| IED ID | IndEnz0018000587 |
| Enzyme Type ID | peroxidase000587 |
| Protein Name |
Basic peroxidase EC 1.11.1.7 ZePrx33.44 ZePrx34.70 |
| Gene Name | POD3; POD4 |
| Organism | Zinnia violacea (Garden zinnia) (Zinnia elegans) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids campanulids Asterales Asteraceae Asteroideae Heliantheae alliance Heliantheae Zinnia Zinnia violacea (Garden zinnia) (Zinnia elegans) |
| Enzyme Sequence | MSYHKSSGTTLMVPLFMLLISVNYFMSCNAQLSTTFYDTTCPTALSTIRTSIRSSVSSNRRNAALVIRLLFHDCFVQGCDASLLLSGAGSERASPANDGVLGYEVIDAAKAAVERVCPGVVSCADILAVAARDASVAVGGPSWTVRLGRRDSTTSNAAQAATDLPRGNMVLSQLISNFANKGLNTREMVALSGSHTLGQARCIRFRGRIYNSTLRIEPNFNRSLSQACPPTGNDATLRPLDLVTPNSFDNNYYRNLVTSRGLLISDQVLFNADSTDSIVTEYVNNPATFAADFAAAMVKMSEIGVVTGTSGIVRTLCGNPS |
| Enzyme Length | 321 |
| Uniprot Accession Number | Q4W1I9 |
| Absorption | |
| Active Site | ACT_SITE 72; /note=Proton acceptor |
| Activity Regulation | |
| Binding Site | BINDING 165; /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; Evidence={ECO:0000269|PubMed:16258008}; |
| 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. Involved in the synthesis of highly polymerized lignins. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Disulfide bond (4); Glycosylation (2); 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:0000255|PROSITE-ProRule:PRU00297}. |
| Modified Residue | MOD_RES 31; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:16258008" |
| Post Translational Modification | PTM: N-glycosylated. |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000269|PubMed:16258008 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 34,233 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=241 uM for p-coumaryl alcohol (in the presence of 10.2 uM H2O2, for a partially glycosylated enzyme) {ECO:0000269|PubMed:16258008}; KM=432 uM for p-coumaryl alcohol (in the presence of 10.2 uM H2O2, for a fully glycosylated enzyme) {ECO:0000269|PubMed:16258008}; KM=83 uM for coniferyl alcohol (in the presence of 10.2 uM H2O2, for a partially glycosylated enzyme) {ECO:0000269|PubMed:16258008}; KM=124 uM for coniferyl alcohol (in the presence of 10.2 uM H2O2, for a fully glycosylated enzyme) {ECO:0000269|PubMed:16258008}; KM=15 uM for sinapyl alcohol (in the presence of 10.2 uM H2O2, for a partially glycosylated enzyme) {ECO:0000269|PubMed:16258008}; KM=13 uM for sinapyl alcohol (in the presence of 10.2 uM H2O2, for a fully glycosylated enzyme) {ECO:0000269|PubMed:16258008}; Note=The full glycosylation reduces the affinity of the enzyme for both p-coumaryl and coniferyl, but not sinapyl, alcohol.; |
| Metal Binding | METAL 73; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 76; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 78; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 80; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 82; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 195; /note=Iron (heme b axial ligand); METAL 196; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 241; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 244; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 249; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
| Rhea ID | RHEA:56136 |
| Cross Reference Brenda |