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Database: UniProt
Entry: A0A1M3M037_9PROT
LinkDB: A0A1M3M037_9PROT
Original site: A0A1M3M037_9PROT 
ID   A0A1M3M037_9PROT        Unreviewed;       456 AA.
AC   A0A1M3M037;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Nitrogenase iron-molybdenum cofactor biosynthesis protein NifN {ECO:0000256|ARBA:ARBA00013282};
GN   ORFNames=BGO92_01330 {ECO:0000313|EMBL:OJX78525.1};
OS   Magnetospirillum sp. 64-120.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=1895778 {ECO:0000313|EMBL:OJX78525.1, ECO:0000313|Proteomes:UP000184435};
RN   [1] {ECO:0000313|EMBL:OJX78525.1, ECO:0000313|Proteomes:UP000184435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=64-120 {ECO:0000313|EMBL:OJX78525.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein may play a role in the biosynthesis of the
CC       prosthetic group of nitrogenase (FeMo cofactor).
CC       {ECO:0000256|ARBA:ARBA00003171}.
CC   -!- PATHWAY: Cofactor biosynthesis; Fe-Mo cofactor biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005155}.
CC   -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family.
CC       {ECO:0000256|ARBA:ARBA00011002, ECO:0000256|RuleBase:RU004021}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OJX78525.1}.
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DR   EMBL; MKVK01000018; OJX78525.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3M037; -.
DR   STRING; 1895778.BGO92_01330; -.
DR   UniPathway; UPA00782; -.
DR   Proteomes; UP000184435; Unassembled WGS sequence.
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   Gene3D; 6.10.250.1090; -; 1.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR000318; Nase_comp1_CS.
DR   InterPro; IPR005975; Nase_Mo-Fe_CF.
DR   NCBIfam; TIGR01285; nifN; 1.
DR   PANTHER; PTHR33712; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1.
DR   PANTHER; PTHR33712:SF7; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
DR   PROSITE; PS00699; NITROGENASE_1_1; 1.
PE   3: Inferred from homology;
KW   Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231,
KW   ECO:0000256|RuleBase:RU004021}.
FT   DOMAIN          19..430
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
FT   REGION          435..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   456 AA;  48782 MW;  2452E9F8A8C2D57E CRC64;
     MALIVSHGHS VTSNPLKLSA PLGASMAFMG MDQTMPLLHG SQGCTAFALV MLVRHFREAI
     PLQTTAMNEV STILGGMDQV EQALLNIAKR TKPKIIGLIS TALTETRGED MKGDLKLILE
     RNPELADIKV IPVSAPDFSG SLETGWGKAV TAIIDNLAEP ASAKQQDCNR VNILPGVHMT
     PGDIETLVDL VEEFGLKANV LPDLSGSVDG HVPDHFIPTT YGGATVDSAK NLGRAKLTIA
     IGEHMRISAE TLREKTGVPY VLFDRLTGLE ASDRLMVCLS TAAGKPVPAK IRRARSQLID
     AMLDGHFYFG GRKFAVAGEP DFLWTWGKLI SDMGGELVAA ITPVHAAHLT ELPCQQVIIG
     DFQDMEDQIL EAGGADLVIS NTNARLSCQA LGVPHFRAGF PVYDRLGGAH RVHVGYRGTR
     DLIFQLANVL IDNPDHGHGP VPHSAEHDHA AAPALG
//
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