Function and Biology Details
Reaction catalysed:
Pyruvate + phosphate + O(2) = acetyl phosphate + CO(2) + H(2)O(2)
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
- Thiamin diphosphate-binding fold
- TPP-binding enzyme, conserved site
- Thiamine pyrophosphate enzyme, TPP-binding
- Pyruvate oxidase POXB-like, PP-binding domain
- Thiamine pyrophosphate enzyme, central domain
- DHS-like NAD/FAD-binding domain superfamily
- Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain
- Pyruvate oxidase/Pyruvate dehydrogenase [ubiquinone]-like
2 more domains
Structure analysis Details
Assembly composition:
homo tetramer (preferred)
Assembly name:
Pyruvate oxidase (preferred)
PDBe Complex ID:
PDB-CPX-153340 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate oxidase
Molecule details ›
Chains: A, B
Length: 603 amino acids
Theoretical weight: 66.25 KDa
Source organism: Lactiplantibacillus plantarum
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 603 amino acids
Theoretical weight: 66.25 KDa
Source organism: Lactiplantibacillus plantarum
Expression system: Escherichia coli
UniProt:
- Canonical:
P37063 (Residues: 1-603; 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
