TORA_SALTY
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 03-AUG-2022, entry version 113.
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 (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX 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., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL22681.1; -; Genomic_DNA.
DR RefSeq; NP_462722.1; NC_003197.2.
DR RefSeq; WP_000790665.1; NC_003197.2.
DR AlphaFoldDB; Q8ZKZ7; -.
DR SMR; Q8ZKZ7; -.
DR STRING; 99287.STM3822; -.
DR PaxDb; Q8ZKZ7; -.
DR EnsemblBacteria; AAL22681; AAL22681; STM3822.
DR GeneID; 1255349; -.
DR KEGG; stm:STM3822; -.
DR PATRIC; fig|99287.12.peg.4046; -.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OMA; GREPLWM; -.
DR PhylomeDB; Q8ZKZ7; -.
DR BioCyc; SENT99287:STM3822-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central.
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 GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
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; Reference proteome;
KW 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_0000019156"
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; 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
