ID   PER3_CAPAN              Reviewed;          45 AA.
AC   P86001;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Peroxidase 3 {ECO:0000250|UniProtKB:Q42578};
DE            EC=1.11.1.7;
DE   Flags: Fragments;
OS   Capsicum annuum (Capsicum pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=4072;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RA   Sabater Jara A.B., Almagro L., 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:Q42578,
CC         ECO:0000255|PROSITE-ProRule:PRU00297};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:Q42578,
CC         ECO:0000255|PROSITE-ProRule:PRU00297};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:Q42578,
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; P86001; -.
DR   Proteomes; UP000189700; Genome assembly.
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..>45
FT                   /note="Peroxidase 3"
FT                   /id="PRO_0000363730"
FT   UNSURE          2
FT                   /note="F or M"
FT   UNSURE          5
FT                   /note="I or L"
FT   UNSURE          8
FT                   /note="I or L"
FT   UNSURE          9
FT                   /note="K or Q"
FT   UNSURE          14
FT                   /note="I or L"
FT   UNSURE          15
FT                   /note="L or I"
FT   UNSURE          23
FT                   /note="K or Q"
FT   UNSURE          24
FT                   /note="M or F"
FT   UNSURE          27
FT                   /note="I or L"
FT   UNSURE          30
FT                   /note="L or I"
FT   UNSURE          37
FT                   /note="I or L"
FT   UNSURE          39
FT                   /note="F or M"
FT   UNSURE          44
FT                   /note="F or M"
FT   UNSURE          45
FT                   /note="K or Q"
FT   NON_CONS        9..10
FT                   /evidence="ECO:0000305"
FT   NON_CONS        23..24
FT                   /evidence="ECO:0000305"
FT   NON_CONS        38..39
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         45
SQ   SEQUENCE   45 AA;  5041 MW;  9052F13737E98315 CRC64;
     GFEVIDNIKD SVVILGGPNW NVKMGDIRPL TGSNGEIRFD NNYFK