ID   A0A1G0SUH4_9BACT        Unreviewed;       733 AA.
AC   A0A1G0SUH4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Nitrate reductase {ECO:0000313|EMBL:OGU76031.1};
GN   ORFNames=A3G43_13810 {ECO:0000313|EMBL:OGU76031.1};
OS   Ignavibacteria bacterium RIFCSPLOWO2_12_FULL_56_21.
OC   Bacteria; Ignavibacteriota; Ignavibacteria.
OX   NCBI_TaxID=1798438 {ECO:0000313|EMBL:OGU76031.1, ECO:0000313|Proteomes:UP000177278};
RN   [1] {ECO:0000313|EMBL:OGU76031.1, ECO:0000313|Proteomes:UP000177278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGU76031.1}.
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DR   EMBL; MHAK01000026; OGU76031.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G0SUH4; -.
DR   Proteomes; UP000177278; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02778; MopB_CT_Thiosulfate-R-like; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..733
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009568004"
FT   DOMAIN          41..97
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   733 AA;  80915 MW;  9DB45329B9E00128 CRC64;
     MTTLSRRKFL KISGATVAAS AVATSGCSLG NSGAGTKESG IRTVATYCDL CFWKCGAIAT
     VKDGRLWKIE GNPLDPLSRG RLCPRGTGGV GAHFDPDRLR TPLLRRKNRG DEEWVAVTWD
     EALGTIAEKM QKIKAEYGPE AIALFSHGIG GNFLKHTLKA FGTPNITAPS FAQCRGPRDV
     GFRLTFGEDV SSPERTDIRN AKCLVLIGSH LGENMHNTQV QEFAEAVGNG ASVIVVDPRF
     SVAASKAKHY LPIKPGTDLA LILAWMNVLV QEGLYDKDYV DQYGFGFDHF AASISTATPE
     WAYIETGIDP DVIRETAREM ARYRPATLVH PGRHVTWYGD DAQRSRAIAL LNALIGSWGR
     KGGFYTPQSM DVPAYPYPPY PKPLKEKVDN PGHRYPFAHE TITTGIREAT ITGMPYPIKG
     WFTYATNLLH ALPNDQETIR AMQNLDLMVV VDVIPSETAG WADVVLPESV YLERHDDLNV
     EWFREPFVAI RQPVVASPHD QKPGWWIALQ LANKLGLEAY FPWKNAEEYL EKRVTAAGLS
     WDELKEKGII RGQHQPIYYS EGVPAEFPTP SGKIEFSSPQ LAQAGFDPVP RYTRPTQGPE
     GSFRLLFGRA PVHSFSRTQS NPILADMMDT NEVWVNANAA ARLDIADGQY VRLRNQDGVV
     SNRVRVKATE RIRPDCVYLV HGFGHTARGL RRPFGKGASD AQLVTRSAVD PLMGGTGMNV
     NFVTIEPAED NHA
//