ID S3WWF3_9ACTN Unreviewed; 1242 AA.
AC S3WWF3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=HMPREF1531_02297 {ECO:0000313|EMBL:EPH02979.1};
OS Propionibacterium sp. oral taxon 192 str. F0372.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=1203605 {ECO:0000313|EMBL:EPH02979.1, ECO:0000313|Proteomes:UP000014567};
RN [1] {ECO:0000313|EMBL:EPH02979.1, ECO:0000313|Proteomes:UP000014567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0372 {ECO:0000313|EMBL:EPH02979.1,
RC ECO:0000313|Proteomes:UP000014567};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Kirega A., Socransky S.S.,
RA Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Propionibacterium sp. oral taxon 192 str. F0372.";
RL Submitted (MAY-2013) 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 -!- 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:EPH02979.1}.
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DR EMBL; ATFL01000014; EPH02979.1; -; Genomic_DNA.
DR RefSeq; WP_016670075.1; NZ_KE340297.1.
DR AlphaFoldDB; S3WWF3; -.
DR STRING; 1203605.HMPREF1531_02297; -.
DR PATRIC; fig|1203605.3.peg.2360; -.
DR eggNOG; COG5013; Bacteria.
DR HOGENOM; CLU_000422_14_1_11; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000014567; 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:UP000014567}.
FT DOMAIN 51..115
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1242 AA; 137858 MW; 6D2F1724EFDE7C6E CRC64;
MTETSTSTGG SPLLRMGSWL RRGRASEDTR QIFLEGGRQA DAFYRQRWSH DKVARSTHGV
NCTGSCSWKI YVKDGIITWE SQQTDYPTTG PDMPEYEPRG CPRGAAFSWY EYSPTRIRFP
YVRSVLLDSF REARARLGDP VDAWGEIVSD PVRSRAYKSA RGTGGMVRVS WEEATEIIAA
AYTYTIKTFG PDRIAGFSVI PAMSMISYGA GSRFHELLGG AMLSFYDWYA DLPPASPQVF
GDQTDVPESG DWFNSQFLIM WGSNVPVTRT PDAHFMAEAR YHGQKVVVVS PDFADNTKFA
DDWLRVQPGT DAALAIAMGH VILNEFHVRR RESMFLDYMK RYSDAPFLIE LDSHSRHEAS
GSKPFVPGKF LTAEKMPIGT TARTENAAFR PLVLDVDGRV KDPGGTLADH FGEQGAGHWN
LDLDGVDPVM SLMDTDDWEP VEVLLPRFDL PPSAGEDSIG GGILRRGVPA RRIGGRLVTT
VFDLLLANYA VAREGLPGEW PTGYDDASAP GTPAWQEEFT GVAAGAAERI GREFALNALE
SNGRSMILMG AGTNHYLHSD TIYRTFLALT TMCATQGVNG GGWAHYVGQE KVRPITGWAS
YAFALDWHRP ARQMIATGWY YLTTDQWRYD GARADQLASP LGAGKLAGKT TADTLVESAK
RGWMPSYPTF DRSPLVLGDE ARAAGKTPAE YVAEELTAGR LHFAAEDPDA EGNIPRILAN
WRTNLLGSSA KGTEFFLRHM LGANNDVNAE ELAEGRRPST MVWRDETPRG KLDLMWTADF
RNTSTTLHSD IVLPAATWYE KNDLSSTDMH PFVHPFTVAI EPPWEARSDF ETYQTLARLI
SMMAVKHLGS HVDAVAAPLN HDTPDELTTP GGVVPDLGEW TPGVTMPKIV AVERDYTRIG
EKFDTLGPLA DELGMVTKGI VFRPDREVTE LGQMNGVATD GAGAGRPLLD TDVKAINSVL
RLSGTTNGRL ATEGFKTLEQ RTGTRLHDLS EGDEEKRISF DDVVIQPRSV ITSPEWSGSE
HGGRRYSAFV QNLERHRPWH TLTGRPQFYM DHDWMIDMGE AMPVFRPPVS LPHLYGEHPV
GYVGTAQEDV AEVAVRYLTI HNKWAIHSQY YDNPHMLTLG RGGQTVWMSP ADATKIGVSD
NEWIEAYNRN GIVSARAIVS HRIPEGTVYM YHAQERVANT PLTERSGRRG GIHNSLTRIL
LKPSHLIGGY AQFSYAFNYY GPTGNQRDEV TLIRRRDQEV QF
//
