REHY_WHEAT
ID REHY_WHEAT Reviewed; 218 AA.
AC Q6W8Q2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=1-Cys peroxiredoxin PER1;
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};
GN Name=PER1;
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. Soissons; TISSUE=Seed;
RA Cazalis R., Aussenac T.;
RT "Cloning and expression of PER1 in wheat seed.";
RL Submitted (MAY-2003) 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}.
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; AY304482; AAQ74769.1; -; mRNA.
DR AlphaFoldDB; Q6W8Q2; -.
DR SMR; Q6W8Q2; -.
DR STRING; 4565.Traes_2BS_CADAA49C9.1; -.
DR Allergome; 6327; Tri a 32.
DR Allergome; 9499; Tri a 32.0101.
DR PeroxiBase; 4381; Ta1CysPrx01-2B.
DR PRIDE; Q6W8Q2; -.
DR EnsemblPlants; TraesCS2B02G174400.1; TraesCS2B02G174400.1; TraesCS2B02G174400.
DR EnsemblPlants; TraesWEE_scaffold_002158_01G000100.1; TraesWEE_scaffold_002158_01G000100.1; TraesWEE_scaffold_002158_01G000100.
DR Gramene; TraesCS2B02G174400.1; TraesCS2B02G174400.1; TraesCS2B02G174400.
DR Gramene; TraesWEE_scaffold_002158_01G000100.1; TraesWEE_scaffold_002158_01G000100.1; TraesWEE_scaffold_002158_01G000100.
DR eggNOG; KOG0854; Eukaryota.
DR HOGENOM; CLU_042529_4_1_1; -.
DR OMA; RLTMLYP; -.
DR Proteomes; UP000019116; Unplaced.
DR Genevisible; Q6W8Q2; TA.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..218
FT /note="1-Cys peroxiredoxin PER1"
FT /id="PRO_0000285104"
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; 23965 MW; 8C98E8F32CC98A5B CRC64;
MPGLTIGDTV PNLELDSTHG KIRIHDYVGN GYVILFSHPG DFTPVCTTEL AAMANYAKEF
EKRGVKLLGI SCDDVQSHKE WTKDIEAYKP GSKVTYPIMA DPDRSAIKQL NMVDPDEKDA
EGQLPSRTLH IVGPDKKVKL SFLYPSCTGR NMDEVVRAVD SLLTAAKHKV ATPANWNPGE
CVVIAPGVSD DEAKKMFPQG FETADLPSKK GYLRFTKV
