ID   PER3_VITVI              Reviewed;          41 AA.
AC   P86015;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Peroxidase 3 {ECO:0000250|UniProtKB:Q39034};
DE            EC=1.11.1.7;
DE   Flags: Fragments;
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RA   Almagro L., Belchi-Navarro S., Pedreno M.A.;
RL   Submitted (JUL-2008) 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. These functions might be dependent on each
CC       isozyme/isoform in each plant tissue. {ECO:0000305}.
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   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:Q39034,
CC         ECO:0000255|PROSITE-ProRule:PRU00297};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000250|UniProtKB:Q39034, ECO:0000255|PROSITE-ProRule:PRU00297};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:Q39034,
CC         ECO:0000255|PROSITE-ProRule:PRU00297};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:Q39034,
CC       ECO:0000255|PROSITE-ProRule:PRU00297};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P84516,
CC       ECO:0000255|PROSITE-ProRule:PRU00297}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC       III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}.
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DR   AlphaFoldDB; P86015; -.
DR   SMR; P86015; -.
DR   PRIDE; P86015; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase; Secreted.
FT   CHAIN           <1..>41
FT                   /note="Peroxidase 3"
FT                   /id="PRO_0000352653"
FT   UNSURE          1
FT                   /note="Q or K"
FT   UNSURE          3
FT                   /note="F or M"
FT   UNSURE          6
FT                   /note="I or L"
FT   UNSURE          10
FT                   /note="L or I"
FT   UNSURE          17
FT                   /note="L or I"
FT   UNSURE          19
FT                   /note="L or I"
FT   UNSURE          24
FT                   /note="F or M"
FT   UNSURE          29
FT                   /note="K or Q"
FT   UNSURE          35
FT                   /note="I or L"
FT   UNSURE          36
FT                   /note="L or I"
FT   UNSURE          38
FT                   /note="M or F"
FT   NON_CONS        11..12
FT                   /evidence="ECO:0000305"
FT   NON_CONS        30..31
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         41
SQ   SEQUENCE   41 AA;  4391 MW;  D5442744DC68035C CRC64;
     QTFVTIPGTL RDHPDNLSLA GDGFDTVIKV SCADILTMAT R