Annotations: 5UCO

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5ucoa1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	Tutsan (Hypericum androsaemum ) [TaxId: 140968 ],	SCOPe (2.08)
B	d5ucob1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	Tutsan (Hypericum androsaemum ) [TaxId: 140968 ],	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	ACP_syn_III_C	e5ucoA1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ACP_syn_III_C	ECOD (1.6)
A	Chal_sti_synt_N	e5ucoA2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: Chal_sti_synt_N	ECOD (1.6)
B	ACP_syn_III_C	e5ucoB1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ACP_syn_III_C	ECOD (1.6)
B	Chal_sti_synt_N	e5ucoB2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: Chal_sti_synt_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	PF02797	Chalcone and stilbene synthases, C-terminal domain (Chal_sti_synt_C)	Chalcone and stilbene synthases, C-terminal domain	This domain of chalcone synthase is reported to be structurally similar to domains in thiolase and beta-ketoacyl synthase. The differences in activity are accounted for by differences in the N-terminal domain.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	2,4,6-trihydroxybenzophenone synthase	acyltransferase activity trihydroxybenzophenone synthase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity tetrahydroxybenzophenone synthase activity	nucleoside phosphate metabolic process benzoyl-CoA metabolic process primary metabolic process purine-containing compound metabolic process nucleobase-containing compound metabolic process acyl-CoA metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process metabolic process cellular process sulfur compound metabolic process small molecule metabolic process amide metabolic process nucleoside phosphate metabolic process benzoyl-CoA metabolic process primary metabolic process purine-containing compound metabolic process nucleobase-containing compound metabolic process acyl-CoA metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process metabolic process cellular process sulfur compound metabolic process small molecule metabolic process amide metabolic process thioester metabolic process phosphorus metabolic process polyketide biosynthetic process secondary metabolite biosynthetic process biosynthetic process polyketide metabolic process secondary metabolic process malonyl-CoA metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR001099	Chalcone/stilbene synthase, N-terminal	Domain
A, B	IPR016039	Thiolase-like	Homologous Superfamily
A, B	IPR012328	Chalcone/stilbene synthase, C-terminal	Domain
A, B	IPR011141	Polyketide synthase, type III	Family

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 R01GM157729.