Function and Biology Details
Reaction catalysed:
2 pyruvate = 2-acetolactate + CO(2)
Biochemical function:
Biological process:
Cellular component:
- not assigned
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
- Acetolactate synthase, large subunit, biosynthetic
- Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain
1 more domain
Structure analysis Details
Assembly composition:
homo tetramer (preferred)
Assembly name:
Acetolactate synthase, chloroplastic (preferred)
PDBe Complex ID:
PDB-CPX-148106 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetolactate synthase, chloroplastic
Molecule details ›
Chain: A
Length: 590 amino acids
Theoretical weight: 64.59 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 590 amino acids
Theoretical weight: 64.59 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P17597 (Residues: 86-667; Coverage: 87%)
Sequence domains:
- Thiamine pyrophosphate enzyme, N-terminal TPP binding domain
- Thiamine pyrophosphate enzyme, central domain
- Thiamine pyrophosphate enzyme, C-terminal TPP binding domain
