Annotations: 3ALE

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	e3aleA2	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	e3aleA1	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	e3aleB2	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	e3aleB1	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)
C	ACP_syn_III_C	e3aleC1	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)
C	Chal_sti_synt_N	e3aleC2	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)
D	ACP_syn_III_C	e3aleD1	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)
D	Chal_sti_synt_N	e3aleD2	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)
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	PF00195	Chalcone and stilbene synthases, N-terminal domain (Chal_sti_synt_N)	Chalcone and stilbene synthases, N-terminal domain	The C-terminal 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 this N-terminal domain.	Domain
A, B, C, D	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, C, D	Os07g0271500 protein	bisdemethoxycurcumin synthase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity identical protein binding protein binding binding	flavonoid metabolic process organic substance metabolic process flavonoid biosynthetic process biosynthetic process organic substance biosynthetic process metabolic process polyketide biosynthetic process secondary metabolite biosynthetic process polyketide metabolic process secondary metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

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