Function and Biology Details
Reactions catalysed:
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH
An acyl-[acyl-carrier protein] + NADP(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein]
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein]
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 = a long-chain fatty acid + (n+1) CoA + n CO(2) + 2n NADP(+)
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:
Sequence domains:
- Alpha/Beta hydrolase fold
- ACP-like superfamily
- Phosphopantetheine binding ACP domain
- NAD(P)-binding domain superfamily
- S-adenosyl-L-methionine-dependent methyltransferase superfamily
- Polyketide synthase, dehydratase domain
- Acyl transferase
- Polyketide synthase, beta-ketoacyl synthase domain
17 more domains
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Fatty acid synthase (preferred)
PDBe Complex ID:
PDB-CPX-107795 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fatty acid synthase
Molecule details ›
Chains: A, B
Length: 2512 amino acids
Theoretical weight: 272.53 KDa
Source organism: Sus scrofa
UniProt:
Sequence domains:
Length: 2512 amino acids
Theoretical weight: 272.53 KDa
Source organism: Sus scrofa
UniProt:
- Canonical:
A5YV76 (Residues: 1-2512; Coverage: 100%)
Sequence domains:
- Beta-ketoacyl synthase, N-terminal domain
- Beta-ketoacyl synthase, C-terminal domain
- Ketoacyl-synthetase C-terminal extension
- Acyl transferase domain
- Polyketide synthase dehydratase domain
- Methyltransferase domain
- Fatty acid synthase, pseudo-KR domain
- Zinc-binding dehydrogenase
- KR domain
- Phosphopantetheine attachment site
- Thioesterase domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SLS BEAMLINE X06SA
Spacegroup:
P21
