| IED ID | IndEnz0018000018 |
| Enzyme Type ID | peroxidase000018 |
| Protein Name |
Peroxidase 33 Atperox P33 EC 1.11.1.7 ATPCa Neutral peroxidase C PERC |
| Gene Name | PER33 P33 PRXCA At3g49110 F2K15.4 T2J13.50 |
| 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 | MQFSSSSITSFTWTVLITVGCLMLCASFSDAQLTPTFYDTSCPTVTNIVRDTIVNELRSDPRIAGSILRLHFHDCFVNGCDASILLDNTTSFRTEKDALGNANSARGFPVIDRMKAAVERACPRTVSCADMLTIAAQQSVTLAGGPSWKVPLGRRDSLQAFLDLANANLPAPFFTLPQLKANFKNVGLDRPSDLVALSGAHTFGKNQCRFIMDRLYNFSNTGLPDPTLNTTYLQTLRGQCPRNGNQSVLVDFDLRTPLVFDNKYYVNLKEQKGLIQSDQELFSSPNATDTIPLVRAYADGTQTFFNAFVEAMNRMGNITPTTGTQGQIRLNCRVVNSNSLLHDVVDIVDFVSSM |
| Enzyme Length | 354 |
| Uniprot Accession Number | P24101 |
| Absorption | |
| Active Site | ACT_SITE 73; /note=Proton acceptor |
| Activity Regulation | |
| Binding Site | BINDING 170; /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.; FUNCTION: May be implicated in the systemic acquired resistance response via the salicylic acid signal transduction pathway. |
| 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); 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: Transiently induced by ozone treatment. Up-regulated during a continuous drought stress. Early induced by benzothiadiazol, a chemical analog of salicylic acid. Enhanced expression following both compatible or incompatible pathogen attacks. {ECO:0000269|PubMed:11101835, ECO:0000269|PubMed:12164808, ECO:0000269|PubMed:12232267}. |
| 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 32; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297" |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12473102; 12535340; 15010611; 15231406; 15247402; 15539469; 16284776; 16889645; 17526915; 18192438; 18650403; 18796151; 18805951; 20736450; 22247251; 22319074; 24393051; 24482432; 25096754; 25849296; 27016889; 27247031; 28254779; 28627464; 30426643; 32005378; 32949889; |
| Motif | |
| Gene Encoded By | |
| Mass | 38,941 |
| Kinetics | |
| Metal Binding | METAL 74; /note=Calcium 1; /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; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 81; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 83; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 201; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 202; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 253; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 256; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 261; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
| Rhea ID | RHEA:56136 |
| Cross Reference Brenda |