ID   TRXB_TREPA              Reviewed;         307 AA.
AC   O83790;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 67.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9;
GN   Name=trxB; OrderedLocusNames=TP_0814;
OS   Treponema pallidum.
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   MEDLINE=98332770; PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M.,
RA   Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D.,
RA   Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M.,
RA   Weidman J.F., Smith H.O., Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis
RT   spirochete.";
RL   Science 281:375-388(1998).
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; AE000520; AAC65780.1; -; Genomic_DNA.
DR   PIR; C71278; C71278.
DR   RefSeq; NP_219250.1; -.
DR   HSSP; Q39243; 1VDC.
DR   IntAct; O83790; 9.
DR   GeneID; 2610892; -.
DR   GenomeReviews; AE000520_GR; TP_0814.
DR   KEGG; tpa:TP0814; -.
DR   NMPDR; fig|243276.1.peg.809; -.
DR   TIGR; TP_0814; -.
DR   HOGENOM; O83790; -.
DR   OMA; O83790; SYTIENY.
DR   BioCyc; TPAL243276:TP_0814-MON; -.
DR   BRENDA; 1.8.1.9; 142600.
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    307       Thioredoxin reductase.
FT                                /FTId=PRO_0000166754.
FT   NP_BIND      34     41       FAD (By similarity).
FT   NP_BIND     275    284       FAD (By similarity).
FT   DISULFID    134    137       Redox-active (By similarity).
SQ   SEQUENCE   307 AA;  32868 MW;  2519A5BA3BB4E012 CRC64;
     METDYDVIIV GAGAAGLSAA QYACRANLRT LVIESKAHGG QALLIDSLEN YPGYATPISG
     FEYAENMKKQ AVAFGAQIAY EEVTTIGKRD SVFHITTGTG AYTAMSVILA TGAEHRKMGI
     PGESEFLGRG VSYCATCDGP FFRNKHVVVI GGGDAACDES LVLSRLTDRV TMIHRRDTLR
     AQKAIAERTL KNPHIAVQWN TTLEAVRGET KVSSVLLKDV KTGETRELAC DAVFFFIGMV
     PITGLLPDAE KDSTGYIVTD DEMRTSVEGI FAAGDVRAKS FRQVITATSD GALAAHAAAS
     YIDTLQN
//