ID A0A0J5LXM1_PLUGE Unreviewed; 1246 AA.
AC A0A0J5LXM1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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:KMK13285.1};
GN ORFNames=ABW06_13380 {ECO:0000313|EMBL:KMK13285.1};
OS Pluralibacter gergoviae (Enterobacter gergoviae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pluralibacter.
OX NCBI_TaxID=61647 {ECO:0000313|EMBL:KMK13285.1, ECO:0000313|Proteomes:UP000036196};
RN [1] {ECO:0000313|EMBL:KMK13285.1, ECO:0000313|Proteomes:UP000036196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS81F13 {ECO:0000313|EMBL:KMK13285.1,
RC ECO:0000313|Proteomes:UP000036196};
RA Greninger A.L., Miller S.;
RT "Genome sequences of Pluralibacter gergoviae.";
RL Submitted (MAY-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMK13285.1}.
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; LDZF01000012; KMK13285.1; -; Genomic_DNA.
DR RefSeq; WP_048279233.1; NZ_VWRP01000016.1.
DR AlphaFoldDB; A0A0J5LXM1; -.
DR STRING; 61647.LG71_17240; -.
DR PATRIC; fig|61647.15.peg.836; -.
DR eggNOG; COG5013; Bacteria.
DR Proteomes; UP000036196; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000036196}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1246 AA; 139920 MW; 782404F8DC03B420 CRC64;
MSKLLDRFRY FKQKGDSFAN GHGQVYNNNR DWEDSYRQRW QFDKIVRSTH GVNCTGSCSW
KIYVKNGLVT WETQQTDYPR TRPDLPNHEP RGCPRGASYS WYLYSANRLK YPLIRKSLIV
MWREALASHP DPVDAWDALM NDPQKCAQYK AARGHGGFVR SSWQELNPLI AAANVWTIKH
YGPDRVAGFS PIPAMSMVSY AAGTRYLSLI GGTCLSFYDW YCDLPPASPM TWGEQTDVPE
SADWYNSSYI IAWGSNVPQT RTPDAHFFTE VRYKGTKTIA ITPDYSEVAK LCDQWLAPKQ
GTDSALAMAM GHVILKEFHL DNPSDYFLNY CRRYTDMPML VMLEAREDGS YAPGRMLRAS
DLVDGLGETN NPQWKTVALS ADNQLVVPNG AIGFRWGEQG KWNLEAVADG RETELRLSLL
DAHDSVVGVA FPYFGGNENP YFRSVKQEPI LIHRLPAKQL ALADGGSGLV VSVYDLILAN
YGLDRGLDDP LAAKDYDDVK AYSPAWAEQI TGVPRQQICK IAREFADTAH KTHGRSMIIL
GAGVNHWYHM DMNYRGMINM LVFCGCVGQS GGGWAHYVGQ EKLRPQNGWL PLAFALDWNR
PPRQMNSTSF FYNHASQWRY EKLNARELLS PLADPAKFSG HLIDFNVRAE RMGWLPSSPQ
LNRNPLTIKA AADAAGVTPA EYTADALRSG EMRMACEQPD SGNNHPRNLF VWRSNLLGSS
GKGHEYMLRY LLGTACGING EEFGSTEDVK PEEVEWQTAA IEGKLDLLVT LDFRMSSTCL
FSDIVLPTAT WYEKDDMNTS DMHPFIHPLS AAVDPAWEAK SDWEIYKGIA EAFSEVCVGH
LGSETDVVLQ PLLHDSPAEL SQPFEVADWR KGECDYVPGR TGPGIAVVER DYPATYARFT
SLGPLMDKLG NGGKGIAWQT QEEVAFLGKL NYVKQDGPAK GRPRIETAID AAEVILTLAP
ETNGEVAVRA WAAQSKVTGR DHTHLARNKE DEKIRFRDIV AQPRKIISSP TWSGLESEHV
SYNASYTNVH ELIPWRTLTG RQQLYQDHLW MRAFGESLVV YRPPIDTRSV SQMKSVPPNG
FPEKALNFLT PHQKWGIHST YSENLLMLTL SRGGPIVWIS ESDARELGIE DNDWIEVFNA
NGALTARAVV SQRVPPGMTM MYHAQERIMN IPGSEVTGRR GGIHNSVTRI CPKPTHMIGG
YAQLAYGFNY YGTVGSNRDE FIMIRKMKHV NWLDDEGNDQ VQEAKQ
//
