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   03-AUG-2022, entry version 99.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9 {ECO:0000250|UniProtKB:P9WHH1};
GN   Name=trxB {ECO:0000303|PubMed:9795994};
OS   Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 607 / DSM 43465 / JCM 20379 / NBRC 3207 / NRRL B-692;
RX   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:
CC       Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC         H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC         Evidence={ECO:0000250|UniProtKB:P9WHH1};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P9WHH1};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P9WHH1};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WHH1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC       {ECO:0000250|UniProtKB:P9WHH1}.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AF023161; AAB80939.1; -; Genomic_DNA.
DR   AlphaFoldDB; O30973; -.
DR   SMR; O30973; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 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
FT                   /note="Thioredoxin reductase"
FT                   /id="PRO_0000166740"
FT   BINDING         15..18
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT   BINDING         37..44
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT   BINDING         53
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT   BINDING         86
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT   BINDING         158
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT   BINDING         177
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT   BINDING         183
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT   BINDING         240
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT   BINDING         260
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT   BINDING         280
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT   BINDING         287..290
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT   BINDING         287
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT   DISULFID        137..140
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHH1"
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