	Thiolase_N	e1m1tD1	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)
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	organic substance metabolic process poly-hydroxybutyrate biosynthetic process biosynthetic process poly(hydroxyalkanoate) biosynthetic process organic substance biosynthetic process metabolic process poly(hydroxyalkanoate) metabolic process poly-hydroxybutyrate metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

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	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 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.