ID   REHY_MEDTR              Reviewed;         218 AA.
AC   Q6E2Z6;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=1-Cys peroxiredoxin;
DE            EC=1.11.1.24 {ECO:0000250|UniProtKB:P30041};
DE   AltName: Full=Rehydrin homolog;
DE   AltName: Full=Thioredoxin peroxidase;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000305};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Paraggio; TISSUE=Embryo;
RA   Boudet J., Buitink J., Satour P., Leprince O.H.L.;
RT   "Expression of 1-Cys peroxiredoxin in relation to desiccation tolerance in
RT   seeds of Medicago truncatula.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively (By similarity). Seems to contribute to the inhibition of
CC       germination during stress (By similarity).
CC       {ECO:0000250|UniProtKB:O04005, ECO:0000250|UniProtKB:P30041}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC         disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC         ChEBI:CHEBI:50058; EC=1.11.1.24;
CC         Evidence={ECO:0000250|UniProtKB:P30041};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O04005}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O04005}.
CC   -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC       residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC       attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC       cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC       cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC       bridge. The disulfide is subsequently reduced by an appropriate
CC       electron donor to complete the catalytic cycle. In this 1-Cys
CC       peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide
CC       with a cysteine from another protein or with a small thiol molecule.
CC       {ECO:0000250|UniProtKB:O35244}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY594329; AAT67997.1; -; mRNA.
DR   AlphaFoldDB; Q6E2Z6; -.
DR   SMR; Q6E2Z6; -.
DR   PeroxiBase; 4377; Mt1CysPrx01.
DR   ExpressionAtlas; Q6E2Z6; differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR   CDD; cd03016; PRX_1cys; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR045020; PRX_1cys.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Antioxidant; Cytoplasm; Nucleus; Oxidoreductase; Peroxidase;
KW   Redox-active center.
FT   CHAIN           1..218
FT                   /note="1-Cys peroxiredoxin"
FT                   /id="PRO_0000285102"
FT   DOMAIN          4..164
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   MOTIF           194..217
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        46
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P30041"
SQ   SEQUENCE   218 AA;  24414 MW;  B6C138B69F698CE4 CRC64;
     MPGLTIGDTI PDLEVDTTQG KIKLHHFCSD SWTILFSHPG DFTPVCTTEL GKMAQYASEF
     NKRGVMLLGM SCDDLESHKE WIKDIEAHTP GAKVNYPIIS DPKREIIKQL NMVDPDEKDS
     NGNLPSRALH IVGPDKKIKL SFLYPAQTGR NMDEVLRVVE SLQKASKYKI ATPANWKPGE
     PVVISPDVTN DQAKEMFPQG FKTADLPSKK EYLRFTNV