| IED ID | IndEnz0018000553 |
| Enzyme Type ID | peroxidase000553 |
| Protein Name |
Peroxidase 15 Prx15 EC 1.11.1.7 Anionic peroxidase |
| Gene Name | pod |
| Organism | Ipomoea batatas (Sweet potato) (Convolvulus batatas) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids lamiids Solanales Convolvulaceae Ipomoeeae Ipomoea Ipomoea batatas (Sweet potato) (Convolvulus batatas) |
| Enzyme Sequence | MASFSPLLAMALAIFIFSSHSNAQLSSTFYSTTCPNVSAIVRTVVQQALQNDARIGGSLIRLHFHDCFVDGCDGSLLLDNNGTTIVSEKDALPNTNSTRGFDVVDNIKTAVENACPGVVSCVDILALASESSVSLAGGPSWNVLLGRRDRRTANQGGANTSLPSPFENLTNLTQKFTNVGLNVNDLVALSGAHTFGRAQCRTFSPRLFNFSNTGNPDPTLNTTYLATLQQICPQGGSGFTVTNLDPTTPDTFDNNYFSNLQTNRGLLQSDQELFSTSGAPTIAIVNNFSANQTAFFESFVQSMINMGNISPLTGSNGEIRSNCRRPN |
| Enzyme Length | 327 |
| Uniprot Accession Number | Q9LEH3 |
| Absorption | BIOPHYSICOCHEMICAL PROPERTIES: Absorption: Abs(max)=408 nm {ECO:0000269|PubMed:17936696}; Note=Exhibits smaller absorbance peaks at 497 and 635 nm. After treatment with stoichiometric amounts of hydrogen peroxide the absorption maximum is shifed to 400 nm. {ECO:0000269|PubMed:17936696}; |
| Active Site | ACT_SITE 65; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012" |
| Activity Regulation | |
| Binding Site | BINDING 163; /note="Substrate; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:Q42578, 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; Evidence={ECO:0000269|PubMed:17936696}; |
| 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. {ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. Retains more than 50% of activity between pH 4 and 7. {ECO:0000269|PubMed:17936696}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Disulfide bond (4); Glycosylation (10); Metal binding (10); Modified residue (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Pyrrolidone carboxylic acid;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297}. |
| Modified Residue | MOD_RES 24; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297" |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 34,956 |
| Kinetics | |
| Metal Binding | METAL 66; /note="Calcium 1"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 69; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 71; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 73; /note="Calcium 1"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 75; /note="Calcium 1"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 193; /note="Iron (heme b axial ligand)"; /evidence="ECO:0000250|UniProtKB:P00433, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 194; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 245; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 248; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 253; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297" |
| Rhea ID | RHEA:56136 |
| Cross Reference Brenda | 1.11.1.7; |