4B0N

Crystal structure of PKS-I from the brown algae Ectocarpus siliculosus

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4b0na1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	BROWN ALGAE (Ectocarpus siliculosus ) [TaxId: 2880 ],	SCOPe (2.08)
B	d4b0nb1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	automated matches	automated matches	BROWN ALGAE (Ectocarpus siliculosus ) [TaxId: 2880 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Chalcone synthase-like	8083973	4000864	SCOP2 (2022-06-29)
A	SCOP2 Family	Chalcone synthase-like	8101786	4000864	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Thiolase-like	8083974	3000122	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Thiolase-like	8101787	3000122	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Thiolase-like	8101787	3000122	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thiolase-like	8083974	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	PF00195	e4b0nA2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF00195	ECOD (1.6)
A	PF02797	e4b0nA1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF02797	ECOD (1.6)
B	PF00195	e4b0nB1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF00195	ECOD (1.6)
B	PF02797	e4b0nB2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: PF02797	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	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	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	POLYKETIDE SYNTHASE III	acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity	biosynthetic process 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 R01GM133198.