ID A0A3B6ATT5_WHEAT Unreviewed; 363 AA. AC A0A3B6ATT5; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 17-JUN-2020, entry version 12. DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215714}; DE EC=1.11.1.7 {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215714}; OS Triticum aestivum (Wheat). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum. OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS2A02G149400.1}; RN [1] {ECO:0000313|EnsemblPlants:TraesCS2A02G149400.1} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (OCT-2018) to UniProtKB. 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. {ECO:0000256|RuleBase:RU362060}. 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|RuleBase:RU362060, CC ECO:0000256|SAAS:SAAS01215718}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362060}. CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class CC III) peroxidase subfamily. {ECO:0000256|RuleBase:RU362060, CC ECO:0000256|SAAS:SAAS01215721}. 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 EnsemblPlants; TraesCS2A02G149400.1; TraesCS2A02G149400.1; TraesCS2A02G149400. DR Gramene; TraesCS2A02G149400.1; TraesCS2A02G149400.1; TraesCS2A02G149400. DR OMA; QCRESEM; -. DR Proteomes; UP000019116; Unplaced. 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; IPR019793; Peroxidases_heam-ligand_BS. DR InterPro; IPR033905; Secretory_peroxidase. 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; PS50873; PEROXIDASE_4; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR600823-5, KW ECO:0000256|SAAS:SAAS00449210}; KW Heme {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215736}; KW Hydrogen peroxide {ECO:0000256|RuleBase:RU362060}; KW Iron {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS01215715}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR600823-3, KW ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215733}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS01215720}; KW Peroxidase {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215725}; KW Reference proteome {ECO:0000313|Proteomes:UP000019116}; KW Secreted {ECO:0000256|RuleBase:RU362060}; KW Signal {ECO:0000256|RuleBase:RU362060}. FT SIGNAL 1..23 FT /evidence="ECO:0000256|RuleBase:RU362060" FT CHAIN 24..363 FT /note="Peroxidase" FT /evidence="ECO:0000256|RuleBase:RU362060" FT /id="PRO_5017098036" FT DOMAIN 64..361 FT /note="PEROXIDASE_4" FT /evidence="ECO:0000259|PROSITE:PS50873" FT REGION 24..60 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 28..60 FT /note="Pro-rich" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 102 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1" FT METAL 103 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 108 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 110 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 112 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 125 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 231 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 232 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 281 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 284 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 289 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 201 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2" FT SITE 98 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4" FT DISULFID 74..151 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 104..109 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 157..357 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 238..268 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" SQ SEQUENCE 363 AA; 39026 MW; 180DF6299C9A76E5 CRC64; MAKLAAALTV LALLGCMARE GQADYGHPSP PPSTPCSPGH PSTPPSTATP PPPAPVPSPP ASAELVVGYY QKTCHRAEDI VRETVRGANA GIMAGLVRLF FHDCFIRGCD ASVLLDLADP SSATEKFGLP NLSLRGFEVI DAAKARIEKE CGNVVSCADV LAFAGRDATY FLSNKKVYFE MPAGRYDGRV SLINETLIHL PPPFATVEQL KANFASKGLS ADEMVTLSGA HTIGVSHCSS FDDDFSDRLN ASTSDMDPKL MASLEKQCRS DTGNDNTVVQ DIKTPNKLDN KYYKNVLSHE VLFASDAALL TADDTSAAVR AYAEDNNVWE EKFKAAMVRM GAIEVKTSAD GEIRRSCRIL NTY //