PR2E2_ORYSJ
ID PR2E2_ORYSJ Reviewed; 225 AA.
AC Q7F8S5; B7E6P6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Peroxiredoxin-2E-2, chloroplastic;
DE EC=1.11.1.25 {ECO:0000250|UniProtKB:A9PCL4};
DE AltName: Full=Glutaredoxin-dependent peroxiredoxin {ECO:0000305};
DE AltName: Full=Peroxiredoxin IIE-2;
DE AltName: Full=Thioredoxin peroxidase 2E-2;
DE Flags: Precursor;
GN Name=PRXIIE-2; OrderedLocusNames=Os02g0192700, LOC_Os02g09940;
GN ORFNames=P0437H03.112, P0453H10.33;
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).
RN [5]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 62-68, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=cv. Nipponbare;
RX PubMed=16758443; DOI=10.1002/pmic.200600043;
RA Nozu Y., Tsugita A., Kamijo K.;
RT "Proteomic analysis of rice leaf, stem and root tissues during growth
RT course.";
RL Proteomics 6:3665-3670(2006).
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; AP000366; BAD15391.1; -; Genomic_DNA.
DR EMBL; AP005785; BAD34026.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF08079.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS77421.1; -; Genomic_DNA.
DR EMBL; AK061629; BAG88043.1; -; mRNA.
DR EMBL; AK065909; BAG89730.1; -; mRNA.
DR RefSeq; XP_015623954.1; XM_015768468.1.
DR AlphaFoldDB; Q7F8S5; -.
DR SMR; Q7F8S5; -.
DR STRING; 4530.OS02T0192700-02; -.
DR PeroxiBase; 4019; OsPrxII0502.
DR PaxDb; Q7F8S5; -.
DR PRIDE; Q7F8S5; -.
DR EnsemblPlants; Os02t0192700-02; Os02t0192700-02; Os02g0192700.
DR GeneID; 4328586; -.
DR Gramene; Os02t0192700-02; Os02t0192700-02; Os02g0192700.
DR KEGG; osa:4328586; -.
DR eggNOG; KOG0541; Eukaryota.
DR HOGENOM; CLU_072440_0_0_1; -.
DR InParanoid; Q7F8S5; -.
DR OMA; NVQPLKC; -.
DR OrthoDB; 1281610at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q7F8S5; 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 1: Evidence at protein level;
KW Antioxidant; Chloroplast; Direct protein sequencing; Oxidoreductase;
KW Peroxidase; Plastid; Redox-active center; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..42
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 43..225
FT /note="Peroxiredoxin-2E-2, chloroplastic"
FT /id="PRO_0000282284"
FT DOMAIN 63..225
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 111
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:A9PCL4"
SQ SEQUENCE 225 AA; 23180 MW; 9ED90A75988B6CD7 CRC64;
MAAPTAAALS TLSTASVTSG KRFITSSFSL SFSSRPLATG VRAAGARAAR RSAASASTVV
ATIAVGDKLP DATLSYFDPA DGELKTVTVA ELTAGRKAVL FAVPGAFTPT CSQKHLPGFI
EKAGELHAKG VDAIACVSVN DAFVMRAWKE SLGLGDADVL LLSDGNLELT RALGVEMDLS
DKPMGLGVRS RRYALLADDG VVKVLNLEEG GAFTTSSAEE MLKAL
