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:
- not assigned
Sequence domains:
- 4Fe-4S ferredoxin-type, iron-sulphur binding 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
- 4Fe-4S ferredoxin, iron-sulphur binding, conserved site
- 2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate
- Pyruvate Synthase Subunit PorD
9 more domains
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-275201 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Pyruvate synthase subunit PorA
Molecule details ›
Chains: A, B
Length: 403 amino acids
Theoretical weight: 44.35 KDa
Source organism: Methanosarcina acetivorans C2A
UniProt:
Sequence domains:
Length: 403 amino acids
Theoretical weight: 44.35 KDa
Source organism: Methanosarcina acetivorans C2A
UniProt:
- Canonical:
Q8TUN4 (Residues: 1-403; Coverage: 100%)
Sequence domains:
Thiamine pyrophosphate enzyme TPP-binding domain-containing protein
Molecule details ›
Chains: C, D
Length: 296 amino acids
Theoretical weight: 31.97 KDa
Source organism: Methanosarcina acetivorans C2A
UniProt:
Sequence domains: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain
Length: 296 amino acids
Theoretical weight: 31.97 KDa
Source organism: Methanosarcina acetivorans C2A
UniProt:
- Canonical: Q8TUN5 (Residues: 1-296; Coverage: 100%)
Sequence domains: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain
Pyruvate synthase subunit PorD
Pyruvate synthase subunit PorC
