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
- Acetolactate synthase large subunit, TPP binding domain
- Thiamine pyrophosphate enzyme, central domain
- DHS-like NAD/FAD-binding domain superfamily
- Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain
- Thiamine pyrophosphate enzyme
1 more domain
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139528 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetolactate synthase catalytic subunit, mitochondrial
Molecule details ›
Chains: A, B
Length: 677 amino acids
Theoretical weight: 73.6 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 677 amino acids
Theoretical weight: 73.6 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P07342 (Residues: 58-687; Coverage: 92%)
Sequence domains:
- Thiamine pyrophosphate enzyme, N-terminal TPP binding domain
- Thiamine pyrophosphate enzyme, central domain
- Thiamine pyrophosphate enzyme, C-terminal TPP binding domain
