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PER1_VITVI
ID   PER1_VITVI              Reviewed;          26 AA.
AC   P86014;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Peroxidase 1 {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   Belchi-Navarro S., Almagro L., Bru R., 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; P86014; -.
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..>26
FT                   /note="Peroxidase 1"
FT                   /id="PRO_0000352652"
FT   BINDING         15
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q39034,
FT                   ECO:0000255|PROSITE-ProRule:PRU00297"
FT   UNSURE          6
FT                   /note="I or L"
FT   UNSURE          7
FT                   /note="L or I"
FT   UNSURE          9
FT                   /note="M or F"
FT   UNSURE          13
FT                   /note="Q or K"
FT   UNSURE          14
FT                   /note="F or M"
FT   UNSURE          20
FT                   /note="K or Q"
FT   UNSURE          22
FT                   /note="L or I"
FT   UNSURE          23
FT                   /note="Q or K"
FT   UNSURE          24
FT                   /note="Q or K"
FT   NON_CONS        12..13
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         26
SQ   SEQUENCE   26 AA;  3007 MW;  92AB1F1B06536742 CRC64;
     VSCADILTMA TRQFDNVYYK NLQQGK
 
 
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