Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P00459

- NIFH1_AZOVI

UniProt

P00459 - NIFH1_AZOVI

Protein

Nitrogenase iron protein 1

Gene

nifH1

Organism
Azotobacter vinelandii
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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

    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 – 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.
    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

    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

    Experimental Info

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

    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: October 1, 2014
    This is version 118 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