Function and Biology Details
Reaction catalysed:
[Biotin carboxyl-carrier protein]-N(6)-carboxybiotinyl-L-lysine + acetyl-CoA = [biotin carboxyl-carrier protein]-N(6)-biotinyl-L-lysine + malonyl-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Acetyl-CoA carboxylase, alpha subunit
- Acetyl-CoA carboxylase carboxyl transferase, beta subunit
- ClpP/crotonase-like domain superfamily
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
- Acetyl-coA carboxylase zinc finger domain
- Acetyl-coenzyme A carboxyltransferase, N-terminal
- Acetyl-coenzyme A carboxyltransferase, C-terminal
- Acetylglutamate kinase-like superfamily
Structure domain:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-532409 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
Molecule details ›
Chain: A
Length: 339 amino acids
Theoretical weight: 37.5 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains: Acetyl co-enzyme A carboxylase carboxyltransferase-like
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1
Length: 339 amino acids
Theoretical weight: 37.5 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical:
P0ABD5 (Residues: 1-319; Coverage: 100%)
Sequence domains: Acetyl co-enzyme A carboxylase carboxyltransferase-like
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
Molecule details ›
Chain: B
Length: 304 amino acids
Theoretical weight: 33.36 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1
Length: 304 amino acids
Theoretical weight: 33.36 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical: P0A9Q5 (Residues: 1-304; Coverage: 100%)
Sequence domains:
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1
