ID   TRXB_MYCSM              Reviewed;         311 AA.
AC   O30973;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9;
GN   Name=trxB;
OS   Mycobacterium smegmatis.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 607 / DSM 43465 / mc(2)6 / NCTC 7017 / NRRL B-692;
RX   MEDLINE=99012086; PubMed=9795994; DOI=10.1016/S0923-2508(99)80004-7;
RA   Asano R.L., Davies J.;
RT   "Molecular characterization of the thioredoxin system of Mycobacterium
RT   smegmatis.";
RL   Res. Microbiol. 149:567-576(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; AF023161; AAB80939.1; -; Genomic_DNA.
DR   HSSP; Q39243; 1VDC.
DR   SMR; O30973; 7-310.
DR   BRENDA; 1.8.1.9; 259.
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   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN         1    311       Thioredoxin reductase.
FT                                /FTId=PRO_0000166740.
FT   NP_BIND      37     44       FAD (By similarity).
FT   NP_BIND     280    289       FAD (By similarity).
FT   DISULFID    137    140       Redox-active (By similarity).
SQ   SEQUENCE   311 AA;  33612 MW;  3EC3896EADCF6493 CRC64;
     MSTSQTVHDV IIIGSGPAGY TAAIYAARAQ LKPLVFEGTQ FGGALMTTTE VENYPGFREG
     ITGPELMDQM REQALRFRAD LRMEDVDAVQ LEGPVKTVVV GDETHQARAV ILAMGAAARH
     LGVPGEEALT GMGVSTCATC DGFFFRDQDI VVVGGGDSAM EEATFLTRFA RSVTLIHRRD
     EFRASKIMLE RARANEKITF LTNTEITQIE GDPKVTGVRL RDTVTGEESK LDVTGVFVAI
     GHDPRSELVR GQVELDDEGY VKVQGRTTYT SLDGVFAAGD LVDHTYRQAI TAAGSGCAAS
     IDAERWLAEQ D
//