| IED ID | IndEnz0018000564 |
| Enzyme Type ID | peroxidase000564 |
| Protein Name |
Peroxidase 22 Atperox P22 EC 1.11.1.7 ATPEa Basic peroxidase E |
| Gene Name | PER22 P22 PRXEA At2g38380 T19C21.13 |
| 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 | MGFSPSFSCSAIGALILGCLLLQASNSNAQLRPDFYFGTCPFVFDIIGNIIVDELQTDPRIAASLLRLHFHDCFVRGCDASILLDNSTSFRTEKDAAPNANSARGFNVIDRMKVALERACPGRVSCADILTIASQISVLLSGGPWWPVPLGRRDSVEAFFALANTALPSPFFNLTQLKTAFADVGLNRTSDLVALSGGHTFGRAQCQFVTPRLYNFNGTNSPDPSLNPTYLVELRRLCPQNGNGTVLVNFDVVTPDAFDSQYYTNLRNGKGLIQSDQELFSTPGADTIPLVNQYSSDMSVFFRAFIDAMIRMGNLRPLTGTQGEIRQNCRVVNPRIRVVENDDGVVSSI |
| Enzyme Length | 349 |
| Uniprot Accession Number | P24102 |
| Absorption | |
| Active Site | ACT_SITE 71; /note=Proton acceptor |
| Activity Regulation | |
| Binding Site | BINDING 168; /note=Substrate; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
| 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Disulfide bond (4); Glycosylation (5); Metal binding (10); Modified residue (1); Sequence conflict (2); Signal peptide (1); Site (1) |
| Keywords | Calcium;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal;Vacuole |
| Interact With | |
| Induction | INDUCTION: Responsiveness to high-salt stress. {ECO:0000269|PubMed:8659887}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Vacuole {ECO:0000305}. Note=Carboxy-terminal extension appears to target the protein to vacuoles. |
| Modified Residue | MOD_RES 30; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297" |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..29; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12953064; 15231406; 15272873; 15449379; 15539469; 15694452; 16262716; 17526915; 17916636; 19880396; 23180292; 23289948; 28627464; |
| Motif | |
| Gene Encoded By | |
| Mass | 38,108 |
| Kinetics | |
| Metal Binding | METAL 72; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 75; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 77; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 79; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 81; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 199; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 200; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 251; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 254; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 259; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
| Rhea ID | RHEA:56136 |
| Cross Reference Brenda |