ID A0A1I1VAQ5_9BACI Unreviewed; 1231 AA.
AC A0A1I1VAQ5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=SAMN05216238_10431 {ECO:0000313|EMBL:SFD77510.1};
OS Lentibacillus persicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX NCBI_TaxID=640948 {ECO:0000313|EMBL:SFD77510.1, ECO:0000313|Proteomes:UP000199474};
RN [1] {ECO:0000313|EMBL:SFD77510.1, ECO:0000313|Proteomes:UP000199474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22530 {ECO:0000313|EMBL:SFD77510.1,
RC ECO:0000313|Proteomes:UP000199474};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; FOMR01000004; SFD77510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1VAQ5; -.
DR STRING; 640948.SAMN05216238_10431; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000199474; Unassembled WGS sequence.
DR GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006468; NarG.
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 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 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}.
FT DOMAIN 45..109
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1231 AA; 139995 MW; A33F6FC571DAB8F0 CRC64;
MRSSNKLFDK LKHIKSGNKL NEGWTEESPR PRDSEDIYRR RWQHDKIVRS THGVNCTGSC
SWKIYVKDGI ITSETQQTDY PSTGDDFPEY EPRGCPRGAS FSWYTYSPIR VKYPYVRSDL
YELWKEERNN HKDPVEAWEN IVSSPEKREQ YVRARGKGGF VRATWRDMSE MIASATIQTI
RKYGPDRVAG FSPIPAMSMI SYSSGTRFLS LIGGTILSFY DWYADLPPAS PQVWGEQTDV
PESADWYNSK YFIIWGTNLP QTRTPDAHFM VEARYNGTKV VGVSPDYAEY EKFADIWLPA
KAGTDAALAM AMTHVILKEF YVNRETPYFT SYAKKFTDLP YLVTLNEHGE EYRSDRFLRA
SDINNDQTLG EWKTLVWDAQ TDHLETPNGS MGFRWDGGRK WNLELDKEDG STIDPELSFI
EKSDETVMVS FPYFAEQDGD IVKRGVPVRH VQNASGETVK VTTVYDLMMA HTGVGRGLEG
DYPADYDDPK PYTPAWQESI TGVNKNHVIK VAKEFADNAE RTNGKSMIAM GGGTNHWYHS
DQIYRAILNL VLLTGSQGVN GGGWAHYVGQ EKVRPQEGWQ QVAFAGDWQK PPRHQNGTSY
FYFITDQFRY ESIPEEPEET EWGSKYNSMH PADLNALSAR LGWLPSYPQF SQNSIDLVKE
SRERGAQTEQ EIIDDVVGQI KQEKIDWAIE NPDDPRNFPR VFFNWRSNLL GDSGKGHEFF
VKHLVGGDNQ VLAEPENSWQ PETINTEGEA PTGKADLLVS VDFRMTSSGL FSDIVLPAAT
WYEKNDISST DLHPFVHPFN AAISPPWEAK SDWNTFREIS KVFSELSEKH LPATEELVMS
PLAHDSPGEI AQAYGKIKDW RKGEVEAIPG KTMPSFKLVE RDYPNVYQKM TTIGPLIKNG
YGGKGVTIPG EEVYQDLEKR LGTSRREGIG KGRPDLYNDE QAINAILAMS GATNGKRAVA
GWKSLEEKTG QKLEDIAKPR AEEDHTLRDL SIQPRNAIST PVWSGLEKDH RRYSPFTVNT
EYNIPWRTLT GRQSFYVDHE MMLDYGEGLP LYLPPLRYGP FLKKEEGVAE NDNKSITVRY
LTPHQKWGIH TMFTDTTAMS QLFRGWQTIW MNEDDAHSID LKDNDFVEVY NRNGAIAARV
VVTYRIPKGM AYMYHAQDRT LGVPATSIEK DGGKRRGGTH NSVTRVTLKG THMIGGYSQL
SYGFNYYGPT GHQRDTIAVI RALKEVDWLE N
//
