IED ID | IndEnz0018000015 |
Enzyme Type ID | peroxidase000015 |
Protein Name |
Peroxidase 59 Atperox P59 EC 1.11.1.7 ATPN Peroxidase N |
Gene Name | PER59 P59 At5g19890 F28I16.40 |
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 | MKTQTKVMGGHVLLTVFTLCMLCSGVRAQLSPDIYAKSCPNLVQIVRKQVAIALKAEIRMAASLIRLHFHDCFVNGCDASLLLDGADSEKLAIPNINSARGFEVIDTIKAAVENACPGVVSCADILTLAARDSVVLSGGPGWRVALGRKDGLVANQNSANNLPSPFEPLDAIIAKFVAVNLNITDVVALSGAHTFGQAKCAVFSNRLFNFTGLGNPDATLETSLLSNLQTVCPLGGNSNITAPLDRSTTDTFDNNYFKNLLEGKGLLSSDQILFSSDLAVNTTKKLVEAYSRSQSLFFRDFTCAMIRMGNISNGASGEVRTNCRVINN |
Enzyme Length | 328 |
Uniprot Accession Number | Q39034 |
Absorption | |
Active Site | ACT_SITE 70; /note=Proton acceptor |
Activity Regulation | |
Binding Site | BINDING 163; /note=Substrate; via carbonyl oxygen |
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); Beta strand (5); Binding site (1); Chain (1); Disulfide bond (4); Glycosylation (5); Helix (17); Metal binding (11); Modified residue (1); Sequence conflict (3); Signal peptide (1); Site (1); Turn (7) |
Keywords | 3D-structure;Calcium;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}. |
Modified Residue | MOD_RES 29; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297" |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1QGJ; |
Mapped Pubmed ID | 12473102; 12481097; 12913156; 14730065; 15047898; 15231406; 15347784; 15546358; 15610358; 16021335; 16258012; 16798948; 17061125; 17149585; 17411438; 18070919; 21333657; 23134674; |
Motif | |
Gene Encoded By | |
Mass | 35,023 |
Kinetics | |
Metal Binding | METAL 71; /note="Calcium 1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:10713531"; METAL 74; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:10713531"; METAL 76; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:10713531"; METAL 78; /note="Calcium 1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:10713531"; METAL 80; /note="Calcium 1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:10713531"; METAL 193; /note="Iron (heme b axial ligand)"; METAL 194; /note="Calcium 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:10713531"; METAL 245; /note="Calcium 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:10713531"; METAL 248; /note="Calcium 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:10713531"; METAL 251; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:10713531"; METAL 253; /note="Calcium 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:10713531" |
Rhea ID | RHEA:56136 |
Cross Reference Brenda |