| Primary Identifier | IPR003965 | Type | Domain |
| Short Name | Fatty_acid_synthase |
| description | The yeast fatty acid synthase (FAS) is a hexameric complex (alpha 6 beta 6) of two multifunctional proteins, alpha and beta []. The alpha subunit contains two of the seven enzymatic activities required for the synthesis of fatty acids, together with the site for attachment of the prosthetic group 4'-phosphopantetheine. The beta subunit contains the remaining five enzyme domains: acetyltransferase and malonyltransferase, s-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier protein]reductase, and 3-hydroxypalmitoyl-[acyl-carrier protein]dehydratase.The sequential order of the five FAS1-encoded enzyme domains is co-linear in Yarrowia lipolytica (Candida lipolytica) and Saccharomyces cerevisiae (Baker's yeast), which observation is consistent with evidence that the functional organisation of FAS genes is similar in related organisms but differs between unrelated species [].Sterigmatocystin (ST) and the aflatoxins (AFs) (related fungal secondary metabolites) are among the most toxic, mutagenic and carcinogenic natural products known []. In Emericella nidulans (Aspergillus nidulans), the ST biosynthetic pathway is believed to involve at least 15 enzymatic activities; some Aspergillus parasiticus, Aspergillus flavus and Aspergillus nomius strains contain additional activities that convert ST to AF. A 60kb region of the A. nidulans genome has been characterised and found to contain virtually all of the genes needed for ST biosynthesis []. The deduced polypeptide sequences of regions within this cluster share a high degree of similarity with enzymes that have activities predicted for ST/AF biosynthesis, including a polyketide synthase, a fatty acid synthase (alpha and beta subunits), five monooxygenases, four dehydrogenases, an esterase, an 0-methyltransferase, a reductase, an oxidase and a zinc cluster DNA binding protein []. |
