ID D6KGS4_9ACTN Unreviewed; 1234 AA.
AC D6KGS4;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=SSTG_06150 {ECO:0000313|EMBL:EFF88194.2};
OS Streptomyces sp. e14.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=645465 {ECO:0000313|EMBL:EFF88194.2, ECO:0000313|Proteomes:UP000004704};
RN [1] {ECO:0000313|EMBL:EFF88194.2, ECO:0000313|Proteomes:UP000004704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=e14 {ECO:0000313|Proteomes:UP000004704};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces sp. strain e14.";
RL Submitted (OCT-2009) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG753633; EFF88194.2; -; Genomic_DNA.
DR AlphaFoldDB; D6KGS4; -.
DR STRING; 645465.SSTG_06150; -.
DR eggNOG; COG5013; Bacteria.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000004704; 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:0042126; P:nitrate metabolic process; IEA:InterPro.
DR CDD; cd02776; MopB_CT_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:UP000004704}.
FT DOMAIN 53..117
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1234 AA; 137652 MW; 7DBF32BAADE2BAB6 CRC64;
MSTSTDRSGE ALDRLMRAAQ YFFPGEQSPD RRVLYREGGR AAEEFYRERW RHDREVRSTH
GVNCTGSCSW RVFVKDGIIT WETQATDYPS VGPDSPEYEP RGCPRGASFS WYTYSPTRIR
YPYVRRPLLQ LWRQARARTD DPVEAWRWLT SDPERCAAYK RARGKGGFVR STWQEVMELI
AAAQVDTVER YGPDRIVGFS PIPAMSIASY SAGTRYLSMI GGTISSFYDW YADLPMASPQ
VFGDQTDVPE SADWWNAGYL IVWGTNLPIT RTPDAHFMTE ARYRGQKVVV VSPDYGDHTK
FADDWLAAAP GTDGALAMAM GHVILTEFYR DRQVPRFTEY AKTYTDLPFL IRLRQRDGGD
GAYVPDKFLT AADLPGAAEE AAEFKTVLLD AATGEPVVPG GSLGFRWTEP EGGPRWNLRL
DGVDPLLSLY GRPGGEAVAV DLPRFDAGPE ESGGAVRRGV PATRIGGHLV TTVFDLVMAQ
YAVGREGLPG RWPTGYDDAD EPCTPAWQEA VTSVPARAAA RVAREFARNA ERTGGRSMIA
MGAGTNHWFH SDQIYRAFLS LTMLTGSQGV NGGGWAHYVG QEKVRPITGW FHLAFGLDWQ
RPTRHMVGTP LFWLATDQWR YEAFPADVLA SPLGRGRLAG RTLPDLNALA ARLGWMPSHP
TFDRNPLDIC DDAQRAGKDV ADHIVDELKA GRLRFAAEDP DDPANFPRVL LIWRANLFAS
SMKGHEYMLR HLLGTDDATT APETPPHLRP KDVTWRDPAP VGKLDLSVAV DFRMTSTCLF
SDVVLPAATW YEKFDLSSTD MHPFVHAFNP AIAPPWQTRS DFDVFHTLAA EFSRLAAGRL
GVRRDVIAAP LAHDTPDELA QPHGVVRDWK AGECEPVPGR TMPRLTVVER DYTKVAEKMA
AVGPLLETLG TATKGVSWHP GEEIEDLRAR NGVVRGGVAD GRPSIARDDQ FCEAVLALSG
TTNGRLAVES LRALEKRTGL RLADLAEERS GDRITFEDTR TQPRAVITSA EWSGTESGGR
RYSPFTVNVE RLKPWHTLTG RQHFFLDHDW MAEFGEQLPV YRPPLNMLAH VGDPRRNPAG
HPELVVRYLT PHSKWSIHSE YQENLHMLTL FRGGPGIWMS PLDAEKIGVA DNDWIEAYNR
NGVVACRAVV THRMPEGTVF MYHTMDRHLN VPRTETSGLH GGGDNSLTRL LIKPTHLIGG
YAQFSYAFNY IGPTGNQRDE ITVVRRRAQE VDFQ
//
