Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabA (IPR010083)

Short name: FabA

Overlapping homologous superfamilies

Family relationships



This enzyme, FabA, shows overlapping substrate specificity with FabZ with regard to chain length in fatty acid biosynthesis. It is commonly designated 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase as if it were specific for that chain length, but its specificity is broader; it is active even in the initiation of fatty acid biosynthesis. This enzyme can also isomerise trans-2-decenoyl-ACP to cis-3-decenoyl-ACP to bypass reduction by FabI and instead allow biosynthesis of unsaturated fatty acids. FabA cannot elongate unsaturated fatty acids.

The FabA structure is a homodimer with two independent active sites located at the dimer interface. Each active site is tunnel-shaped and completely inaccessible to solvent. No metal ions or cofactors are required for ligand binding or catalysis [PMID: 8805534].

GO terms

Biological Process

GO:0006633 fatty acid biosynthetic process

Molecular Function

GO:0008693 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity

Cellular Component

GO:0005737 cytoplasm

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.