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Database: UniProt
Entry: A0A095TDV4_9GAMM
LinkDB: A0A095TDV4_9GAMM
Original site: A0A095TDV4_9GAMM 
ID   A0A095TDV4_9GAMM        Unreviewed;      1245 AA.
AC   A0A095TDV4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
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:KGD74897.1};
GN   ORFNames=HA49_06305 {ECO:0000313|EMBL:KGD74897.1};
OS   Tatumella morbirosei.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Tatumella.
OX   NCBI_TaxID=642227 {ECO:0000313|EMBL:KGD74897.1, ECO:0000313|Proteomes:UP000029577};
RN   [1] {ECO:0000313|EMBL:KGD74897.1, ECO:0000313|Proteomes:UP000029577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 23360 {ECO:0000313|EMBL:KGD74897.1,
RC   ECO:0000313|Proteomes:UP000029577};
RA   Smits T.H., Palmer M., Venter S.N., Duffy B., Steenkamp E.T., Chan W.Y.,
RA   Coutinho T.A., Coetzee M.P., De Maayer P.;
RT   "The draft genome of the Tatumella morbirosei type strain, LMG23360T
RT   isolated from pineapple rot.";
RL   Submitted (DEC-2014) 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:KGD74897.1}.
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DR   EMBL; JPKR02000004; KGD74897.1; -; Genomic_DNA.
DR   RefSeq; WP_038017977.1; NZ_JPKR02000004.1.
DR   AlphaFoldDB; A0A095TDV4; -.
DR   STRING; 642227.HA49_06305; -.
DR   eggNOG; COG5013; Bacteria.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000029577; 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.
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:UP000029577}.
FT   DOMAIN          43..107
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1245 AA;  140656 MW;  8246E529D2B193B3 CRC64;
     MSKLLDKLRY FKQKEGTFSQ EHGQMMNSNR DWEDGYRQRW QHDKIVRSTH GVNCTGSCSW
     KIYVKNGLVT WETQQTDYPR TRADLPNHEP RGCPRGASYS WYIYSANRLK YPLVRKQLIR
     LWREALQQHS DPVMAWDSIV NDEAKSASYK QARGRGGFVR SDWNELNQLI AAANIWTVKN
     YGPDRVAGFS PIPAMSMVSY AAGTRYLSLM GGTCLSFYDW YCDLPPASPM TWGEQTDVPE
     SADWYNSAYI IAWGSNVPQT RTPDAHFFTE VRYKGTKTVA ITPDYAEVAK LSDHWLAPKQ
     GTDAALAMAM GHVILKEFHI TNPSDYFLNY CRRYTDMPML VLLEHTSEGY YRPGRLLRAA
     DLPENLGETN NPDWKTVAFN QQGQLVIPNG SAGFRWGQQG KWNLEARAAD QDQELRLTMA
     DGYDDLCGVA FPYFGGQESP HFRHVKQSPI LIHTLPVRQI TLADGRQGQV VSVYDLTLAN
     YGVERGFGDE QSAASYDELK ACTPAWAEQI CGVPRQQIIR IAREFADTAH KTHGRSMIIV
     GAGMNHWYHM DMNYRGLMNM LIFCGCVGQT GGGWAHYVGQ EKLRPQTGWQ PLAFALDWAR
     PPRHMNSTSF FYNHSGQWRY EKLTVKELLS PLANPDEFTG QLIDFNVRAE RMGWLPSSPQ
     LNTNPLNIAQ HAKTAGLSPV DYTVEALQNG KLRFASEQPD SGSNHPRNLF VWRSNLLGSS
     AKGHEYMLRY LLGIEHGIQG SETVAVPGMS PEEVDWQTKA REGKLDLLVT LDFRMSSTCL
     FSDIVLPTAT WYEKDDMNTS DMHPFIHPLS AAVDPVWESR SDWDIYKGIA KTFSALCPGH
     LGVESDVVLL PIQHDSPAEL AQPYEVKQWH KGECALQPGK NAPHIMVVER DYPALSERFG
     SVGPLLEKLG NGGKGISWNT EKEVELLRQL NHRCDSGAGK GQPQLNTAID AAEMILALAP
     ETNGQVAVKA WQALGKITGR DHTHLAMPKQ DEKIRFRDIQ AQPRKIISSP TWSGLEDEHV
     SYNACYTNVH ELIPWRTLTG RQQLYQDHPW MRAFGESLVS YRPPVNTRSV EQLSHIPSNG
     YPEKTLNFLT PHQKWGIHST YSENLLMLTL SRGGPIVWMS EQDAQEMGIR DNDWIEAFNS
     NGALTARAVV SQRVPAGMTM MYHAQERITN IPGSEVTGMR GGIHNSVTRI SPKPTHMIGG
     YVHQCYGFNY YGTVGSNRDE FIIVRKMKNI SWLDDEGRDQ IQEAE
//
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