Function and Biology Details
Reaction catalysed:
2 pyruvate = 2-acetolactate + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Thiamin diphosphate-binding fold
- TPP-binding enzyme, conserved site
- Thiamine pyrophosphate enzyme, TPP-binding
- Thiamine pyrophosphate enzyme, central domain
- DHS-like NAD/FAD-binding domain superfamily
- Acetolactate synthase, catabolic
- Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain
- Thiamine pyrophosphate enzyme
Structure analysis Details
Assembly composition:
homo tetramer (preferred)
Assembly name:
Acetolactate synthase, catabolic (preferred)
PDBe Complex ID:
PDB-CPX-151056 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetolactate synthase, catabolic
Molecule details ›
Chains: A, B, C, D
Length: 566 amino acids
Theoretical weight: 61.36 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 566 amino acids
Theoretical weight: 61.36 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P27696 (Residues: 1-559; Coverage: 100%)
Sequence domains:
- Thiamine pyrophosphate enzyme, N-terminal TPP binding domain
- Thiamine pyrophosphate enzyme, central domain
- Thiamine pyrophosphate enzyme, C-terminal TPP binding domain
