ID   TRXB_ECO57              Reviewed;         321 AA.
AC   P0A9P5; P09625;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9;
GN   Name=trxB; OrderedLocusNames=Z1232, ECs0973;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   MEDLINE=21074935; PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   MEDLINE=21156231; PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide
CC       + NADPH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; AE005174; AAG55375.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34396.1; -; Genomic_DNA.
DR   PIR; C85614; C85614.
DR   PIR; E90750; E90750.
DR   RefSeq; NP_286765.1; -.
DR   RefSeq; NP_309000.1; -.
DR   SMR; P0A9P5; 2-317.
DR   GeneID; 917715; -.
DR   GeneID; 958846; -.
DR   GenomeReviews; AE005174_GR; Z1232.
DR   GenomeReviews; BA000007_GR; ECs0973.
DR   KEGG; ece:Z1232; -.
DR   KEGG; ecs:ECs0973; -.
DR   HOGENOM; P0A9P5; -.
DR   OMA; P0A9P5; PSCGPCH.
DR   BioCyc; ECOL83334:ECS0973-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP;
KW   Oxidoreductase; Redox-active center.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    321       Thioredoxin reductase.
FT                                /FTId=PRO_0000166730.
FT   NP_BIND      36     43       FAD (By similarity).
FT   NP_BIND     287    296       FAD (By similarity).
FT   DISULFID    136    139       Redox-active (By similarity).
SQ   SEQUENCE   321 AA;  34623 MW;  8E5AF86FB195CC82 CRC64;
     MGTTKHSKLL ILGSGPAGYT AAVYAARANL QPVLITGMEK GGQLTTTTEV ENWPGDPNDL
     TGPLLMERMH EHATKFETEI IFDHINKVDL QNRPFRLNGD NGEYTCDALI IATGASARYL
     GLPSEEAFKG RGVSACATCD GFFYRNQKVA VIGGGNTAVE EALYLSNIAS EVHLIHRRDG
     FRAEKILIKR LMDKVENGNI ILHTNRTLEE VTGDQMGVTG VRLRDTQNSD NIESLDVAGL
     FVAIGHSPNT AIFEGQLELE NGYIKVQSGI HGNATQTSIP GVFAAGDVMD HIYRQAITSA
     GTGCMAALDA ERYLDGLADA K
//