P54800 · NIFH2_METBA
- ProteinNitrogenase iron protein 2
- GenenifH2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids273 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.
Catalytic activity
- 16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H+ + H2 + 2 NH4+ + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 phosphate
16 CHEBI:30616 + 16 CHEBI:15377 + CHEBI:17997 + 8 RHEA-COMP:10001 = 16 CHEBI:456216 + 6 CHEBI:15378 + CHEBI:18276 + 2 CHEBI:28938 + 8 RHEA-COMP:10000 + 16 CHEBI:43474
Cofactor
Note: Binds 1 [4Fe-4S] cluster per dimer.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | ATP binding | |
Molecular Function | carbonyl sulfide nitrogenase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nitrogenase activity | |
Biological Process | nitrogen fixation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Nitrogenase component 2 (also called the iron protein) functions as dinitrogenase reductase as it reduces nitrogenase component 1.
Names & Taxonomy
Protein names
- Recommended nameNitrogenase iron protein 2
- EC number
- Alternative names
Gene names
- Community suggested namesNitrogenase iron protein; Nitrogenase component 2.
Organism names
- Organism
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanosarcinales > Methanosarcinaceae > Methanosarcina
Accessions
- Primary accessionP54800
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000139536 | 1-273 | Nitrogenase iron protein 2 | |||
Sequence: MRQIAIYGKGGIGKSTTTQNLTASLSTMGNKIMLVGCDPKADSTRMLLGGLNQKTVLDTLRSEGDEGVDLDVVMQRGFGDIKCVESGGPEPGVGCAGRGIITSIGLLENLGAYTDDLDYVFYDVLGDVVCGGFAMPIREGKAKEIYIVASGELMAIYAANNICKGLAKFAKGGARLGGIICNSRNVDGERELLDAFAKKLGSHLIHFIPRDNIVQRAEINRKTVIDFDPESNQAKEYLTLAHNVQNNDKLVVPTPLPMEELEAMMVEFGIVDL | ||||||
Modified residue | 98 | ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase | ||||
Sequence: R |
Post-translational modification
The reversible ADP-ribosylation of Arg-98 inactivates the nitrogenase reductase and regulates nitrogenase activity.
Keywords
- PTM
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length273
- Mass (Da)29,346
- Last updated1996-10-01 v1
- Checksum147F73F02DD6B7AA
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 11-13 | in Ref. 1 | ||||
Sequence: GIG → WELE |