TORA_ECOLI
ID TORA_ECOLI Reviewed; 848 AA.
AC P33225; P78227;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 179.
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=b0997, JW0982;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 40-46.
RC STRAIN=K12;
RX PubMed=8022286; DOI=10.1111/j.1365-2958.1994.tb00393.x;
RA Mejean V., Iobbi-Nivol C., Lepelletier M., Giordano G., Chippaux M.,
RA Pascal M.-C.;
RT "TMAO anaerobic respiration in Escherichia coli: involvement of the tor
RT operon.";
RL Mol. Microbiol. 11:1169-1179(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 767-848.
RC STRAIN=K12;
RX PubMed=8302830; DOI=10.1073/pnas.91.3.1054;
RA Ueguchi C., Kakeda M., Yamada H., Mizuno T.;
RT "An analogue of the DnaJ molecular chaperone in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1054-1058(1994).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=2512991; DOI=10.1016/0167-4838(89)90220-3;
RA Silvestro A., Pommier J., Pascal M.-C., Giordano G.;
RT "The inducible trimethylamine N-oxide reductase of Escherichia coli K12:
RT its localization and inducers.";
RL Biochim. Biophys. Acta 999:208-216(1989).
RN [7]
RP SEC-INDEPENDENT TRANSLOCATION, AND PROBABLE EXPORT VIA TAT-SYSTEM.
RX PubMed=9427745; DOI=10.1093/emboj/17.1.101;
RA Santini C.-L., Ize B., Chanal A., Mueller M., Giordano G., Wu L.-F.;
RT "A novel Sec-independent periplasmic protein translocation pathway in
RT Escherichia coli.";
RL EMBO J. 17:101-112(1998).
RN [8]
RP EXPORT VIA THE TAT-SYSTEM.
RX PubMed=17218314; DOI=10.1074/jbc.m610507200;
RA Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B.,
RA Palmer T., Georgiou G.;
RT "Export pathway selectivity of Escherichia coli twin arginine translocation
RT signal peptides.";
RL J. Biol. Chem. 282:8309-8316(2007).
CC -!- FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an
CC anaerobic reaction coupled to energy-yielding reactions.
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 -!- SUBUNIT: Interacts with the N-terminal domain of TorC.
CC -!- INTERACTION:
CC P33225; P0A9M0: lon; NbExp=2; IntAct=EBI-557008, EBI-547203;
CC P33225; P33226: torC; NbExp=3; IntAct=EBI-557008, EBI-553710;
CC P33225; P36662: torD; NbExp=24; IntAct=EBI-557008, EBI-6406226;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:2512991}.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has been experimentally proven.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; X73888; CAA52095.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74082.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36139.1; -; Genomic_DNA.
DR EMBL; D16500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C64841; C64841.
DR RefSeq; NP_415517.1; NC_000913.3.
DR RefSeq; WP_001062091.1; NZ_SSUW01000007.1.
DR AlphaFoldDB; P33225; -.
DR SMR; P33225; -.
DR BioGRID; 4260701; 16.
DR ComplexPortal; CPX-319; Trimethylamine-N-oxide reductase TorAC complex.
DR DIP; DIP-11013N; -.
DR IntAct; P33225; 17.
DR MINT; P33225; -.
DR STRING; 511145.b0997; -.
DR TCDB; 5.A.3.4.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR PaxDb; P33225; -.
DR PRIDE; P33225; -.
DR EnsemblBacteria; AAC74082; AAC74082; b0997.
DR EnsemblBacteria; BAA36139; BAA36139; BAA36139.
DR GeneID; 946267; -.
DR KEGG; ecj:JW0982; -.
DR KEGG; eco:b0997; -.
DR PATRIC; fig|1411691.4.peg.1274; -.
DR EchoBASE; EB1761; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR InParanoid; P33225; -.
DR OMA; GREPLWM; -.
DR PhylomeDB; P33225; -.
DR BioCyc; EcoCyc:TORA-MON; -.
DR BioCyc; MetaCyc:TORA-MON; -.
DR SABIO-RK; P33225; -.
DR PRO; PR:P33225; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:ComplexPortal.
DR GO; GO:1904852; C:trimethylamine-N-oxide reductase (cytochrome c) complex; IPI:ComplexPortal.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IDA:EcoCyc.
DR GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IDA:EcoCyc.
DR GO; GO:0009060; P:aerobic respiration; IDA:ComplexPortal.
DR GO; GO:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal.
DR GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR GO; GO:0006885; P:regulation of pH; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; Molybdenum; Oxidoreductase;
KW Periplasm; Reference proteome; Signal.
FT SIGNAL 1..39
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:8022286"
FT CHAIN 40..848
FT /note="Trimethylamine-N-oxide reductase 1"
FT /id="PRO_0000019151"
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"
FT CONFLICT 173
FT /note="L -> R (in Ref. 1; CAA52095)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="A -> R (in Ref. 1; CAA52095)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="A -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="V -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="R -> G (in Ref. 1; CAA52095)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="Q -> E (in Ref. 1; CAA52095)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="T -> S (in Ref. 1; CAA52095)"
FT /evidence="ECO:0000305"
FT CONFLICT 503..504
FT /note="KL -> NV (in Ref. 1; CAA52095)"
FT /evidence="ECO:0000305"
FT CONFLICT 713..714
FT /note="QQ -> HE (in Ref. 1; CAA52095)"
FT /evidence="ECO:0000305"
FT CONFLICT 751
FT /note="L -> M (in Ref. 1; CAA52095)"
FT /evidence="ECO:0000305"
FT CONFLICT 781
FT /note="P -> L (in Ref. 1; CAA52095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 848 AA; 94456 MW; 59DDACB00B1843E7 CRC64;
MNNNDLFQAS RRRFLAQLGG LTVAGMLGPS LLTPRRATAA QAATDAVISK EGILTGSHWG
AIRATVKDGR FVAAKPFELD KYPSKMIAGL PDHVHNAARI RYPMVRVDWL RKRHLSDTSQ
RGDNRFVRVS WDEALDMFYE ELERVQKTHG PSALLTASGW QSTGMFHNAS GMLAKAIALH
GNSVGTGGDY STGAAQVILP RVVGSMEVYE QQTSWPLVLQ NSKTIVLWGS DLLKNQQANW
WCPDHDVYEY YAQLKAKVAA GEIEVISIDP VVTSTHEYLG REHVKHIAVN PQTDVPLQLA
LAHTLYSENL YDKNFLANYC VGFEQFLPYL LGEKDGQPKD AAWAEKLTGI DAETIRGLAR
QMAANRTQII AGWCVQRMQH GEQWAWMIVV LAAMLGQIGL PGGGFGFGWH YNGAGTPGRK
GVILSGFSGS TSIPPVHDNS DYKGYSSTIP IARFIDAILE PGKVINWNGK SVKLPPLKMC
IFAGTNPFHR HQQINRIIEG LRKLETVIAI DNQWTSTCRF ADIVLPATTQ FERNDLDQYG
NHSNRGIIAM KQVVPPQFEA RNDFDIFREL CRRFNREEAF TEGLDEMGWL KRIWQEGVQQ
GKGRGVHLPA FDDFWNNKEY VEFDHPQMFV RHQAFREDPD LEPLGTPSGL IEIYSKTIAD
MNYDDCQGHP MWFEKIERSH GGPGSQKYPL HLQSVHPDFR LHSQLCESET LRQQYTVAGK
EPVFINPQDA SARGIRNGDV VRVFNARGQV LAGAVVSDRY APGVARIHEG AWYDPDKGGE
PGALCKYGNP NVLTIDIGTS QLAQATSAHT TLVEIEKYNG TVEQVTAFNG PVEMVAQCEY
VPASQVKS
