LMPD Database

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LMP007293

UniProt Annotations

Entry Information
Gene Nametrifunctional fatty acid synthase subunit FAS2
Protein EntryFAS2_YEAST
UniProt IDP19097
SpeciesYeast (S288c)
Comments
Comment typeDescription
Catalytic Activity(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
Catalytic ActivityAcetyl-CoA + n malonyl-CoA + 2n NADPH = long- chain-acyl-CoA + n CoA + n CO(2) + 2n NADP(+).
Catalytic ActivityAcyl-[acyl-carrier-protein] + malonyl-[acyl- carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
Enzyme RegulationInhibited by cerulenin by covalent binding to active site of the ketoacyl synthase (KS) region
Enzyme RegulationInhibited by cerulenin by covalent binding to active site of the ketoacyl synthase (KS) region. {ECO:0000269|PubMed:18725634}.
FunctionFatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3- oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl- carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.
InteractionP07149:FAS1; NbExp=3; IntAct=EBI-6806, EBI-6795;
MiscellaneousPresent with 17000 molecules/cell in log phase SD medium
MiscellaneousPresent with 17000 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.
Ptm4'-phosphopantetheine is transferred from CoA to a specific serine of the Acyl carrier domain by the C-terminal PPT domain. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
SimilarityBelongs to the fungal fatty acid synthetase subunit alpha family
SimilarityBelongs to the fungal fatty acid synthetase subunit alpha family. {ECO:0000305}.
SimilarityContains 1 acyl carrier domain
SimilarityContains 1 acyl carrier domain. {ECO:0000305}.
Subunit[Alpha(6)beta(6)] hexamers of two multifunctional subunits (alpha and beta). {ECO:0000269|PubMed:17431182, ECO:0000269|PubMed:17448991, ECO:0000269|PubMed:18725634, ECO:0000269|PubMed:19679086}.