ID A0A1Q4VWD1_9ACTN Unreviewed; 1242 AA.
AC A0A1Q4VWD1;
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=A6A06_13715 {ECO:0000313|EMBL:OKI02134.1};
OS Streptomyces sp. CB02923.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718985 {ECO:0000313|EMBL:OKI02134.1, ECO:0000313|Proteomes:UP000185893};
RN [1] {ECO:0000313|EMBL:OKI02134.1, ECO:0000313|Proteomes:UP000185893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02923 {ECO:0000313|EMBL:OKI02134.1,
RC ECO:0000313|Proteomes:UP000185893};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKI02134.1}.
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; LWKZ01000023; OKI02134.1; -; Genomic_DNA.
DR RefSeq; WP_073762726.1; NZ_LWKZ01000023.1.
DR AlphaFoldDB; A0A1Q4VWD1; -.
DR STRING; 1718985.A6A06_13715; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000185893; 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:UP000185893}.
FT DOMAIN 57..121
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1242 AA; 136448 MW; F2C429D8B7C8F2A7 CRC64;
MWRGRAKAER AAADAAERLM AAGRLLSRAP VSADGRAVFR TDQSVNDAPY RERWAHDKVV
RSTHGVNCTG SCSWQVFVKD GLITWETQAT DYPTTGPDRP EYEPRGCPRG ASFSWYTYSP
TRVRHPYARG VLVEMYREER ERLGDPVAAW AEVTGDPDKR RRYQRARGKG GLVRIGWDEA
LEIAAAAHVH TIRTHGPDRV AGFSPIPAMS MASHAVGARF MALLGAPMLS FYDWYADLPI
ASPQVFGDQT DVPESGDWWD AAYLMLWGSN VPVTRTPDAH WMAEARYRGQ KVVVVSPDYA
DATKFADEWL HPHPGTDGAL AMAMGHVILR ECFVDRQVPY FTDYVKRFTD LPFLVELEEY
GTGGAGAEGG AARVPGRFVT AQDVGAATDA DAEARRWMPV LVDAVTGGPV VPGGTLGDRW
REGGEGRWNL DLGEVDPQLS LYGRPDATAA RVVLPRFDQE QGTPEREQST PEWEQGTLER
EVPALRVGGR LVTTVFDLLL AQYGVGRAGL GGQWPGSYED ADVPCTPAWQ ETLTSVSARA
AVRAAREFAR TAEQTRGRCM IVMGAGTNHW FHSDTIYRSF LSLLLLTGCQ GVNGGGWAHY
VGQEKVRPYA GWQQLSTAAD WVRPSRQMAS TPYWYLHTGQ WRYDRAPADA LASPVGRGLF
ARQHTADLVA RSARRGWMPS YPTFDANPLD LGRRVRRAGA EPGRWVADEL DAGRLSYACE
DPDAPANWPR VLTVWRANLI GSSAKGNEYF LGHLLGADDD AGAQEAPPEV RPRDVTWREQ
APRGKLDLLL ALDFRMTSTT LFADLVLPAA TWYEKHDLSS TDMHPYVHAF SPAIDPPWQA
RTDFEIFHGL AREVSRLAAG RLDDACDLVA TALQHDTAAG EAPPPGPTGP RFTLVERDYG
ALADRLAALG PLPREQGMTV KGVTVHAGPE TDWLAARCGT AAGGAARGRP LLDTDVKLCE
AILALSGTTN GRLAAEGFRA LAGRCGTGRG LEELAASVAE RRIVFSDTQA RPVQVSASFE
WSGKEAPERR YAPFTVNTEH GKPWHTLTGR QHFYLDHEWI AEFGEQLPVY RPPLDLTALG
ELPRPGASAE RSVTVRYVTP HSKWSIHSEF QENLLMQTLA RGGPVIWMSV ADAEAVGVTD
NDWIEAVNAN GVVVARAVVS HRMPPGTVFM YHVQERLVNV PLSQTTGRRG GVNNALTRLL
IKPTHLIGGH AQLSFAPNYY GPTGNQRDAV TTIRRRSQEV SY
//
