Function and Biology Details
Reactions catalysed:
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]
Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO(2) + 2n NADP(+)
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH
Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein]
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein]
Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-carrier-protein] + oleate
A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H(2)O
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero octadecamer (preferred)
Assembly name:
Fatty-acyl-CoA synthase and unmapped proteins (preferred)
PDBe Complex ID:
PDB-CPX-139406 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Fatty acid synthase subunit alpha
Molecule details ›
Chains: A, D, G
Length: 1688 amino acids
Theoretical weight: 171.12 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
Sequence domains:
Length: 1688 amino acids
Theoretical weight: 171.12 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
- Canonical:
P19097 (Residues: 671-1744; Coverage: 57%)
Sequence domains:
Fatty acid synthase subunit beta
Molecule details ›
Chains: B, E, H
Length: 2006 amino acids
Theoretical weight: 191.51 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
Sequence domains:
Length: 2006 amino acids
Theoretical weight: 191.51 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
- Canonical: P07149 (Residues: 1-1941; Coverage: 92%)
Sequence domains:
- N-terminal domain in fatty acid synthase subunit beta
- Starter unit:ACP transacylase in aflatoxin biosynthesis
- Fatty acid synthase subunit beta/Fas1-like, helical
- Fatty acid synthase meander beta sheet domain
- N-terminal half of MaoC dehydratase
- MaoC like domain
- Acyl transferase domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ALS BEAMLINE 8.2.2, APS BEAMLINE 24-ID-C, NSLS BEAMLINE X25, CHESS BEAMLINE A1
Spacegroup:
P43212
