ID   TRXM_MAIZE              Reviewed;         167 AA.
AC   Q41864;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Thioredoxin M-type, chloroplastic;
DE            Short=Trx-M;
DE   Flags: Precursor;
GN   Name=TRM1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. B23; TISSUE=Leaf;
RA   Trevanion S.J., Ashton A.R.;
RT   "Isolation of a full-length cDNA clone for thioredoxin-m from maize.";
RL   (er) Plant Gene Register PGR95-129(1995).
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; L40957; AAA92464.1; -; mRNA.
DR   PIR; T03957; T03957.
DR   AlphaFoldDB; Q41864; -.
DR   SMR; Q41864; -.
DR   STRING; 4577.GRMZM2G181258_P01; -.
DR   PaxDb; Q41864; -.
DR   EnsemblPlants; Zm00001eb138600_T001; Zm00001eb138600_P001; Zm00001eb138600.
DR   Gramene; Zm00001eb138600_T001; Zm00001eb138600_P001; Zm00001eb138600.
DR   MaizeGDB; 114054; -.
DR   eggNOG; KOG0910; Eukaryota.
DR   OMA; CSIGAKS; -.
DR   Proteomes; UP000007305; Chromosome 3.
DR   ExpressionAtlas; Q41864; baseline and differential.
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..53
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           54..167
FT                   /note="Thioredoxin M-type, chloroplastic"
FT                   /id="PRO_0000034175"
FT   DOMAIN          54..165
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        89..92
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   167 AA;  18073 MW;  30679958A20C005E CRC64;
     MAMETCFRAW ALHAPAGSKD RLLVGNLVLP SKRALAPLSV GRVATRRPRH VCQSKNAVDE
     VVVADEKNWD GLVMACETPV LVEFWAPWCG PCRMIAPVID ELAKDYAGKI TCCKVNTDDS
     PNVASTYGIR SIPTVLIFKG GEKKESVIGA VPKSTLTTLI DKYIGSS