ID   THIO1_DICDI             Reviewed;         105 AA.
AC   P29445;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Thioredoxin-1;
DE            Short=Trx-1;
GN   Name=trxA; Synonyms=trx1; ORFNames=DDB_G0294447;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=AX3;
RX   PubMed=1577820; DOI=10.1016/s0021-9258(19)50177-6;
RA   Wetterauer B., Jacquot J.-P., Veron M.;
RT   "Thioredoxins from Dictyostelium discoideum are a developmentally regulated
RT   multigene family.";
RL   J. Biol. Chem. 267:9895-9904(1992).
RN   [2]
RP   FUNCTION.
RX   PubMed=1330554; DOI=10.1111/j.1432-1033.1992.tb17331.x;
RA   Wetterauer B., Veron M., Miginiac-Maslow M., Decottignies P.,
RA   Jacquot J.-P.;
RT   "Biochemical characterization of thioredoxin 1 from Dictyostelium
RT   discoideum.";
RL   Eur. J. Biochem. 209:643-649(1992).
RN   [3]
RP   FUNCTION, ACTIVE SITES, AND MUTAGENESIS OF CYS-32 AND CYS-35.
RX   PubMed=15653432; DOI=10.1515/bc.2004.153;
RA   Brodegger T., Stockmann A., Oberstrass J., Nellen W., Follmann H.;
RT   "Novel thioredoxin targets in Dictyostelium discoideum identified by two-
RT   hybrid analysis: interactions of thioredoxin with elongation factor 1alpha
RT   and yeast alcohol dehydrogenase.";
RL   Biol. Chem. 385:1185-1192(2004).
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       {ECO:0000269|PubMed:1330554, ECO:0000269|PubMed:15653432}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC   -!- CAUTION: Has not been found in the genome sequence, yet it seems to be
CC       really from D.discoideum. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M91384; AAA33258.1; -; mRNA.
DR   PIR; A46264; A46264.
DR   AlphaFoldDB; P29445; -.
DR   SMR; P29445; -.
DR   OMA; EQISHTT; -.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:dictyBase.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IDA:dictyBase.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:dictyBase.
DR   GO; GO:0045454; P:cell redox homeostasis; IDA:dictyBase.
DR   GO; GO:0006457; P:protein folding; IDA:dictyBase.
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   Disulfide bond; Electron transport; Redox-active center; Transport.
FT   CHAIN           1..105
FT                   /note="Thioredoxin-1"
FT                   /id="PRO_0000120029"
FT   DOMAIN          2..105
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        32
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:15653432"
FT   ACT_SITE        35
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:15653432"
FT   SITE            26
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            33
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            34
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        32..35
FT                   /note="Redox-active"
FT   MUTAGEN         32
FT                   /note="C->S: Loss of activity; when associated with S-35."
FT                   /evidence="ECO:0000269|PubMed:15653432"
FT   MUTAGEN         35
FT                   /note="C->S: Loss of activity; when associated with S-32."
FT                   /evidence="ECO:0000269|PubMed:15653432"
SQ   SEQUENCE   105 AA;  11926 MW;  0BC12C2867CEB1F5 CRC64;
     MSNRVIHVSS CEELDKHLRD ERVVVDFSAV WCGPCRAISP VFEKLSNEFI TFTFLHVDID
     KLNVHPIVSK IKSVPTFHFY RNGSKVSEFS GASESILRST LEANK