Function and Biology Details
Reactions catalysed:
CO + H(2)O + 2 oxidized ferredoxin = CO(2) + 2 reduced ferredoxin + 2 H(+)
Acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- CO dehydrogenase/acetyl-CoA synthase complex beta subunit
- Prismane-like, alpha/beta-sandwich
- Ni-containing CO dehydrogenase
- Hydroxylamine reductase/Ni-containing CO dehydrogenase
- Prismane-like superfamily
- CO dehydrogenase/acetyl-CoA synthase complex beta subunit , C-terminal
- Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase, domain 3 superfamily
- Carbon monoxide dehydrogenase subunit alpha ,N-terminal
1 more domain
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151140 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta
Molecule details ›
Chains: A, B, C, D
Length: 674 amino acids
Theoretical weight: 73.01 KDa
Source organism: Moorella thermoacetica
UniProt:
Length: 674 amino acids
Theoretical weight: 73.01 KDa
Source organism: Moorella thermoacetica
UniProt:
- Canonical:
P27989 (Residues: 1-674; Coverage: 100%)
Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha
Molecule details ›
Chains: M, N, O, P
Length: 729 amino acids
Theoretical weight: 81.82 KDa
Source organism: Moorella thermoacetica
UniProt:
Length: 729 amino acids
Theoretical weight: 81.82 KDa
Source organism: Moorella thermoacetica
UniProt:
- Canonical: P27988 (Residues: 1-729; Coverage: 100%)
