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Protein

Nitrogenase iron protein 1

Gene

nifH1

Organism
Azotobacter vinelandii
Status
Reviewed-Annotation score: Annotation score: 5 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 (component 2) and a component 1 which is either a molybdenum-iron protein, a vanadium-iron, or an iron-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 bindingi98 – 981Iron-sulfur (4Fe-4S); shared with dimeric partner
Metal bindingi133 – 1331Iron-sulfur (4Fe-4S); shared with dimeric partner

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 178ATP

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. ATP binding Source: UniProtKB-HAMAP
  3. carbonyl sulfide nitrogenase activity Source: UniProtKB-EC
  4. metal ion binding Source: UniProtKB-KW
  5. nitrogenase activity Source: CACAO

GO - Biological processi

  1. nitrogen fixation Source: UniProtKB-HAMAP
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:MONOMER-16519.

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
OrganismiAzotobacter vinelandii
Taxonomic identifieri354 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Subcellular locationi

GO - Cellular componenti

  1. molybdenum-iron nitrogenase complex Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 161K → Q or P: Loss of nitrogen fixation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 290289Nitrogenase iron protein 1PRO_0000139490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferaseBy similarity

Post-translational modificationi

The reversible ADP-ribosylation of Arg-101 inactivates the nitrogenase reductase and regulates nitrogenase activity.By similarity

Keywords - PTMi

ADP-ribosylation

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
290
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Helixi12 – 143Combined sources
Helixi16 – 2914Combined sources
Beta strandi34 – 396Combined sources
Beta strandi41 – 433Combined sources
Turni44 – 463Combined sources
Helixi47 – 504Combined sources
Beta strandi52 – 543Combined sources
Helixi58 – 636Combined sources
Beta strandi65 – 673Combined sources
Helixi68 – 703Combined sources
Helixi73 – 764Combined sources
Beta strandi77 – 804Combined sources
Helixi81 – 833Combined sources
Beta strandi85 – 884Combined sources
Turni94 – 963Combined sources
Helixi99 – 11214Combined sources
Helixi115 – 1173Combined sources
Beta strandi121 – 1288Combined sources
Helixi129 – 1313Combined sources
Turni134 – 1374Combined sources
Helixi138 – 1414Combined sources
Beta strandi147 – 1526Combined sources
Helixi156 – 17318Combined sources
Beta strandi179 – 1868Combined sources
Beta strandi188 – 1903Combined sources
Helixi193 – 20412Combined sources
Beta strandi208 – 2125Combined sources
Helixi216 – 2238Combined sources
Helixi228 – 2314Combined sources
Beta strandi233 – 2353Combined sources
Helixi236 – 25015Combined sources
Helixi262 – 27110Combined sources
Helixi280 – 2823Combined sources
Turni287 – 2893Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00459.
SMRiP00459. Positions 2-290.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00459.

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.
InterProiIPR000392. Nitogenase_NifH/Reductase_ChlL.
IPR005977. Nitrogenase_Fe_NifH.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00142. Fer4_NifH. 1 hit.
[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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00459-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAMRQCAIYG KGGIGKSTTT QNLVAALAEM GKKVMIVGCD PKADSTRLIL
60 70 80 90 100
HSKAQNTIME MAAEAGTVED LELEDVLKAG YGGVKCVESG GPEPGVGCAG
110 120 130 140 150
RGVITAINFL EEEGAYEDDL DFVFYDVLGD VVCGGFAMPI RENKAQEIYI
160 170 180 190 200
VCSGEMMAMY AANNISKGIV KYANSGSVRL GGLICNSRNT DREDELIIAL
210 220 230 240 250
ANKLGTQMIH FVPRDNVVQR AEIRRMTVIE YDPKAKQADE YRALARKVVD
260 270 280 290
NKLLVIPNPI TMDELEELLM EFGIMEVEDE SIVGKTAEEV
Length:290
Mass (Da):31,516
Last modified:January 23, 2007 - v2
Checksum:iC36EFC0D9A27F64D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451A → P in AAA22142. (PubMed:3863780)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20568 Genomic DNA. Translation: AAA64709.1.
M11579 Genomic DNA. Translation: AAA22142.1.
X06886 Genomic DNA. Translation: CAA30003.1.
PIRiA94666. NIAVF.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20568 Genomic DNA. Translation: AAA64709.1.
M11579 Genomic DNA. Translation: AAA22142.1.
X06886 Genomic DNA. Translation: CAA30003.1.
PIRiA94666. NIAVF.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00459.
SMRiP00459. Positions 2-290.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16519.

Miscellaneous databases

EvolutionaryTraceiP00459.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00533. NifH.
InterProiIPR000392. Nitogenase_NifH/Reductase_ChlL.
IPR005977. Nitrogenase_Fe_NifH.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00142. Fer4_NifH. 1 hit.
[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. "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).

Entry informationi

Entry nameiNIFH1_AZOVI
AccessioniPrimary (citable) accession number: P00459
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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

External Data

Dasty 3

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 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.