AC PRU00297; DC Family; TR PROSITE; PS50873; PEROXIDASE_4; 1; level=0 XX Names: Plant heme peroxidase Function: Removal of H(2)O(2), oxidation of toxic reductants XX case and and and 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. CC -!- CATALYTIC ACTIVITY: CC Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:17499; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 2 calcium ions per subunit.; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class CC III) peroxidase subfamily. end case XX case DR PROSITE; PS00435; PEROXIDASE_1; 1; trigger=no end case case DR PROSITE; PS00436; PEROXIDASE_2; 1; trigger=no end case XX case and and and GO GO:0016491; F:oxidoreductase activity GO GO:0004601; F:peroxidase activity GO GO:0009055; F:electron transfer activity GO GO:0006979; P:response to oxidative stress GO GO:0042744; P:hydrogen peroxide catabolic process KW Secreted KW Oxidoreductase KW Peroxidase KW Hydrogen peroxide end case case GO GO:0020037; F:heme binding GO GO:0005506; F:iron ion binding KW Iron KW Heme end case case KW Pyrrolidone carboxylic acid end case case or GO GO:0005509; F:calcium ion binding KW Calcium end case case or or KW Metal-binding end case case KW Disulfide bond end case FT From: PS50873 FT BINDING 43 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: [DE] FT BINDING 46 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: [VI] FT BINDING 48 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: G FT BINDING 50 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: [DE] FT BINDING 52 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: [ST] FT BINDING 169 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#2" FT Group: 2; Condition: [TS] FT BINDING 222 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#2" FT Group: 2; Condition: [DE] FT BINDING 225 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#2" FT Group: 2; Condition: [TS] FT BINDING 230 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#2" FT Group: 2; Condition: [DE] FT SITE 38 FT /note="Transition state stabilizer" FT Group: 3; Condition: R FT ACT_SITE 42 FT /note="Proton acceptor" FT Group: 3; Condition: H FT BINDING 168 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Group: 3; Condition: H FT DISULFID 11..90 FT Tag: disulf; Condition: C-x*-C FT DISULFID 44..49 FT Tag: disulf, viacarbo; Condition: C-x*-C FT DISULFID 96..298 FT Tag: disulf; Condition: C-x*-C FT DISULFID 175..207 FT Tag: disulf; Condition: C-x*-C FT MOD_RES 1 FT /note="Pyrrolidone carboxylic acid" FT Condition: Q case FT BINDING 138 FT /ligand="substrate" FT Condition: P end case XX Chop: Nter=0; Cter=0; Size: 250-384; Related: None; Repeats: 1; Topology: Undefined; Example: P0DI10; Q67Z07; Scope: Eukaryota Comments: None XX # Revision 1.37 2022/11/19 //