ID A0A077LJS3_9PSED Unreviewed; 1254 AA.
AC A0A077LJS3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=PSCI_4163 {ECO:0000313|EMBL:BAP44865.1};
OS Pseudomonas sp. StFLB209.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP44865.1, ECO:0000313|Proteomes:UP000031652};
RN [1] {ECO:0000313|EMBL:BAP44865.1, ECO:0000313|Proteomes:UP000031652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StFLB209 {ECO:0000313|EMBL:BAP44865.1,
RC ECO:0000313|Proteomes:UP000031652};
RX PubMed=25323715; DOI=10.1128/genomeA.01037-14;
RA Morohoshi T., Kato T., Someya N., Ikeda T.;
RT "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing Pseudomonas
RT sp. Strain StFLB209, Isolated from Potato Phyllosphere.";
RL Genome Announc. 2:e01037-e01014(2014).
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; AP014637; BAP44865.1; -; Genomic_DNA.
DR RefSeq; WP_045490682.1; NZ_AP014637.1.
DR AlphaFoldDB; A0A077LJS3; -.
DR STRING; 1028989.PSCI_4163; -.
DR KEGG; pses:PSCI_4163; -.
DR HOGENOM; CLU_000422_14_1_6; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000031652; 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.
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:UP000031652}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1254 AA; 140844 MW; A1318A97D2E22C36 CRC64;
MSLFIDRLRY LVKRPPQFAD GHGETRDESR EWEDSYRQRW QFDKIARSTH GVNCTGSCSW
KIYVKNGLVT WETQQTDYPR TRPDLPDHEP RGCPRGASYS WYLYSANRLK YPMVRKVLLQ
LWRDAVAEHK DPVRAWSSIV ENPNKARQYK SIRGRGGFVR ADWDELQTLV AAANVHTIAQ
YGPDRIAGFS PIPAMSMVSY AAGTRYLSLL GGVCLSFYDW YCDLPPASPQ TWGEQTDVPE
SADWYNSGYI IAWGSNVPQT RTPDAHFFTE VRYKGTKTVA ITPDYAEVAK LCDEWMSAKQ
GTDAALAIAM GHVIFKEFHL DNPSAYFTDY IRRYTDMPIL VELEQREDGK LVPGRQLRAS
DFADNLQQAD NPDWKTLAWD QASERLVVPR GSIGFRWGGS GQWNLEPVDA DGQPVTLCLS
LLDRHDEVAR VAFPYFGGIA HEHFPSSPLR EVIYHHVPAK RLRLADGRDV LAVTVFDLTA
ANYGIDRGLQ ASVGGSGDDD GATGYEQARP YTPAWQQAIT GVPAEQVIRI AREFASNADK
TRGRSMIIVG AGINHWYHMD MTYRGLINML ILCGCIGQSG GGWAHYVGQE KLRPQTGWTP
LAFALDWQRP PRQMNSTSFF YNHSSQWRYE KLQVKELLSP LARPEEFTGS LVDCNVRAER
MGWLPSAPQL DRNPLHLAGA AHSAGQSTAD YCVEQLTKGT LRFASEDPDN PKNHPRNLFV
WRSNLLGSSG KGHEYMLKYL LGTRHGLLGK DLGQDGSQKP EEVVWQEQAI EGKLDLLVTL
DFRMSTTCLY SDVVLPTATW YEKDDLNTSD MHPFIHPLTA ATDPAWEARS DWQIYDGIAK
AFSQVCVGHL GEETDLVTLP LQHDSPSELA QAQVLDWKKG ECPPIPGKTM PSLIEVKRNY
PQTWERFSSV GPLLDEIGNG GKGIAWQTAE EVELLGKLNH RKPDGPTEGR PQLASAVDAA
EMILTLAPET NGQVAVKAWA ALSKVTGRDH THLARAKHDE KIRFHDLVAQ PRKIISSPTW
SGLEDEHVSY TANYTNIHEL IPWRTLTGRQ QFYQDHPWMR AFGESLMVYR PPINTKAAAS
VTAPNDNGNP QIALNWLTPH QKWGIHSTYS DNLLMQTLSR GGPIVWLCES DAQAIGVADN
DWIELYNANG AIAARAVVSQ RVRVGTAMMY HAQERILNIP GSEMTGTRGG IHNSVTRACP
KPTHMIGGYA QLSYGFNYYG TVGSNRDEFV IVRKMRDIDW LDGEHNDYRQ EAVK
//
