PER1_CATRO
ID PER1_CATRO Reviewed; 46 AA.
AC P85439;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Peroxidase 1;
DE EC=1.11.1.7;
DE Flags: Fragments;
OS Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Catharanthinae; Catharanthus.
OX NCBI_TaxID=4058;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RA Varman P.A.M., Ranjitha Kumari B.D.;
RL Submitted (JAN-2008) to UniProtKB.
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: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 -!- 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P84516,
CC ECO:0000255|PROSITE-ProRule:PRU00297}.
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; P85439; -.
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.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase; Secreted.
FT CHAIN <1..>46
FT /note="Peroxidase 1"
FT /id="PRO_0000324678"
FT NON_CONS 24..25
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 46
SQ SEQUENCE 46 AA; 4764 MW; 95DE73C8F37F8DEB CRC64;
LVCFVVVVFM AAAAAMAGAD RELKYLSHGG VDFPVPAGRL DGVVSR