ID   NIFN_AZOVI              Reviewed;         458 AA.
AC   P10336;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Nitrogenase iron-molybdenum cofactor biosynthesis protein NifN;
GN   Name=nifN;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX   PubMed=2644218; DOI=10.1128/jb.171.2.1017-1027.1989;
RA   Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., Wilson M.S.,
RA   Cash V.L., Beynon J., Newton W.E., Dean D.R.;
RT   "Physical and genetic map of the major nif gene cluster from Azotobacter
RT   vinelandii.";
RL   J. Bacteriol. 171:1017-1027(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3470285; DOI=10.1128/jb.169.4.1547-1553.1987;
RA   Brigle K.E., Weiss M.C., Newton W.E., Dean D.R.;
RT   "Products of the iron-molybdenum cofactor-specific biosynthetic genes, nifE
RT   and nifN, are structurally homologous to the products of the nitrogenase
RT   molybdenum-iron protein genes, nifD and nifK.";
RL   J. Bacteriol. 169:1547-1553(1987).
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; M20568; AAA64717.1; -; Genomic_DNA.
DR   EMBL; M15815; AAA22158.1; -; Genomic_DNA.
DR   PIR; A26940; A26940.
DR   AlphaFoldDB; P10336; -.
DR   SMR; P10336; -.
DR   DIP; DIP-59676N; -.
DR   IntAct; P10336; 1.
DR   BioCyc; MetaCyc:MON-19487; -.
DR   UniPathway; UPA00782; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016163; F:nitrogenase activity; IEA:InterPro.
DR   GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IMP:CACAO.
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..458
FT                   /note="Nitrogenase iron-molybdenum cofactor biosynthesis
FT                   protein NifN"
FT                   /id="PRO_0000153126"
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   458 AA;  49208 MW;  038EBEC4C1E91328 CRC64;
     MAEIINRNKA LAVSPLKASQ TMGAALAILG LALSMPLFHG SQGCTAFAKV FFVRHFREPV
     PLQTTAMDQV SSVMGADENV VEALKTICER QNPSVIGLLT TGLSETQGCD LHTALHEFRT
     QYEEYKDVPI VPVNTPDFSG CFESGFAAAV KAIVETLVPE RRDQVGKRPR QVNVLCSANL
     TPGDLEYIAE SIESFGLRPL LIPDLSGSLD GHLDENRFNA LTTGGLSVAE LATAGQSVAT
     LVVGQSLAGA ADALAERTGV PDRRFGMLYG LDAVDAWLMA LAEISGNPVP DRYKRQRAQL
     QDAMLDTHFM LSSARTAIAA DPDLLLGFDA LLRSMGAHTV AAVVPARAAA LVDSPLPSVR
     VGDLEDLEHA ARAGQAQLVI GNSHALASAR RLGVPLLRAG FPQYDLLGGF QRCWSGYRGS
     SQVLFDLANL LVEHHQGIQP YHSIYAQKPA TEQPQWRH