ID C3KR82_SINFN Unreviewed; 885 AA.
AC C3KR82;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Assimilatory nitrate reductase {ECO:0000313|EMBL:ACP22590.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:ACP22590.1};
GN Name=narB {ECO:0000313|EMBL:ACP22590.1};
GN OrderedLocusNames=NGR_b11370 {ECO:0000313|EMBL:ACP22590.1};
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234b {ECO:0000313|Proteomes:UP000001054}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP22590.1, ECO:0000313|Proteomes:UP000001054};
RN [1] {ECO:0000313|Proteomes:UP000001054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX PubMed=14702322; DOI=10.1128/JB.186.2.535-542.2004;
RA Streit W.R., Schmitz R.A., Perret X., Staehelin C., Deakin W.J., Raasch C.,
RA Liesegang H., Broughton W.J.;
RT "An evolutionary hot spot: the pNGR234b replicon of Rhizobium sp. strain
RT NGR234.";
RL J. Bacteriol. 186:535-542(2004).
RN [2] {ECO:0000313|EMBL:ACP22590.1, ECO:0000313|Proteomes:UP000001054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
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 -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
CC {ECO:0000256|ARBA:ARBA00008747}.
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DR EMBL; CP000874; ACP22590.1; -; Genomic_DNA.
DR RefSeq; WP_015887235.1; NC_012586.1.
DR RefSeq; YP_002823343.1; NC_012586.1.
DR AlphaFoldDB; C3KR82; -.
DR KEGG; rhi:NGR_b11370; -.
DR PATRIC; fig|394.7.peg.1540; -.
DR HOGENOM; CLU_000422_13_4_5; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234b.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR CDD; cd02754; MopB_Nitrate-R-NapA-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACP22590.1}; Plasmid {ECO:0000313|EMBL:ACP22590.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT DOMAIN 2..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 885 AA; 95107 MW; 1C27E98CF857EBBD CRC64;
MAHEVKTTCP YCGVGCGVIA RVSDDGAVSV KGDPEHPANF GRLCSKGAAL AETLDLDGRL
LHPEIGGRRA GWDEALDLVA EKFSQSIAEH GPDSVALYVS GQLLTEDYYL ANKLMKGFIG
SANIDTNSRL CMSSSVAGHR RAFGSDTVPG SYEDLELADL VILTGSNMAW CHPVLYQRLA
AAKANRPEMQ VVVIDPRRTM TADIADMHLA IAPDGDVALF NGLLVHLAES GAIGWDYVSA
NTNGFAEALQ AASGLDLPAL SDATGLAQKQ LREFFRLFEA TEKVVTCYSQ GVNQSSAGTD
KVNAILNCHL AAGRIGRPGM GPFSLTGQPN AMGGREVGGL ANMLAAHLDI EKSVDRDLVR
RFWGAPAVAS KPGLKAVDMF RAVADGRIKA LWIMATNPVV SMPDADAVEA AIKACPFVVV
SEMQRQTDTA RHAHVALPSL GWGEKDGTVT NSERRISRQR AFLAAPGEAR ADWWQLAEVA
RRMGFQEAFR HSSQSEIFAE HAALSGFEND GRRDFDISAH AVIETAAYDA LAPFQWPQPK
DKAPQERRFF AEGGFYHADG RARFIAVQAP QPRRVDAAFP YTLNTGRVRD HWHTMTRSGK
SARLSSHLAE PFVEIHPRDA QTIGVSDADL VTIESPLGAA IVRALVTDRQ AEGNLFVPMH
WNDQFASKAR IDALVAPLTD PFSGQPASKN VAVRAKRFSA KTYGFAVSAT KPEGLDAAYW
AVAKAEGGWR MELAQTDVDG DWIDWCRKAF SIPAEIDPIG YTDRTSGEFR LAFFDGERLL
AALFLSPRPV AVARNWAVSQ LSASHANLSK RFAVAAGRPG ADKPDPGATV CSCFSVGVNQ
ITAAIREGCH SVEAVGQKTS AGTNCGSCRS EIRGIIHACL AAAAE
//
