ID   THIO_CYAM1              Reviewed;         102 AA.
AC   O22022;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA; Synonyms=trxM;
OS   Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC   Cyanidioschyzon.
OX   NCBI_TaxID=280699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Ohta N., Sato N., Ueda K., Kuroiwa T.;
RT   "Analysis of a plastid gene cluster reveals a close relationship between
RT   Cyanidioschyzon and Cyanidium.";
RL   J. Plant Res. 110:235-245(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3377 / 10D;
RX   PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA   Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K.,
RA   Shin-i T., Kohara Y., Kuroiwa T.;
RT   "Complete sequence and analysis of the plastid genome of the unicellular
RT   red alga Cyanidioschyzon merolae.";
RL   DNA Res. 10:67-77(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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; D63675; BAA22818.1; -; Genomic_DNA.
DR   EMBL; AB002583; BAC76106.1; -; Genomic_DNA.
DR   RefSeq; NP_848944.1; NC_004799.1.
DR   AlphaFoldDB; O22022; -.
DR   SMR; O22022; -.
DR   STRING; 45157.CMV012CT; -.
DR   EnsemblPlants; CMV012CT; CMV012CT; CMV012C.
DR   GeneID; 845059; -.
DR   Gramene; CMV012CT; CMV012CT; CMV012C.
DR   KEGG; cme:CymeCp012; -.
DR   eggNOG; KOG0910; Eukaryota.
DR   HOGENOM; CLU_090389_10_2_1; -.
DR   Proteomes; UP000007014; Chloroplast.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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   Chloroplast; Disulfide bond; Electron transport; Plastid;
KW   Redox-active center; Reference proteome; Transport.
FT   CHAIN           1..102
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120068"
FT   DOMAIN          2..102
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        29
FT                   /note="Nucleophile"
FT   ACT_SITE        32
FT                   /note="Nucleophile"
FT   SITE            23
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            30
FT                   /note="Contributes to redox potential value"
FT   SITE            31
FT                   /note="Contributes to redox potential value"
FT   DISULFID        29..32
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   102 AA;  11657 MW;  84365185B46F7D1D CRC64;
     MLHIDELTFE NEVLQSEKLV LVDFWAPWCG PCRMIGPILE EIAKEFNLKV VQVNTDENPN
     LATFYGIRSI PTLMLFKKGQ RVDTVIGAVP KSILIHTINK YL