P26254 (NIFH_TRITH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 83.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Nitrogenase iron protein EC=1.18.6.1 Alternative name(s): Nitrogenase Fe protein Nitrogenase component II Nitrogenase reductase | ||
| Gene names |
| ||
| Organism | Trichodesmium thiebautii | ||
| Taxonomic identifier | 1208 [NCBI] | ||
| Taxonomic lineage | Bacteria › Cyanobacteria › Oscillatoriophycideae › Oscillatoriales › Trichodesmium![]() |
Protein attributes
| Sequence length | 294 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| 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 By similarity. HAMAP-Rule MF_00533 |
| Catalytic activity | 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate. HAMAP-Rule MF_00533 |
| Cofactor | Binds 1 4Fe-4S cluster per dimer By similarity. HAMAP-Rule MF_00533 |
| Subunit structure | Homodimer By similarity. HAMAP-Rule MF_00533 |
| Post-translational modification | The reversible ADP-ribosylation of Arg-100 inactivates the nitrogenase reductase and regulates nitrogenase activity By similarity. HAMAP-Rule MF_00533 |
| Sequence similarities | Belongs to the NifH/BchL/ChlL family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nitrogen fixation |
| Ligand | 4Fe-4S ATP-binding Iron Iron-sulfur Metal-binding Nucleotide-binding |
| Molecular function | Oxidoreductase |
| PTM | ADP-ribosylation |
| Gene Ontology (GO) | |
| Biological_process | nitrogen fixation Inferred from electronic annotation. Source: HAMAP |
| Cellular_component | molybdenum-iron nitrogenase complex Inferred from electronic annotation. Source: InterPro |
| Molecular_function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW ATP bindingInferred from electronic annotation. Source: HAMAP carbonyl sulfide nitrogenase activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW nitrogenase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 294 | 294 | Nitrogenase iron protein HAMAP-Rule MF_00533 | PRO_0000139534 | |||||
Regions | |||||||||
| Nucleotide binding | 8 – 15 | 8 | ATP Potential | ||||||
Sites | |||||||||
| Metal binding | 97 | 1 | Iron-sulfur (4Fe-4S); shared with dimeric partner By similarity | ||||||
| Metal binding | 131 | 1 | Iron-sulfur (4Fe-4S); shared with dimeric partner By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 100 | 1 | ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 50 | 1 | D → N in AAA27368. Ref.2 | ||||||
Sequences
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References
| [1] | "Isolation of nifH and part of nifD by modified capture PCR from a natural population of the marine cyanobacterium Trichodesmium thiebautii." Sroga G.E., Landegren U., Bergman B., Lagerstrom-Fermer M. Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Use of degenerate oligonucleotides for amplification of the nifH gene from the marine cyanobacterium Trichodesmium thiebautii." Zehr J.P., McReynolds L.A. Appl. Environ. Microbiol. 55:2522-2526(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-156. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U23507 Genomic DNA. Translation: AAA77022.1. M29709 Genomic DNA. Translation: AAA27368.1. |
| PIR | A43635. |
3D structure databases | |
| ProteinModelPortal | P26254. |
| SMR | P26254. Positions 1-273. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| HAMAP | MF_00533. NifH. |
| InterPro | IPR000392. Nitogenase_NifH/Reductase_ChlL. IPR005977. Nitrogenase_Fe_NifH. IPR027417. P-loop_NTPase. [Graphical view] |
| Pfam | PF00142. Fer4_NifH. 1 hit. [Graphical view] |
| PIRSF | PIRSF000363. Nitrogenase_iron. 1 hit. |
| PRINTS | PR00091. NITROGNASEII. |
| SUPFAM | SSF52540. SSF52540. 1 hit. |
| TIGRFAMs | TIGR01287. nifH. 1 hit. |
| PROSITE | PS00746. NIFH_FRXC_1. 1 hit. PS00692. NIFH_FRXC_2. 1 hit. PS51026. NIFH_FRXC_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NIFH_TRITH | ||||||||
| Accession | Primary (citable) accession number: P26254 Secondary accession number(s): Q56373 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
