ID   NIFN_SINFN              Reviewed;         469 AA.
AC   P55674;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Nitrogenase iron-molybdenum cofactor biosynthesis protein NifN;
GN   Name=nifN; OrderedLocusNames=NGR_a01090; ORFNames=y4vO;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
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   [2]
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 secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: This protein may play a role in the biosynthesis of the
CC       prosthetic group of nitrogenase (FeMo cofactor).
CC   -!- PATHWAY: Cofactor biosynthesis; Fe-Mo cofactor biosynthesis.
CC   -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR   EMBL; U00090; AAB91903.1; -; Genomic_DNA.
DR   RefSeq; NP_444116.1; NC_000914.2.
DR   RefSeq; WP_010875150.1; NC_000914.2.
DR   AlphaFoldDB; P55674; -.
DR   SMR; P55674; -.
DR   STRING; 394.NGR_a01090; -.
DR   EnsemblBacteria; AAB91903; AAB91903; NGR_a01090.
DR   KEGG; rhi:NGR_a01090; -.
DR   PATRIC; fig|394.7.peg.93; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_025876_2_0_5; -.
DR   OMA; HFYFGGK; -.
DR   OrthoDB; 397330at2; -.
DR   UniPathway; UPA00782; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016163; F:nitrogenase activity; IEA:InterPro.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   GO; GO:0065003; P:protein-containing complex assembly; IEA:InterPro.
DR   CDD; cd01966; Nitrogenase_NifN_1; 1.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR000318; Nase_comp1_CS.
DR   InterPro; IPR005975; Nase_Mo-Fe_CF.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   TIGRFAMs; TIGR01285; nifN; 1.
DR   PROSITE; PS00699; NITROGENASE_1_1; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Nitrogen fixation; Plasmid; Reference proteome.
FT   CHAIN           1..469
FT                   /note="Nitrogenase iron-molybdenum cofactor biosynthesis
FT                   protein NifN"
FT                   /id="PRO_0000153132"
FT   BINDING         44
FT                   /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT                   /ligand_id="ChEBI:CHEBI:30409"
FT                   /ligand_note="cofactor"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   469 AA;  51114 MW;  C30FEE4601D831B2 CRC64;
     MVHIHRQSKS ATVNPLKSSQ PLGAALAFLG VDGAIPLFHG SQGCTSFALV LCVRHFKETI
     PLQTTAMDEL ATVLGGAAHL EEAILNLKKR ANPRLIGICT TALVETRSED FARQIANIKM
     THAEELAGTE VVLANTPDFD GALEEGWARA VAAMIQQITL RRQQAPRSRK ATLIERITKP
     SEQPWKQQKV AILPGWHLTV GDIEQLREMV EGFGLRPVIV PDVSGSLDGT VPDRWMPTAY
     GGTSIEDIQE LGRAVRCIAI GEHMRRPAEL LQTLTGVPYV LVQSLTGLKN VDQFVSLLSE
     ISCVPAPAKI HRHRSQLQDA LLDGHFHFAG KKIAIATEPD QLYQFATFFT GLGAEIISAV
     TTTGESEIIE KVPAEKVQIG DLGDLEDLAG GADLLVTHSH GRQAAERLGI PLLRIGFPIF
     DRLGSQHKLT VLYRGTRDLI FEAANIIQAN QPAPSLEQID AMRKRRNAG