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P00459

- NIFH1_AZOVI

UniProt

P00459 - NIFH1_AZOVI

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Protein

Nitrogenase iron protein 1

Gene
nifH1
Organism
Azotobacter vinelandii
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

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

Cofactori

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 – 178ATPUniRule annotation

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 1UniRule annotationPRO_0000139490Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

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 – 107
Helixi12 – 143
Helixi16 – 2914
Beta strandi34 – 396
Beta strandi41 – 433
Turni44 – 463
Helixi47 – 504
Beta strandi52 – 543
Helixi58 – 636
Beta strandi65 – 673
Helixi68 – 703
Helixi73 – 764
Beta strandi77 – 804
Helixi81 – 833
Beta strandi85 – 884
Turni94 – 963
Helixi99 – 11214
Helixi115 – 1173
Beta strandi121 – 1288
Helixi129 – 1313
Turni134 – 1374
Helixi138 – 1414
Beta strandi147 – 1526
Helixi156 – 17318
Beta strandi179 – 1868
Beta strandi188 – 1903
Helixi193 – 20412
Beta strandi208 – 2125
Helixi216 – 2238
Helixi228 – 2314
Beta strandi233 – 2353
Helixi236 – 25015
Helixi262 – 27110
Helixi280 – 2823
Turni287 – 2893

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP00459.

Family & Domainsi

Sequence similaritiesi

Belongs to the NifH/BchL/ChlL family.

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

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MAMRQCAIYG KGGIGKSTTT QNLVAALAEM GKKVMIVGCD PKADSTRLIL    50
HSKAQNTIME MAAEAGTVED LELEDVLKAG YGGVKCVESG GPEPGVGCAG 100
RGVITAINFL EEEGAYEDDL DFVFYDVLGD VVCGGFAMPI RENKAQEIYI 150
VCSGEMMAMY AANNISKGIV KYANSGSVRL GGLICNSRNT DREDELIIAL 200
ANKLGTQMIH FVPRDNVVQR AEIRRMTVIE YDPKAKQADE YRALARKVVD 250
NKLLVIPNPI TMDELEELLM EFGIMEVEDE SIVGKTAEEV 290
Length:290
Mass (Da):31,516
Last modified:January 23, 2007 - v2
Checksum:iC36EFC0D9A27F64D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451A → P in AAA22142. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M20568 Genomic DNA. Translation: AAA64709.1 .
M11579 Genomic DNA. Translation: AAA22142.1 .
X06886 Genomic DNA. Translation: CAA30003.1 .
PIRi A94666. NIAVF.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DE0 X-ray 2.40 A/B 2-290 [» ]
1FP6 X-ray 2.15 A/B/C/D 2-290 [» ]
1G1M X-ray 2.25 A/B 2-290 [» ]
1G20 X-ray 2.20 E/F/G/H 1-290 [» ]
1G21 X-ray 3.00 E/F/G/H 1-290 [» ]
1G5P X-ray 2.20 A/B 2-290 [» ]
1M1Y X-ray 3.20 E/F/G/H/M/N/O/P 2-290 [» ]
1M34 X-ray 2.30 E/F/G/H/M/N/O/P 2-290 [» ]
1N2C X-ray 3.00 E/F/G/H 2-290 [» ]
1NIP X-ray 2.90 A/B 2-290 [» ]
1RW4 X-ray 2.50 A 2-273 [» ]
1XCP X-ray 3.20 A/B/C/D 2-290 [» ]
1XD8 X-ray 2.70 A/B 2-290 [» ]
1XD9 X-ray 2.80 A/B 2-290 [» ]
1XDB X-ray 2.80 A/B 2-290 [» ]
2AFH X-ray 2.10 E/F 2-290 [» ]
2AFI X-ray 3.10 E/F/G/H/M/N/O/P 2-290 [» ]
2AFK X-ray 2.30 E/F/G/H 2-290 [» ]
2C8V X-ray 2.50 A 2-290 [» ]
2NIP X-ray 2.20 A/B 2-290 [» ]
ProteinModelPortali P00459.
SMRi P00459. Positions 2-290.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-16519.

Miscellaneous databases

EvolutionaryTracei P00459.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00533. NifH.
InterProi IPR000392. Nitogenase_NifH/Reductase_ChlL.
IPR005977. Nitrogenase_Fe_NifH.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00142. Fer4_NifH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000363. Nitrogenase_iron. 1 hit.
PRINTSi PR00091. NITROGNASEII.
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01287. nifH. 1 hit.
PROSITEi PS00746. NIFH_FRXC_1. 1 hit.
PS00692. NIFH_FRXC_2. 1 hit.
PS51026. NIFH_FRXC_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 117 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

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