ID   PER1_CAPAN              Reviewed;          51 AA.
AC   P85999;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Suberization-associated anionic peroxidase 1 {ECO:0000250|UniProtKB:P15004};
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   -!- FUNCTION: Suggested to catalyze the deposition of the aromatic residues
CC       of suberin on the cell wall and thus play a role in cell-suberization.
CC       {ECO:0000250|UniProtKB:P15004}.
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:P15004,
CC         ECO:0000255|PROSITE-ProRule:PRU00297};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000250|UniProtKB:P15004, ECO:0000255|PROSITE-ProRule:PRU00297};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P15004,
CC         ECO:0000255|PROSITE-ProRule:PRU00297};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:P15004,
CC       ECO:0000255|PROSITE-ProRule:PRU00297};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P15004,
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; P85999; -.
DR   Proteomes; UP000189700; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
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.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   SUPFAM; SSF48113; SSF48113; 1.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase; Secreted.
FT   CHAIN           <1..>51
FT                   /note="Suberization-associated anionic peroxidase 1"
FT                   /id="PRO_0000363728"
FT   BINDING         30
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P15004,
FT                   ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         31
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P15004,
FT                   ECO:0000255|PROSITE-ProRule:PRU00297"
FT   UNSURE          2
FT                   /note="F or M"
FT   UNSURE          5
FT                   /note="I or L"
FT   UNSURE          7
FT                   /note="Q or K"
FT   UNSURE          9
FT                   /note="K or Q"
FT   UNSURE          10
FT                   /note="L or I"
FT   UNSURE          13
FT                   /note="Q or K"
FT   UNSURE          19
FT                   /note="L or I"
FT   UNSURE          23
FT                   /note="M or F"
FT   UNSURE          26
FT                   /note="L or I"
FT   UNSURE          34
FT                   /note="F or M"
FT   UNSURE          37
FT                   /note="M or F"
FT   UNSURE          40
FT                   /note="L or I"
FT   UNSURE          47
FT                   /note="Q or K"
FT   UNSURE          48
FT                   /note="L or I"
FT   UNSURE          50
FT                   /note="I or L"
FT   NON_CONS        9..10
FT                   /evidence="ECO:0000305"
FT   NON_CONS        21..22
FT                   /evidence="ECO:0000305"
FT   NON_CONS        36..37
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         51
SQ   SEQUENCE   51 AA;  5227 MW;  5858CC24E8119BA2 CRC64;
     GFEVIAQAKL GGQTYTVALG REMVALAGAH TVGFARMGNL PPSAGAQLEI R