ID   TORA_VIBVY              Reviewed;         820 AA.
AC   Q7MLQ2;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Trimethylamine-N-oxide reductase;
DE            Short=TMAO reductase;
DE            Short=Trimethylamine oxidase;
DE            EC=1.7.2.3;
DE   Flags: Precursor;
GN   Name=torA; OrderedLocusNames=VV1375;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an
CC       anaerobic reaction coupled to energy-yielding reactions. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(III)-[cytochrome c] + H2O + trimethylamine = 2 Fe(II)-
CC         [cytochrome c] + 3 H(+) + trimethylamine N-oxide;
CC         Xref=Rhea:RHEA:24236, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15724,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:58389; EC=1.7.2.3;
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC       Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC       bis-MGD) cofactor per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; BA000037; BAC94139.1; -; Genomic_DNA.
DR   RefSeq; WP_011150040.1; NC_005139.1.
DR   AlphaFoldDB; Q7MLQ2; -.
DR   SMR; Q7MLQ2; -.
DR   STRING; 672.VV93_v1c12880; -.
DR   EnsemblBacteria; BAC94139; BAC94139; BAC94139.
DR   KEGG; vvy:VV1375; -.
DR   PATRIC; fig|196600.6.peg.1364; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_6; -.
DR   OMA; KPWVRHA; -.
DR   OrthoDB; 88184at2; -.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-EC.
DR   CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR041954; CT_DMSOR/BSOR/TMAOR.
DR   InterPro; IPR041460; Molybdopterin_N.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   InterPro; IPR011887; TorA.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF18364; Molybdopterin_N; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   TIGRFAMs; TIGR02164; torA; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Molybdenum; Oxidoreductase; Periplasm; Reference proteome;
KW   Signal.
FT   SIGNAL          1..33
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           34..820
FT                   /note="Trimethylamine-N-oxide reductase"
FT                   /id="PRO_0000019162"
FT   BINDING         179
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   820 AA;  92469 MW;  763E05D67D3DB90C CRC64;
     MAITRRSFLK GVATTSAASV IGPSLLASAS ANAVETTGTW KVSGSHWGAF RAHIYAGKVQ
     EIKPIELDQN PTEMLNGIKG IIYSPSRVRY PMVRLDWLKK HKYSADTRGN NRFVRVTWDE
     ALDLFYRELE RVQKEYGPWA LHAGQTGWNQ TGSFNNCTAH MQRAVGMHGN YITKVGDYST
     GAGQTILPYV LGSTEVYAQG TSWSEILENA DNIILWANDP VKNLQVGWNC ETHESYAYLA
     QLKEKVAKGE INVISVDPVK NKTQRYLEND HLYVNPMTDV PFMLAIAHVL YTENLYDKKF
     IETYCLGFEE FINYVQGKTK DKVEKTPEWA APICGVKADK IREFARMLVK GRTQILMGWC
     IQRQEHGEQP YWAAAVVAAM IGQIGLPGGG ISYGHHYSSI GVPSTGFAGP GGFPRNLDAG
     MKPKWDNNDF NGYSRTIPVA RWIDCLLEPG KEINYNGGKV KLPDFKMMVI SGCNPWHHHQ
     DRNRMKQAFQ KLQTVVTIDF AWTATCRFSD IVLPACTQWE RNDIDVYGSY SSRGLIAMHR
     LVDPLFQSKP DFQIMKELTE RFGRSEEYSR GMSEMDWIRS LYNDCKKSNE GKFEMPEFDE
     FWEKSVLDFG QGQPWVRHAD FRQDPEINPL GTPSGFIEIT SRKIGRYGYE HCQEHPMWFE
     KSERSHGGPG SDKHPFWLQS CHPDKRLHSQ MCESEEFRAT YAVKGREPVY INPLDAKAKG
     IKEGDLVRVF NDRGQLLAGA VLTDSYPRGV IRIEEGAWYG PLSEKVGAIC TYGDPNTLTQ
     DIGSSELAQA TSANTCIVDF EKFTGKVPPV TSFGGPIEVA