ID A0A1P8YGX2_9NOCA Unreviewed; 1224 AA.
AC A0A1P8YGX2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=BTZ20_2893 {ECO:0000313|EMBL:AQA23374.1};
OS Rhodococcus sp. MTM3W5.2.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1805827 {ECO:0000313|EMBL:AQA23374.1, ECO:0000313|Proteomes:UP000187995};
RN [1] {ECO:0000313|EMBL:AQA23374.1, ECO:0000313|Proteomes:UP000187995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTM3W5.2 {ECO:0000313|EMBL:AQA23374.1,
RC ECO:0000313|Proteomes:UP000187995};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; CP019572; AQA23374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8YGX2; -.
DR STRING; 1805827.BTZ20_2893; -.
DR Proteomes; UP000187995; 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: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 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 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 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 Oxidoreductase {ECO:0000313|EMBL:AQA23374.1}.
FT DOMAIN 47..111
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1224 AA; 135719 MW; 826061604B72202D CRC64;
MGTDLADSLL KFGKHFQRGE ASEDLRTLYQ IGGRSSDEFY RDRMSYDKVV RSTHGVNCTG
SCSWKIYVKD GIITWEAQQT DYPSIGPDKP EYEPRGCPRG ASFSWYTYSP ARVRYPYVRG
VLLEMYRDAK ERLKDPVLAW EDIASDPEKS KRYKSARGKG GFVRAEWWEA AEIVAAAHVH
TIKKYGPDRV AGFSPIPAMS MVSHAVGTRF ISLIGGAMLS FYDWYADLPE ASPQVFGDQT
DVPESADWFD AGYLIMWGSN VPVTRTPDAH YMTEARYRGQ KVVVVSPDYA DNTKFADQWL
PARPGTDGAL AMAMGHVILK EFFVEKNTER FTDYVKKYTD LPYLITLDER GDGYVPGKFL
TAADLGDSAE GAEHKTVLLN AETGETVVPG GSLGHRFTES GKGHWNLDLH GVDPLMTMHE
DPDMATNAVA VDFPRYDTST PGVLRRGVPT RMVAGRRVTT VFDLMLAQYG VGRPDLPGNW
PTGYDDTEEP YTPAWQEGIT GVSAAAAARV AREFADNADR SGGRSMILMG AGTNHWFHSD
QIYRSFLTLT MLTGCQGVNG GGWAHYVGQE KCRPVTGWAT LAFGSDWSRP ARQMQGTIFW
YLATDQWRYD PFTAEVMSSP LANGTFAGRT AADNIALATR LGWMPSYPTF NRNPLDLADE
ADRLGKSAAE HVVDGLKTGH LQFAVEDPDA PENFPRCLTV WRSNLLGSSA KGNEYFLKHL
LGADSNLNAR DSEGIRPEEL IWRDEAPAGK LDLLTTLDFR MTSTTLFSDV VLPAATWYEK
HDLSSTDMHP FVHAFSPAIS PPWETKTDFE AFHRIARGFS WLAEKHLGTR RDIVAMPLIH
DTNDATAQPG GLVLDWKRGE CEPIPGKTMP KIVVVERDYS AIAEKLGALG PLVEELGLTT
KGVTTHPTEE VEYLRGVNGT VQTGVAAGRP SLAKDKHACE AILALSGTTN GRLATQGFEH
LQERTGTELV DLAAENEGTR IRFADTQARP VPVITSPEWS GSETGGRRYS PFTINTERLK
PWHTLTGRQH FYLDHDWMAE LGEQLPIFRP PLDMTALFSE PAVGETHGNG VGGTVTVRYL
TPHSKWSIHS AYQDNLHMLT LSRGGQSIWM SDVDAAKIGV ADNDWIEASN RNGIVVARAI
VSHRMPEGTV FMYHAQDRAV DVPRTERTGK RGGIHNALTR LMIKPSHLIG GYAQQSFAMN
YHGPTGNQRD EVTTIRRRDQ EVTY
//
