ID   TRXH_PICMA              Reviewed;         125 AA.
AC   O65049;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Thioredoxin H-type;
DE            Short=Trx-H;
GN   Name=SB09;
OS   Picea mariana (Black spruce) (Abies mariana).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX   NCBI_TaxID=3335;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9611216; DOI=10.1093/genetics/149.2.1089;
RA   Perry D.J., Bousquet J.;
RT   "Sequence-tagged-site (STS) markers of arbitrary genes: development,
RT   characterization and analysis of linkage in black spruce.";
RL   Genetics 149:1089-1098(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 (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; AF051206; AAC32111.1; -; mRNA.
DR   PIR; T50866; T50866.
DR   AlphaFoldDB; O65049; -.
DR   SMR; O65049; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Disulfide bond; Electron transport; Redox-active center;
KW   Transport.
FT   CHAIN           1..125
FT                   /note="Thioredoxin H-type"
FT                   /id="PRO_0000120058"
FT   DOMAIN          2..112
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        38
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        41
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            32
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            39
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            40
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        38..41
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   125 AA;  13732 MW;  37E1A22E0B5E229F CRC64;
     MAEGNVFACH STEGWRSKLQ EAIDTKRLVA VDFTATWCGP CRVIGPVFVE LSKKFPEIFF
     LKVDVDELRD VAQEWDVEAM PTFIFIKDGK AVDKVVGAKK DDLERKVAAL AAAATTTEAT
     LPAQA