IED ID | IndEnz0018000550 |
Enzyme Type ID | peroxidase000550 |
Protein Name |
Peroxidase 12 Atperox P12 EC 1.11.1.7 ATP4a PRXR6 |
Gene Name | PER12 P12 At1g71695 F14O23.6 F26A9.5 |
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 | MTKAYSTRVLTFLILISLMAVTLNLFPTVEAKKRSRDAPIVKGLSWNFYQKACPKVENIIRKELKKVFKRDIGLAAAILRIHFHDCFVQGCEASVLLAGSASGPGEQSSIPNLTLRQQAFVVINNLRALVQKKCGQVVSCSDILALAARDSVVLSGGPDYAVPLGRRDSLAFASQETTLNNLPPPFFNASQLIADFANRNLNITDLVALSGGHTIGIAHCPSFTDRLYPNQDPTMNQFFANSLKRTCPTANSSNTQVNDIRSPDVFDNKYYVDLMNRQGLFTSDQDLFVDKRTRGIVESFAIDQQLFFDYFTVAMIKMGQMSVLTGTQGEIRSNCSARNTQSFMSVLEEGIEEAISMI |
Enzyme Length | 358 |
Uniprot Accession Number | Q96520 |
Absorption | |
Active Site | ACT_SITE 84; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012" |
Activity Regulation | |
Binding Site | BINDING 183; /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: 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); Glycosylation (4); Metal binding (10); Sequence conflict (1); Signal peptide (1); Site (1) |
Keywords | Calcium;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Secreted;Signal;Vacuole |
Interact With | |
Induction | INDUCTION: Induced either by incompatible fungal pathogen attack, or by methyl jasmonate, a plant defense-related signaling molecule. {ECO:0000269|PubMed:11027363}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Vacuole {ECO:0000305}. Note=Carboxy-terminal extension appears to target the protein to vacuoles. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 12169696; 12473102; 12805628; 15231406; 15539469; 16287169; 16367961; 17432890; 18650403; 18796151; |
Motif | |
Gene Encoded By | |
Mass | 39,559 |
Kinetics | |
Metal Binding | METAL 85; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 88; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 90; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 92; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 94; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 213; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 214; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 259; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 262; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 267; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
Rhea ID | RHEA:56136 |
Cross Reference Brenda |