ID   THIO_PEPAC              Reviewed;         110 AA.
AC   P21610;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA;
OS   Peptoclostridium acidaminophilum (Eubacterium acidaminophilum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoclostridium.
OX   NCBI_TaxID=1731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49065 / DSM 3953 / al-2;
RX   PubMed=8223622; DOI=10.1111/j.1432-1033.1993.tb18307.x;
RA   Luebbers M., Andreesen J.R.;
RT   "Components of glycine reductase from Eubacterium acidaminophilum. Cloning,
RT   sequencing and identification of the genes for thioredoxin reductase,
RT   thioredoxin and selenoprotein PA.";
RL   Eur. J. Biochem. 217:791-798(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-46.
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; L04500; AAB93304.1; -; Genomic_DNA.
DR   PIR; S38989; S38989.
DR   AlphaFoldDB; P21610; -.
DR   SMR; P21610; -.
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   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..110
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120106"
FT   DOMAIN          2..110
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        33..36
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   CONFLICT        2
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        45
FT                   /note="E -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   110 AA;  12142 MW;  E8B74CF8CAF19414 CRC64;
     MSALLVEIDK DQFQAEVLEA EGYVLVDYFS DGCVPCKALM PDVEELAAKY EGKVAFRKFN
     TSSARRLAIS QKILGLPTIT LYKGGQKVEE VTKDDATREN IDAMIAKHVG