PR2E1_ORYSJ
ID PR2E1_ORYSJ Reviewed; 232 AA.
AC Q69TY4; B7E2V4;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Peroxiredoxin-2E-1, chloroplastic;
DE EC=1.11.1.25 {ECO:0000250|UniProtKB:A9PCL4};
DE AltName: Full=Glutaredoxin-dependent peroxiredoxin {ECO:0000305};
DE AltName: Full=Peroxiredoxin IIE-1;
DE AltName: Full=Thioredoxin peroxidase 2E-1;
DE Flags: Precursor;
GN Name=PRXIIE-1; OrderedLocusNames=Os06g0625500, LOC_Os06g42000;
GN ORFNames=OSJNBa0029G06.40, OSJNBa0072A21.9;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides (By similarity). May be involved in
CC chloroplast redox homeostasis (By similarity).
CC {ECO:0000250|UniProtKB:A9PCL4, ECO:0000250|UniProtKB:Q949U7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[glutaredoxin]-dithiol + a hydroperoxide = [glutaredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62624, Rhea:RHEA-
CC COMP:10729, Rhea:RHEA-COMP:10730, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.25;
CC Evidence={ECO:0000250|UniProtKB:A9PCL4};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q949U7}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000250|UniProtKB:Q949U7}.
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:A9PCL4}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AP004680; BAD35693.1; -; Genomic_DNA.
DR EMBL; AP004737; BAD37738.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF20027.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS98695.1; -; Genomic_DNA.
DR EMBL; AK058459; BAG86701.1; -; mRNA.
DR EMBL; AK104130; BAG96441.1; -; mRNA.
DR RefSeq; XP_015640940.1; XM_015785454.1.
DR AlphaFoldDB; Q69TY4; -.
DR SMR; Q69TY4; -.
DR STRING; 4530.OS06T0625500-01; -.
DR PeroxiBase; 4018; OsPrxII0501.
DR CarbonylDB; Q69TY4; -.
DR PaxDb; Q69TY4; -.
DR PRIDE; Q69TY4; -.
DR EnsemblPlants; Os06t0625500-01; Os06t0625500-01; Os06g0625500.
DR EnsemblPlants; Os06t0625500-03; Os06t0625500-03; Os06g0625500.
DR GeneID; 4341570; -.
DR Gramene; Os06t0625500-01; Os06t0625500-01; Os06g0625500.
DR Gramene; Os06t0625500-03; Os06t0625500-03; Os06g0625500.
DR KEGG; osa:4341570; -.
DR eggNOG; KOG0541; Eukaryota.
DR HOGENOM; CLU_072440_0_0_1; -.
DR InParanoid; Q69TY4; -.
DR OMA; TPSCHAN; -.
DR OrthoDB; 1281610at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q69TY4; OS.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR CDD; cd03013; PRX5_like; 1.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10430; PTHR10430; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Antioxidant; Chloroplast; Oxidoreductase; Peroxidase; Plastid;
KW Redox-active center; Reference proteome; Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..232
FT /note="Peroxiredoxin-2E-1, chloroplastic"
FT /id="PRO_0000282283"
FT DOMAIN 71..232
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 119
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:A9PCL4"
SQ SEQUENCE 232 AA; 23688 MW; 25F27641D0858785 CRC64;
MAAAASTLAS LSATAAAAAG KRLLLSSPSR SLSLSLASRG RIAVMPHLRA GILSAAPRRA
VSASAPAAAT IAVGDKLPDA TLSYFDSPDG ELKTVTVRDL TAGKKVVLFA VPGAFTPTCT
QKHVPGFVAK AGELRAKGVD AVACVSVNDA FVMRAWKESL GVGDEVLLLS DGNGELARAM
GVELDLSDKP AGLGVRSRRY ALLAEDGVVK VLNLEEGGAF TTSSAEEMLK AL
