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Database: UniProt
Entry: Q8Z2M4
LinkDB: Q8Z2M4
Original site: Q8Z2M4 
ID   TORA_SALTI              Reviewed;         850 AA.
AC   Q8Z2M4;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   01-OCT-2014, entry version 84.
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=STY3956, t3696;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P.,
RA   Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J.,
RA   Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K.,
RA   Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C.,
RA   Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K.,
RA   Whitehead S., Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella
RT   enterica serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/JB.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J.,
RA   Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2
RT   and CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into
CC       trimethylamine; an anaerobic reaction coupled to energy-yielding
CC       reactions. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Trimethylamine + 2 (ferricytochrome c)-subunit
CC       + H(2)O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit +
CC       2 H(+).
CC   -!- COFACTOR: Binds 1 molybdenum-bis(molybdopterin guanine
CC       dinucleotide) (Mo-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
CC       the 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; AL513382; CAD03172.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO71191.1; -; Genomic_DNA.
DR   RefSeq; NP_458117.1; NC_003198.1.
DR   RefSeq; NP_807331.1; NC_004631.1.
DR   ProteinModelPortal; Q8Z2M4; -.
DR   SMR; Q8Z2M4; 52-834.
DR   STRING; 220341.STY3956; -.
DR   EnsemblBacteria; AAO71191; AAO71191; t3696.
DR   EnsemblBacteria; CAD03172; CAD03172; CAD03172.
DR   GeneID; 1250203; -.
DR   KEGG; sty:STY3956; -.
DR   PATRIC; 18546109; VBISalEnt120419_4042.
DR   eggNOG; COG0243; -.
DR   KO; K07811; -.
DR   OMA; DINWNGK; -.
DR   OrthoDB; EOG6NWBKD; -.
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:InterPro.
DR   GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009033; F:trimethylamine-N-oxide reductase activity; IEA:InterPro.
DR   InterPro; IPR009010; Asp_de-COase-like_dom.
DR   InterPro; IPR006658; BisC.
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; 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   Complete proteome; Metal-binding; Molybdenum; Oxidoreductase;
KW   Periplasm; Signal.
FT   SIGNAL        1     39       Tat-type signal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00648}.
FT   CHAIN        40    850       Trimethylamine-N-oxide reductase.
FT                                /FTId=PRO_0000019155.
FT   METAL       191    191       Molybdenum. {ECO:0000250}.
SQ   SEQUENCE   850 AA;  94675 MW;  06B76E03E1FCC987 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
     GKGRGIHLPT FEVFWNQQEY IEFDHPQMFV RHQAFREDPD LEPLGTPSGL IEIYSKTIAD
     MQYDDCQGHP MWFEKIERSH GGPGSQRWPL HLQSVHPDFR LHSQLCESET LRQQYAVGGK
     EPVFINPQDA SARGIRNGDI VRVFNARGQV LAGAVVSDRY APGVARIHEG AWYDPDKGGD
     LNALCKYGNP NVLTLDTGTS QLAQATSAHT TLVEIEKYTG PMDNVTAFNG PAEMVAQCEY
     VPASQGNPHD
//
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