ID A0A3Q9QVX6_9BACI Unreviewed; 1226 AA.
AC A0A3Q9QVX6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=CHR53_17895 {ECO:0000313|EMBL:AZU62972.1};
OS Neobacillus mesonae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1193713 {ECO:0000313|EMBL:AZU62972.1, ECO:0000313|Proteomes:UP000282892};
RN [1] {ECO:0000313|EMBL:AZU62972.1, ECO:0000313|Proteomes:UP000282892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H20-5 {ECO:0000313|EMBL:AZU62972.1,
RC ECO:0000313|Proteomes:UP000282892};
RA Kim S.Y., Song H., Sang M.K., Weon H.-Y., Song J.;
RT "The complete genome sequence of Bacillus mesonae strain H20-5, an
RT efficient strain improving plant abiotic stress resistance.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + nitrate = a quinone + H2O + nitrite;
CC Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301,
CC ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001854};
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP022572; AZU62972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q9QVX6; -.
DR STRING; 1193713.GCA_001636315_00414; -.
DR KEGG; nmk:CHR53_17895; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000282892; Chromosome.
DR GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:InterPro.
DR GO; GO:0042126; P:nitrate metabolic process; IEA:InterPro.
DR CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR CDD; cd02750; MopB_Nitrate-R-NarG-like; 1.
DR Gene3D; 3.40.50.12440; -; 1.
DR Gene3D; 4.10.1200.10; nitrate reductase tail; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-like.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006468; NarG.
DR InterPro; IPR028189; Nitr_red_alph_N.
DR InterPro; IPR044906; Nitr_red_alph_N_sf.
DR NCBIfam; TIGR01580; narG; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR PANTHER; PTHR43105:SF2; RESPIRATORY NITRATE REDUCTASE 2 ALPHA CHAIN; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF14710; Nitr_red_alph_N; 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.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000282892}.
FT DOMAIN 46..110
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1226 AA; 139353 MW; 533B5F82F96FE2FD CRC64;
MEKKKNNLLH SLRHLVRGER INDGWTEENP RPRDWESVYR NRWAHDKVVR STHGVNCTGS
CSWKIHVKDG IITWETQQTD YPSTGDDFPE YEPRGCPRGA SFSWYTYSPT RVKHPYVRGD
LYALWQDELK KTNNPVQAWE NIVSDPKKRE RYVKARGKGG FVRGTWKEIC QMIAAASIYT
IKKYGPDRIA GFSPIPAMSM VSYSGGTRFL SLIGGTILSF YDWYADLPPA SPQVWGDQTD
VPESGDWYNS KYFIIWGTNI PQTRTPDAHF MVESRYNGTK VVGVSPDYAE YEKFADMWLP
AKAGTDGALA MAMTHVILKE FYVDKETPYF IEYVKKYTDL PYLIILDKKN GKFRSDRFLR
ASDFSDQHSL GEWKTIVWDE NSKGLVIPNG SQGFRWDGTS QWNLDLTAAD GSEINPLLSF
LELKDDVAMV EFPYFAKKEG GTIERAVPIK YFKDKSGEEL AVTTVFDLML AHTGITRGLK
GEYPADYNDA DKPYTPAWQE SITGVKKEHV IQVAREFAEN AALTKGKSMI AMGGGTNHWF
HSDQIYRSIL NLVLLTGSQG VNGGGWAHYV GQEKVRPLEG FSQIAFANDW VKAPRFMNGT
SFFYFATEQF RYEYDFNDSQ TDWGSQYAKM HPADFNALSA RLGWLPSFPQ LSQNSLDVLK
EARAKNSDDQ AVTAFIAKQL TEGKLDFAIE NPNDPRNFPR VFFNWRSNLL GDSGKGHEYF
VKHLIGGTDS VLTNSDNSWQ PENVNISEIP PEGKTDLFVS MDFRMTSSGL FSDIILPAAT
WYEKFDISST DLHPFVHPFN AAISPPWETR SDWDAFREIA KTFSELAKEH LPPQEDLVMS
PLAHDTINEI AQPFGKVMDW RKGEIEGIPG KTMPNFNFVN RDYPHVYDMW ITVGPNIKNG
YGTKGVRIPG EKVYKELLDR LGPSKREGIG KGMPDLYSDK KAINAILLMS GATNGKRAVE
GWKSMEEKTG KKLGHISEGR EEEDYTLDAL TVQPRQAIST PVWSGLENDN RRYSPFTVNK
EFHIPWHTLT GRQSFYLDHE VMLDYGEGLP LYIPPINKGP FIKGESEIEN SGKSITLRYM
TPHQKWGIHT MFTDTTNMVQ LFRGWQVVWM NEKDAASIGI KDNDWIEVYN RNGVVTARAV
LTYRMPPGAV YMHHAQDRTM GVPGNTINKV RGGTHNSVTR IYPKATHMIG GYSQLSYGFN
YYGPTGSQRD TLAIIRPMKE VDWLEN
//
