|
|
||
|
|
|
|
|
UniProt functional annotation for P19097 | ||
|
|
|
|
|
|
||
| UniProt code: P19097. |
|
||
| Organism: | |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). |
| Taxonomy: | |
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. |
|
||
|
||
| Function: | |
Fatty 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. |
|
||
| Catalytic activity: | |
Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83139; EC=2.3.1.86; |
| Catalytic activity: | |
Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; EC=2.3.1.41; |
| Catalytic activity: | |
Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA- COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100; |
| Activity regulation: | |
Inhibited by cerulenin by covalent binding to active site of the ketoacyl synthase (KS) region. {ECO:0000269|PubMed:18725634}. |
| 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}. |
| Ptm: | |
4'-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. |
| Miscellaneous: | |
Present with 17000 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}. |
| Similarity: | |
Belongs to the thiolase-like superfamily. Fungal fatty acid synthetase subunit alpha family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.