ID   TORZ_ECOL6              Reviewed;         809 AA.
AC   Q8CVZ3;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   25-NOV-2008, entry version 41.
DE   RecName: Full=Trimethylamine-N-oxide reductase 2;
DE            Short=TMAO reductase 2;
DE            Short=Trimethylamine oxidase 2;
DE            EC=1.7.2.3;
DE   Flags: Precursor;
GN   Name=torZ; Synonyms=bisZ; OrderedLocusNames=c2286;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into
CC       trimethylamine; an anaerobic reaction coupled to energy-yielding
CC       reactions. Can also reduce other N- and S-oxide compounds such as
CC       4-methylmorpholine-N-oxide and biotin sulfoxide (BSO), but with a
CC       lower catalytic efficiency (By similarity).
CC   -!- CATALYTIC ACTIVITY: Trimethylamine + 2 (ferricytochrome c)-subunit
CC       + H(2)O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit +
CC       2 H(+).
CC   -!- COFACTOR: Molybdenum (molybdopterin) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Periplasm (By similarity).
CC   -!- PTM: Predicted to be exported by the Tat system. The position of
CC       the signal peptide cleavage has not been experimentally proven.
CC   -!- MISCELLANEOUS: Expression of torYZ allows E.coli to grow
CC       anaerobically on a wider range of substrates than does expression
CC       of torCAD (By similarity).
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family.
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DR   EMBL; AE014075; AAN80743.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_754178.1; -.
DR   HSSP; Q52675; 1E61.
DR   GeneID; 1036854; -.
DR   GenomeReviews; AE014075_GR; c2286.
DR   KEGG; ecc:c2286; -.
DR   NMPDR; fig|199310.1.peg.2221; -.
DR   HOGENOM; Q8CVZ3; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
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 (cytochrom...; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR009010; Asp_de-COase-like_fold.
DR   InterPro; IPR006658; BisC.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR006657; MPT_dinuc_bd.
DR   InterPro; IPR006311; Tat.
DR   Gene3D; G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 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   3: Inferred from homology;
KW   Complete proteome; Molybdenum; Oxidoreductase; Periplasm; Signal.
FT   SIGNAL        1     31       Tat-type signal (Potential).
FT   CHAIN        32    809       Trimethylamine-N-oxide reductase 2.
FT                                /FTId=PRO_0000019164.
SQ   SEQUENCE   809 AA;  89006 MW;  07087EB335CDEF22 CRC64;
     MTLTRREFIK HSGIAAGTLV VTSAAPLPAW AEEKGGKILT AGRWGAMNVE VKDGKIVSST
     GALAKTIPNS LQSTAADQVH TTARIQHPMV RKSYLDNPLQ PVKGRGEDTY VQVSWEQALK
     LIHEQHDRIR KANGPSAIFA GSYGWRSSGV LHKAQTLLQR YMNLAGGYSG HSGDYSTGAA
     QVIMPHVVGS VEVYEQQTSW PLILENSQVV VLWGMNPLNT LKIAWSSTDE QGLEYFHQLK
     KSGKPVIAID PIRSETIEFF GDNATWIAPN MGTDVALMLG IAHTLMTQGK HDKVFLEKYT
     TGYPQFEEYL TGKSDNTPKS AAWAAEITGV PEAQIVKLAE LMAANRTMLM AGWGIQRQQY
     GEQKHWMLVT LAAMLGQIGT PGGGFGFSYH YSNGGNPTRV GGVLPEMSAA IAGQASEAAD
     DGGMTAIPVA RIVDALENPG GKYQHNGKEQ TYPNIKMIWW AGGGNFTHHQ DTNRLIKAWQ
     KPEMIVVSEC YWTAAAKHAD IVLPITTSFE RNDLTMTGDY SNQHIVLMKQ AVAPQFEARN
     DFDVFADLAE LLKPGGKEIY TEGKDEMAWL KFFYDAAQKG ARAQRVTMPM FNAFWQQNKL
     IEMRRSEKNE QYIRYGDFRA DPVKNALGTP SGKIEIYSRT LEKFGYKDCP AHPTWLAPDE
     WKGTADEKQL QLLTAHPAHR LHSQLNYAEL RKKYAVADRE PITIHTEDAA RFGIANGDLV
     RVWNKRGQIL TGAVVTDGIK KGVVCVHEGA WPDLENGLCK NGSANVLTAD IPSSQLANAC
     AGNSALVYIE KYTGNALKLT AFDQPAVQA
//