ID   THIO_PEPLI              Reviewed;         107 AA.
AC   P21609;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA;
OS   Peptoclostridium litorale (Clostridium litorale).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoclostridium.
OX   NCBI_TaxID=1557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49638 / DSM 5388 / W6;
RX   PubMed=8529640; DOI=10.1111/j.1432-1033.1995.192_c.x;
RA   Kreimer S., Andreesen J.R.;
RT   "Glycine reductase of Clostridium litorale. Cloning, sequencing, and
RT   molecular analysis of the grdAB operon that contains two in-frame TGA
RT   codons for selenium incorporation.";
RL   Eur. J. Biochem. 234:192-199(1995).
RN   [2]
RP   PRELIMINARY PROTEIN SEQUENCE OF 1-45.
RX   PubMed=1995593; DOI=10.1128/jb.173.4.1509-1513.1991;
RA   Meyer M., Dietrichs D., Schmidt B., Andreesen J.R.;
RT   "Thioredoxin elicits a new dihydrolipoamide dehydrogenase activity by
RT   interaction with the electron-transferring flavoprotein in Clostridium
RT   litoralis and Eubacterium acidaminophilum.";
RL   J. Bacteriol. 173:1509-1513(1991).
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   EMBL; U24268; AAC43576.1; -; Genomic_DNA.
DR   PIR; S63991; S63991.
DR   AlphaFoldDB; P21609; -.
DR   SMR; P21609; -.
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.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Electron transport;
KW   Redox-active center; Transport.
FT   CHAIN           1..107
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120090"
FT   DOMAIN          2..106
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        29..32
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   107 AA;  11874 MW;  7F1117FFDBF3FAF9 CRC64;
     MLMLDKDTFK TEVLEGTGYV LVDYFSDGCV PCKALMPAVE ELSKKYEGRV VFAKLNTTGA
     RRLAISQKIL GLPTLSLYKD GVKVDEVTKD DATIENIEAM VEEHISK