Function and Biology Details
Reaction catalysed:
Methyl-CoM + CoB = CoM-S-S-CoB + methane
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Methyl-coenzyme M reductase, gamma subunit
- Methyl-coenzyme M reductase, alpha/beta subunit, C-terminal
- Methyl-coenzyme M reductase, ferredoxin-like fold
- Methyl-coenzyme M reductase, beta subunit
- Methyl-coenzyme M reductase, alpha subunit, N-terminal subdomain 2
- Methyl coenzyme M reductase, alpha subunit
- Methyl-coenzyme M reductase, gamma subunit superfamily
- Methyl-coenzyme M reductase, beta subunit, C-terminal
4 more domains
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
Assembly name:
Methyl-coenzyme M reductase (preferred)
PDBe Complex ID:
PDB-CPX-124723 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Methyl-coenzyme M reductase subunit alpha
Molecule details ›
Chains: A, D
Length: 552 amino acids
Theoretical weight: 61.18 KDa
Source organism: Methanotorris formicicus Mc-S-70
UniProt:
Sequence domains:
Length: 552 amino acids
Theoretical weight: 61.18 KDa
Source organism: Methanotorris formicicus Mc-S-70
UniProt:
- Canonical:
H1KXL5 (Residues: 1-552; Coverage: 100%)
Sequence domains:
- Methyl-coenzyme M reductase alpha subunit, N-terminal domain
- Methyl-coenzyme M reductase alpha subunit, C-terminal domain
Methyl-coenzyme M reductase subunit beta
Molecule details ›
Chains: B, E
Length: 444 amino acids
Theoretical weight: 47.54 KDa
Source organism: Methanotorris formicicus Mc-S-70
UniProt:
Sequence domains:
Length: 444 amino acids
Theoretical weight: 47.54 KDa
Source organism: Methanotorris formicicus Mc-S-70
UniProt:
- Canonical: H1KXL9 (Residues: 1-444; Coverage: 100%)
Sequence domains:
- Methyl-coenzyme M reductase beta subunit, N-terminal domain
- Methyl-coenzyme M reductase beta subunit, C-terminal domain
Methyl-coenzyme M reductase subunit gamma
