ID   TRXH_FAGES              Reviewed;         116 AA.
AC   Q96419;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Thioredoxin H-type;
DE            Short=Trx-H;
OS   Fagopyrum esculentum (Common buckwheat) (Polygonum fagopyrum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Polygonaceae; Polygonoideae; Fagopyreae; Fagopyrum.
OX   NCBI_TaxID=3617;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Kitayuki;
RA   Fujino K., Funatsuki H., Kikuta Y.;
RT   "Buckwheat cDNA from immature seeds.";
RL   Submitted (SEP-1996) 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 H
CC       form is known to activate a number of cytosolic enzymes (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily.
CC       {ECO:0000305}.
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DR   EMBL; D87984; BAA13524.1; -; mRNA.
DR   PIR; T10739; T10739.
DR   AlphaFoldDB; Q96419; -.
DR   SMR; Q96419; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Disulfide bond; Electron transport; Redox-active center;
KW   Transport.
FT   CHAIN           1..116
FT                   /note="Thioredoxin H-type"
FT                   /id="PRO_0000120056"
FT   DOMAIN          2..115
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        39
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        42
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            33
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            40
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            41
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        39..42
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   116 AA;  13071 MW;  65592078363D0165 CRC64;
     MAEEAQVIAC HTVQEWNEKF QKAKDSGKLI VIDFTASWCG PCRVITPYVS ELAKKFPHVA
     FFKVDVDDLK DVAEEYKVEA MPSFVILKEG QEVERIVGAR KDELLHKIAV HAPITA