Function and Biology Details
Reaction catalysed:
ATP + a long-chain fatty acid + an [acyl-carrier-protein] = AMP + diphosphate + a long-chain acyl-[acyl-carrier-protein]
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106482 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Long-chain-fatty-acid--AMP ligase FadD32
Molecule details ›
Chain: A
Length: 630 amino acids
Theoretical weight: 68.31 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli
UniProt:
Sequence domains: AMP-binding enzyme
Length: 630 amino acids
Theoretical weight: 68.31 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli
UniProt:
- Canonical:
A0R618 (Residues: 1-630; Coverage: 100%)
Sequence domains: AMP-binding enzyme
Ubiquitin-like protein SMT3
Molecule details ›
Chain: B
Length: 74 amino acids
Theoretical weight: 8.7 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 74 amino acids
Theoretical weight: 8.7 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
- Canonical: Q12306 (Residues: 21-94; Coverage: 73%)
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
