ID   B4WRU8_SYNS7            Unreviewed;       937 AA.
AC   B4WRU8;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Nitrogenase iron-molybdenum cofactor biosynthesis protein NifE {ECO:0000256|ARBA:ARBA00013280};
DE   AltName: Full=Nitrogenase iron-molybdenum cofactor biosynthesis protein NifN {ECO:0000256|ARBA:ARBA00013282};
GN   ORFNames=S7335_1681 {ECO:0000313|EMBL:EDX83984.1};
OS   Synechococcus sp. (strain ATCC 29403 / PCC 7335).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=91464 {ECO:0000313|EMBL:EDX83984.1, ECO:0000313|Proteomes:UP000005766};
RN   [1] {ECO:0000313|EMBL:EDX83984.1, ECO:0000313|Proteomes:UP000005766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29403 / PCC 7335 {ECO:0000313|Proteomes:UP000005766};
RA   Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) 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}.
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DR   EMBL; DS989904; EDX83984.1; -; Genomic_DNA.
DR   RefSeq; WP_006453728.1; NZ_DS989904.1.
DR   AlphaFoldDB; B4WRU8; -.
DR   STRING; 91464.S7335_1681; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_013317_0_0_3; -.
DR   OrthoDB; 9767044at2; -.
DR   UniPathway; UPA00782; -.
DR   Proteomes; UP000005766; 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; cd01968; Nitrogenase_NifE_I; 1.
DR   CDD; cd01966; Nitrogenase_NifN_1; 1.
DR   Gene3D; 6.10.250.1090; -; 1.
DR   Gene3D; 3.40.50.12380; Nitrogenase MoFe cofactor biosynthesis protein NifE, C-terminal; 1.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 4.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR000318; Nase_comp1_CS.
DR   InterPro; IPR005975; Nase_Mo-Fe_CF.
DR   InterPro; IPR005973; NifE.
DR   NCBIfam; TIGR01283; nifE; 1.
DR   NCBIfam; TIGR01285; nifN; 1.
DR   PANTHER; PTHR42956; NITROGENASE IRON-MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN NIFE; 1.
DR   PANTHER; PTHR42956:SF1; NITROGENASE IRON-MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN NIFE; 1.
DR   Pfam; PF00148; Oxidored_nitro; 2.
DR   SUPFAM; SSF53807; Helical backbone' metal receptor; 2.
DR   PROSITE; PS00699; NITROGENASE_1_1; 2.
PE   3: Inferred from homology;
KW   Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231,
KW   ECO:0000256|RuleBase:RU004021};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005766}.
FT   DOMAIN          45..440
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
FT   DOMAIN          497..918
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
FT   REGION          12..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   937 AA;  101498 MW;  45C33E51A00B0C12 CRC64;
     MKMSAGKINE LLTQPGCEHN HKKGEKGKNK ACQQTAQPGA AQGGCAFDGA SIALVPITDV
     AHLVHGPIAC SGNSWGSRGS LSSGPMIYKM GFTTDLSEND IIFGGEKKLY KAIQEVKSRY
     SPAAVFVYLT CVTALIGDDL EAVCQAASEK FDIPVVPVTS PGFVGSKNLG NRIGGEALLE
     YVLGTREPEY TTPYDINLIG EYNIAGEMWG VLPLLEKLGV RVLSKITGDA RYHEVACAHR
     AKLNVMICSK ALINMAHKME TRYGIPYIEE SIYGVEDVNH LLRNVAARLG DADLQARADD
     LIKAETAKLD QALAPYRQRL KSKRIVLYTG GVKSWSIISA ANDLGIDVVA TSSKKSTEED
     KARIKKLLGK DGIMMDKGNA KKLLEVIAKT NADMLIAGGR NQYTALKARI PFLDINQERH
     HPYAGYVGMI EMAKELDGAL HSPIWKQVRS PAPWQPSVAS LSPSEEPTEE STEKPRAEPT
     KVVARRKAVT VNPLKQSQPL GATLAYLGIK DMMPLMHGSQ GCTAFAKVML VRHFREAIPM
     STTAMSEVTT ILGGEDNIET ALLTLLEKSN PVIVGLCSTG LTETRGDDMR GILKELRDRN
     PKIAALPLAY ASTPDFKGAL QDGYAAAVEA IVRDIPNSDS DNQFDGSEAL SYAVPGLPSQ
     VTVLAGPSLA PGDVQALKDM VKAFGLNPVV LPDLSTSLDG HLIDRNYSGN TSGGTPLNQI
     KALSTSAFTL AVGHSMKLSA EILQQRFGTE FKLFDGLTGL DTVDSFLRTL SDISSRPVPE
     TFRQQRCQLQ DAILDAHFFF NRKRVALALE PDLLHSIAWW LTSVGAEVHA AVTTTKSVLL
     KDLPVDTVTI GDLEDFEELA QGADLLIANS SAKSLAQRLE IPLYRMGFPV FDRLGNGRRC
     SVGYDGTTQL LFDIGNIFME ADEAHTHAQV HAWREGL
//