Function and Biology Details
Reaction catalysed:
H(2) + 2 ferricytochrome c3 = 2 H(+) + 2 ferrocytochrome c3
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- [NiFe]-hydrogenase, small subunit
- Nickel-dependent hydrogenase, large subunit, nickel binding site
- [NiFe]-hydrogenase, large subunit
- Nickel-dependent 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
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Periplasmic [NiFe] hydrogenase (preferred)
PDBe Complex ID:
PDB-CPX-146396 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Periplasmic [NiFe] hydrogenase small subunit
Molecule details ›
Chains: A, B
Length: 264 amino acids
Theoretical weight: 28.35 KDa
Source organism: Megalodesulfovibrio gigas
UniProt:
Sequence domains:
Structure domains:
Length: 264 amino acids
Theoretical weight: 28.35 KDa
Source organism: Megalodesulfovibrio gigas
UniProt:
- Canonical:
P12943 (Residues: 25-288; Coverage: 100%)
Sequence domains:
Structure domains:
Periplasmic [NiFe] hydrogenase large subunit
Molecule details ›
Chains: H, I
Length: 536 amino acids
Theoretical weight: 59.66 KDa
Source organism: Megalodesulfovibrio gigas
UniProt:
Sequence domains: Nickel-dependent hydrogenase
Structure domains: Cytochrome-c3 Hydrogenase, chain B
Length: 536 amino acids
Theoretical weight: 59.66 KDa
Source organism: Megalodesulfovibrio gigas
UniProt:
- Canonical: P12944 (Residues: 1-536; Coverage: 97%)
Sequence domains: Nickel-dependent hydrogenase
Structure domains: Cytochrome-c3 Hydrogenase, chain B
