Function and Biology Details
Reaction catalysed:
H(2) + 2 ferricytochrome c3 = 2 H(+) + 2 ferrocytochrome c3
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 domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Periplasmic [NiFe] hydrogenase (preferred)
PDBe Complex ID:
PDB-CPX-148312 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Periplasmic [NiFe] hydrogenase small subunit
Molecule details ›
Chain: S
Length: 264 amino acids
Theoretical weight: 28.42 KDa
Source organism: Solidesulfovibrio fructosivorans
UniProt:
Sequence domains:
Structure domains:
Length: 264 amino acids
Theoretical weight: 28.42 KDa
Source organism: Solidesulfovibrio fructosivorans
UniProt:
- Canonical:
P18187 (Residues: 51-161, 163-314; Coverage: 99%)
Sequence domains:
Structure domains:
Periplasmic [NiFe] hydrogenase large subunit
Molecule details ›
Chain: L
Length: 564 amino acids
Theoretical weight: 61.67 KDa
Source organism: Solidesulfovibrio fructosivorans
UniProt:
Sequence domains: Nickel-dependent hydrogenase
Structure domains: Cytochrome-c3 Hydrogenase, chain B
Length: 564 amino acids
Theoretical weight: 61.67 KDa
Source organism: Solidesulfovibrio fructosivorans
UniProt:
- Canonical: P18188 (Residues: 1-564; Coverage: 100%)
Sequence domains: Nickel-dependent hydrogenase
Structure domains: Cytochrome-c3 Hydrogenase, chain B
