ID   PER3_BETPN              Reviewed;          19 AA.
AC   P85334;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   02-SEP-2026, entry version 26.
DE   RecName: Full=Peroxidase 3;
DE            EC=1.11.1.7;
DE   Flags: Fragment;
OS   Betula pendula (European white birch) (Betula verrucosa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Betulaceae; Betula.
OX   NCBI_TaxID=3505;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=PC-1121; TISSUE=Callus;
RX   PubMed=19055540; DOI=10.1111/j.1399-3054.2008.01185.x;
RA   Novo Uzal E., Gomez Ros L.V., Pomar F., Bernal M.A., Paradela A.,
RA   Albar J.P., Ros Barcelo A.;
RT   "The presence of sinapyl lignin in Ginkgo biloba cell cultures changes our
RT   views of the evolution of lignin biosynthesis.";
RL   Physiol. Plantarum 135:196-213(2009).
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=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P22195, ECO:0000255|PROSITE-
CC         ProRule:PRU00297};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:P22195,
CC       ECO:0000255|PROSITE-ProRule:PRU00297};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P22195, ECO:0000255|PROSITE-
CC         ProRule:PRU00297};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000250|UniProtKB:P22195, 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; P85334; -.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase; Secreted.
FT   CHAIN           <1..>19
FT                   /note="Peroxidase 3"
FT                   /id="PRO_0000314640"
FT   BINDING         6
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22195,
FT                   ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         9
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22195,
FT                   ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         14
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22195,
FT                   ECO:0000255|PROSITE-ProRule:PRU00297"
FT   NON_TER         1
FT   NON_TER         19
SQ   SEQUENCE   19 AA;  2198 MW;  BA127D88EF62A3F4 CRC64;
     NLAPLDLQTP TAFDNNYYK
//