ID   REHY_BROSE              Reviewed;         202 AA.
AC   P52571;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Probable 1-Cys peroxiredoxin;
DE            EC=1.11.1.24 {ECO:0000250|UniProtKB:P30041};
DE   AltName: Full=Dormancy-associated protein PBS128;
DE   AltName: Full=Rehydrin homolog;
DE   AltName: Full=Thioredoxin peroxidase;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000305};
DE   Flags: Fragment;
OS   Bromus secalinus (Rye brome).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Bromeae; Bromus.
OX   NCBI_TaxID=4502;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   PubMed=1377965; DOI=10.1007/bf00023391;
RA   Goldmark P.J., Curry J., Morris C.F., Walker-Simmons M.K.;
RT   "Cloning and expression of an embryo-specific mRNA up-regulated in hydrated
RT   dormant seeds.";
RL   Plant Mol. Biol. 19:433-441(1992).
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   -!- TISSUE SPECIFICITY: Embryos.
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; X63202; CAA44884.1; -; mRNA.
DR   PIR; S22499; S22499.
DR   AlphaFoldDB; P52571; -.
DR   SMR; P52571; -.
DR   PeroxiBase; 4976; Bse1CysPrx.
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..202
FT                   /note="Probable 1-Cys peroxiredoxin"
FT                   /id="PRO_0000135108"
FT   DOMAIN          <1..148
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   MOTIF           178..201
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        30
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P30041"
FT   NON_TER         1
SQ   SEQUENCE   202 AA;  22380 MW;  89F8814921B45656 CRC64;
     STHGKIRIHD YVANGYVILF SHPGDFTPVC TTELAAMANY AKEFEKRGVK LLGISCDDVQ
     SHKEWTKDIE AYKPGSKVTY PIMADPDRSA IKQLNMVDPD EKDAEGQLPS RTLHIVGPDK
     KVKLSFLYPS CTGRNMDEVV RAVDSLLTAA KHKVATPANW KPGECVVIAP GVSDEEAKKL
     FPQGFETKDL PSKKGYLRFT KV