ID   THIO_RICFE              Reviewed;         105 AA.
AC   Q4UNK3;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA; OrderedLocusNames=RF_0002;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY60853.1; Type=Erroneous initiation; Evidence={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; CP000053; AAY60853.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_039594746.1; NC_007109.1.
DR   AlphaFoldDB; Q4UNK3; -.
DR   SMR; Q4UNK3; -.
DR   STRING; 315456.RF_0002; -.
DR   EnsemblBacteria; AAY60853; AAY60853; RF_0002.
DR   KEGG; rfe:RF_0002; -.
DR   eggNOG; COG3118; Bacteria.
DR   HOGENOM; CLU_090389_10_2_5; -.
DR   OrthoDB; 1630944at2; -.
DR   Proteomes; UP000008548; 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_0000272627"
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;  11953 MW;  4ED3EC8FA0D2D68C CRC64;
     MANNVTDSSF KKEVLESDLP VLVDFWAEWC GPCKMLTPII DEISKELKGK VKVLKMNIDE
     NPNIPSEYGI RSIPTIMLFK NGEQKDTKIG LQQKNSLLDW INKSI