2HFK

Pikromycin thioesterase in complex with product 10-deoxymethynolide

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	d2hfka_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Thioesterase domain of polypeptide, polyketide and fatty acid synthases	Picromycin polyketide synthase	(Streptomyces venezuelae ) [TaxId: 54571 ],	SCOPe (2.08)
B	d2hfkb_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Thioesterase domain of polypeptide, polyketide and fatty acid synthases	Picromycin polyketide synthase	(Streptomyces venezuelae ) [TaxId: 54571 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	alpha/beta-Hydrolases	8042183	3000102	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	alpha/beta-Hydrolases	8042183	3000102	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	Hydrolase_4_1	e2hfkA1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4_1	ECOD (1.6)
B	Hydrolase_4_1	e2hfkB1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
B	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00975	Thioesterase domain (Thioesterase)	Thioesterase domain	Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of v ...	Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Type I polyketide synthase PikAIV	vitamin binding amide binding modified amino acid binding binding phosphopantetheine binding small molecule binding acyltransferase activity 3-oxoacyl-[acyl-carrier-protein] synthase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity fatty acid synthase activity	cellular component biogenesis cellular component organization peptidoglycan-based cell wall biogenesis cellular component assembly cell wall biogenesis DIM/DIP cell wall layer assembly cell wall organization or biogenesis cellular process Actinobacterium-type cell wall biogenesis cellular component organization or biogenesis fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process cellular component biogenesis cellular component organization peptidoglycan-based cell wall biogenesis cellular component assembly cell wall biogenesis DIM/DIP cell wall layer assembly cell wall organization or biogenesis cellular process Actinobacterium-type cell wall biogenesis cellular component organization or biogenesis fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process biosynthetic process small molecule metabolic process metabolic process monocarboxylic acid metabolic process lipid metabolic process macrolide biosynthetic process polyketide metabolic process macrolide metabolic process secondary metabolic process antibiotic biosynthetic process antibiotic metabolic process polyketide biosynthetic process secondary metabolite biosynthetic process lactone metabolic process lactone biosynthetic process	cell periphery cellular anatomical structure plasma membrane membrane intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR016035	Acyl transferase/acyl hydrolase/lysophospholipase	Homologous Superfamily
A, B	IPR014031	Beta-ketoacyl synthase, C-terminal	Domain
A, B	IPR016036	Malonyl-CoA ACP transacylase, ACP-binding	Homologous Superfamily
A, B	IPR050091	Polyketide and Nonribosomal Peptide Biosynthesis Enzymes	Family
A, B	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain	Domain
A, B	IPR036736	ACP-like superfamily	Homologous Superfamily
A, B	IPR014043	Acyl transferase domain	Domain
A, B	IPR015083	Polyketide synthase, docking domain	Domain
A, B	IPR032821	Polyketide synthase, C-terminal extension	Domain
A, B	IPR009081	Phosphopantetheine binding ACP domain	Domain
A, B	IPR020806	Polyketide synthase-like, phosphopantetheine-binding domain	Domain
A, B	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily
A, B	IPR020802	Polyketide synthase, thioesterase domain	Domain
A, B	IPR016039	Thiolase-like	Homologous Superfamily
A, B	IPR001227	Acyl transferase domain superfamily	Homologous Superfamily
A, B	IPR018201	Beta-ketoacyl synthase, active site	Active Site
A, B	IPR014030	Beta-ketoacyl synthase-like, N-terminal	Domain
A, B	IPR001031	Thioesterase	Domain

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.