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ProRule PRU00297


General rule information [?]

Accession PRU00297
Dates 12-DEC-2003 (Created)
19-NOV-2022 (Last updated, Version 37)
Data class Family;
Predictors PROSITE; PS50873; PEROXIDASE_4
Name Plant heme peroxidase
Function Removal of H(2)O(2), oxidation of toxic reductants
Scope(s) Eukaryota
Example(s) P0DI10 (PER1_ARATH); Q67Z07 (PER2_ARATH);

Propagated annotation [?]

Comments [?]

case <FTGroup:1> and <FTGroup:2> and <FTGroup:3> and <FTTag:viacarbo>
FUNCTIONRemoval of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
CATALYTIC ACTIVITY Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499;
COFACTOR Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
COFACTOR Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 2 calcium ions per subunit.;
SUBCELLULAR LOCATIONSecreted.
SIMILARITYBelongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.
end case

Keywords [?]

case <FTGroup:1> and <FTGroup:2> and <FTGroup:3> and <FTTag:viacarbo>
Secreted
Oxidoreductase
Peroxidase
Hydrogen peroxide
end case
case <FT:12>
Iron
Heme
end case
case <FT:17>
Pyrrolidone carboxylic acid
end case
case <FTGroup:1> or <FTGroup:2>
Calcium
end case
case <FT:12> or <FTGroup:1> or <FTGroup:2>
Metal-binding
end case
case <FTTag:disulf>
Disulfide bond
end case

Gene Ontology [?]

case <FTGroup:1> and <FTGroup:2> and <FTGroup:3> and <FTTag:viacarbo>
GO:0016491; Molecular function:oxidoreductase activity
GO:0004601; Molecular function:peroxidase activity
GO:0009055; Molecular function:electron transfer activity
GO:0006979; Biological process:response to oxidative stress
GO:0042744; Biological process:hydrogen peroxide catabolic process
end case
case <FT:12>
GO:0020037; Molecular function:heme binding
GO:0005506; Molecular function:iron ion binding
end case
case <FTGroup:1> or <FTGroup:2>
GO:0005509; Molecular function:calcium ion binding
end case

Cross-references [?]

PROSITE PS00435; PEROXIDASE_1; 1;
PROSITE PS00436; PEROXIDASE_2; 1;

Features [?]

From: PS50873
Key From To Description Tag Condition FTGroup
BINDING 43 43 /ligand="Ca(2+)"
/ligand_id="ChEBI:CHEBI:29108"
/ligand_label="#1"		 [DE] 1
BINDING 46 46 /ligand="Ca(2+)"
/ligand_id="ChEBI:CHEBI:29108"
/ligand_label="#1"		 [VI] 1
BINDING 48 48 /ligand="Ca(2+)"
/ligand_id="ChEBI:CHEBI:29108"
/ligand_label="#1"		 G 1
BINDING 50 50 /ligand="Ca(2+)"
/ligand_id="ChEBI:CHEBI:29108"
/ligand_label="#1"		 [DE] 1
BINDING 52 52 /ligand="Ca(2+)"
/ligand_id="ChEBI:CHEBI:29108"
/ligand_label="#1"		 [ST] 1
BINDING 169 169 /ligand="Ca(2+)"
/ligand_id="ChEBI:CHEBI:29108"
/ligand_label="#2"		 [TS] 2
BINDING 222 222 /ligand="Ca(2+)"
/ligand_id="ChEBI:CHEBI:29108"
/ligand_label="#2"		 [DE] 2
BINDING 225 225 /ligand="Ca(2+)"
/ligand_id="ChEBI:CHEBI:29108"
/ligand_label="#2"		 [TS] 2
BINDING 230 230 /ligand="Ca(2+)"
/ligand_id="ChEBI:CHEBI:29108"
/ligand_label="#2"		 [DE] 2
SITE 38 38 /note="Transition state stabilizer" R 3
ACT_SITE 42 42 /note="Proton acceptor" H 3
BINDING 168 168 /ligand="heme b"
/ligand_id="ChEBI:CHEBI:60344"
/ligand_part="Fe"
/ligand_part_id="ChEBI:CHEBI:18248"
/note="axial binding residue"		 H 3
DISULFID 11 90 disulf C-x*-C
DISULFID 44 49 disulf, viacarbo C-x*-C
DISULFID 96 298 disulf C-x*-C
DISULFID 175 207 disulf C-x*-C
MOD_RES 1 1 /note="Pyrrolidone carboxylic acid" Q
case <FTTag:viacarbo>
BINDING 138 138 /ligand="substrate" P
end case

Additional information [?]

Size range 250-384 amino acids
Related rules None
Fusion None
Repeats 1
Topology Undefined

Copyright

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.



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UniProtKB rule member sequences [?]