CATH Classification

Domain Context

CATH Clusters

Superfamily NAD(P)-binding Rossmann-like Domain
Functional Family Fatty acid synthase subunit alpha

Enzyme Information
3-oxoacyl-[acyl-carrier-protein] reductase.
based on mapping to UniProt P19097
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl- carrier-protein] + NADPH.
-!- Exhibits a marked preference for [acyl-carrier-protein] derivatives over CoA derivatives as substrates.
Beta-ketoacyl-[acyl-carrier-protein] synthase I.
based on mapping to UniProt P19097
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
-!- Responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. -!- Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. -!- Can use fatty acyl thioesters of ACP (C(2) to C(16)) as substrates, as well as fatty acyl thioesters of Co-A (C(4) to C(16)). -!- The substrate specificity is very similar to that of EC with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C(16)-Delta(9)) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature.
Fatty-acyl-CoA synthase.
based on mapping to UniProt P19097
Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO(2) + 2n NADP(+).
-!- The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi- functional protein complex composed of two subunits. -!- One subunit catalyzes the reactions EC and EC, while the other subunit catalyzes the reactions of EC, EC, EC, EC and EC -!- The enzyme differs from the animal enzyme (EC in that the enoyl reductase domain requires FMN as a cofactor, and the ultimate product is an acyl-CoA (usually palmitoyl-CoA) instead of a free fatty acid.

UniProtKB Entries (1)

Saccharomyces cerevisiae S288C
Fatty acid synthase subunit beta

PDB Structure

External Links
Primary Citation
Structural Basis for Substrate Delivery by Acyl Carrier Protein in the Yeast Fatty Acid Synthase
Leibundgut, M., Jenni, S., Frick, C., Ban, N.