ID   TORA_VIBPA              Reviewed;         820 AA.
AC   Q87QI7;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=VP1162;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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; BA000031; BAC59425.1; -; Genomic_DNA.
DR   RefSeq; NP_797541.1; NC_004603.1.
DR   RefSeq; WP_005462326.1; NC_004603.1.
DR   AlphaFoldDB; Q87QI7; -.
DR   SMR; Q87QI7; -.
DR   STRING; 223926.28806150; -.
DR   EnsemblBacteria; BAC59425; BAC59425; BAC59425.
DR   GeneID; 1188667; -.
DR   KEGG; vpa:VP1162; -.
DR   PATRIC; fig|223926.6.peg.1103; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_6; -.
DR   OMA; KPWVRHA; -.
DR   Proteomes; UP000002493; Chromosome 1.
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_0000019160"
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;  92542 MW;  9D2E92390C187151 CRC64;
     MAITRRSFLK GVATTSAASV IGPSLLASAS ANAAESTGTW KVTGSHWGAF RAHIYAGKVQ
     EIKPLELDKN PTEMLNGIKG IIYSPSRVRY PMVRLDWLKK HKYSADTRGN NRFIRVTWDE
     ALDLFYRELE RVQKEYGPWA LHAGQTGWNQ TGSFNNCTAH MQRAVGMHGN FITKVGDYST
     GAGQTIMPYV LGSTEVYAQG TSWSEILENS DNIILWANDP VKNLQVGWNC ETHESFKYLA
     ELKEKVAKGE INVLSVDPVK NKTQRYLEND HLYINPMTDV AFMLAVAHVL YNENLYDKKF
     IDTYCLGFEE FIQYVQGKTK DKVEKTPEWA AAICGVKADK IREFARMLVS GRTQILMGWC
     IQRQEHGEQP YWAAAVVAAM VGQIGLPGGG ISYGHHYSSI GVPSTGFAGP GGFPRNLDQG
     MKPKWDNNDF NGYSRTIPVA RWIDCLLEPG KEINYNGGKV KLPDFKMMVI SGCNPWHHHQ
     DRNRMKKAFR KLQTVVTIEF AWTATCRFSD IVLPACTQWE RNDIDVYGSY SNKGLIAMHR
     LVDPLFQSKP DFQIMSELTQ RFGRREEYTR GMSEMEWIES LYNDCKKANE GKFEMPEFNE
     FWEKSVLDFG EGKPWVRHAD FRKDPELNPL GTPSGFIEIT SRKIGRYGYE HCQEHPMWFE
     KSERSHGGPG SDKYPFWLQS CHPDKRLHSQ MCESEEFRAT YAVQGREPVY INPIDAKAKG
     IKDGDLVRVF NGRGQLLAGA VLTDSYPRGV IRIEEGAWYG PLNEKEGAIC TYGDPNTLTQ
     DIGSSELAQA TSANTCIVDF EKFTGKVPPV TSFGGPIEVA