ID   TRXM_WHEAT              Reviewed;         175 AA.
AC   Q9ZP21;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Thioredoxin M-type, chloroplastic;
DE            Short=Trx-M;
DE   Flags: Precursor;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Dyer T.A., Catley M.A., Robertson E.J., Dunford R.P.;
RT   "The thioredoxins m and f of plants and their role in the redox regulation
RT   of chloroplast enxymes.";
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. Plant M-type subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ005840; CAA06735.1; -; mRNA.
DR   AlphaFoldDB; Q9ZP21; -.
DR   SMR; Q9ZP21; -.
DR   STRING; 4565.Traes_5BS_B72CD04F2.1; -.
DR   PRIDE; Q9ZP21; -.
DR   EnsemblPlants; TraesCAD_scaffold_024492_01G000100.1; TraesCAD_scaffold_024492_01G000100.1; TraesCAD_scaffold_024492_01G000100.
DR   EnsemblPlants; TraesCLE_scaffold_009635_01G000100.1; TraesCLE_scaffold_009635_01G000100.1; TraesCLE_scaffold_009635_01G000100.
DR   EnsemblPlants; TraesCS5B02G111800.1; TraesCS5B02G111800.1; TraesCS5B02G111800.
DR   EnsemblPlants; TraesPAR_scaffold_139521_01G000100.1; TraesPAR_scaffold_139521_01G000100.1; TraesPAR_scaffold_139521_01G000100.
DR   EnsemblPlants; TraesROB_scaffold_109278_01G000100.1; TraesROB_scaffold_109278_01G000100.1; TraesROB_scaffold_109278_01G000100.
DR   EnsemblPlants; TraesWEE_scaffold_177150_01G000100.1; TraesWEE_scaffold_177150_01G000100.1; TraesWEE_scaffold_177150_01G000100.
DR   Gramene; TraesCAD_scaffold_024492_01G000100.1; TraesCAD_scaffold_024492_01G000100.1; TraesCAD_scaffold_024492_01G000100.
DR   Gramene; TraesCLE_scaffold_009635_01G000100.1; TraesCLE_scaffold_009635_01G000100.1; TraesCLE_scaffold_009635_01G000100.
DR   Gramene; TraesCS5B02G111800.1; TraesCS5B02G111800.1; TraesCS5B02G111800.
DR   Gramene; TraesPAR_scaffold_139521_01G000100.1; TraesPAR_scaffold_139521_01G000100.1; TraesPAR_scaffold_139521_01G000100.
DR   Gramene; TraesROB_scaffold_109278_01G000100.1; TraesROB_scaffold_109278_01G000100.1; TraesROB_scaffold_109278_01G000100.
DR   Gramene; TraesWEE_scaffold_177150_01G000100.1; TraesWEE_scaffold_177150_01G000100.1; TraesWEE_scaffold_177150_01G000100.
DR   eggNOG; KOG0910; Eukaryota.
DR   HOGENOM; CLU_090389_0_2_1; -.
DR   OMA; ADVAMDY; -.
DR   Proteomes; UP000019116; Unplaced.
DR   Genevisible; Q9ZP21; TA.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Chloroplast; Disulfide bond; Electron transport; Plastid;
KW   Redox-active center; Reference proteome; Transit peptide; Transport.
FT   TRANSIT         1..62
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           63..175
FT                   /note="Thioredoxin M-type, chloroplastic"
FT                   /id="PRO_0000034179"
FT   DOMAIN          63..174
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        98..101
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   175 AA;  19132 MW;  E24AF38E45D8DD74 CRC64;
     MALETCLRGW ALYAPQAGIR ERLSSGSYAP SRPRTAAPAV VSPSPYKSAL VAARRPSRFV
     CKCKNVVDEV IVADEKNWDN MVIACESPVL VEFWAPWCGP CRMIAPVIDE LAKDYVGKIK
     CCKVNTDDCP NIASTYGIRS IPTVLMFKDG EKKESVIGAV PKTTLCTIID KYIGS