ID   PER9_CYCRE              Reviewed;           9 AA.
AC   P85976;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   23-FEB-2022, entry version 22.
DE   RecName: Full=Peroxidase 9 {ECO:0000250|UniProtKB:Q42578};
DE            EC=1.11.1.7;
DE   Flags: Fragment;
OS   Cycas revoluta (Sago palm).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Cycadidae; Cycadales; Cycadaceae; Cycas.
OX   NCBI_TaxID=3396;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Callus {ECO:0000269|PubMed:19157640};
RX   PubMed=19157640; DOI=10.1016/j.jplph.2008.11.009;
RA   Uzal E.N., Gomez-Ros L.V., Hernandez J.A., Pedreno M.A., Cuello J.,
RA   Ros Barcelo A.;
RT   "Analysis of the soluble cell wall proteome of gymnosperms.";
RL   J. Plant Physiol. 166:831-843(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=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:Q42578,
CC       ECO:0000255|PROSITE-ProRule:PRU00297}. Secreted, cell wall
CC       {ECO:0000269|PubMed:19157640}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC       III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297,
CC       ECO:0000269|PubMed:19157640}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PRIDE; P85976; -.
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; Cell wall; Direct protein sequencing; Heme; Hydrogen peroxide;
KW   Iron; Metal-binding; Oxidoreductase; Peroxidase; Secreted.
FT   CHAIN           <1..>9
FT                   /note="Peroxidase 9"
FT                   /id="PRO_0000355099"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:19157640"
FT   NON_TER         9
FT                   /evidence="ECO:0000303|PubMed:19157640"
SQ   SEQUENCE   9 AA;  1062 MW;  DD355AA440505B19 CRC64;
     AFEIINDIK