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
- Acetolactate synthase, large subunit, biosynthetic
2 more domains
Structure analysis Details
Assembly composition:
homo tetramer (preferred)
Assembly name:
Acetolactate synthase (preferred)
PDBe Complex ID:
PDB-CPX-103401 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetolactate synthase
Molecule details ›
Chain: A
Length: 682 amino acids
Theoretical weight: 74.32 KDa
Source organism: Candida albicans SC5314
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 682 amino acids
Theoretical weight: 74.32 KDa
Source organism: Candida albicans SC5314
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
A0A1D8PJF9 (Residues: 47-683; Coverage: 93%)
Sequence domains:
- Thiamine pyrophosphate enzyme, N-terminal TPP binding domain
- Thiamine pyrophosphate enzyme, central domain
- Thiamine pyrophosphate enzyme, C-terminal TPP binding domain
Ligands and Environments
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup:
P6222
Expression system: Escherichia coli BL21(DE3)
