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
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
Assembly name:
Acetyl-CoA decarbonylase/synthase complex 2 (preferred)
PDBe Complex ID:
PDB-CPX-278831 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Acetyl-CoA decarbonylase/synthase complex subunit alpha 2
Molecule details ›
Chains: A, B
Length: 803 amino acids
Theoretical weight: 87.86 KDa
Source organism: Methanosarcina thermophila
UniProt:
Sequence domains:
Length: 803 amino acids
Theoretical weight: 87.86 KDa
Source organism: Methanosarcina thermophila
UniProt:
- Canonical:
Q9C4Z4 (Residues: 1-803; Coverage: 100%)
Sequence domains:
Acetyl-CoA decarbonylase/synthase complex subunit epsilon 2
Molecule details ›
Chains: C, D
Length: 170 amino acids
Theoretical weight: 18.59 KDa
Source organism: Methanosarcina thermophila
UniProt:
Sequence domains: CO dehydrogenase beta subunit/acetyl-CoA synthase epsilon subunit
Length: 170 amino acids
Theoretical weight: 18.59 KDa
Source organism: Methanosarcina thermophila
UniProt:
- Canonical: Q9C4Z3 (Residues: 1-170; Coverage: 100%)
Sequence domains: CO dehydrogenase beta subunit/acetyl-CoA synthase epsilon subunit
Acetyl-CoA decarbonylase/synthase complex subunit beta 2
