Function and Biology Details
Reaction catalysed:
2 glyoxylate = tartronate semialdehyde + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Thiamin diphosphate-binding fold
- Thiamine pyrophosphate enzyme, TPP-binding
- Glyoxylate carboligase, 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
- Glyoxylate carboligase
1 more domain
Structure analysis Details
Assembly composition:
homo tetramer (preferred)
Assembly name:
Glyoxylate carboligase (preferred)
PDBe Complex ID:
PDB-CPX-142481 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glyoxylate carboligase
Molecule details ›
Chains: A, B, C, D, E, F
Length: 616 amino acids
Theoretical weight: 68.44 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 616 amino acids
Theoretical weight: 68.44 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical:
P0AEP7 (Residues: 1-593; 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
