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P00459 (NIFH1_AZOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismAzotobacter vinelandii
Taxonomic identifier354 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 (component 2) and a component 1 which is either a molybdenum-iron protein, a vanadium-iron, or an iron-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-101 inactivates the nitrogenase reductase and regulates nitrogenase activity By similarity. HAMAP-Rule MF_00533

Miscellaneous

This subunit is associated with the molybdenum-iron nitrogenase component 2.

Sequence similarities

Belongs to the NifH/BchL/ChlL family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 290289Nitrogenase iron protein 1 HAMAP-Rule MF_00533
PRO_0000139490

Regions

Nucleotide binding10 – 178ATP HAMAP-Rule MF_00533

Sites

Metal binding981Iron-sulfur (4Fe-4S); shared with dimeric partner
Metal binding1331Iron-sulfur (4Fe-4S); shared with dimeric partner

Amino acid modifications

Modified residue1011ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase By similarity

Experimental info

Mutagenesis161K → Q or P: Loss of nitrogen fixation. Ref.5
Sequence conflict1451A → P in AAA22142. Ref.2

Secondary structure

............................................................... 290
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00459 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: C36EFC0D9A27F64D

FASTA29031,516
        10         20         30         40         50         60 
MAMRQCAIYG KGGIGKSTTT QNLVAALAEM GKKVMIVGCD PKADSTRLIL HSKAQNTIME 

        70         80         90        100        110        120 
MAAEAGTVED LELEDVLKAG YGGVKCVESG GPEPGVGCAG RGVITAINFL EEEGAYEDDL 

       130        140        150        160        170        180 
DFVFYDVLGD VVCGGFAMPI RENKAQEIYI VCSGEMMAMY AANNISKGIV KYANSGSVRL 

       190        200        210        220        230        240 
GGLICNSRNT DREDELIIAL ANKLGTQMIH FVPRDNVVQR AEIRRMTVIE YDPKAKQADE 

       250        260        270        280        290 
YRALARKVVD NKLLVIPNPI TMDELEELLM EFGIMEVEDE SIVGKTAEEV 

« Hide

References

[1]"Physical and genetic map of the major nif gene cluster from Azotobacter vinelandii."
Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., Wilson M.S., Cash V.L., Beynon J., Newton W.E., Dean D.R.
J. Bacteriol. 171:1017-1027(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete nucleotide sequence of the Azotobacter vinelandii nitrogenase structural gene cluster."
Brigle K.E., Newton W.E., Dean D.R.
Gene 37:37-44(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The amino acid sequence of the nitrogenase iron protein from Azotobacter vinelandii."
Hausinger R.P., Howard J.B.
J. Biol. Chem. 257:2483-2490(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-290.
[4]"Sequence of a 1.4 kb Eco RI fragment of Azotobacter vinelandii nif DNA."
Hiratsuka K., Roy K.L.
Nucleic Acids Res. 16:1207-1207(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 271-290.
Strain: ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW.
[5]"Mapping the site(s) of MgATP and MgADP interaction with the nitrogenase of Azotobacter vinelandii. Lysine 15 of the iron protein plays a major role in MgATP interaction."
Seefeldt L.C., Morgan T.V., Dean D.R., Mortenson L.E.
J. Biol. Chem. 267:6680-6688(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-16.
[6]"Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii."
Georgiadis M.M., Komiya H., Chakrabarti P., Woo D., Kornuc J.J., Rees D.C.
Science 257:1653-1659(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[7]"Structure of ADP x [AlF(4)](-)-stabilized nitrogenase complex and its implications for signal transduction."
Schindelin H., Kisker C., Schlessman J.L., Howard J.B., Rees D.C.
Nature 387:370-376(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[8]"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 (2.2 ANGSTROMS).
[9]"Insights into nucleotide signal transduction in nitrogenase: structure of an iron protein with MgADP bound."
Jang S.B., Seefeldt L.C., Peters J.W.
Biochemistry 39:14745-14752(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
[10]"Crystal structure of the all-ferrous [4Fe-4S]0 form of the nitrogenase iron protein from Azotobacter vinelandii."
Strop P., Takahara P.M., Chiu H., Angove H.C., Burgess B.K., Rees D.C.
Biochemistry 40:651-656(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[11]"MgATP-bound and nucleotide-free structures of a nitrogenase protein complex between the Leu 127Delta-Fe-protein and the MoFe-protein."
Chiu H.-J., Peters J.W., Lanzilotta W.N., Ryle M.J., Seefeldt L.C., Howard J.B., Rees D.C.
Biochemistry 40:641-650(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20568 Genomic DNA. Translation: AAA64709.1.
M11579 Genomic DNA. Translation: AAA22142.1.
X06886 Genomic DNA. Translation: CAA30003.1.
PIRNIAVF. A94666.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DE0X-ray2.40A/B2-290[»]
1FP6X-ray2.15A/B/C/D2-290[»]
1G1MX-ray2.25A/B2-290[»]
1G20X-ray2.20E/F/G/H1-290[»]
1G21X-ray3.00E/F/G/H1-290[»]
1G5PX-ray2.20A/B2-290[»]
1M1YX-ray3.20E/F/G/H/M/N/O/P2-290[»]
1M34X-ray2.30E/F/G/H/M/N/O/P2-290[»]
1N2CX-ray3.00E/F/G/H2-290[»]
1NIPX-ray2.90A/B2-290[»]
1RW4X-ray2.50A2-273[»]
1XCPX-ray3.20A/B/C/D2-290[»]
1XD8X-ray2.70A/B2-290[»]
1XD9X-ray2.80A/B2-290[»]
1XDBX-ray2.80A/B2-290[»]
2AFHX-ray2.10E/F2-290[»]
2AFIX-ray3.10E/F/G/H/M/N/O/P2-290[»]
2AFKX-ray2.30E/F/G/H2-290[»]
2C8VX-ray2.50A2-290[»]
2NIPX-ray2.20A/B2-290[»]
ProteinModelPortalP00459.
SMRP00459. Positions 2-290.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16519.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
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

EvolutionaryTraceP00459.

Entry information

Entry nameNIFH1_AZOVI
AccessionPrimary (citable) accession number: P00459
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 117 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references