ID   NIFN_RHILO              Reviewed;         460 AA.
AC   Q98AP3;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Nitrogenase iron-molybdenum cofactor biosynthesis protein NifN;
GN   Name=nifN; OrderedLocusNames=mlr5909;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB52279.1; -; Genomic_DNA.
DR   RefSeq; WP_010913612.1; NC_002678.2.
DR   AlphaFoldDB; Q98AP3; -.
DR   SMR; Q98AP3; -.
DR   STRING; 266835.14025679; -.
DR   EnsemblBacteria; BAB52279; BAB52279; BAB52279.
DR   KEGG; mlo:mlr5909; -.
DR   PATRIC; fig|266835.9.peg.4704; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_025876_2_0_5; -.
DR   OMA; HFYFGGK; -.
DR   OrthoDB; 397330at2; -.
DR   UniPathway; UPA00782; -.
DR   Proteomes; UP000000552; Chromosome.
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.
FT   CHAIN           1..460
FT                   /note="Nitrogenase iron-molybdenum cofactor biosynthesis
FT                   protein NifN"
FT                   /id="PRO_0000153130"
FT   REGION          436..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..460
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   460 AA;  49805 MW;  684347E05FC24DAA CRC64;
     MVRILRKIKS AAVNPLKSSQ PLGAAFAFLG VEGAMPLFHG SQGCTSFALV LFVRHFKEAI
     PLQTTAMDEV ATILGGADHL EEAILNLKTR TKPKLIGVCT TALVETRGED CASDIANVKL
     KHVEELAGTE VVLANTPDFD GAIEEGWAKA VAAMIEGITR SGERTRQPKK IAILPGCNLT
     VADVEHLRDM VESFGLKPVI LPDVSGSLDG TVPDRWVTTT YGGTSVEEIR ELGTAAQCIV
     IGEHMRHPAK TLHGLTGVPY AVFQSLTGLK AVDRFVSLLS AVSGAAVPDR VRRHRAQLED
     ALLDGHFHFG GKKIAIAAEP DQLYQLATFF TGMGCDIAAA VTTTDMSKIL QKVPAEWVQI
     GDLGDLEALA AGADLLVTHS HGRQASRRLE IPLMRVGFPI FDRLGSQHKL TILYRGTRDL
     IFDVANIFQA NQHAPTPEAL DPFRKREMPD ELRSSPLTRH