ID   THIO_MYCSM              Reviewed;         112 AA.
AC   O30974;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA;
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   -!- FUNCTION: Participates in various redox reactions through the
CC       reversible oxidation of its active center dithiol to a disulfide and
CC       catalyzes dithiol-disulfide exchange reactions. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; AF023161; AAB80940.1; -; Genomic_DNA.
DR   PDB; 5VO7; NMR; -; A=1-112.
DR   PDBsum; 5VO7; -.
DR   AlphaFoldDB; O30974; -.
DR   BMRB; O30974; -.
DR   SMR; O30974; -.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PIRSF; PIRSF000077; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01068; thioredoxin; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Electron transport; Redox-active center;
KW   Transport.
FT   CHAIN           1..112
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120116"
FT   DOMAIN          2..112
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        35..38
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   HELIX           16..19
FT                   /evidence="ECO:0007829|PDB:5VO7"
FT   STRAND          26..30
FT                   /evidence="ECO:0007829|PDB:5VO7"
FT   TURN            38..41
FT                   /evidence="ECO:0007829|PDB:5VO7"
FT   HELIX           42..51
FT                   /evidence="ECO:0007829|PDB:5VO7"
FT   TURN            52..55
FT                   /evidence="ECO:0007829|PDB:5VO7"
FT   STRAND          56..60
FT                   /evidence="ECO:0007829|PDB:5VO7"
FT   HELIX           69..74
FT                   /evidence="ECO:0007829|PDB:5VO7"
FT   STRAND          82..87
FT                   /evidence="ECO:0007829|PDB:5VO7"
FT   STRAND          90..96
FT                   /evidence="ECO:0007829|PDB:5VO7"
FT   HELIX           101..111
FT                   /evidence="ECO:0007829|PDB:5VO7"
SQ   SEQUENCE   112 AA;  11838 MW;  48F4ABF1CEE6D746 CRC64;
     MSEDSATVAV TDDSFSTDVL GSSKPVLVDF WATWCGPCKM VAPVLEEIAA EKGDQLTVAK
     IDVDVDANPA TARDFQVVSI PTMILFKDGA PVKRIVGAKG KAALLRELSD AL