ID   TRXH1_TOBAC             Reviewed;         126 AA.
AC   P29449;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Thioredoxin H-type 1;
DE            Short=Trx-H1;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. White Burley;
RX   PubMed=1868216; DOI=10.1007/bf00036817;
RA   Marty I., Meyer Y.;
RT   "Nucleotide sequence of a cDNA encoding a tobacco thioredoxin.";
RL   Plant Mol. Biol. 17:143-147(1991).
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; X58527; CAA41415.1; -; mRNA.
DR   PIR; S16590; S16590.
DR   RefSeq; XP_016435914.1; XM_016580428.1.
DR   AlphaFoldDB; P29449; -.
DR   SMR; P29449; -.
DR   ProMEX; P29449; -.
DR   GeneID; 107762104; -.
DR   KEGG; nta:107762104; -.
DR   OMA; ELGANSM; -.
DR   OrthoDB; 1482186at2759; -.
DR   PhylomeDB; P29449; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; 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   2: Evidence at transcript level;
KW   Cytoplasm; Disulfide bond; Electron transport; Redox-active center;
KW   Reference proteome; Transport.
FT   CHAIN           1..126
FT                   /note="Thioredoxin H-type 1"
FT                   /id="PRO_0000120061"
FT   DOMAIN          2..120
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        46
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        49
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            40
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            47
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            48
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..49
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   126 AA;  13956 MW;  07D3931222968CEA CRC64;
     MAANDATSSE EGQVFGCHKV EEWNEYFKKG VETKKLVVVD FTASWCGPCR FIAPILADIA
     KKMPHVIFLK VDVDELKTVS AEWSVEAMPT FVFIKDGKEV DRVVGAKKEE LQQTIVKHAA
     PATVTA