ID   TORA_SALTY              Reviewed;         850 AA.
AC   Q8ZKZ7;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   16-JUN-2009, entry version 42.
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=STM3822;
OS   Salmonella typhimurium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   MEDLINE=21534948; PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
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; AE008878; AAL22681.1; -; Genomic_DNA.
DR   RefSeq; NP_462722.1; -.
DR   HSSP; O87948; 1TMO.
DR   GeneID; 1255349; -.
DR   GenomeReviews; AE006468_GR; STM3822.
DR   KEGG; stm:STM3822; -.
DR   NMPDR; fig|99287.1.peg.3696; -.
DR   HOGENOM; Q8ZKZ7; -.
DR   OMA; Q8ZKZ7; LRQQYAV.
DR   BioCyc; STYP99287:STM3822-MON; -.
DR   BRENDA; 1.7.2.3; 2.
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    850       Trimethylamine-N-oxide reductase.
FT                                /FTId=PRO_0000019156.
SQ   SEQUENCE   850 AA;  94727 MW;  EEC83F902A3322EA CRC64;
     MKNKDSLHVS RRRFLAQLGG LTVAGMLGPS LLTPRSARAA DAVAPGAATK EGILTGSHWG
     AIRATVVDGR FVAAKPFEQD KYPSKMIAGL PDHVHNAARI RYPMVRVDWM RKGHQSDTSQ
     RGDNRFVRVS WDEALDLFYQ ELERVQKTYG PSALLTASGW QSTGMFHNAS GMLARAIALH
     GNSVSTGGDY STGAAQVILP RVVGSMEVYE QQTSWPLVLQ NSKTIVLWGS DMVKNQQANW
     WCPDHDVYQY YEQLKEKVAS GAISVISIDP VVTSTHDYLG RDKVKHIAIN PQTDVPLQLA
     LAHTLYSEKL YDKNFLDNYC VGFDQFLPYL LGEKDGQPKD AAWAEKLCGI DADTIRALAR
     QMAGDRTQII AGWCVQRMQH GEQWSWMVVV LAAMLGQIGL PGGGFGFGWH YNGAGTPGRK
     GIILSGFSGS TTVPPVHDST DYKGYSSTIP IARFMDAILE PGKIINWNGK SVKLPPLKMC
     VFAGTNPFHR HQQINRIIEG WRKLETVIAI DNQWTSTCRF ADIVLPATTQ FERNDLDQFG
     NHSNRGIIAM KQVVSPQFEA RNDFDIFRDL CRRFNREAAF TEGLDEMGWL KRIWQEGSQQ
     GKGRGIHLPI FEVFWNQQEY IEFDHPQMFV RHQAFREDPD LEPLGTPSGL IEIYSKTIAD
     MQYDDCQGHP MWFEKIERSH GGPGSQRWPL HLQSVHPDFR LHSQLCESET LRQQYAVGGK
     EPVFINPQDA SARGIRNGDI VRVFNARGQV LAGAVVSDRY APGVARIHEG AWYDPDKGGD
     LNALCKYGNP NVLTLDIGTS QLAQATSAHT TLVEIEKYTG PMDNVTAFNG PVEMVAQCEY
     VPASQGNPHD
//