ID   TRXB_RICTY              Reviewed;         310 AA.
AC   Q68WT3;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   16-JUN-2009, entry version 37.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9;
GN   Name=trxB; OrderedLocusNames=RT0432;
OS   Rickettsia typhi.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=785;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/JB.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K.,
RA   Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C.,
RA   Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G.,
RA   Gibbs R.A., Hong C., Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with
RT   sequences of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; AE017197; AAU03909.1; -; Genomic_DNA.
DR   RefSeq; YP_067391.1; -.
DR   GeneID; 2958952; -.
DR   GenomeReviews; AE017197_GR; RT0432.
DR   KEGG; rty:RT0432; -.
DR   HOGENOM; Q68WT3; -.
DR   OMA; Q68WT3; PSCGPCH.
DR   BioCyc; RTYP257363:RT0432-MON; -.
DR   BRENDA; 1.8.1.9; 281221.
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   CHAIN         1    310       Thioredoxin reductase.
FT                                /FTId=PRO_0000274792.
FT   NP_BIND      34     41       FAD (By similarity).
FT   NP_BIND     281    290       FAD (By similarity).
FT   DISULFID    135    138       Redox-active (By similarity).
SQ   SEQUENCE   310 AA;  33699 MW;  C1D1EB4A96A5DE49 CRC64;
     MKITTKVLII GSGPAGLSAA IYTARSSLKP ILINGMQPGG QLTMTTDVEN YPGFAKTIQG
     PWLMEQMSIQ AKNVGTEIIN DYVERVDLSK RPFKIFTGTG NKYEADSIII CTGAESKWLG
     ITSEQEFRGF GVSSCAICDG FFFKNQDIVV VGGGNSALEE ALYLTNHANK VTVVHRRNSF
     RAEKILQDRL FKNPKISVIW DHVIDEIVGS NQPKTVTGVK IKNVYTNEIN LVNCSGVFIA
     IGHTPNTTLF NGQIAIDDDN YIITQTGSTR TSVEGVFAAG DVQDKIYRQA ITAAASGCMA
     ALEVAKFLNK
//