ID   THIO_BUCBP              Reviewed;         109 AA.
AC   P59527;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-APR-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA; OrderedLocusNames=bbp_539;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27238.1; -; Genomic_DNA.
DR   RefSeq; WP_011091639.1; NC_004545.1.
DR   AlphaFoldDB; P59527; -.
DR   SMR; P59527; -.
DR   STRING; 224915.bbp_539; -.
DR   EnsemblBacteria; AAO27238; AAO27238; bbp_539.
DR   GeneID; 56471073; -.
DR   KEGG; bab:bbp_539; -.
DR   eggNOG; COG3118; Bacteria.
DR   HOGENOM; CLU_090389_10_2_6; -.
DR   OMA; QVGVAPK; -.
DR   OrthoDB; 1630944at2; -.
DR   Proteomes; UP000000601; Chromosome.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
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; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Electron transport; Redox-active center;
KW   Reference proteome; Transport.
FT   CHAIN           1..109
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120080"
FT   DOMAIN          2..109
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"
SQ   SEQUENCE   109 AA;  12396 MW;  64D333E010A67DD0 CRC64;
     MTNCIVELTD GIFKQYILES KKAVLVDFWA EWCNPCKILA PILEDIAKEY EHKLIVTKIN
     IDKNPNTAPK YSIRGIPALL LFKNSELVGT KVGALSKVQL KDFLNLYLK