ID   A0A3B6ATT5_WHEAT        Unreviewed;       363 AA.
AC   A0A3B6ATT5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   29-SEP-2021, entry version 18.
DE   RecName: Full=Peroxidase {ECO:0000256|ARBA:ARBA00012313, ECO:0000256|RuleBase:RU362060};
DE            EC=1.11.1.7 {ECO:0000256|ARBA:ARBA00012313, ECO:0000256|RuleBase:RU362060};
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|ARBA:ARBA00000189,
CC         ECO:0000256|RuleBase:RU362060};
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}.
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DR   SMR; A0A3B6ATT5; -.
DR   EnsemblPlants; TraesCS2A02G149400.1; TraesCS2A02G149400.1; TraesCS2A02G149400.
DR   Gramene; TraesCAD_scaffold_072676_01G000100.1; TraesCAD_scaffold_072676_01G000100.1; TraesCAD_scaffold_072676_01G000100.
DR   Gramene; TraesCLE_scaffold_199769_01G000100.1; TraesCLE_scaffold_199769_01G000100.1; TraesCLE_scaffold_199769_01G000100.
DR   Gramene; TraesCS2A02G149400.1; TraesCS2A02G149400.1; TraesCS2A02G149400.
DR   Gramene; TraesPAR_scaffold_188974_01G000100.1; TraesPAR_scaffold_188974_01G000100.1; TraesPAR_scaffold_188974_01G000100.
DR   Gramene; TraesSTA2A01G156000.1; TraesSTA2A01G156000.1; TraesSTA2A01G156000.
DR   Gramene; TraesWEE_scaffold_157589_01G000100.1; TraesWEE_scaffold_157589_01G000100.1; TraesWEE_scaffold_157589_01G000100.
DR   OMA; QCRESEM; -.
DR   Proteomes; UP000019116; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009505; C:plant-type cell wall; IBA:GO_Central.
DR   GO; GO:0009506; C:plasmodesma; IBA:GO_Central.
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; IBA:GO_Central.
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|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR600823-3};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR600823-5};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, 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|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU362060};
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 residues"
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
//