Function and Biology Details
Reaction catalysed:
H(2) + A = AH(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- [NiFe]-hydrogenase, small subunit
- Nickel-dependent hydrogenase, large subunit, nickel binding site
- Nickel-dependent hydrogenase, large subunit
- [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
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Periplasmic [NiFeSe] hydrogenase (preferred)
PDBe Complex ID:
PDB-CPX-146465 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Periplasmic [NiFeSe] hydrogenase small subunit
Molecule details ›
Chain: S
Length: 283 amino acids
Theoretical weight: 30.89 KDa
Source organism: Desulfomicrobium baculatum
UniProt:
Structure domains:
Length: 283 amino acids
Theoretical weight: 30.89 KDa
Source organism: Desulfomicrobium baculatum
UniProt:
- Canonical:
P13063 (Residues: 33-315; Coverage: 100%)
Structure domains:
Periplasmic [NiFeSe] hydrogenase large subunit
Molecule details ›
Chain: L
Length: 498 amino acids
Theoretical weight: 55.22 KDa
Source organism: Desulfomicrobium baculatum
UniProt:
Structure domains: Cytochrome-c3 Hydrogenase, chain B
Length: 498 amino acids
Theoretical weight: 55.22 KDa
Source organism: Desulfomicrobium baculatum
UniProt:
- Canonical: P13065 (Residues: 2-499; Coverage: 97%)
Structure domains: Cytochrome-c3 Hydrogenase, chain B
