Function and Biology Details
Reaction catalysed:
Methane + NAD(P)H + O(2) = methanol + NAD(P)(+) + H(2)O
Biochemical function:
Biological process:
- not assigned
Cellular component:
Sequence domains:
- Ammonia monooxygenase/particulate methane monooxygenase, subunit A
- Ammonia monooxygenase/particulate methane monooxygenase, subunit C
- Ammonia monooxygenase/particulate methane monooxygenase, subunit B
- Ammonia monooxygenase/particulate methane monooxygenase, subunit C domain superfamily
- Ammonia/particulate methane monooxygenase, subunit A superfamily
- Ammonia/methane monooxygenase, subunit B, C-terminal
- Ammonia/methane monooxygenase, subunit B, hairpin domain superfamily
- Ammonia/methane monooxygenase, subunitB, N-terminal
Structure analysis Details
Assembly composition:
hetero nonamer (preferred)
Assembly name:
Particulate methane monooxygenase, (preferred)
PDBe Complex ID:
PDB-CPX-124447 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Particulate methane monooxygenase, B subunit
Molecule details ›
Chains: A, D, E
Length: 414 amino acids
Theoretical weight: 45.6 KDa
Source organism: Methylotuvimicrobium alcaliphilum 20Z
UniProt:
Sequence domains: Monooxygenase subunit B protein
Length: 414 amino acids
Theoretical weight: 45.6 KDa
Source organism: Methylotuvimicrobium alcaliphilum 20Z
UniProt:
- Canonical:
G4SZ64 (Residues: 1-414; Coverage: 100%)
Sequence domains: Monooxygenase subunit B protein
Particulate methane monooxygenase, A subunit
Molecule details ›
Chains: B, F, G
Length: 247 amino acids
Theoretical weight: 28.28 KDa
Source organism: Methylotuvimicrobium alcaliphilum 20Z
UniProt:
Sequence domains: Ammonia monooxygenase
Length: 247 amino acids
Theoretical weight: 28.28 KDa
Source organism: Methylotuvimicrobium alcaliphilum 20Z
UniProt:
- Canonical: G4SZ63 (Residues: 1-247; Coverage: 100%)
Sequence domains: Ammonia monooxygenase
Particulate methane monooxygenase, C subunit
