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Database: UniProt
Entry: A0A0T6AJ19_9DELT
LinkDB: A0A0T6AJ19_9DELT
Original site: A0A0T6AJ19_9DELT 
ID   A0A0T6AJ19_9DELT        Unreviewed;      1217 AA.
AC   A0A0T6AJ19;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   08-NOV-2023, entry version 31.
DE   RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE            EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN   ORFNames=XU12_C0001G0177 {ECO:0000313|EMBL:KRT74986.1};
OS   Deltaproteobacteria bacterium CSP1-8.
OC   Bacteria; Deltaproteobacteria.
OX   NCBI_TaxID=1640514 {ECO:0000313|EMBL:KRT74986.1, ECO:0000313|Proteomes:UP000051991};
RN   [1] {ECO:0000313|EMBL:KRT74986.1, ECO:0000313|Proteomes:UP000051991}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-8 {ECO:0000313|EMBL:KRT74986.1};
RA   Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA   Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT   "Critical biogeochemical functions in the subsurface are associated with
RT   bacteria from new phyla and little studied lineages.";
RL   Submitted (MAY-2015) 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:KRT74986.1}.
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DR   EMBL; LDXO01000001; KRT74986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T6AJ19; -.
DR   STRING; 1640514.XU12_C0001G0177; -.
DR   PATRIC; fig|1640514.3.peg.190; -.
DR   Proteomes; UP000051991; 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   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; PS00932; MOLYBDOPTERIN_PROK_3; 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:KRT74986.1}.
FT   DOMAIN          26..90
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1217 AA;  137536 MW;  9FD0E88F25AE6C85 CRC64;
     MSWIRDIADP RNRRWEEFYR NRWQHDKVVR STHGVNCTGG CSWMVHVKDG IITWELQATD
     YPRLAGDLPP YEPRGCQRGI STSWYVYSPI RVKYPYVRGA LMDLWRKARA KHDDPVAAWT
     SLMEDGESRR AYQRARGKGG FRRASWEEVL EIIAASAIHT VKRHGADRII GFSPIPAMSM
     LSYAGGSRFL QLLGGVNLSF YDWYSDLPPA SPEVWGEQTD VAESADWYNS KYIVVMGANL
     GMTRTPDVHF AAEARHNGSK LVVLSPDFSM VSKYADWWIP ANAGQDGAFW MAVNHVILRE
     FFAEKRTPYF EDYLKRYSDA PFLVVVDSRG EAGSGGPVAD SKRLLRARCL NRYRDVENAD
     WKFLVWDDTT GGPRMPLGSV GFRWQEEKGK WNLGMKDGLD GKEISPRLSM LGVHDDVLPL
     EVADFSENRT FARGVPVKYV ETDGGKVAVA TVFDLIMAQF GVSRGLPGEY PERYEDEAIP
     YTPAWQEKFT GIEAKTVLQF AREFASTAEK TEGRCSIIIG AGVNHWYHNN LMYRAGIVGL
     ILCGCVGKNG GGLNHYVGQE KLAPLAPWST LAFALDWGKP PRLQNAPSFH YVHSCQWRYE
     RGFDEYNSPL TAGAGNGDGR FTRGHTMDLQ AKAVRMGWLP FYPQFNENPL DIVREAEEAG
     AKADGEIVRR VTERLKEGSL RFAVEDPDAP ENWPRLWIIW RGNALMSSAK GHEYFLRHYL
     GTHHNMVSEE IAEGTSAEIS WREPAPEGKL DLVVDINFRM DTSALYSDIV LPTATWYEKN
     DLNSTDLHSY IHPLSAAVPP CWESKSDWDI FKAIAEKVSN LAPAHFPGKV RDIVAVPLLH
     DTPAELAQPV VKDWKAGECD LVPGKTMPNL VVVERDYANL YRRFLSFGPL ARKDGIGVHG
     LSWPIEDLYD ELAQRRPTAE WNGRAYPSVE EAVDAANLIL HLAPETNGES AYRAFKAEEK
     KVGLPLADLA EGVREVRYTF EELARQPRRL LTTPCWTGIT NKGRAYSAYC LNVERLVPWR
     TLTGRQHLYL DHEGYIAFGE HLPTYKPIPD PRSMGDISRS RPEGKSVLLN YLTPHGKWHI
     HSTFFDNERM LTLSRGIEPL WMNDRDAADA GIADNDWVEL YNDHGVVVTR AAVSARLPRK
     MCMLYHSPER TISVPRSPLR GNRRAGGHNS LTRTRLKPVL MMGGYAQFTY GFNYWGPTGV
     NRDTFVYVRK LPGAPAW
//
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