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NIFH_FRACC
ID   NIFH_FRACC              Reviewed;         287 AA.
AC   Q2J4F8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Nitrogenase iron protein {ECO:0000255|HAMAP-Rule:MF_00533};
DE            EC=1.18.6.1 {ECO:0000255|HAMAP-Rule:MF_00533};
DE   AltName: Full=Nitrogenase Fe protein {ECO:0000255|HAMAP-Rule:MF_00533};
DE   AltName: Full=Nitrogenase component II {ECO:0000255|HAMAP-Rule:MF_00533};
DE   AltName: Full=Nitrogenase reductase {ECO:0000255|HAMAP-Rule:MF_00533};
GN   Name=nifH {ECO:0000255|HAMAP-Rule:MF_00533};
GN   OrderedLocusNames=Francci3_4488;
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / CcI3).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=106370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45818 / CECT 9043 / CcI3;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
CC   -!- FUNCTION: The key enzymatic reactions in nitrogen fixation are
CC       catalyzed by the nitrogenase complex, which has 2 components: the iron
CC       protein and the molybdenum-iron protein. {ECO:0000255|HAMAP-
CC       Rule:MF_00533}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16
CC         ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16
CC         phosphate; Xref=Rhea:RHEA:21448, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC         COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17997,
CC         ChEBI:CHEBI:18276, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=1.18.6.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00533};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00533};
CC       Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000255|HAMAP-
CC       Rule:MF_00533};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00533}.
CC   -!- PTM: The reversible ADP-ribosylation of Arg-99 inactivates the
CC       nitrogenase reductase and regulates nitrogenase activity.
CC       {ECO:0000255|HAMAP-Rule:MF_00533}.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000255|HAMAP-
CC       Rule:MF_00533}.
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DR   EMBL; CP000249; ABD13834.1; -; Genomic_DNA.
DR   RefSeq; WP_011438842.1; NZ_JENI01000001.1.
DR   AlphaFoldDB; Q2J4F8; -.
DR   SMR; Q2J4F8; -.
DR   STRING; 106370.Francci3_4488; -.
DR   EnsemblBacteria; ABD13834; ABD13834; Francci3_4488.
DR   KEGG; fra:Francci3_4488; -.
DR   eggNOG; COG1348; Bacteria.
DR   HOGENOM; CLU_059373_0_0_11; -.
DR   OMA; YVCDYYL; -.
DR   OrthoDB; 729012at2; -.
DR   PhylomeDB; Q2J4F8; -.
DR   Proteomes; UP000001937; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0018697; F:carbonyl sulfide nitrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016163; F:nitrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00533; NifH; 1.
DR   InterPro; IPR030655; NifH/chlL_CS.
DR   InterPro; IPR000392; NifH/frxC.
DR   InterPro; IPR005977; Nitrogenase_Fe_NifH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR42864; PTHR42864; 1.
DR   Pfam; PF00142; Fer4_NifH; 1.
DR   PIRSF; PIRSF000363; Nitrogenase_iron; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01287; nifH; 1.
DR   PROSITE; PS00746; NIFH_FRXC_1; 1.
DR   PROSITE; PS00692; NIFH_FRXC_2; 1.
DR   PROSITE; PS51026; NIFH_FRXC_3; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; ADP-ribosylation; ATP-binding; Iron; Iron-sulfur; Metal-binding;
KW   Nitrogen fixation; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..287
FT                   /note="Nitrogenase iron protein"
FT                   /id="PRO_1000211870"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00533"
FT   BINDING         96
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00533"
FT   BINDING         130
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00533"
FT   MOD_RES         99
FT                   /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT                   ribosyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00533"
SQ   SEQUENCE   287 AA;  31423 MW;  E2798FFCDCDB77D8 CRC64;
     MRQIAFYGKG GIGKSTTQQN TMAAMAEMGK KVMIVGCDPK ADSTRLILHS KAQTSVIQLA
     AEKGSVEDLE LDEVLVEGQW GIKCVESGGP EPGVGCAGRG VITSISYLEE AGAYEDLDFV
     TYDVLGDVVC GGFAMPIRQG KAQEIYIVTS GEMMAMYAAN NIARGILKYA HSGGVRLGGL
     ICNSRNTDRE DELIIELARR LNTQMIHFIP RNNVVQHAEL RRMTVIEYDP KNEQADQYRQ
     LAKKIVDNDM KTIPTPITMD ELEELLIEFG IMEQEDESII GKAAAVA
 
 
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