IED ID | IndEnz0018000644 |
Enzyme Type ID | peroxidase000644 |
Protein Name |
Peroxidase 54 Atperox P54 EC 1.11.1.7 ATP29a |
Gene Name | PER54 P54 At5g06730 MPH15.9 |
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 | MAVTSSSSTCDGFFIISLIVIVSSLFGTSSAQLNATFYSGTCPNASAIVRSTIQQALQSDARIGGSLIRLHFHDCFVNGCDGSLLLDDTSSIQSEKNAPANANSTRGFNVVDSIKTALENACPGIVSCSDILALASEASVSLAGGPSWTVLLGRRDGLTANLSGANSSLPSPFEGLNNITSKFVAVGLKTTDVVSLSGAHTFGRGQCVTFNNRLFNFNGTGNPDPTLNSTLLSSLQQLCPQNGSNTGITNLDLSTPDAFDNNYFTNLQSNNGLLQSDQELFSNTGSATVPIVNSFASNQTLFFEAFVQSMIKMGNISPLTGSSGEIRQDCKVVNGQSSATEAGDIQLQSDGPVSVADM |
Enzyme Length | 358 |
Uniprot Accession Number | Q9FG34 |
Absorption | |
Active Site | ACT_SITE 73; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012" |
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. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Binding site (1); Chain (1); Disulfide bond (4); Glycosylation (10); 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 | |
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 | 12169696; 12473102; 15231406; 15235117; 15539469; 16998091; 17151019; 17665211; 17786563; |
Motif | |
Gene Encoded By | |
Mass | 37,290 |
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 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 |