ID Q69RI4_ORYSJ Unreviewed; 349 AA. AC Q69RI4; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 29-MAY-2024, entry version 21. DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU362060}; DE EC=1.11.1.7 {ECO:0000256|RuleBase:RU362060}; GN Name=P0446F04.127 {ECO:0000313|EMBL:BAD31111.1}; GN OrderedLocusNames=Os07g0104400 {ECO:0000313|EMBL:BAF20606.1}; 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 {ECO:0000313|EMBL:BAD31111.1, ECO:0000313|Proteomes:UP000000763}; RN [1] {ECO:0000313|EMBL:BAD31111.1} RP NUCLEOTIDE SEQUENCE. RA Sasaki T., Matsumoto T., Katayose Y.; RT "Oryza sativa nipponbare(GA3) genomic DNA, chromosome 7, PAC RT clone:P0446F04."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BAF20606.1, ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RA Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N., RA Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y., RA Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N., RA Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M., RA Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., RA Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K., RA Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., Kobayashi N., RA Machita K., Maehara T., Masukawa M., Mizubayashi T., Mukai Y., Nagasaki H., RA Nagata Y., Naito S., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M., RA Meguro A., Negishi M., Ohta I., Ohta T., Okamoto M., Ono N., Saji S., RA Sakaguchi M., Sakai K., Shibata M., Shimokawa T., Song J., Takazaki Y., RA Terasawa K., Tsugane M., Tsuji K., Ueda S., Waki K., Yamagata H., RA Yamamoto M., Yamamoto S., Yamane H., Yoshiki S., Yoshihara R., Yukawa K., RA Zhong H., Yano M., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K., RA Moffat K., Hill J., Bera J., Fadrosh D., Jin S., Johri S., Kim M., RA Overton L., Reardon M., Tsitrin T., Vuong H., Weaver B., Ciecko A., RA Tallon L., Jackson J., Pai G., Aken S.V., Utterback T., Reidmuller S., RA Feldblyum T., Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R., RA Ying K., Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J., RA Weng Q., Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X., RA Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., Samain S., RA Cattolico L., Pelletier E., Couloux A., Segurens B., Wincker P., D'Hont A., RA Scarpelli C., Weissenbach J., Salanoubat M., Quetier F., Yu Y., Kim H.R., RA Rambo T., Currie J., Collura K., Luo M., Yang T., Ammiraju J.S.S., RA Engler F., Soderlund C., Wing R.A., Palmer L.E., de la Bastide M., RA Spiegel L., Nascimento L., Zutavern T., O'Shaughnessy A., Dike S., RA Dedhia N., Preston R., Balija V., McCombie W.R., Chow T., Chen H., RA Chung M., Chen C., Shaw J., Wu H., Hsiao K., Chao Y., Chu M., Cheng C., RA Hour A., Lee P., Lin S., Lin Y., Liou J., Liu S., Hsing Y., Raghuvanshi S., RA Mohanty A., Bharti A.K., Gaur A., Gupta V., Kumar D., Ravi V., Vij S., RA Kapur A., Khurana P., Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K., RA Singh A., Dalal V., Srivastava S., Dixit A., Pal A.K., Ghazi I.A., RA Yadav M., Pandit A., Bhargava A., Sureshbabu K., Batra K., Sharma T.R., RA Mohapatra T., Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S., RA Keizer G., Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K., RA Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., Zimmer P.D., RA Malone G., Dellagostin O., de Oliveira A.C., Bevan M., Bancroft I., RA Minx P., Cordum H., Wilson R., Cheng Z., Jin W., Jiang J., Leong S.A., RA Iwama H., Gojobori T., Itoh T., Niimura Y., Fujii Y., Habara T., Sakai H., RA Sato Y., Wilson G., Kumar K., McCouch S., Juretic N., Hoen D., Wright S., RA Bruskiewich R., Bureau T., Miyao A., Hirochika H., Nishikawa T., RA Kadowaki K., Sugiura M., Burr B., Sasaki T.; RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [3] {ECO:0000313|EMBL:BAF20606.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16381971; DOI=10.1093/nar/gkj094; RA Ohyanagi H., Tanaka T., Sakai H., Shigemoto Y., Yamaguchi K., Habara T., RA Fujii Y., Antonio B.A., Nagamura Y., Imanishi T., Ikeo K., Itoh T., RA Gojobori T., Sasaki T.; RT "The Rice Annotation Project Database (RAP-DB): hub for Oryza sativa ssp. RT japonica genome information."; RL Nucleic Acids Res. 34:D741-D744(2006). RN [4] {ECO:0000313|EMBL:BAF20606.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RA Itoh T., Tanaka T., Barrero R.A., Yamasaki C., Fujii Y., Hilton P.B., RA Antonio B.A., Aono H., Apweiler R., Bruskiewich R., Bureau T., Burr F., RA Costa de Oliveira A., Fuks G., Habara T., Haberer G., Han B., Harada E., RA Hiraki A.T., Hirochika H., Hoen D., Hokari H., Hosokawa S., Hsing Y., RA Ikawa H., Ikeo K., Imanishi T., Ito Y., Jaiswal P., Kanno M., Kawahara Y., RA Kawamura T., Kawashima H., Khurana J.P., Kikuchi S., Komatsu S., RA Koyanagi K.O., Kubooka H., Lieberherr D., Lin Y.C., Lonsdale D., RA Matsumoto T., Matsuya A., McCombie W.R., Messing J., Miyao A., Mulder N., RA Nagamura Y., Nam J., Namiki N., Numa H., Nurimoto S., O'donovan C., RA Ohyanagi H., Okido T., Oota S., Osato N., Palmer L.E., Quetier F., RA Raghuvanshi S., Saichi N., Sakai H., Sakai Y., Sakata K., Sakurai T., RA Sato F., Sato Y., Schoof H., Seki M., Shibata M., Shimizu Y., Shinozaki K., RA Shinso Y., Singh N.K., Smith-White B., Takeda J., Tanino M., Tatusova T., RA Thongjuea S., Todokoro F., Tsugane M., Tyagi A.K., Vanavichit A., Wang A., RA Wing R.A., Yamaguchi K., Yamamoto M., Yamamoto N., Yu Y., Zhang H., RA Zhao Q., Higo K., Burr B., Gojobori T., Sasaki T.; RT "Curated Genome Annotation of Oryza sativa ssp. japonica and Comparative RT Genome Analysis with Arabidopsis thaliana."; RL Genome Res. 17:175-183(2007). RN [5] {ECO:0000313|EMBL:BAF20606.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RA Tanaka T., Antonio B.A., Kikuchi S., Matsumoto T., Nagamura Y., Numa H., RA Sakai H., Wu J., Itoh T., Sasaki T., Aono R., Fujii Y., Habara T., RA Harada E., Kanno M., Kawahara Y., Kawashima H., Kubooka H., Matsuya A., RA Nakaoka H., Saichi N., Sanbonmatsu R., Sato Y., Shinso Y., Suzuki M., RA Takeda J., Tanino M., Todokoro F., Yamaguchi K., Yamamoto N., Yamasaki C., RA Imanishi T., Okido T., Tada M., Ikeo K., Tateno Y., Gojobori T., Lin Y.C., RA Wei F.J., Hsing Y.I., Zhao Q., Han B., Kramer M.R., McCombie R.W., RA Lonsdale D., O'Donovan C.C., Whitfield E.J., Apweiler R., Koyanagi K.O., RA Khurana J.P., Raghuvanshi S., Singh N.K., Tyagi A.K., Haberer G., RA Fujisawa M., Hosokawa S., Ito Y., Ikawa H., Shibata M., Yamamoto M., RA Bruskiewich R.M., Hoen D.R., Bureau TE., Namiki N., Ohyanagi H., Sakai Y., RA Nobushima S., Sakata K., Barrero R.A., Sato Y., Souvorov A., RA Smith-White B., Tatusova T., An S., An G., OOta S., Fuks G., Messing J., RA Christie K.R., Lieberherr D., Kim H., Zuccolo A., Wing R.A., Nobuta K., RA Green P.J., Lu C., Meyers BC., Chaparro C., Piegu B., Panaud O., RA Echeverria M.; RT "The Rice Annotation Project Database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [6] {ECO:0000313|Proteomes:UP000000763} RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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 [7] {ECO:0000313|EMBL:BAF20606.1} RP NUCLEOTIDE SEQUENCE. RG IRGSP(International Rice Genome Sequencing Project); RT "Oryza sativa nipponbare(GA3) genomic DNA, chromosome 7."; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:BAF20606.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RT "The Second Rice Annotation Project Meeting (RAP2)."; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00002322}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; CC Evidence={ECO:0000256|ARBA:ARBA00000189, CC ECO:0000256|RuleBase:RU362060}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3, CC ECO:0000256|RuleBase:RU362060}; CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR600823- CC 3, ECO:0000256|RuleBase:RU362060}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3, CC ECO:0000256|RuleBase:RU362060}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. CC {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362060}. CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase CC subfamily. {ECO:0000256|ARBA:ARBA00006873}. CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class CC III) peroxidase subfamily. {ECO:0000256|RuleBase:RU362060}. 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; AP005187; BAD31111.1; -; Genomic_DNA. DR EMBL; AP008213; BAF20606.1; -; Genomic_DNA. DR RefSeq; XP_015645804.1; XM_015790318.1. DR AlphaFoldDB; Q69RI4; -. DR GeneID; 4342186; -. DR KEGG; osa:4342186; -. DR OrthoDB; 356633at2759; -. DR Proteomes; UP000000763; Chromosome 7. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0009505; C:plant-type cell wall; IEA:TreeGrafter. DR GO; GO:0009506; C:plasmodesma; IEA:TreeGrafter. DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule. DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. 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 Gene3D; 1.10.520.10; -; 1. DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1. DR InterPro; IPR002016; Haem_peroxidase. DR InterPro; IPR010255; Haem_peroxidase_sf. DR InterPro; IPR000823; Peroxidase_pln. DR InterPro; IPR019793; Peroxidases_heam-ligand_BS. DR InterPro; IPR033905; Secretory_peroxidase. DR PANTHER; PTHR31235:SF239; PEROXIDASE; 1. DR PANTHER; PTHR31235; PEROXIDASE 25-RELATED; 1. DR Pfam; PF00141; peroxidase; 1. DR PRINTS; PR00458; PEROXIDASE. DR PRINTS; PR00461; PLPEROXIDASE. DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1. DR PROSITE; PS00435; PEROXIDASE_1; 1. DR PROSITE; PS50873; PEROXIDASE_4; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR600823-3}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR600823-5}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Heme {ECO:0000256|RuleBase:RU362060}; KW Hydrogen peroxide {ECO:0000256|RuleBase:RU362060}; KW Iron {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR600823-3, KW ECO:0000256|RuleBase:RU362060}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362060}; KW Peroxidase {ECO:0000256|RuleBase:RU362060, ECO:0000313|EMBL:BAD31111.1}; KW Pyrrolidone carboxylic acid {ECO:0000256|ARBA:ARBA00023283}; KW Secreted {ECO:0000256|RuleBase:RU362060}; KW Signal {ECO:0000256|RuleBase:RU362060}. FT SIGNAL 1..36 FT /evidence="ECO:0000256|RuleBase:RU362060" FT CHAIN 37..349 FT /note="Peroxidase" FT /evidence="ECO:0000256|RuleBase:RU362060" FT /id="PRO_5039740446" FT DOMAIN 45..347 FT /note="Plant heme peroxidase family profile" FT /evidence="ECO:0000259|PROSITE:PS50873" FT ACT_SITE 86 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1" FT BINDING 87 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 90 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 92 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 94 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 96 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 108 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 182 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2" FT BINDING 212 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:0000256|PIRSR:PIRSR600823-3" FT BINDING 213 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 265 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 273 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT SITE 82 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4" FT DISULFID 55..134 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 88..93 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 140..343 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 219..249 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" SQ SEQUENCE 349 AA; 37483 MW; 311CD3416AE06000 CRC64; MAAAAAARIS STASQLRLSW LMVMLMLVAS NNNAAAAPPA AAAGQLRTGY YRETCPHAEE MVFRETARII RASPDLAAAL LRLHYHDCFV QGCDASVLLD STRANAAERD SDPNKSLRGF DSVARVKAKL EAACPATVSC ADLLALMARD AVVLAKGPYW HVPLGRRDGR SSTAASCGGQ LPPLCGNVSR MVDSFAAKGL DVKDLVVLSA AHTLGKAHCP NFADRLYGPG ADPPLKLDGA YADRLRKQCK EGAPPYDGNV TAEMDPGSFT RFDSSYFRQV VRRRALLRSD ACLMDHPFTS AYIRLAATGR YDGHFFQDFA HSMVKMGAIG VLTGDQGEIR LKCNVVNST //