CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.470 | Ribosomal Protein L22; Chain A |
|
3.90.470.20 | 4'-phosphopantetheinyl transferase domain |
Domain Context
CATH Clusters
| Superfamily | 4'-phosphopantetheinyl transferase domain |
| Functional Family | Fatty acid synthase alpha subunit FasA |
Enzyme Information
| 1.1.1.100 |
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.
|
| 2.3.1.41 |
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 2.3.1.179 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.
|
| 2.3.1.86 |
Fatty-acyl-CoA synthase system.
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 1.1.1.100 and EC 2.3.1.41, while the other subunit catalyzes the reactions of EC 2.3.1.38, EC 2.3.1.39, EC 4.2.1.59, EC 1.3.1.10 and EC 1.1.1.279. -!- The enzyme differs from the animal enzyme (EC 2.3.1.85) 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)
| P19097 |
FAS2_YEAST
Saccharomyces cerevisiae S288C
Fatty acid synthase subunit alpha
|
PDB Structure
| PDB | 2WAS |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Multimeric Options for the Auto-Activation of the Saccharomyces Cerevisiae Fas Type I Megasynthase.
Structure
|
