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NIFH_ALKMQ
ID   NIFH_ALKMQ              Reviewed;         272 AA.
AC   A6TTY3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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}; OrderedLocusNames=Amet_3524;
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QYMF;
RX   PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA   Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA   Richardson P., Fields M.W.;
RT   "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT   alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT   leachate ponds.";
RL   Genome Announc. 4:0-0(2016).
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-97 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; CP000724; ABR49651.1; -; Genomic_DNA.
DR   RefSeq; WP_012064614.1; NC_009633.1.
DR   AlphaFoldDB; A6TTY3; -.
DR   SMR; A6TTY3; -.
DR   STRING; 293826.Amet_3524; -.
DR   EnsemblBacteria; ABR49651; ABR49651; Amet_3524.
DR   KEGG; amt:Amet_3524; -.
DR   eggNOG; COG1348; Bacteria.
DR   HOGENOM; CLU_059373_0_0_9; -.
DR   OMA; YVCDYYL; -.
DR   OrthoDB; 729012at2; -.
DR   Proteomes; UP000001572; 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..272
FT                   /note="Nitrogenase iron protein"
FT                   /id="PRO_1000211852"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00533"
FT   BINDING         94
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         129
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         97
FT                   /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT                   ribosyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00533"
SQ   SEQUENCE   272 AA;  29479 MW;  7BA571450AC27A92 CRC64;
     MRQIAIYGKG GIGKSTTTQN LTAALGESGK KIMIVGCDPK ADSTRLILGG LTQKTVMDTL
     REEGEDIDLE DILKPGFSGI KCVESGGPEP GVGCAGRGII TSINMLESLG AYESDLDYVF
     YDVLGDVVCG GFAMPIREGK AQEIYIVASG ELMALYAANN IAKGIQKYAK SGGTRLGGII
     CNSRQVDYEH ELLEAFAKEL GSQLIYFVPR DNIVQRAEIN KKAVIEFEPE CGQANEYRAL
     AKSIDENKMF VIPKPMHTDR LEELMMEHGV LG
 
 
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