ID   THIO_RICCN              Reviewed;         105 AA.
AC   Q92JR5;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA; OrderedLocusNames=RC0002;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL02540.1; -; Genomic_DNA.
DR   PIR; B97700; B97700.
DR   RefSeq; WP_004997015.1; NC_003103.1.
DR   AlphaFoldDB; Q92JR5; -.
DR   SMR; Q92JR5; -.
DR   EnsemblBacteria; AAL02540; AAL02540; RC0002.
DR   KEGG; rco:RC0002; -.
DR   HOGENOM; CLU_090389_10_2_5; -.
DR   OMA; QVGVAPK; -.
DR   Proteomes; UP000000816; 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_0000120123"
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;  11971 MW;  7D0391B157EE94E8 CRC64;
     MANNVMDSSF KKEVLESDLP VLVDFWAEWC GPCKMLTPII DEISKELQGK VKVLKMNIDE
     NPNTPSEYGI RSIPTIMLFK NGEQKDTKIG LQQKNSLLDW INKSI