Detail Information for IndEnz0018000015
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