TRXH_WHEAT
ID TRXH_WHEAT Reviewed; 127 AA.
AC O64394;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Thioredoxin H-type;
DE Short=Trx-H;
DE AltName: Full=TrxTa;
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].
RC STRAIN=cv. Capitole; TISSUE=Seed;
RX PubMed=9523703; DOI=10.1046/j.1432-1327.1998.2520314.x;
RA Gautier M.-F., Lullien-Pellerin V., de Lamotte-Guery F., Guirao A.,
RA Joudrier P.;
RT "Characterization of wheat thioredoxin h cDNA and production of an active
RT Triticum aestivum protein in Escherichia coli.";
RL Eur. J. Biochem. 252:314-324(1998).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily.
CC {ECO:0000305}.
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DR EMBL; X69915; CAA49540.1; -; mRNA.
DR AlphaFoldDB; O64394; -.
DR SMR; O64394; -.
DR STRING; 4565.Traes_1AL_11FF51731.1; -.
DR PRIDE; O64394; -.
DR EnsemblPlants; TraesCAD_scaffold_030558_01G000100.1; TraesCAD_scaffold_030558_01G000100.1; TraesCAD_scaffold_030558_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_065456_01G000200.1; TraesCLE_scaffold_065456_01G000200.1; TraesCLE_scaffold_065456_01G000200.
DR EnsemblPlants; TraesCS1B02G338800.1; TraesCS1B02G338800.1; TraesCS1B02G338800.
DR EnsemblPlants; TraesPAR_scaffold_045811_01G000200.1; TraesPAR_scaffold_045811_01G000200.1; TraesPAR_scaffold_045811_01G000200.
DR EnsemblPlants; TraesROB_scaffold_032069_01G000200.1; TraesROB_scaffold_032069_01G000200.1; TraesROB_scaffold_032069_01G000200.
DR EnsemblPlants; TraesWEE_scaffold_083098_01G000100.1; TraesWEE_scaffold_083098_01G000100.1; TraesWEE_scaffold_083098_01G000100.
DR Gramene; TraesCAD_scaffold_030558_01G000100.1; TraesCAD_scaffold_030558_01G000100.1; TraesCAD_scaffold_030558_01G000100.
DR Gramene; TraesCLE_scaffold_065456_01G000200.1; TraesCLE_scaffold_065456_01G000200.1; TraesCLE_scaffold_065456_01G000200.
DR Gramene; TraesCS1B02G338800.1; TraesCS1B02G338800.1; TraesCS1B02G338800.
DR Gramene; TraesPAR_scaffold_045811_01G000200.1; TraesPAR_scaffold_045811_01G000200.1; TraesPAR_scaffold_045811_01G000200.
DR Gramene; TraesROB_scaffold_032069_01G000200.1; TraesROB_scaffold_032069_01G000200.1; TraesROB_scaffold_032069_01G000200.
DR Gramene; TraesWEE_scaffold_083098_01G000100.1; TraesWEE_scaffold_083098_01G000100.1; TraesWEE_scaffold_083098_01G000100.
DR eggNOG; KOG0907; Eukaryota.
DR OMA; KEANPWI; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; O64394; baseline and differential.
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 2: Evidence at transcript level;
KW Cytoplasm; Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..127
FT /note="Thioredoxin H-type"
FT /id="PRO_0000120063"
FT DOMAIN 2..127
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 52
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 55
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 46
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 53
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 54
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 52..55
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 127 AA; 13524 MW; 30B7C73433DF70E6 CRC64;
MAASAATATA TAAAVGAGEV ISVHSLEQWT MQIEEANAAK KLVVIDFTAS WCGPCRIMAP
IFADLAKKFP AAVFLKVDVD ELKPIAEQFS VEAMPTFLFM KEGDVKDRVV GAIKEELTTK
VGLHAAQ
