ID   TRXH2_TOBAC             Reviewed;         118 AA.
AC   Q07090;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Thioredoxin H-type 2;
DE            Short=Trx-H2;
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 [GENOMIC DNA].
RX   PubMed=8479434; DOI=10.1007/bf00279557;
RA   Brugidou C., Marty I., Chartier Y., Meyer Y.;
RT   "The Nicotiana tabacum genome encodes two cytoplasmic thioredoxin genes
RT   which are differently expressed.";
RL   Mol. Gen. Genet. 238:285-293(1993).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z11803; CAA77847.1; -; Genomic_DNA.
DR   PIR; S34812; S34812.
DR   AlphaFoldDB; Q07090; -.
DR   SMR; Q07090; -.
DR   STRING; 4097.Q07090; -.
DR   Proteomes; UP000084051; Unplaced.
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   Reference proteome; Transport.
FT   CHAIN           1..118
FT                   /note="Thioredoxin H-type 2"
FT                   /id="PRO_0000120062"
FT   DOMAIN          2..113
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   118 AA;  13047 MW;  8370BBC6C62DAC06 CRC64;
     MAEEGQVIGV HTVDAWNEHL QKGIDDKKLI VVDFTASWCG PCKFIASFYA ELAKKMPTVT
     FLKVDVDELK SVATDWAVEA MPTFMFLKEG KIVDKVVGAK KDELQQTIAK HISSTSTA