Function and Biology Details
Reaction catalysed:
CO + H(2)O + 2 oxidized ferredoxin = CO(2) + 2 reduced ferredoxin + 2 H(+)
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Acetyl-CoA decarbonylase/synthase complex subunit epsilon
- Hydroxylamine reductase/Ni-containing CO dehydrogenase
- Acetyl-CoA decarbonylase/synthase complex subunit alpha
- 4Fe-4S ferredoxin-type, iron-sulphur binding domain
- Prismane-like, alpha/beta-sandwich
- DHS-like NAD/FAD-binding domain superfamily
- 4Fe-4S ferredoxin, iron-sulphur binding, conserved site
- Prismane-like superfamily
Structure analysis Details
Assemblies composition:
Assembly name:
Acetyl-CoA decarbonylase/synthase complex 1 (preferred)
PDBe Complex ID:
PDB-CPX-175181 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Acetyl-CoA decarbonylase/synthase complex subunit alpha 1
Molecule details ›
Chain: A
Length: 807 amino acids
Theoretical weight: 88.66 KDa
Source organism: Methanosarcina barkeri
UniProt:
Sequence domains:
Structure domains: Rossmann fold
Length: 807 amino acids
Theoretical weight: 88.66 KDa
Source organism: Methanosarcina barkeri
UniProt:
- Canonical:
Q46G04 (Residues: 1-741, 742-806; Coverage: 100%)
Sequence domains:
Structure domains: Rossmann fold
Acetyl-CoA decarbonylase/synthase complex subunit epsilon 1
Molecule details ›
Chain: G
Length: 170 amino acids
Theoretical weight: 18.47 KDa
Source organism: Methanosarcina barkeri
UniProt:
Sequence domains: CO dehydrogenase beta subunit/acetyl-CoA synthase epsilon subunit
Structure domains: TPP-binding domain
Length: 170 amino acids
Theoretical weight: 18.47 KDa
Source organism: Methanosarcina barkeri
UniProt:
- Canonical: Q46G05 (Residues: 1-170; Coverage: 100%)
Sequence domains: CO dehydrogenase beta subunit/acetyl-CoA synthase epsilon subunit
Structure domains: TPP-binding domain
