8B72

Crystal structure of 3-hydroxydecanoyl-acyl carrier protein dehydratase (FabA) from Pseudomonas aeruginosa in complex with Z30857828

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF07977	e8b72A1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF07977	ECOD (1.6)
B	PF07977	e8b72B1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF07977	ECOD (1.6)
C	PF07977	e8b72C1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF07977	ECOD (1.6)
D	PF07977	e8b72D1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF07977	ECOD (1.6)
E	PF07977	e8b72E1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF07977	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E	PF07977	FabA-like domain (FabA)	FabA-like domain	This enzyme domain has a HotDog fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E	3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase	(3R)-3-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity isomerase activity intramolecular oxidoreductase activity, transposing C=C bonds intramolecular oxidoreductase activity trans-2-decenoyl-acyl-carrier-protein isomerase activity (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity	unsaturated fatty acid metabolic process oxoacid metabolic process cellular biosynthetic process lipid biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process cellular metabolic process unsaturated fatty acid metabolic process oxoacid metabolic process cellular biosynthetic process lipid biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process cellular metabolic process carboxylic acid metabolic process primary metabolic process fatty acid biosynthetic process unsaturated fatty acid biosynthetic process biosynthetic process cellular lipid metabolic process metabolic process cellular process monocarboxylic acid metabolic process lipid metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E	IPR010083	Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabA	Family
A, B, C, D, E	IPR013114	Beta-hydroxydecanoyl thiol ester dehydrase, FabA/FabZ	Family
A, B, C, D, E	IPR029069	HotDog domain superfamily	Homologous Superfamily

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.