ID   TRXM_BRANA              Reviewed;         177 AA.
AC   Q9XGS0; O03043;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Thioredoxin M-type, chloroplastic;
DE            Short=Trx-M;
DE   Flags: Precursor;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS.
RX   PubMed=11295436; DOI=10.1016/s0167-4838(01)00150-9;
RA   Duek P.D., Wolosiuk R.A.;
RT   "Rapeseed chloroplast thioredoxin-m. Modulation of the affinity for target
RT   proteins.";
RL   Biochim. Biophys. Acta 1546:299-311(2001).
CC   -!- FUNCTION: Participates in various redox reactions through the
CC       reversible oxidation of the active center dithiol to a disulfide. The M
CC       form is known to activate NADP-malate dehydrogenase (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin
CC       reductase (FTR) and ferredoxin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. Plant M-type subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U76831; AAB52409.1; -; mRNA.
DR   EMBL; AF160870; AAD45358.1; -; mRNA.
DR   PIR; T09495; T09495.
DR   AlphaFoldDB; Q9XGS0; -.
DR   SMR; Q9XGS0; -.
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   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01068; thioredoxin; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Disulfide bond; Electron transport; Plastid;
KW   Redox-active center; Transit peptide; Transport.
FT   TRANSIT         1..64
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           65..177
FT                   /note="Thioredoxin M-type, chloroplastic"
FT                   /id="PRO_0000034173"
FT   DOMAIN          65..177
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        101
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        104
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            95
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            102
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            103
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        101..104
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   MUTAGEN         99
FT                   /note="P->E: Reduces chloroplast FBPase activity."
FT                   /evidence="ECO:0000269|PubMed:11295436"
FT   MUTAGEN         99
FT                   /note="P->K: Enhances chloroplast FBPase activity."
FT                   /evidence="ECO:0000269|PubMed:11295436"
SQ   SEQUENCE   177 AA;  19269 MW;  7584958FD2E5C987 CRC64;
     MAAFTCTSSP PISLRSEMMI ASSKTVSLST RQMFSVGGLR TRVSLSSVSK NSRASRLRRG
     GIICEAQDTA TGIPMVNDST WESLVLKADE PVVVDFWAPW CGPCKMIDPI VNELAQQYTG
     KIKFFKLNTD DSPATPGKYG VRSIPTIMIF VKGEKKDTII GAVPKTTLAT SIDKFLQ