PER22_ORYSJ
ID PER22_ORYSJ Reviewed; 317 AA.
AC Q7F1U0; O22438; Q0D3N1; Q43006;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Peroxidase 22.3 {ECO:0000305};
DE EC=1.11.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=POX22.3 {ECO:0000303|PubMed:9304860}; Synonyms=PRX111 {ECO:0000305};
GN OrderedLocusNames=Os07g0677200 {ECO:0000312|EMBL:BAT03206.1},
GN LOC_Os07g48020 {ECO:0000305};
GN ORFNames=OJ1167_G06.125 {ECO:0000312|EMBL:BAC83103.1};
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 [MRNA].
RX PubMed=16653172; DOI=10.1104/pp.100.3.1611;
RA Reimmann C., Ringli C., Dudler R.;
RT "Complementary DNA cloning and sequence analysis of a pathogen-induced
RT putative peroxidase from rice.";
RL Plant Physiol. 100:1611-1612(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC TISSUE=Leaf;
RX PubMed=9304860; DOI=10.1094/mpmi.1997.10.7.861;
RA Chittoor J.M., Leach J.E., White F.F.;
RT "Differential induction of a peroxidase gene family during infection of
RT rice by Xanthomonas oryzae pv. oryzae.";
RL Mol. Plant Microbe Interact. 10:861-871(1997).
RN [3]
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 [4]
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 [5]
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 [6]
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: Removal of H(2)O(2), oxidation of toxic reductants,
CC biosynthesis and degradation of lignin, suberization, auxin catabolism,
CC response to environmental stresses such as wounding, pathogen attack
CC and oxidative stress. These functions might be dependent on each
CC isozyme/isoform in each plant tissue. {ECO:0000255|PROSITE-
CC ProRule:PRU00297}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17499; Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00297};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- INDUCTION: Induced by infection with the bacterial pathogen Xanthomonas
CC oryzae pv oryzae, and wounding in mature leaves.
CC {ECO:0000269|PubMed:16653172}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}.
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DR EMBL; X66125; CAA46916.1; -; mRNA.
DR EMBL; AF014467; AAC49818.1; -; mRNA.
DR EMBL; AP003817; BAC83103.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF22542.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT03206.1; -; Genomic_DNA.
DR EMBL; AK073202; BAG93342.1; -; mRNA.
DR EMBL; AK104710; BAG96895.1; -; mRNA.
DR PIR; S22087; S22087.
DR RefSeq; XP_015647952.1; XM_015792466.1.
DR AlphaFoldDB; Q7F1U0; -.
DR SMR; Q7F1U0; -.
DR STRING; 4530.OS07T0677200-01; -.
DR PeroxiBase; 1121; OsPrx111.
DR PaxDb; Q7F1U0; -.
DR PRIDE; Q7F1U0; -.
DR EnsemblPlants; Os07t0677200-01; Os07t0677200-01; Os07g0677200.
DR Gramene; Os07t0677200-01; Os07t0677200-01; Os07g0677200.
DR KEGG; osa:4344278; -.
DR eggNOG; ENOG502QSXF; Eukaryota.
DR HOGENOM; CLU_010543_0_0_1; -.
DR InParanoid; Q7F1U0; -.
DR OMA; CFFIGIV; -.
DR OrthoDB; 902776at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR ExpressionAtlas; Q7F1U0; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:UniProtKB-UniRule.
DR CDD; cd00693; secretory_peroxidase; 1.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR000823; Peroxidase_pln.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31388; PTHR31388; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00458; PEROXIDASE.
DR PRINTS; PR00461; PLPEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..317
FT /note="Peroxidase 22.3"
FT /id="PRO_5013421034"
FT ACT_SITE 67
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 189
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 63
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT MOD_RES 26
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 36..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 69..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 117..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 196..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 234
FT /note="P -> A (in Ref. 2; AAC49818)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="L -> V (in Ref. 1; CAA46916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 32890 MW; 94C7371A604029AB CRC64;
MASATNSSLS LMLLVAAAMA SVASAQLSAT FYDTSCPNAL STIKSVITAA VNSEARMGAS
LLRLHFHDCF VQGCDASVLL SGQEQNAGPN VGSLRGFSVI DNAKARVEAI CNQTVSCADI
LAVAARDSVV ALGGPSWTVL LGRRDSTTAS EALANTDLPA PSSSLAELIG NFSRKGLDAT
DMVALSGAHT IGQAQCQNFR DRIYNETNID SAFATQRQAN CPRPTGSGDS NLAPLDTTTP
NAFDNAYYSN LLSNKGLLHS DQVLFNGGSA DNTVRNFASN AAAFSSAFTT AMVKMGNISP
LTGTQGQIRL SCSKVNS
