IED ID | IndEnz0018000659 |
Enzyme Type ID | peroxidase000659 |
Protein Name |
Peroxidase 64 Atperox P64 EC 1.11.1.7 ATP17a PRXR4 |
Gene Name | PER64 P64 At5g42180 MJC20.29 |
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 | MNAHMLNLLVIVIFVVSFDVQALSPHYYDHTCPQADHIVTNAVKKAMSNDQTVPAALLRMHFHDCFVRGCDGSVLLDSKGKNKAEKDGPPNISLHAFYVIDNAKKALEEQCPGIVSCADILSLAARDAVALSGGPTWAVPKGRKDGRISKAIETRQLPAPTFNISQLRQNFGQRGLSMHDLVALSGGHTLGFAHCSSFQNRLHKFNTQKEVDPTLNPSFAARLEGVCPAHNTVKNAGSNMDGTVTSFDNIYYKMLIQGKSLFSSDESLLAVPSTKKLVAKYANSNEEFERAFVKSMIKMSSISGNGNEVRLNCRRVR |
Enzyme Length | 317 |
Uniprot Accession Number | Q43872 |
Absorption | |
Active Site | ACT_SITE 63; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
Activity Regulation | |
Binding Site | BINDING 158; /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 (1); Metal binding (10); Signal peptide (1); Site (1) |
Keywords | Calcium;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Secreted;Signal |
Interact With | |
Induction | INDUCTION: Pathogen and elicitor-induced. Up-regulated transiently by a cold treatment. {ECO:0000269|PubMed:12172015, ECO:0000269|PubMed:8425063}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 12473102; 15047898; 15231406; 15272873; 15937231; 16287169; 18296723; 18783601; 19453502; 19582540; 26124109; 27247031; 28815457; 29481639; 32699027; 33139576; |
Motif | |
Gene Encoded By | |
Mass | 34,706 |
Kinetics | |
Metal Binding | METAL 64; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 67; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 69; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 71; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 73; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 188; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 189; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 241; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 243; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 248; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
Rhea ID | RHEA:56136 |
Cross Reference Brenda |