ID A0A1G5EC88_9BACL Unreviewed; 1238 AA.
AC A0A1G5EC88;
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=SAMN05720606_103241 {ECO:0000313|EMBL:SCY24576.1};
OS Paenibacillus polysaccharolyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=582692 {ECO:0000313|EMBL:SCY24576.1, ECO:0000313|Proteomes:UP000198538};
RN [1] {ECO:0000313|EMBL:SCY24576.1, ECO:0000313|Proteomes:UP000198538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL9 {ECO:0000313|EMBL:SCY24576.1,
RC ECO:0000313|Proteomes:UP000198538};
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 -!- 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; FMVM01000003; SCY24576.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5EC88; -.
DR STRING; 582692.SAMN05720606_103241; -.
DR Proteomes; UP000198538; Unassembled WGS sequence.
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; PS00490; MOLYBDOPTERIN_PROK_2; 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 46..110
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1238 AA; 140132 MW; 9C1B11F097816D6C CRC64;
MSSKSMPWMG KLKYFAKREK NAEGWSEMSP VNRDWEDVYR RRWQHDKVVR STHGVNCTGS
CSWQIYVKDG IVTWETQATD YPSTGPDMPD FEPRGCPRGA SFSWYLYSPL RVKHPYVRGA
LLEMWREALK THGDPVKAWQ SIANDPVKVK RYKSVRGKGG LVRASWGEVT QIIAASMIHT
IKDYGPDRII GFSPIPAMSM VSYAAGSRFL SLVGSPLLSF YDWYADLPPA SPQIWGDQTD
VPESSDWYNS GYILVWGSNL PMTRTPDAHF LAEARYKGTK VVSISPDYAE YVKFADTWMS
VKQGTDGALA MAMGHIILKE FYLDHPTEYF MSYAKQYTDF PNLLIVEEKD GANIAGRFLL
GEDLGIQGNN MAWKTLVYDE NTASYAIPKG SMGFRWGEEG TWNLKMEQVD TGEPIDPRLS
MLGVHHDLVT VQLPYFDDEG SHVMERQIPV RRIWVDDRWI TVTSVYDLVL AKYGVDREMT
RSADSTEIVA GVVMEAEEDK PFTPAWQEKI TRVDRDTVVQ IAREFAQNAV DTQGRSMIIM
GAGINHWYNS DVIYRAIINL LLMTGCQGVN GGGWAHYVGQ EKLRPAEGWQ TIAFARDWSG
PARLQNGTSF FYFATDQWRY EETKVGELTS ALEGDPRFEH VADYNVMAAR MGWLPSYPQF
NRNSIDLHQD ALDAGAKTNE EIGAYVASEL QNKNLKFSIE QPDDPANFPR VLFVWRANLI
SSSGKGHEYF LKHLLGATNG LLNDDDLGLR PEHVEWLEHA PEGKLDLMVN MDFRMAGTAM
YSDIVLPAAT WYEKSDLSST DMHPFVHPFN PAVATQWESR SDWDTFKEIA RVFSDMAAQQ
FDGPQKEILT TPLLHDSPDE LAQPYGEIKD WSAGECEAIP GKTMPHIHVV ERDYAAVYNK
MISLGPNVKD KPIGTKGISW SATEEYEKLK GILGVNRKDG IGQGCPDLST DRNVAEAILT
LSTTTNGKMA VRAWESLEKK TALHLKDLAE ERSEECFTFD EITSKPKTVI TSPAFSGSEK
GGRRYSPFTT NVERLIPWRT LTGRQQFYID HAMLREFGET LATFKPILKH TPFHPNSKRP
IEGGKEIVLN YMTPHNKWSI HSMYYDAQPM LTLFRGGPTI WMNHEDAEDA GLVDNDWIEC
FNRNGVVVAR AVVTHRIPRG VAFMYHAQDR HINVPGTKIS QTRGGTHNSP TRIHVKPTHM
IGGYAQLSYG FNYYGPTGNQ RDLNVIIRKL QEVDWLED
//
