ID B7MUQ2_ECO81 Unreviewed; 1246 AA.
AC B7MUQ2;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN Name=narZ {ECO:0000313|EMBL:CAR07818.2};
GN OrderedLocusNames=ECED1_1621 {ECO:0000313|EMBL:CAR07818.2};
OS Escherichia coli O81 (strain ED1a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585397 {ECO:0000313|EMBL:CAR07818.2, ECO:0000313|Proteomes:UP000000748};
RN [1] {ECO:0000313|Proteomes:UP000000748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED1a {ECO:0000313|Proteomes:UP000000748};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU928162; CAR07818.2; -; Genomic_DNA.
DR RefSeq; WP_012601497.1; NC_011745.1.
DR AlphaFoldDB; B7MUQ2; -.
DR KEGG; ecq:ECED1_1621; -.
DR HOGENOM; CLU_000422_14_1_6; -.
DR Proteomes; UP000000748; 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:0045333; P:cellular respiration; IEA:UniProt.
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.
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 Oxidoreductase {ECO:0000313|EMBL:CAR07818.2}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1246 AA; 140124 MW; 8F33A0C492ACB7C9 CRC64;
MSKLLDRFRY FKQKGETFAD GHGQVMHSNR DWEDSYRQRW QFDKIVRSTH GVNCTGSCSW
KIYVKNGLVT WEIQQTDYPR TRPDLPNHEP RGCPRGASYS WYLYSANRLK YPLIRKRLIE
LWREALKQHS DPVLAWASIM NDPQKSLSYK QVRGRGGFIR SNWQELNQLI AAANVWTIKT
YGPDRVAGFS PIPAMSMVSY AAGTRYLSLL GGTCLSFYDW YCDLPPASPM TWGEQTDVPE
SADWYNSSYI IAWGSNVPQT RTPDAHFFTE VRYKGTKTIA ITPDYSEVAK LCDQWLAPKQ
GTDSALAMAM GHVILKEFHL DNPSDYFINY CRRYSDMPML VMLEPRDDGS YVPGRMIRAS
DLVDGLGESN NPQWKTVAVN TAGELVVPNG SIGFRWGEKG KWNLESIAAG TETELSLTLL
GQHDAVAGVA FPYFGGIENP HFRSVKHNPV LVRQLPVKNL TLADGSTCPV VSVYDLVLAN
YGLDRGLEDE NSAKDYAEIK PYTPAWGEQI TGVPRQYIET IAREFADTAH KTHGRSMIIL
GAGVNHWYHM DMNYRGMINM LIFCGCVGQS GGGWAHYVGQ EKLRPQTGWL PLAFALDWNR
PPRQMNSTSF FYNHSSQWRY EKVSAQELLS PLADASKYSG HLIDFNVRAE RMGWLPSAPQ
LGRNPLGIKA EADKAGLSPT EFTAQALKSG DLRMACEQPD SGSNHPRNLF VWRSNLLGSS
GKGHEYMQKY LLGTESGIQG QELGASDGIK PEEVEWQTAA IEGKLDLLVT LDFRMSSTCL
FSDIVLPTAT WYEKDDMNTS DMHPFIHPLS AAVDPAWESR SDWEIYKGIA KAFSQLCVGH
LGKETDVVLQ PLLHDSPAEL SQPCEVLDWR KGECDLIPGK TAPNIVAVER DYPATYERFT
SLGPLMDKLG NGGKGISWNT QDEIDFLGKL NYTKRDGPAQ GRPLIDTAID ASEVILALAP
ETNGHVAVKA WQALGEITGR EHTHLALHKE DEKIRFRDIQ AQPRKIISSP TWSGLESDHV
SYNAGYTNVH ELIPWRTLSG RQQVYQDHPW MRAFGESLVA YRPPIDTRSV SEMRQIPPNG
FPEKALNFLT PHQKWGIHST YSENLLMLTL SRGGPIVWIS ETDARELTIV DNDWVEVFNA
NGALTARAVV SQRVPPGMTM MYHAQERIMN IPGSEVTGMR GGIHNSVTRV CPKPTHMIGG
YAQLAWGFNY YGTVGSNRDE FIMIRKMKNV NWLDDEGRDQ VQEAKK
//
