| IED ID | IndEnz0018000591 |
| Enzyme Type ID | peroxidase000591 |
| Protein Name |
Peroxidase 34 Atperox P34 EC 1.11.1.7 ATPCb |
| Gene Name | PER34 P34 PRXCB At3g49120 F2K15.3 T2J13.40 |
| 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 | MHFSSSSTSSTWTILITLGCLMLHASLSAAQLTPTFYDRSCPNVTNIVRETIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAFGNANSARGFPVIDRMKAAVERACPRTVSCADMLTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLELANANLPAPFFTLPQLKASFRNVGLDRPSDLVALSGGHTFGKNQCQFILDRLYNFSNTGLPDPTLNTTYLQTLRGLCPLNGNRSALVDFDLRTPTVFDNKYYVNLKERKGLIQSDQELFSSPNATDTIPLVRAYADGTQTFFNAFVEAMNRMGNITPTTGTQGQIRLNCRVVNSNSLLHDVVDIVDFVSSM |
| Enzyme Length | 353 |
| Uniprot Accession Number | Q9SMU8 |
| Absorption | |
| Active Site | ACT_SITE 72; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012" |
| Activity Regulation | |
| Binding Site | BINDING 169; /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. Exhibits a Ca(2+)-pectate binding affinity which could be interpreted in vivo as a specificity to interact with the pectic structure of the cell wall. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Disulfide bond (4); Frameshift (1); Glycosylation (6); Metal binding (10); Modified residue (1); Sequence conflict (3); 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: Late-induced by Al treatment. Expression increased over 48 hours of Al treatment. Induced by oxidative stress. 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:10712528, ECO:0000269|PubMed:11101835, ECO:0000269|PubMed:11748215, ECO:0000269|PubMed:12164808, ECO:0000269|PubMed:9449849}. |
| 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 31; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297" |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12169696; 12473102; 12805589; 14558660; 14595688; 14730673; 14742872; 15144382; 15181204; 15231406; 15489280; 15539469; 15694452; 15708347; 15728341; 15824099; 16284776; 16889645; 16900325; 17149585; 17151019; 17189325; 17194768; 17526915; 17704230; 18192438; 18538804; 18612100; 18650403; 18684332; 18796151; 18805951; 20615517; 21166475; 22112216; 22247251; 22319074; 22363647; 24064926; 24482432; 25096754; 25145265; 26029221; 27247031; 28254779; 28627464; 29106622; 30426643; 32005378; 32949889; |
| Motif | |
| Gene Encoded By | |
| Mass | 38,832 |
| Kinetics | |
| Metal Binding | METAL 73; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 76; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 78; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 80; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 82; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 200; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 201; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 252; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 255; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 260; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
| Rhea ID | RHEA:56136 |
| Cross Reference Brenda |