ID   THIO_CHLTR              Reviewed;         102 AA.
AC   O84544;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA; OrderedLocusNames=CT_539;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(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   EMBL; AE001273; AAC68141.1; -; Genomic_DNA.
DR   PIR; B71503; B71503.
DR   RefSeq; NP_220054.1; NC_000117.1.
DR   RefSeq; WP_009871903.1; NC_000117.1.
DR   AlphaFoldDB; O84544; -.
DR   SMR; O84544; -.
DR   STRING; 813.O172_02965; -.
DR   EnsemblBacteria; AAC68141; AAC68141; CT_539.
DR   GeneID; 884317; -.
DR   KEGG; ctr:CT_539; -.
DR   PATRIC; fig|272561.5.peg.584; -.
DR   HOGENOM; CLU_090389_10_4_0; -.
DR   InParanoid; O84544; -.
DR   OMA; KIKICKF; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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   3: Inferred from homology;
KW   Disulfide bond; Electron transport; Redox-active center;
KW   Reference proteome; Transport.
FT   CHAIN           1..102
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120085"
FT   DOMAIN          1..102
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        28..31
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   102 AA;  11197 MW;  8FAE022A5C980BE1 CRC64;
     MVQVVSQENF ADSIASGLVL IDFFAEWCGP CKMLTPVLEA LAAELPHVTI LKVDIDSSPR
     PAEQYSVSSI PTLILFKDGK EVERSVGLKD KDSLIKLISK HQ