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
- [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-142263 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Hydrogenase-1 large chain
Molecule details ›
Chains: L, M
Length: 582 amino acids
Theoretical weight: 64.75 KDa
Source organism: Escherichia coli str. K-12 substr. MC4100
UniProt:
Sequence domains: Nickel-dependent hydrogenase
Structure domains: Cytochrome-c3 Hydrogenase, chain B
Length: 582 amino acids
Theoretical weight: 64.75 KDa
Source organism: Escherichia coli str. K-12 substr. MC4100
UniProt:
- Canonical:
P0ACD8 (Residues: 1-582; Coverage: 98%)
Sequence domains: Nickel-dependent hydrogenase
Structure domains: Cytochrome-c3 Hydrogenase, chain B
Hydrogenase-1 small chain
Molecule details ›
Chains: S, T
Length: 278 amino acids
Theoretical weight: 30.91 KDa
Source organism: Escherichia coli str. K-12 substr. MC4100
UniProt:
Sequence domains:
Structure domains:
Length: 278 amino acids
Theoretical weight: 30.91 KDa
Source organism: Escherichia coli str. K-12 substr. MC4100
UniProt:
- Canonical: P69739 (Residues: 46-311; Coverage: 81%)
Sequence domains:
Structure domains:
