ID   TORA_ECOL6              Reviewed;         848 AA.
AC   Q8CW73;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Trimethylamine-N-oxide reductase 1;
DE            Short=TMAO reductase 1;
DE            Short=Trimethylamine oxidase 1;
DE            EC=1.7.2.3;
DE   Flags: Precursor;
GN   Name=torA; OrderedLocusNames=c1133;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN79601.1; -; Genomic_DNA.
DR   RefSeq; WP_001063183.1; NC_004431.1.
DR   AlphaFoldDB; Q8CW73; -.
DR   SMR; Q8CW73; -.
DR   STRING; 199310.c1133; -.
DR   EnsemblBacteria; AAN79601; AAN79601; c1133.
DR   KEGG; ecc:c1133; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_6; -.
DR   OMA; GREPLWM; -.
DR   BioCyc; ECOL199310:C1133-MON; -.
DR   Proteomes; UP000001410; Chromosome.
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; IPR006658; BisC.
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; 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; TIGR00509; bisC_fam; 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; Signal.
FT   SIGNAL          1..39
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           40..848
FT                   /note="Trimethylamine-N-oxide reductase 1"
FT                   /id="PRO_0000019152"
FT   BINDING         191
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   848 AA;  94628 MW;  5C5AB5570EC67249 CRC64;
     MNNNDLFQAS RRRFLAQLGG LTVAGMLGTS LLTPRRATAA QAATEAVISK EGILTGSHWG
     AIRATVKDGR FVAAKPFELD KYPSKMIAGL PDHVHNAARI RYPMVRVDWL RKRHLSDTSQ
     RGDNRFVRVS WDEALDMFYE ELERVQKTHG PSALLTASGW QSTGMFHNAS GMLAKAIALH
     GNSVGTGGDY STGAAQVILP RVVGSMEVYE QQTSWPLVLQ NSKTIVLWGS DLLKNQQANW
     WCPDHDVYEY YEQLKAKVAA GEIEVISIDP VVTSTHEYLG REHVKHIAVN PQTDVPLQLA
     LAHTLYSENL YDKNFLANYC VGFEQFLPYL LGEKDGQPKD AAWAEKLTGI DAETIRGLAR
     QMAANRTQII AGWCVQRMQH GEQWAWMIVV LAAMLGQIGL PGGGFGFGWH YNGAGTPGRK
     GVILSGFSGS TSIPPVHDNS DYKGYSSTIP IARFIDAILE PGKVINWNGK SVKLPPLKMC
     IFAGTNPFHR HQQINRIIEG WRKLETVIAI DNQWTSTCRF ADIVLPATTQ FERNDLDQYG
     NHSNRGIIAM KQVVPPQFEA RNDFDIFREL CRRFNREEAF TEGLDEMGWL KRIWQEGVQQ
     GKGRGVHLPA FNDFWNNKEY VEFDHPQMFV RHQAFREDPD LEPLGTPSGL IEIYSKTIAD
     MNYDDCQGHP MWFEKIERSH GGPGSQKYPL HLQSVHPDFR LHSQLCESET LRQQYTVAGK
     EPVFISPKDA SARGIRHGDV VRVFNVRGQV LAGAVVSDRY APGVARIHEG AWYDPDKGGE
     PGALCKYGNP NVLTIDIGTS QLAQATSAHT TLVEIEKYNG TVEQVTAFNG PVEMVAQCEY
     VPASQVKS