ID   PER_CYNCS               Reviewed;          43 AA.
AC   P84714;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Peroxidase;
DE            EC=1.11.1.7;
DE   Flags: Fragments;
OS   Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC   Carduinae; Cynara.
OX   NCBI_TaxID=59895;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   STRAIN=cv. Violetto di Provenza {ECO:0000269|Ref.1};
RC   TISSUE=Leaf {ECO:0000269|Ref.1};
RX   AGRICOLA=IND44019705; DOI=10.1002/jsfa.2882;
RA   Cardinali A., Sergio L., Di Venere D., Linsalata V., Fortunato D.,
RA   Conti A., Lattanzio V.;
RT   "Purification and characterization of a cationic peroxidase from artichoke
RT   leaves.";
RL   J. Sci. Food Agric. 87:1417-1423(2007).
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:P00433,
CC         ECO:0000255|PROSITE-ProRule:PRU00297};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:P00433,
CC       ECO:0000255|PROSITE-ProRule:PRU00297};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P00433,
CC         ECO:0000255|PROSITE-ProRule:PRU00297};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000250|UniProtKB:P00433, ECO:0000255|PROSITE-ProRule:PRU00297};
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 9.3,
CC       its MW is: 38249 kDa. {ECO:0000269|Ref.1}.
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; P84714; -.
DR   SMR; P84714; -.
DR   PRIDE; P84714; -.
DR   BRENDA; 1.11.1.7; 1789.
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.
FT   CHAIN           <1..>43
FT                   /note="Peroxidase"
FT                   /id="PRO_0000055606"
FT   NON_CONS        13..14
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_CONS        28..29
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_TER         43
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   43 AA;  4616 MW;  C93CBF95846E20CC CRC64;
     VVSCADITAL AARQGLFTSD QDLYTDSRMG QLNVLTGTQG EIR