ID Q9EWF3_STRCO Unreviewed; 1227 AA.
AC Q9EWF3;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN Name=narG3 {ECO:0000313|EMBL:CAD30933.1};
GN OrderedLocusNames=SCO4947 {ECO:0000313|EMBL:CAD30933.1};
GN ORFNames=2SCK31.07 {ECO:0000313|EMBL:CAD30933.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAD30933.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAD30933.1, ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145
RC {ECO:0000313|Proteomes:UP000001973};
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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; AL939122; CAD30933.1; -; Genomic_DNA.
DR RefSeq; NP_629099.1; NC_003888.3.
DR AlphaFoldDB; Q9EWF3; -.
DR STRING; 100226.gene:17762596; -.
DR PaxDb; 100226-SCO4947; -.
DR PATRIC; fig|100226.15.peg.5027; -.
DR eggNOG; COG5013; Bacteria.
DR HOGENOM; CLU_000422_14_1_11; -.
DR InParanoid; Q9EWF3; -.
DR OrthoDB; 9759518at2; -.
DR PhylomeDB; Q9EWF3; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0009061; P:anaerobic respiration; IBA:GO_Central.
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 Reference proteome {ECO:0000313|Proteomes:UP000001973}.
FT DOMAIN 46..110
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1227 AA; 135064 MW; 68FE936C17D4DB6F CRC64;
MADAADRLLK AGQLLRRSPT TLDLRAVYRT DQNVNDRPYR ERWAHDKVVR STHGVNCTGS
CSWKVYVKDG LITWETQQTD YPSVGPDRPE YEPRGCPRGA SFSWYTYSPT RVRHPLARGV
LVEMYRDAKR RHGGDPVAAW AELTSDPEKR RRYQSARGRG GFVRVDWDEA LEIAAAAQVH
TIAEYGPDRV AGFSPIPAMS MASHAVGARY HSLIGAPMIS FYDWYADLPI ASPQVFGDQT
DVPESGDWWD AAYLMLWGSN VPVTRTPDAH WMAEARYRGQ KVVVVSPDYA DATKFADEWL
HPHPGTDGAL AMAMGHVLLT EFFVRRQVPY FTDYVKRFTD LPFLVALDEH AAGRWTPGKF
VTAADLGLGR HADAGARAWM PVLIDADTDD VVVPNGTLGD RWGKGGEGRW NLDLGGTDPL
LTLHGHTGGR GDNGVEVVLP RFDEPGATVV RGVPAREIGG RLVTTVYDLL LAQYAVARPG
LAGHWPTGYD DAEQPCTPAW QERLTSVPAE AAVRAAREFA RTAEQTRGRC MIVMGAGTNH
WFHSDTIYRS FLSLLILTGC QGVNGGGWAH YVGQEKVRPY TGWQQLSTAA DWVRPSRQMA
GTPYWYLHTG QWRYESHAAD ALASPTAPGT LAGLHTADLV AQSARLGWMP SYPTFDANPL
DLGRRARESG QEPGDWIAEQ LGSGAVDFAC EDPDAPRNWP RVLTVWRANL IGSSAKGNEY
FLRHLLGARD GATSSEAPPE HRPRSVAWRD DAPEGKLDLL LSLDFRMTST TLFSDLVLPA
ATWYEKHDLS STDMHPFVHA FSPAINPPWQ ARTDFEIFHS LARRLSELAA GRLGTAHDLV
ATALQHDTPG ETAQPGGRVT DWRDGRTPIE PGRNAPQVSL VERDYTAVAD RLAAFGPLAE
EHGMTVKGVT VNPHEESRWL AARCGTAPAG PARGRPLLDT DVKFCEAILA LSGTTNGRLA
AEGFDRLADR VGPGAGLAEL AASVGERRVV FSDTQERPVQ VGASFEWSGK EAPDRRYSPF
TVNTEHKKPW HTLTGRQHFY VDHDWMAELG EQLPVYRPPL NLAELGDAPI PTGDGRAVTV
RYLTPHAKWS IHSEYQENLL MQTLARGGPV VWMSPADADA IGAADNDWVE AVNAHGVVVA
RAIVSHRVPD GTVLMYHVQE RLVNVPKSEA NGRRGGVHNS LTKLLVKPTH LIGGYGQLSF
APNYYGPTGN QRDAVTTIRR RSQEVTY
//
