| IED ID | IndEnz0018000643 |
| Enzyme Type ID | peroxidase000643 |
| Protein Name |
Peroxidase 53 Atperox P53 EC 1.11.1.7 ATPA2 |
| Gene Name | PER53 P53 At5g06720 MPH15.8 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MAVTNLPTCDGLFIISLIVIVSSIFGTSSAQLNATFYSGTCPNASAIVRSTIQQALQSDTRIGASLIRLHFHDCFVNGCDASILLDDTGSIQSEKNAGPNVNSARGFNVVDNIKTALENACPGVVSCSDVLALASEASVSLAGGPSWTVLLGRRDSLTANLAGANSSIPSPIESLSNITFKFSAVGLNTNDLVALSGAHTFGRARCGVFNNRLFNFSGTGNPDPTLNSTLLSTLQQLCPQNGSASTITNLDLSTPDAFDNNYFANLQSNDGLLQSDQELFSTTGSSTIAIVTSFASNQTLFFQAFAQSMINMGNISPLTGSNGEIRLDCKKVNGS |
| Enzyme Length | 335 |
| Uniprot Accession Number | Q42578 |
| Absorption | |
| Active Site | ACT_SITE 72; /note=Proton acceptor |
| Activity Regulation | |
| Binding Site | BINDING 169; /note=Substrate; via carbonyl oxygen |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; |
| DNA Binding | |
| EC Number | 1.11.1.7 |
| Enzyme Function | FUNCTION: Removal 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.; FUNCTION: Closely linked to lignin formation by showing monolignol substrate specificity. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (6); Binding site (1); Chain (1); Disulfide bond (4); Glycosylation (8); Helix (18); Metal binding (10); Modified residue (1); Sequence conflict (4); Signal peptide (1); Site (1); Turn (4) |
| Keywords | 3D-structure;Calcium;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}. |
| Modified Residue | MOD_RES 31; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:8977116" |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1PA2; 1QO4; |
| Mapped Pubmed ID | 12169696; 12473102; 15047898; 15231406; 15235117; 15694452; 15918878; 17022476; 17991993; 18650403; 18686036; 21333657; 22210598; 22212122; 23183257; 23738689; 25137070; 26567581; 32423827; |
| Motif | |
| Gene Encoded By | |
| Mass | 34,989 |
| Kinetics | |
| Metal Binding | METAL 73; /note=Calcium 1; METAL 76; /note=Calcium 1; via carbonyl oxygen; METAL 78; /note=Calcium 1; via carbonyl oxygen; METAL 80; /note=Calcium 1; METAL 82; /note=Calcium 1; METAL 199; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 200; /note=Calcium 2; METAL 251; /note=Calcium 2; METAL 254; /note=Calcium 2; METAL 259; /note=Calcium 2 |
| Rhea ID | RHEA:56136 |
| Cross Reference Brenda |