TORZ_ECOLI
ID TORZ_ECOLI Reviewed; 809 AA.
AC P46923; P76292; P97187;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Trimethylamine-N-oxide reductase 2;
DE Short=TMAO reductase 2;
DE Short=Trimethylamine oxidase 2;
DE EC=1.7.2.3 {ECO:0000269|PubMed:11004177};
DE Flags: Precursor;
GN Name=torZ; Synonyms=bisZ; OrderedLocusNames=b1872, JW1861;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / ACC5;
RX PubMed=8919859; DOI=10.1007/bf02198832;
RA del Campillo-Campbell A., Campbell A.M.;
RT "Alternative gene for biotin sulfoxide reduction in Escherichia coli K-
RT 12.";
RL J. Mol. Evol. 42:85-90(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(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 PROTEIN SEQUENCE OF 32-39, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11004177; DOI=10.1128/jb.182.20.5779-5786.2000;
RA Gon S., Patte J.-C., Mejean V., Iobbi-Nivol C.;
RT "The torYZ (yecK bisZ) operon encodes a third respiratory trimethylamine N-
RT oxide reductase in Escherichia coli.";
RL J. Bacteriol. 182:5779-5786(2000).
RN [6]
RP EXPORT VIA THE TAT-SYSTEM AND THE SEC-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. Can also
CC reduce other N- and S-oxide compounds such as 4-methylmorpholine-N-
CC oxide and biotin sulfoxide (BSO), but with a lower catalytic
CC efficiency. {ECO:0000269|PubMed:11004177}.
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 Evidence={ECO:0000269|PubMed:11004177};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24238;
CC Evidence={ECO:0000305|PubMed:11004177};
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:0000269|PubMed:11004177}.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has been experimentally proven. Can also be exported by the
CC Sec system.
CC -!- MISCELLANEOUS: Expression of torYZ allows E.coli to grow anaerobically
CC on a wider range of substrates than does expression of torCAD.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a biotin sulfoxide reductase.
CC {ECO:0000305|PubMed:8919859}.
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DR EMBL; U38839; AAC44131.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74942.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15682.1; -; Genomic_DNA.
DR PIR; H64949; H64949.
DR RefSeq; NP_416386.4; NC_000913.3.
DR RefSeq; WP_000176781.1; NZ_LN832404.1.
DR AlphaFoldDB; P46923; -.
DR SMR; P46923; -.
DR BioGRID; 4263502; 53.
DR DIP; DIP-9226N; -.
DR IntAct; P46923; 19.
DR STRING; 511145.b1872; -.
DR PaxDb; P46923; -.
DR PRIDE; P46923; -.
DR EnsemblBacteria; AAC74942; AAC74942; b1872.
DR EnsemblBacteria; BAA15682; BAA15682; BAA15682.
DR GeneID; 946389; -.
DR KEGG; ecj:JW1861; -.
DR KEGG; eco:b1872; -.
DR PATRIC; fig|1411691.4.peg.376; -.
DR EchoBASE; EB3061; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR InParanoid; P46923; -.
DR OMA; DQMPKHV; -.
DR PhylomeDB; P46923; -.
DR BioCyc; EcoCyc:G7022-MON; -.
DR BioCyc; MetaCyc:G7022-MON; -.
DR PRO; PR:P46923; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
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; IDA:EcoCyc.
DR GO; GO:0009061; P:anaerobic respiration; IMP:EcoCyc.
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; IPR019546; TAT_signal_bac_arc.
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; TIGR01409; TAT_signal_seq; 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..31
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:11004177"
FT CHAIN 32..809
FT /note="Trimethylamine-N-oxide reductase 2"
FT /id="PRO_0000019163"
FT BINDING 176
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 76
FT /note="A -> T (in Ref. 1; AAC44131)"
FT /evidence="ECO:0000305"
FT CONFLICT 291..292
FT /note="HD -> TI (in Ref. 1; AAC44131)"
FT /evidence="ECO:0000305"
FT CONFLICT 299..304
FT /note="YTTGYP -> TLPGIR (in Ref. 1; AAC44131)"
FT /evidence="ECO:0000305"
FT CONFLICT 406..409
FT /note="EMSA -> DFSGP (in Ref. 1; AAC44131)"
FT /evidence="ECO:0000305"
FT CONFLICT 801..803
FT /note="AFD -> GFG (in Ref. 1; AAC44131)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 809 AA; 88964 MW; 44A84F6302531D09 CRC64;
MTLTRREFIK HSGIAAGALV VTSAAPLPAW AEEKGGKILT AGRWGAMNVE VKDGKIVSST
GALAKTIPNS LQSTAADQVH TTARIQHPMV RKSYLDNPLQ PAKGRGEDTY VQVSWEQALK
LIHEQHDRIR KANGPSAIFA GSYGWRSSGV LHKAQTLLQR YMNLAGGYSG HSGDYSTGAA
QVIMPHVVGS VEVYEQQTSW PLILENSQVV VLWGMNPLNT LKIAWSSTDE QGLEYFHQLK
KSGKPVIAID PIRSETIEFF DDNATWIAPN MGTDVALMLG IAHTLMTQGK HDKVFLEKYT
TGYPQFEEYL TGKSDNTPKS AVWAAEITGV PEAQIVKLAE LMAANRTMLM AGWGIQRQQY
GEQKHWMLVT LAAMLGQIGT PGGGFGFSYH YSNGGNPTRV GGVLPEMSAA IAGHASEAAD
DGGMTAIPVA RIVDALENPG GKYQHNGKEQ TYPNIKMIWW AGGGNFTHHQ DTNRLIKAWQ
KPEMIVVSEC YWTAAAKHAD IVLPITTSFE RNDLTMTGDY SNQHIVPMKQ AVAPQFEARN
DFDVFADLAE LLKPGGKEIY TEGKDEMAWL KFFYDAAQKG ARAQRVTMPM FNAFWQQNKL
IEMRHSEKNE QYVRYGDFRA DPVKNALGTP SGKIEIYSKT LEKFGYKDCP AHPTWLAPDE
WKGTADEKQL QLLTAHPAHR LHSQLNYAEL RKKYAIADRE PITIHTEDAA RFGIANGDLV
RVWNKRGQIL TGAVVTDGIK KGVVCVHEGA WPDLENGLCK NGSANVLTAD IPSSQLANAC
AGNSALVYIE KYTGNAPKLT AFDQPAVQA
