ID   A0A3B6ATT5_WHEAT        Unreviewed;       363 AA.
AC   A0A3B6ATT5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   16-OCT-2019, entry version 8.
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, ECO:0000313|Proteomes:UP000019116};
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
CC       catabolism, response to environmental stresses such as wounding,
CC       pathogen attack and oxidative stress.
CC       {ECO:0000256|RuleBase:RU362060}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor +
CC         2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521;
CC         EC=1.11.1.7; 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
CC       (class III) peroxidase subfamily. {ECO:0000256|RuleBase:RU362060,
CC       ECO:0000256|SAAS:SAAS01215721}.
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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|RuleBase:RU362060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019116};
KW   Disulfide bond {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|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215715};
KW   Metal-binding {ECO:0000256|RuleBase:RU362060,
KW   ECO:0000256|SAAS:SAAS01215733};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362060,
KW   ECO:0000256|SAAS:SAAS01215720};
KW   Peroxidase {ECO:0000256|RuleBase:RU362060,
KW   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       {ECO:0000256|RuleBase:RU362060}.
FT   CHAIN        24    363       Peroxidase. {ECO:0000256|RuleBase:
FT                                RU362060}.
FT                                /FTId=PRO_5017098036.
FT   DOMAIN       64    361       PEROXIDASE_4. {ECO:0000259|PROSITE:
FT                                PS50873}.
FT   REGION       24     60       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     28     60       Pro-rich. {ECO:0000256|SAM:MobiDB-lite}.
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
//