ID   REHY_MAIZE              Reviewed;         229 AA.
AC   A2SZW8;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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; Synonyms=PER-1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Ohio 43; TISSUE=Endosperm;
RA   Chen Z.-Y., Brown R.L., Damann K.E., Cleveland T.E.;
RT   "Comparisons of endosperm proteins of domestic corn genotypes resistant or
RT   susceptible to Aspergillus flavus infection/aflatoxin production using
RT   proteomics.";
RL   Submitted (JAN-2006) 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; DQ378060; ABD24377.1; -; mRNA.
DR   RefSeq; NP_001105998.1; NM_001112528.1.
DR   AlphaFoldDB; A2SZW8; -.
DR   SMR; A2SZW8; -.
DR   STRING; 4577.GRMZM2G129761_P01; -.
DR   Allergome; 9885; Zea m 32.
DR   PeroxiBase; 4964; Zm1CysPrx.
DR   PaxDb; A2SZW8; -.
DR   PRIDE; A2SZW8; -.
DR   GeneID; 100037830; -.
DR   KEGG; zma:100037830; -.
DR   eggNOG; KOG0854; Eukaryota.
DR   OrthoDB; 1129256at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; A2SZW8; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004601; F:peroxidase activity; IMP:AgBase.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR   GO; GO:0050832; P:defense response to fungus; IEP:AgBase.
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..229
FT                   /note="1-Cys peroxiredoxin PER1"
FT                   /id="PRO_0000285101"
FT   DOMAIN          4..173
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   MOTIF           205..228
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   229 AA;  24905 MW;  5423753AD1B778D7 CRC64;
     MPGLTIGDTV PNLELDSTHG KIRIHDYVGD GYAIIFSHPA DFTPVCTTEM AAMAGYAKEF
     EKRGVKLLGI SCDDVESHRQ WTKDVEAYGG KQQQQQATTT KVTFPILADP ARDAIRQLNM
     VDPDEKDAAG RSMPSRALHV VGPDKAVKLS FLYPATTGRN MDEVLRAVDS LLTAAKHGGK
     VATPANWKPG ECAVIAPGVS DEEARKMFPQ GFETADLPSK KGYLRFTKV