TORA_SALTI
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 03-AUG-2022, entry version 125.
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; Enterobacterales;
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., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT 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., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(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; AL513382; CAD03172.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO71191.1; -; Genomic_DNA.
DR RefSeq; NP_458117.1; NC_003198.1.
DR RefSeq; WP_000790669.1; NZ_WSUR01000056.1.
DR AlphaFoldDB; Q8Z2M4; -.
DR SMR; Q8Z2M4; -.
DR STRING; 220341.16504805; -.
DR PRIDE; Q8Z2M4; -.
DR EnsemblBacteria; AAO71191; AAO71191; t3696.
DR KEGG; stt:t3696; -.
DR KEGG; sty:STY3956; -.
DR PATRIC; fig|220341.7.peg.4042; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OMA; GREPLWM; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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..850
FT /note="Trimethylamine-N-oxide reductase"
FT /id="PRO_0000019155"
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 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
