ID O86717_STRCO Unreviewed; 1231 AA.
AC O86717;
DT 01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 138.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN Name=narG {ECO:0000313|EMBL:CAA20632.1};
GN OrderedLocusNames=SCO6535 {ECO:0000313|EMBL:CAA20632.1};
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:CAA20632.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAA20632.1, 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; AL939128; CAA20632.1; -; Genomic_DNA.
DR PIR; T35227; T35227.
DR RefSeq; NP_630616.1; NC_003888.3.
DR RefSeq; WP_003972444.1; NZ_VNID01000002.1.
DR AlphaFoldDB; O86717; -.
DR STRING; 100226.gene:17764192; -.
DR PaxDb; 100226-SCO6535; -.
DR PATRIC; fig|100226.15.peg.6638; -.
DR eggNOG; COG5013; Bacteria.
DR HOGENOM; CLU_000422_14_1_11; -.
DR InParanoid; O86717; -.
DR OrthoDB; 9759518at2; -.
DR PhylomeDB; O86717; -.
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 53..117
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1231 AA; 135896 MW; F9695F3FDB08E704 CRC64;
MTDTRTPPTE PGAALLRAGR FFRPGTAAPD LHSVGLVGGR ESDAFYRDRW SHDKVVTSTH
GVNCTGSCRW NVFVKDGIIT WETQATDYPS VGPDRPEYEP RGCPRGAAFS WYTYSPTRVR
YPYVRGVLLE MYREAKARLT DPVLAWADIQ GDPQRRQRYQ RARGKGGLVR ASWDEAVEMV
AAAHVHTIRT HGPDRIAGFS PIPAMSMVSH AAGARFHSLI GAPMLSFYDW YADLPVASPQ
VFGDQTDVPE SGDWWDAAYL IMWGTNVPVT RTPDAHWMAE ARYRGQKVVV VSPDYADNTK
FADQWLHPHP GTDAALAMAM GHVVLKEFFV DRVTPFFDDY VRRFTDLPFL VTLTERDGAY
VPDKFLRAAD LGQGGDDAYW KTVVLDEATG RAVVPNGSLG FRWNEADQGK WNLDLGDVRP
RLSLHGHEMA SGVEVLLPRF DTEGGTHGQG RGDVLRRGVP ATRLGGATGP LVTTVFDLML
AQYGVTRPDL PGDWPASYED ADAPATPAWQ ETHTSVPAAA CVRIAREFAR TAERSKGRCM
ILMGAGTNHW FHSETIYRGF LALLQLTGCQ GRNGGGWAHY VGQEKCRPVT GWASLAAASD
WSRPPRQAIG TGYWYLHTDQ WRYDRFRADV LASPLGEGRL AGMAGADCLA LSARTGWMPS
YPTFDRNPLE LGETFGDPVA NAVAELRAGT LRFAGEDPDA PENWPRIVTL WRANLLGSSG
KGAEYFTKHL LGTQSSLRAE EAAPGERPRD VVWHEEAPEG KADLLLSLDF RHTSSTLLSD
VVLPAATWYE KHDLSSTDMH PYVHAFSPAV NPPWQARTDF DTFKVLAEKL SELAEDHLGV
RKDLVAAPLQ HDTPGEIAQP GGVVRDWRRG ECEPEPGKTM PNLVVVERDY TAIGAKFAAL
GPLVETKGLP AKGITLKPDE EVARLRELNG AVRGGPADGR PALDTAVKAA NTILALSGTT
NGRLATQGFH TLEAKTGQEM AHLAAEHEGK RITYADTQAA PVPVITSPEW SGSEAGGRRY
TAFTLNTEHL KPWHTLTGRQ HFFVDHDWMH ELGEALPVYR PPLDMHRLFG EPRLGPDGHR
EVTVRYLTPH NKWSIHSEYQ DNLFMLALSR GGQTIWMSAE DAAAIGVADD DWIEAVNRNG
VVVARAIVSH RMPPGTVFMH HAQERTVNVP LTETTGKRGG VHNSLTRLLL KPTHLIGGYA
QLSWAFNYLG PTGNQRDEVT VIRRRSQEVE Y
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