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Database: UniProt
Entry: NIFH_SINFN
LinkDB: NIFH_SINFN
Original site: NIFH_SINFN 
ID   NIFH_SINFN              Reviewed;         296 AA.
AC   P19068; P55672;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   28-MAR-2018, entry version 121.
DE   RecName: Full=Nitrogenase iron protein;
DE            EC=1.18.6.1;
DE   AltName: Full=Nitrogenase Fe protein;
DE   AltName: Full=Nitrogenase component II;
DE   AltName: Full=Nitrogenase reductase;
GN   Name=nifH1; OrderedLocusNames=NGR_a01130; ORFNames=y4vK;
GN   and
GN   Name=nifH2; OrderedLocusNames=NGR_a00890; ORFNames=y4xA;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ANU 240;
RX   PubMed=2744485; DOI=10.1016/0378-1119(89)90368-5;
RA   Badenoch-Jones J., Holton T.A., Morrison C.M., Scott K.F., Shine J.;
RT   "Structural and functional analysis of nitrogenase genes from the
RT   broad-host-range Rhizobium strain ANU240.";
RL   Gene 77:141-153(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: The key enzymatic reactions in nitrogen fixation are
CC       catalyzed by the nitrogenase complex, which has 2 components: the
CC       iron protein and the molybdenum-iron protein. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 8 reduced ferredoxin + 8 H(+) + N(2) + 16 ATP
CC       + 16 H(2)O = 8 oxidized ferredoxin + H(2) + 2 NH(3) + 16 ADP + 16
CC       phosphate.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         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-102 inactivates the
CC       nitrogenase reductase and regulates nitrogenase activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000305}.
DR   EMBL; M26961; AAA26329.1; -; Genomic_DNA.
DR   EMBL; U00090; AAB91899.1; -; Genomic_DNA.
DR   EMBL; U00090; AAB91923.1; -; Genomic_DNA.
DR   PIR; JS0238; JS0238.
DR   RefSeq; NP_444112.1; NC_000914.2.
DR   RefSeq; NP_444136.1; NC_000914.2.
DR   RefSeq; WP_010875130.1; NC_000914.2.
DR   ProteinModelPortal; P19068; -.
DR   SMR; P19068; -.
DR   EnsemblBacteria; AAB91899; AAB91899; NGR_a01130.
DR   EnsemblBacteria; AAB91923; AAB91923; NGR_a00890.
DR   GeneID; 24960505; -.
DR   GeneID; 962478; -.
DR   GeneID; 962500; -.
DR   KEGG; rhi:NGR_a00890; -.
DR   KEGG; rhi:NGR_a01130; -.
DR   PATRIC; fig|394.7.peg.78; -.
DR   HOGENOM; HOG000228826; -.
DR   KO; K02588; -.
DR   OMA; PGDIVCG; -.
DR   OrthoDB; POG091H0230; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
DR   GO; GO:0016612; C:molybdenum-iron nitrogenase complex; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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-EC.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   CDD; cd02040; NifH; 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; Complete proteome; Iron;
KW   Iron-sulfur; Metal-binding; Nitrogen fixation; Nucleotide-binding;
KW   Oxidoreductase; Plasmid; Reference proteome.
FT   CHAIN         1    296       Nitrogenase iron protein.
FT                                /FTId=PRO_0000139525.
FT   NP_BIND      11     18       ATP. {ECO:0000255}.
FT   METAL        99     99       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000250}.
FT   METAL       133    133       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000250}.
FT   MOD_RES     102    102       ADP-ribosylarginine; by dinitrogenase
FT                                reductase ADP-ribosyltransferase.
FT                                {ECO:0000250}.
FT   CONFLICT    262    262       T -> N (in Ref. 1; AAA26329).
FT                                {ECO:0000305}.
SQ   SEQUENCE   296 AA;  31747 MW;  58ADF69DB677BA7A CRC64;
     MAGLRQIAFY GKGGIGKSTT SQNTLAALVD LGQKILIVGC DPKADSTRLI LNAKAQDTVL
     HLAAKEGSVE DLEVEDVLKV GYKGIKCVES GGPEPGVGCA GRGVITSINF LEENGAYDDV
     DYVSYDVLGD VVCGGFAMPI RENKAQEIYI VMSGEMMALY AANNIAKGIL KYAHSGGVRL
     GGLICNERQT DRELDLAEAL AAKLNSRLIH FVPRDNIVQH AELRKMTVIQ YAPESQQAAE
     YRALADKIHA NSGQGTVPTP ITMEELEDML LDFGVMKTDE QMLAELQAKE AAAAAQ
//
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