Function and Biology Details
Reaction catalysed:
H(2) + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H(+)
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
- 4Fe-4S ferredoxin-type, iron-sulphur binding domain
- Iron hydrogenase, small subunit
- 2Fe-2S ferredoxin-type iron-sulfur binding domain
- Iron hydrogenase, small subunit superfamily
- Iron hydrogenase, large subunit, C-terminal
- 4Fe-4S ferredoxin, iron-sulphur binding, conserved site
- Iron hydrogenase
- Iron hydrogenase, subset
2 more domains
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Iron hydrogenase 1 (preferred)
PDBe Complex ID:
PDB-CPX-151361 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Iron hydrogenase 1
Molecule details ›
Chains: A, B
Length: 583 amino acids
Theoretical weight: 64.98 KDa
Source organism: Clostridium pasteurianum
Expression system: Escherichia coli
UniProt:
Length: 583 amino acids
Theoretical weight: 64.98 KDa
Source organism: Clostridium pasteurianum
Expression system: Escherichia coli
UniProt:
- Canonical:
P29166 (Residues: 1-574; Coverage: 100%)
- 2Fe-2S iron-sulfur cluster binding domain
- Iron hydrogenase 1-like, iron-sulfur centre-binding domain
- 4Fe-4S dicluster domain
- Iron only hydrogenase large subunit, C-terminal domain
- Iron hydrogenase small subunit
