PER2_CYCRE
ID PER2_CYCRE Reviewed; 15 AA.
AC P85347;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Peroxidase 2;
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=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P22195,
CC ECO:0000255|PROSITE-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,
CC ECO:0000255|PROSITE-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}. 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}.
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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 InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
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..>15
FT /note="Peroxidase 2"
FT /id="PRO_0000315884"
FT BINDING 9
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:P22195,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 10
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 /evidence="ECO:0000303|PubMed:19157640"
FT NON_TER 15
FT /evidence="ECO:0000303|PubMed:19157640"
SQ SEQUENCE 15 AA; 1509 MW; D6D047F4379189B9 CRC64;
DLVALSGAHT IGQAR
