ID A0A0B5DSV8_9ACTN Unreviewed; 1242 AA.
AC A0A0B5DSV8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=BJY54_006635 {ECO:0000313|EMBL:MBB4796023.1}, CP978_33905
GN {ECO:0000313|EMBL:QEV42873.1}, SNOD_33670
GN {ECO:0000313|EMBL:AJE44385.1};
OS Streptomyces nodosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=40318 {ECO:0000313|EMBL:AJE44385.1, ECO:0000313|Proteomes:UP000031526};
RN [1] {ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|Proteomes:UP000031526};
RA Sweeney P., Stephens N., Murphy C., Caffrey P.;
RT "Sequence of the Streptomyces nodosus genome.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AJE44385.1, ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:AJE44385.1,
RC ECO:0000313|Proteomes:UP000031526};
RX PubMed=26497174;
RA Sweeney P., Murphy C.D., Caffrey P.;
RT "Exploiting the genome sequence of Streptomyces nodosus for enhanced
RT antibiotic production.";
RL Appl. Microbiol. Biotechnol. 100:1285-1295(2016).
RN [3] {ECO:0000313|EMBL:QEV42873.1, ECO:0000313|Proteomes:UP000325763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:QEV42873.1,
RC ECO:0000313|Proteomes:UP000325763};
RA Lee N., Cho B.-K.;
RT "Streptomyces genome completion.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:MBB4796023.1, ECO:0000313|Proteomes:UP000544950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40109 {ECO:0000313|EMBL:MBB4796023.1,
RC ECO:0000313|Proteomes:UP000544950};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) 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 -!- 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; CP009313; AJE44385.1; -; Genomic_DNA.
DR EMBL; JACHMR010000001; MBB4796023.1; -; Genomic_DNA.
DR EMBL; CP023747; QEV42873.1; -; Genomic_DNA.
DR RefSeq; WP_043447479.1; NZ_JACHMR010000001.1.
DR STRING; 40318.SNOD_33670; -.
DR KEGG; snq:CP978_33905; -.
DR HOGENOM; CLU_000422_14_1_11; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000031526; Chromosome.
DR Proteomes; UP000325763; Chromosome.
DR Proteomes; UP000544950; Unassembled WGS sequence.
DR GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; 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.
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:MBB4796023.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031526}.
FT DOMAIN 57..121
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1242 AA; 137712 MW; E6FB2B223B870D69 CRC64;
MENDESARPS QRRAGQGWPL AARRLLTRRE VSADGRAVFG EGDPKWEGFY RDRWAHDRVV
RSTHGVNCTG SCSWMVYVKD GIITWEHQAT DYPSIGTDCP EYEPRGCPRG ASFSWYTYSP
SRVRYPYVRG ALLELWREAR RRLGDPVAAW AEIAGDPVKA RAYKRARGKG GLVRADWDEV
AELVAAAQVH TIKAYGPDRV AGFSPIPAMS MASFAAGSRF MSLIGGTLLS FYDWYADLPV
ASPQVFGDQT DVPEAADWWN AGYLIMWGSN IPVTRTPDAH FLTETRYNGT KVVAVSPDYA
DNVKFADEWL APHPGTDGAL AMAMGHVILR EFLVDHEVPY FRDYLRTYTD APFLVTLRDG
AHGLVPDGFL TAADLGREAE GDTESAETTE NAEFKTVLLD RATGEPVVPG GSLGFRWDKA
GQGRWNLDLG DVVPELSLLE SAEDLVRVAL PRFDEGATEG GSVMVRGVPV RRVGGRLVTT
VFDLMLAQYG VARPGLPGVW PLGYDDASQP YTPAWQETVT SVPAEQAARI AREFARNAER
TNGRSMIAMG AGTNHWFHSD TIYRAFLALT TMTGCQGVNG GGWAHYVGQE KVRPLTGFQH
LAFAFDWQRP TRHMTGTSYW YLNTDQWRYE AFGPEELASP LGAGRFRGKA FADCLAQAVR
LGWTPGHPGF DRNPLDLADE AAARGRGVAE HIVDELKAGR LRFAAEDPDD PANFPRVLTV
WRANLLGSSG KGSEYFLRHL LGADAAVRSA ETPPGERPEE VVWHEEAPEG KLDLLVTMDF
RMTSTGLLSD VVLPAATWYE KDDLSSTDMH PFVHAFTPAI APPWQARTDY DTFLTIADRF
SELAAEHLGT RTDVLAVPLT HDTPDELAQP GGVVRDWKAG ECEPVPGRTM PKLVVVERDY
GAVAQKIRAV GPLLDTLGTT TKGVTVHPDR EIEELRHRCG TVRDGIGAGR PSLATASDMC
EAILALSGTA NGRLATEGFR ELERQTGSKG LVELASEREA ERITFADTRT QPRAVMTSYE
WSGSETGGRR YSPFVINVEH KKPWHTLTGR QHFFVQHDWM AELGEQLPVY RPPLNAIRHY
GDEHLHEDGR AEVTVRYLTP HSKWSIHSEY QDNAYMLALS RGGPVIWMST ADAEKIGVKD
NEWIEAYNRN GVVVARAVVT HRMPEGTVYM YHAKDRTVNV PKTEVSGKRG GIHNSLTRLL
VKPTHLAGGY AQFTYAFNYY GPTGNQRDEV TVIRRRSQQV EY
//
