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P33178 (NIFH_ANASL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Nitrogenase iron protein

EC=1.18.6.1
Alternative name(s):
Nitrogenase Fe protein
Nitrogenase component II
Nitrogenase reductase
Gene names
Name:nifH
OrganismAnabaena sp. (strain L31)
Taxonomic identifier29412 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Protein existenceInferred 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. HAMAP 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 MF_00533

Cofactor

Binds 1 4Fe-4S cluster per dimer.

Subunit structure

Homodimer.

Post-translational modification

The reversible ADP-ribosylation of Arg-104 inactivates the nitrogenase reductase and regulates nitrogenase activity By similarity. HAMAP MF_00533

Sequence similarities

Belongs to the NifH/BchL/ChlL family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 294294Nitrogenase iron protein HAMAP MF_00533
PRO_0000139480

Regions

Nucleotide binding13 – 208ATP Potential

Sites

Metal binding1011Iron-sulfur (4Fe-4S); shared with dimeric partner By similarity
Metal binding1351Iron-sulfur (4Fe-4S); shared with dimeric partner By similarity

Amino acid modifications

Modified residue1041ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase By similarity

Sequences

Sequence LengthMass (Da)Tools
P33178 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 86BC996AC22B32CC

FASTA29432,092
        10         20         30         40         50         60 
MTDENIRQIA FYGKGGIGKS TTSQNTLAAM AEMGQRIMIV GCDPKADSTR LMLHAKAQTT 

        70         80         90        100        110        120 
VLHLAAERGA VEDLELEEVM LTGFRGVKCV ESGGPEPGVG CAGRGIITAI NFLEENGAYQ 

       130        140        150        160        170        180 
DLDFVSYDVL GDVVCGGFAM PIREGKAQEI YIVTSGEMMA MYAANNIARG ILKYAHSGGV 

       190        200        210        220        230        240 
RLGGLICNSR KTDREAELIE NLAERLNTQM IHFVPRDNIV QHAELRRMTV NEYAPDSNQG 

       250        260        270        280        290 
QEYRALAKKI INNDKLTIPT PIEMDELEAL LIEYGILDDD TKHAEIIGKP ANAK 

« Hide

References

[1]"Cloning and nucleotide sequence of the gene for dinitrogenase reductase (nifH) from the heterocyst-forming cyanobacterium Anabaena sp. L31."
Murphy S.T., Jackman D.M., Mulligan M.E.
Biochim. Biophys. Acta 1171:337-340(1993) [PubMed: 8424961] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04499 Genomic DNA. Translation: AAA22014.1.

3D structure databases

ProteinModelPortalP33178.
SMRP33178. Positions 6-291.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16469.

Family and domain databases

HAMAPMF_00533. NifH.
[Tree]
InterProIPR000392. Nitogenase_NifH/Reductase_ChlL.
IPR005977. Nitrogenase_Fe_NifH.
[Graphical view]
PANTHERPTHR13696:SF32. PTHR13696:SF32. 1 hit.
PfamPF00142. Fer4_NifH. 1 hit.
[Graphical view]
PIRSFPIRSF000363. Nitrogenase_iron. 1 hit.
PRINTSPR00091. NITROGNASEII.
TIGRFAMsTIGR01287. NifH. 1 hit.
PROSITEPS00746. NIFH_FRXC_1. 1 hit.
PS00692. NIFH_FRXC_2. 1 hit.
PS51026. NIFH_FRXC_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNIFH_ANASL
AccessionPrimary (citable) accession number: P33178
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 19, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families