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