Function and Biology Details
Reaction catalysed:
Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- 4Fe-4S ferredoxin, iron-sulphur binding, conserved site
- 4Fe-4S ferredoxin-type, iron-sulphur binding domain
- Pyruvate-flavodoxin oxidoreductase, EKR domain
- Pyruvate-flavodoxin oxidoreductase, central domain
- Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II
- Pyruvate flavodoxin/ferredoxin oxidoreductase, pyrimidine binding domain
- Thiamin diphosphate-binding fold
- Pyruvate-flavodoxin oxidoreductase
4 more domains
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Pyruvate:ferredoxin oxidoreductase (preferred)
PDBe Complex ID:
PDB-CPX-161130 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate:ferredoxin oxidoreductase
Molecule details ›
Chains: A, B
Length: 1231 amino acids
Theoretical weight: 133.7 KDa
Source organism: Desulfocurvibacter africanus
UniProt:
Sequence domains:
Length: 1231 amino acids
Theoretical weight: 133.7 KDa
Source organism: Desulfocurvibacter africanus
UniProt:
- Canonical:
P94692 (Residues: 2-1232; Coverage: 100%)
Sequence domains:
- Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg
- Pyruvate:ferredoxin oxidoreductase core domain II
- Pyruvate ferredoxin/flavodoxin oxidoreductase
- Domain of unknown function
- 4Fe-4S binding domain
- Pyruvate-ferredoxin oxidoreductase, insertion domain
- Thiamine pyrophosphate enzyme, C-terminal TPP binding domain
