ID   THIO_GRIPA              Reviewed;         109 AA.
AC   P50338;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA;
OS   Griffithsia pacifica (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Ceramiales;
OC   Ceramiaceae; Griffithsia.
OX   NCBI_TaxID=35689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8003693; DOI=10.1007/bf00024194;
RA   Reynolds A.E., Chesnick J.M., Woolford J., Cattolica R.A.;
RT   "Chloroplast encoded thioredoxin genes in the red algae Porphyra yezoensis
RT   and Griffithsia pacifica: evolutionary implications.";
RL   Plant Mol. Biol. 25:13-21(1994).
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; X76611; CAA54076.1; -; Genomic_DNA.
DR   PIR; S46522; S46522.
DR   AlphaFoldDB; P50338; -.
DR   SMR; P50338; -.
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; Transport.
FT   CHAIN           1..109
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120069"
FT   DOMAIN          2..107
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        31
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        34
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            25
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            32
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            33
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..34
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   109 AA;  12210 MW;  8B42FEDA431F47D3 CRC64;
     MSISQVIDTS FHEEVINSRQ PVLVDFWAPW CGPCRMIAST IDEIAHDYKD KLKVVKVNTD
     QNPTIATEYG IRSIPTVMIF INGKKVDTVV GAVPKLTLLN TLQKHLKST