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P00456 (NIFH1_CLOPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Nitrogenase iron protein 1

EC=1.18.6.1
Alternative name(s):
Nitrogenase Fe protein 1
Nitrogenase component II
Nitrogenase reductase
Gene names
Name:nifH1
OrganismClostridium pasteurianum
Taxonomic identifier1501 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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-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.

Subunit structure

Homodimer.

Post-translational modification

The reversible ADP-ribosylation of Arg-97 inactivates the nitrogenase reductase and regulates nitrogenase activity By similarity. HAMAP-Rule MF_00533

Sequence similarities

Belongs to the NifH/BchL/ChlL family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 273273Nitrogenase iron protein 1 HAMAP-Rule MF_00533
PRO_0000139498

Regions

Nucleotide binding8 – 158ATP Potential

Sites

Metal binding941Iron-sulfur (4Fe-4S); shared with dimeric partner
Metal binding1291Iron-sulfur (4Fe-4S); shared with dimeric partner

Amino acid modifications

Modified residue971ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase HAMAP-Rule MF_00533

Secondary structure

.............................................. 273
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00456 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: A4EC06C5F58F08EC

FASTA27329,662
        10         20         30         40         50         60 
MRQVAIYGKG GIGKSTTTQN LTSGLHAMGK TIMVVGCDPK ADSTRLLLGG LAQKSVLDTL 

        70         80         90        100        110        120 
REEGEDVELD SILKEGYGGI RCVESGGPEP GVGCAGRGII TSINMLEQLG AYTDDLDYVF 

       130        140        150        160        170        180 
YDVLGDVVCG GFAMPIREGK AQEIYIVASG EMMALYAANN ISKGIQKYAK SGGVRLGGII 

       190        200        210        220        230        240 
CNSRKVANEY ELLDAFAKEL GSQLIHFVPR SPMVTKAEIN KQTVIEYDPT CEQAEEYREL 

       250        260        270 
ARKVDANELF VIPKPMTQER LEEILMQYGL MDL 

« Hide

References

[1]"The presence of five nifH-like sequences in Clostridium pasteurianum: sequence divergence and transcription properties."
Wang S.-Z., Chen J.-S., Johnson J.L.
Nucleic Acids Res. 16:439-454(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structural features of multiple nifH-like sequences and very biased codon usage in nitrogenase genes of Clostridium pasteurianum."
Chen K.C.K., Chen J.-S., Johnson J.L.
J. Bacteriol. 166:162-172(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The amino acid sequence of Clostridium pasteurianum iron protein, a component of nitrogenase. III. The NH2-terminal and COOH-terminal sequences, tryptic peptides of large cyanogen bromide peptides, and the complete sequence."
Tanaka M., Haniu M., Yasunobu K.T., Mortenson L.E.
J. Biol. Chem. 252:7093-7100(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[4]"Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum."
Schlessman J.L., Woo D., Joshua-Tor L., Howard J.B., Rees D.C.
J. Mol. Biol. 280:669-685(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS).
Strain: ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07472 Genomic DNA. Translation: CAA30359.1.
AY603957 Genomic DNA. Translation: AAT37644.1.
PIRNICLFP. A00533.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CP2X-ray1.93A/B1-269[»]
ProteinModelPortalP00456.
SMRP00456. Positions 1-269.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:NIFH1CP-MONOMER.

Family and domain databases

HAMAPMF_00533. NifH.
InterProIPR000392. Nitogenase_NifH/Reductase_ChlL.
IPR005977. Nitrogenase_Fe_NifH.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00142. Fer4_NifH. 1 hit.
[Graphical view]
PIRSFPIRSF000363. Nitrogenase_iron. 1 hit.
PRINTSPR00091. NITROGNASEII.
SUPFAMSSF52540. SSF52540. 1 hit.
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...

Other

EvolutionaryTraceP00456.

Entry information

Entry nameNIFH1_CLOPA
AccessionPrimary (citable) accession number: P00456
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 29, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families