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P07329

- NIFK_AZOVI

UniProt

P07329 - NIFK_AZOVI

Protein

Nitrogenase molybdenum-iron protein beta chain

Gene

nifK

Organism
Azotobacter vinelandii
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.

    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 8Fe-7S cluster per heterodimer.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi70 – 701Iron-sulfur (8Fe-7S); shared with alpha chain
    Metal bindingi95 – 951Iron-sulfur (8Fe-7S); shared with alpha chain
    Metal bindingi153 – 1531Iron-sulfur (8Fe-7S); shared with alpha chain
    Metal bindingi188 – 1881Iron-sulfur (8Fe-7S); shared with alpha chain

    GO - Molecular functioni

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

    GO - Biological processi

    1. nitrogen fixation Source: CACAO

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Nitrogen fixation

    Keywords - Ligandi

    ATP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nitrogenase molybdenum-iron protein beta chain (EC:1.18.6.1)
    Alternative name(s):
    Dinitrogenase
    Nitrogenase component I
    Gene namesi
    Name:nifK
    OrganismiAzotobacter vinelandii
    Taxonomic identifieri354 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

    Subcellular locationi

    GO - Cellular componenti

    1. molybdenum-iron nitrogenase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 523522Nitrogenase molybdenum-iron protein beta chainPRO_0000153091Add
    BLAST

    Interactioni

    Subunit structurei

    Tetramer of two alpha and two beta chains. Forms complex with the iron protein (nitrogenase component 2).

    Protein-protein interaction databases

    MINTiMINT-1508555.

    Structurei

    Secondary structure

    1
    523
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 73
    Helixi11 – 144
    Helixi18 – 3114
    Helixi37 – 4610
    Helixi50 – 578
    Beta strandi63 – 653
    Helixi71 – 8010
    Beta strandi85 – 917
    Helixi93 – 10715
    Beta strandi114 – 1174
    Helixi120 – 1234
    Helixi128 – 14215
    Beta strandi145 – 1517
    Helixi153 – 1586
    Helixi162 – 17110
    Beta strandi177 – 1793
    Beta strandi188 – 1914
    Helixi193 – 20917
    Helixi210 – 2156
    Turni218 – 2214
    Beta strandi224 – 2274
    Helixi234 – 24613
    Beta strandi251 – 2555
    Turni258 – 2614
    Beta strandi266 – 2683
    Helixi278 – 2836
    Helixi284 – 2863
    Beta strandi287 – 2948
    Helixi295 – 2973
    Helixi299 – 3079
    Helixi321 – 33616
    Helixi342 – 36221
    Beta strandi366 – 3705
    Helixi373 – 38513
    Beta strandi389 – 3957
    Helixi400 – 41112
    Helixi414 – 4163
    Beta strandi420 – 4245
    Helixi427 – 43610
    Beta strandi440 – 4445
    Helixi448 – 45811
    Helixi460 – 4623
    Beta strandi466 – 4683
    Beta strandi475 – 4784
    Helixi479 – 4813
    Helixi486 – 50823
    Turni512 – 5154
    Helixi516 – 5183

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FP4X-ray2.50B/D1-523[»]
    1G20X-ray2.20B/D1-523[»]
    1G21X-ray3.00B/D1-523[»]
    1L5HX-ray2.30B2-523[»]
    1M1NX-ray1.16B/D/F/H2-523[»]
    1M1YX-ray3.20B/D/J/L2-523[»]
    1M34X-ray2.30B/D/J/L2-523[»]
    1N2CX-ray3.00B/D2-523[»]
    2AFHX-ray2.10B/D2-523[»]
    2AFIX-ray3.10B/D/J/L2-523[»]
    2AFKX-ray2.30B/D2-523[»]
    2MINX-ray2.03B/D2-523[»]
    3K1AX-ray2.23B/D2-523[»]
    3MINX-ray2.03B/D2-523[»]
    3U7QX-ray1.00B/D1-523[»]
    4ND8X-ray2.00B/D1-523[»]
    ProteinModelPortaliP07329.
    SMRiP07329. Positions 2-523.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07329.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the NifD/NifK/NifE/NifN family.Curated

    Family and domain databases

    InterProiIPR000510. Nase/OxRdtase_comp1.
    IPR000318. Nase_comp1_CS.
    IPR005976. Nase_Mo-Fe_CF_bsu.
    IPR024564. Nase_Mo-Fe_CF_bsu_N.
    [Graphical view]
    PfamiPF11844. DUF3364. 1 hit.
    PF00148. Oxidored_nitro. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01286. nifK. 1 hit.
    PROSITEiPS00699. NITROGENASE_1_1. 1 hit.
    PS00090. NITROGENASE_1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P07329-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQQVDKIKA SYPLFLDQDY KDMLAKKRDG FEEKYPQDKI DEVFQWTTTK    50
    EYQELNFQRE ALTVNPAKAC QPLGAVLCAL GFEKTMPYVH GSQGCVAYFR 100
    SYFNRHFREP VSCVSDSMTE DAAVFGGQQN MKDGLQNCKA TYKPDMIAVS 150
    TTCMAEVIGD DLNAFINNSK KEGFIPDEFP VPFAHTPSFV GSHVTGWDNM 200
    FEGIARYFTL KSMDDKVVGS NKKINIVPGF ETYLGNFRVI KRMLSEMGVG 250
    YSLLSDPEEV LDTPADGQFR MYAGGTTQEE MKDAPNALNT VLLQPWHLEK 300
    TKKFVEGTWK HEVPKLNIPM GLDWTDEFLM KVSEISGQPI PASLTKERGR 350
    LVDMMTDSHT WLHGKRFALW GDPDFVMGLV KFLLELGCEP VHILCHNGNK 400
    RWKKAVDAIL AASPYGKNAT VYIGKDLWHL RSLVFTDKPD FMIGNSYGKF 450
    IQRDTLHKGK EFEVPLIRIG FPIFDRHHLH RSTTLGYEGA MQILTTLVNS 500
    ILERLDEETR GMQATDYNHD LVR 523
    Length:523
    Mass (Da):59,460
    Last modified:January 23, 2007 - v3
    Checksum:iB6ECD633A24998F2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti103 – 1031F → L in AAA22144. (PubMed:3863780)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20568 Genomic DNA. Translation: AAA64711.1.
    M11579 Genomic DNA. Translation: AAA22144.1.
    PIRiB43049. NIAVMB.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20568 Genomic DNA. Translation: AAA64711.1 .
    M11579 Genomic DNA. Translation: AAA22144.1 .
    PIRi B43049. NIAVMB.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FP4 X-ray 2.50 B/D 1-523 [» ]
    1G20 X-ray 2.20 B/D 1-523 [» ]
    1G21 X-ray 3.00 B/D 1-523 [» ]
    1L5H X-ray 2.30 B 2-523 [» ]
    1M1N X-ray 1.16 B/D/F/H 2-523 [» ]
    1M1Y X-ray 3.20 B/D/J/L 2-523 [» ]
    1M34 X-ray 2.30 B/D/J/L 2-523 [» ]
    1N2C X-ray 3.00 B/D 2-523 [» ]
    2AFH X-ray 2.10 B/D 2-523 [» ]
    2AFI X-ray 3.10 B/D/J/L 2-523 [» ]
    2AFK X-ray 2.30 B/D 2-523 [» ]
    2MIN X-ray 2.03 B/D 2-523 [» ]
    3K1A X-ray 2.23 B/D 2-523 [» ]
    3MIN X-ray 2.03 B/D 2-523 [» ]
    3U7Q X-ray 1.00 B/D 1-523 [» ]
    4ND8 X-ray 2.00 B/D 1-523 [» ]
    ProteinModelPortali P07329.
    SMRi P07329. Positions 2-523.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1508555.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P07329.

    Family and domain databases

    InterProi IPR000510. Nase/OxRdtase_comp1.
    IPR000318. Nase_comp1_CS.
    IPR005976. Nase_Mo-Fe_CF_bsu.
    IPR024564. Nase_Mo-Fe_CF_bsu_N.
    [Graphical view ]
    Pfami PF11844. DUF3364. 1 hit.
    PF00148. Oxidored_nitro. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01286. nifK. 1 hit.
    PROSITEi PS00699. NITROGENASE_1_1. 1 hit.
    PS00090. NITROGENASE_1_2. 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. "Isolation and partial characterization of two different subunits from the molybdenum-iron protein of Azotobacter vinelandii nitrogenase."
      Lundell D.J., Howard J.B.
      J. Biol. Chem. 253:3422-3426(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-20 AND 521-523.
    4. "Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii."
      Kim J., Rees D.C.
      Nature 360:553-560(1992)
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    5. "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).
    6. "Redox-dependent structural changes in the nitrogenase P-cluster."
      Peters J.W., Stowell M.H.B., Soltis S.M., Finnegan M.G., Johnson M.K., Rees D.C.
      Biochemistry 36:1181-1187(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    7. "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).
    8. "Mechanistic features and structure of the nitrogenase alpha-Gln195 MoFe protein."
      Soerlie M., Christiansen J., Lemon B.J., Peters J.W., Dean D.R., Hales B.J.
      Biochemistry 40:1540-1549(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLN-195.
    9. "Biochemical and structural characterization of the cross-linked complex of nitrogenase: comparison to the ADP-AlF4(-)-stabilized structure."
      Schmid B., Einsle O., Chiu H.J., Willing A., Yoshida M., Howard J.B., Rees D.C.
      Biochemistry 41:15557-15565(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF CROSS-LINKED HETERODIMER WITH FE-PROTEIN.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    11. "Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor."
      Einsle O., Tezcan F.A., Andrade S.L.A., Schmid B., Yoshida M., Howard J.B., Rees D.C.
      Science 297:1696-1700(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS).

    Entry informationi

    Entry nameiNIFK_AZOVI
    AccessioniPrimary (citable) accession number: P07329
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 96 of the entry and version 3 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

    External Data

    Dasty 3