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Protein

Nitrogenase iron protein 1

Gene

nifH1

Organism
Clostridium pasteurianum
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate.

Cofactori

[4Fe-4S] clusterNote: Binds 1 [4Fe-4S] cluster per dimer.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi94 – 941Iron-sulfur (4Fe-4S); shared with dimeric partner
Metal bindingi129 – 1291Iron-sulfur (4Fe-4S); shared with dimeric partner

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 158ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Nitrogen fixation

Keywords - Ligandi

4Fe-4S, ATP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:NIFH1CP-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrogenase iron protein 1 (EC:1.18.6.1)
Alternative name(s):
Nitrogenase Fe protein 1
Nitrogenase component II
Nitrogenase reductase
Gene namesi
Name:nifH1
OrganismiClostridium pasteurianum
Taxonomic identifieri1501 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 273273Nitrogenase iron protein 1PRO_0000139498Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei97 – 971ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferaseBy similarity

Post-translational modificationi

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

Keywords - PTMi

ADP-ribosylation

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
273
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Helixi14 – 2613Combined sources
Turni27 – 293Combined sources
Beta strandi32 – 376Combined sources
Helixi45 – 484Combined sources
Helixi56 – 638Combined sources
Helixi64 – 663Combined sources
Helixi69 – 724Combined sources
Helixi77 – 793Combined sources
Beta strandi81 – 844Combined sources
Helixi95 – 10814Combined sources
Beta strandi117 – 1248Combined sources
Turni130 – 1334Combined sources
Helixi134 – 1374Combined sources
Beta strandi143 – 1486Combined sources
Helixi152 – 16817Combined sources
Beta strandi175 – 1828Combined sources
Beta strandi185 – 1873Combined sources
Helixi190 – 20011Combined sources
Beta strandi204 – 2085Combined sources
Helixi212 – 2198Combined sources
Helixi224 – 2274Combined sources
Helixi232 – 24615Combined sources
Helixi258 – 26811Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CP2X-ray1.93A/B1-269[»]
ProteinModelPortaliP00456.
SMRiP00456. Positions 1-269.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00456.

Family & Domainsi

Sequence similaritiesi

Belongs to the NifH/BchL/ChlL family.Curated

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00533. NifH.
InterProiIPR030655. NifH/chlL_CS.
IPR000392. Nitogenase_NifH/Reductase_ChlL.
IPR005977. Nitrogenase_Fe_NifH.
IPR027417. P-loop_NTPase.
[Graphical view]
PIRSFiPIRSF000363. Nitrogenase_iron. 1 hit.
PRINTSiPR00091. NITROGNASEII.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01287. nifH. 1 hit.
PROSITEiPS00746. NIFH_FRXC_1. 1 hit.
PS00692. NIFH_FRXC_2. 1 hit.
PS51026. NIFH_FRXC_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00456-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRQVAIYGKG GIGKSTTTQN LTSGLHAMGK TIMVVGCDPK ADSTRLLLGG
60 70 80 90 100
LAQKSVLDTL REEGEDVELD SILKEGYGGI RCVESGGPEP GVGCAGRGII
110 120 130 140 150
TSINMLEQLG AYTDDLDYVF YDVLGDVVCG GFAMPIREGK AQEIYIVASG
160 170 180 190 200
EMMALYAANN ISKGIQKYAK SGGVRLGGII CNSRKVANEY ELLDAFAKEL
210 220 230 240 250
GSQLIHFVPR SPMVTKAEIN KQTVIEYDPT CEQAEEYREL ARKVDANELF
260 270
VIPKPMTQER LEEILMQYGL MDL
Length:273
Mass (Da):29,662
Last modified:July 21, 1986 - v1
Checksum:iA4EC06C5F58F08EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07472 Genomic DNA. Translation: CAA30359.1.
AY603957 Genomic DNA. Translation: AAT37644.1.
PIRiA00533. NICLFP.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07472 Genomic DNA. Translation: CAA30359.1.
AY603957 Genomic DNA. Translation: AAT37644.1.
PIRiA00533. NICLFP.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CP2X-ray1.93A/B1-269[»]
ProteinModelPortaliP00456.
SMRiP00456. Positions 1-269.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:NIFH1CP-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP00456.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00533. NifH.
InterProiIPR030655. NifH/chlL_CS.
IPR000392. Nitogenase_NifH/Reductase_ChlL.
IPR005977. Nitrogenase_Fe_NifH.
IPR027417. P-loop_NTPase.
[Graphical view]
PIRSFiPIRSF000363. Nitrogenase_iron. 1 hit.
PRINTSiPR00091. NITROGNASEII.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01287. nifH. 1 hit.
PROSITEiPS00746. NIFH_FRXC_1. 1 hit.
PS00692. NIFH_FRXC_2. 1 hit.
PS51026. NIFH_FRXC_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiNIFH1_CLOPA
AccessioniPrimary (citable) accession number: P00456
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 14, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.