PER7_CYCRE
ID PER7_CYCRE Reviewed; 24 AA.
AC P85433;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Peroxidase 7;
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 AlphaFoldDB; P85433; -.
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; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR Pfam; PF00141; peroxidase; 1.
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..>24
FT /note="Peroxidase 7"
FT /id="PRO_0000320214"
FT BINDING 18
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 19
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 24
FT /evidence="ECO:0000303|PubMed:19157640"
SQ SEQUENCE 24 AA; 2469 MW; 9D79FE7DD4DCB220 CRC64;
FNALGLSTRD LVALSGAHTI GQAR
