PER8_CYCRE
ID PER8_CYCRE Reviewed; 15 AA.
AC P85434;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Peroxidase 8;
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:Q39034,
CC ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000250|UniProtKB:Q39034, ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q39034,
CC ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:Q39034,
CC 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 8"
FT /id="PRO_0000320215"
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:Q39034,
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:Q39034,
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; 1553 MW; D6D047E4369188FC CRC64;
ELVTLSGAHT IGQAR
