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   16-JUN-2009, entry version 45.
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.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into
CC       trimethylamine; an anaerobic reaction coupled to energy-yielding
CC       reactions (By similarity).
CC   -!- CATALYTIC ACTIVITY: Trimethylamine + 2 (ferricytochrome c)-subunit
CC       + H(2)O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit +
CC       2 H(+).
CC   -!- COFACTOR: Molybdenum (molybdopterin) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Periplasm (By similarity).
CC   -!- PTM: Predicted to be exported by the Tat system. The position of
CC       the signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family.
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DR   EMBL; AE014075; AAN79601.1; -; Genomic_DNA.
DR   RefSeq; NP_753058.1; -.
DR   HSSP; O87948; 1TMO.
DR   GeneID; 1039106; -.
DR   GenomeReviews; AE014075_GR; c1133.
DR   KEGG; ecc:c1133; -.
DR   NMPDR; fig|199310.1.peg.1101; -.
DR   HOGENOM; Q8CW73; -.
DR   OMA; Q8CW73; LRQQYAV.
DR   BRENDA; 1.7.2.3; 292881.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrom...; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR009010; Asp_de-COase-like_fold.
DR   InterPro; IPR006658; BisC.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR006657; MPT_dinuc_bd.
DR   InterPro; IPR006311; Tat.
DR   InterPro; IPR011887; TorA.
DR   InterPro; IPR017909; Twin_arg_translocation_Tat.
DR   Gene3D; G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   TIGRFAMs; TIGR00509; bisC_fam; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   TIGRFAMs; TIGR02164; torA; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; FALSE_NEG.
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   Complete proteome; Molybdenum; Oxidoreductase; Periplasm; Signal.
FT   SIGNAL        1     39       Tat-type signal (Potential).
FT   CHAIN        40    848       Trimethylamine-N-oxide reductase 1.
FT                                /FTId=PRO_0000019152.
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
//