ID   THIO_CLOSG              Reviewed;          40 AA.
AC   P81108;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
DE   Flags: Fragment;
GN   Name=trxA;
OS   Clostridium sporogenes.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1509;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=DSM 633 / W28delta;
RX   PubMed=9534247; DOI=10.1099/00221287-144-3-793;
RA   Harms C., Meyer M.A., Andreesen J.R.;
RT   "Fast purification of thioredoxin reductases and of thioredoxins with an
RT   unusual redox-active centre from anaerobic, amino-acid-utilizing
RT   bacteria.";
RL   Microbiology 144:793-800(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.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   AlphaFoldDB; P81108; -.
DR   SMR; P81108; -.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Electron transport;
KW   Redox-active center; Transport.
FT   CHAIN           1..>40
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120091"
FT   DISULFID        29..32
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   NON_TER         40
SQ   SEQUENCE   40 AA;  4525 MW;  C7BE3C913E3E2909 CRC64;
     MLVLDKKTFE EEVLKTKGYV LVDYFGDGCV PCEALMPDVE