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NIFH1_NOSS1
ID   NIFH1_NOSS1             Reviewed;         295 AA.
AC   P00457;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Nitrogenase iron protein 1;
DE            EC=1.18.6.1;
DE   AltName: Full=Nitrogenase Fe protein 1;
DE   AltName: Full=Nitrogenase component II;
DE   AltName: Full=Nitrogenase reductase;
GN   Name=nifH1; Synonyms=nifH; OrderedLocusNames=all1455;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16592916; DOI=10.1073/pnas.77.11.6476;
RA   Mevarech M., Rice D., Haselkorn R.;
RT   "Nucleotide sequence of a cyanobacterial nifH gene coding for nitrogenase
RT   reductase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 77:6476-6480(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- PTM: The reversible ADP-ribosylation of Arg-104 inactivates the
CC       nitrogenase reductase and regulates nitrogenase activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000305}.
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DR   EMBL; V01482; CAA24729.1; -; Genomic_DNA.
DR   EMBL; V00001; CAA23398.1; -; Genomic_DNA.
DR   EMBL; J05111; AAA22008.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB73411.1; -; Genomic_DNA.
DR   PIR; A00534; NIAIF.
DR   PIR; AC1988; AC1988.
DR   RefSeq; WP_010995626.1; NZ_RSCN01000040.1.
DR   AlphaFoldDB; P00457; -.
DR   SMR; P00457; -.
DR   STRING; 103690.17130801; -.
DR   EnsemblBacteria; BAB73411; BAB73411; BAB73411.
DR   KEGG; ana:all1455; -.
DR   eggNOG; COG1348; Bacteria.
DR   OMA; TTMMDTL; -.
DR   OrthoDB; 729012at2; -.
DR   Proteomes; UP000002483; 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..295
FT                   /note="Nitrogenase iron protein 1"
FT                   /id="PRO_0000139481"
FT   BINDING         13..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         101
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         104
FT                   /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT                   ribosyltransferase"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        251
FT                   /note="Missing (in Ref. 1; CAA24729/CAA23398)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        271
FT                   /note="L -> K (in Ref. 1; CAA24729/CAA23398/AAA22008)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        295
FT                   /note="K -> NRSCRN (in Ref. 1; CAA24729/CAA23398)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   295 AA;  32310 MW;  411E6C6C9E58A69E CRC64;
     MTDENIRQIA FYGKGGIGKS TTSQNTLAAM AEMGQRIMIV GCDPKADSTR LMLHSKAQTT
     VLHLAAERGA VEDLELHEVM LTGFRGVKCV ESGGPEPGVG CAGRGIITAI NFLEENGAYQ
     DLDFVSYDVL GDVVCGGFAM PIREGKAQEI YIVTSGEMMA MYAANNIARG ILKYAHSGGV
     RLGGLICNSR KVDREDELIM NLAERLNTQM IHFVPRDNIV QHAELRRMTV NEYAPDSNQG
     QEYRALAKKI INNDKLTIPT PMEMDELEAL LIEYGLLDDD TKHSEIIGKP AEATK
 
 
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