Function and Biology Details
Reactions catalysed:
H(2) + menaquinone = menaquinol
H(2) + A = AH(2)
Biochemical function:
Biological process:
- not assigned
Cellular component:
Sequence domains:
- [NiFe]-hydrogenase, small subunit
- Nickel-dependent hydrogenase, large subunit, nickel binding site
- [NiFe]-hydrogenase, large subunit
- [NiFe]-hydrogenase, small subunit, C-terminal domain superfamily
- Cytochrome-c3 hydrogenase, C-terminal
- NADH:ubiquinone oxidoreductase-like, 20kDa subunit
- [NiFe]-hydrogenase, small subunit, N-terminal domain superfamily
- Nickel-dependent hydrogenase, large subunit
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123456 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Uptake hydrogenase large subunit
Molecule details ›
Chains: A, C
Length: 596 amino acids
Theoretical weight: 66.57 KDa
Source organism: Hydrogenovibrio marinus
UniProt:
Sequence domains: Nickel-dependent hydrogenase
Structure domains: Cytochrome-c3 Hydrogenase, chain B
Length: 596 amino acids
Theoretical weight: 66.57 KDa
Source organism: Hydrogenovibrio marinus
UniProt:
- Canonical:
F2Z6J6 (Residues: 1-596; Coverage: 98%)
Sequence domains: Nickel-dependent hydrogenase
Structure domains: Cytochrome-c3 Hydrogenase, chain B
hydrogenase (acceptor)
Molecule details ›
Chains: B, D
Length: 283 amino acids
Theoretical weight: 31.31 KDa
Source organism: Hydrogenovibrio marinus
UniProt:
Sequence domains:
Structure domains:
Length: 283 amino acids
Theoretical weight: 31.31 KDa
Source organism: Hydrogenovibrio marinus
UniProt:
- Canonical: F2Z6J5 (Residues: 41-323; Coverage: 78%)
Sequence domains:
Structure domains:
