ID   THIO_RICTY              Reviewed;         105 AA.
AC   Q68Y00;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA; OrderedLocusNames=RT0002;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- FUNCTION: Component of the thioredoxin-thioredoxin reductase system.
CC       Participates in various redox reactions through the reversible
CC       oxidation of its active center dithiol to a disulfide and catalyzes
CC       dithiol-disulfide exchange reactions (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; AE017197; AAU03492.1; -; Genomic_DNA.
DR   RefSeq; WP_011190479.1; NC_006142.1.
DR   AlphaFoldDB; Q68Y00; -.
DR   SMR; Q68Y00; -.
DR   STRING; 257363.RT0002; -.
DR   EnsemblBacteria; AAU03492; AAU03492; RT0002.
DR   KEGG; rty:RT0002; -.
DR   eggNOG; COG3118; Bacteria.
DR   HOGENOM; CLU_090389_10_2_5; -.
DR   OMA; QVGVAPK; -.
DR   OrthoDB; 1630944at2; -.
DR   Proteomes; UP000000604; Chromosome.
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   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; Transport.
FT   CHAIN           1..105
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000272628"
FT   DOMAIN          1..105
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        30..33
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   105 AA;  12065 MW;  AFE1028AAFAA9A9D CRC64;
     MVNNVTDISF KNEVLESDLP VIVDFWAEWC GPCKMLIPII DEISKELQDK VKVLKMNIDE
     NPKTPSEYGV RSIPTIMLFK NGEQKDTKIG LQQKKSLLDW INKSI