| IED ID | IndEnz0018000558 |
| Enzyme Type ID | peroxidase000558 |
| Protein Name |
Peroxidase 1 EC 1.11.1.7 Plasma membrane-bound peroxidase 1 pmPOX1 |
| Gene Name | PER1 POX1 PRX1 |
| Organism | Zea mays (Maize) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae PACMAD clade Panicoideae Andropogonodae Andropogoneae Tripsacinae Zea Zea mays (Maize) |
| Enzyme Sequence | MAKESKLTAGVAAALTVVAACALCLLLPATARAQLRVGFYDTSCPNAEALVRQAVAAAFAKDAGIAAGLIRLHFHDCFVRGCDGSVLLTVNPGGGQTERDALPNNPSLRGFDVIDAAKTAVEQSCPRTVSCADIVAFAARDSISLTGSVSYQVPAGRRDGRVSNATETVDLPPPTSTAQSLTDLFKAKELSVEDMVVLSGAHTVGRSFCASFFKRVWNTSTNPATAIVDAGLSPSYAQLLRALCPSNTTQTTPITTAMDPGTPNVLDNNYYKLLPRGMGLFFSDNQLRVNPQMAALVSSFASNETLWKEKFAAAMVKMGRIQVQTGTCGEVRLNCGVVNPSLYSSSSAVELGSSAPAAVGEEGYAAS |
| Enzyme Length | 367 |
| Uniprot Accession Number | A5H8G4 |
| Absorption | |
| Active Site | ACT_SITE 75; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012" |
| Activity Regulation | |
| Binding Site | BINDING 172; /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. {ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:12857829}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Disulfide bond (4); Frameshift (1); Glycosylation (4); 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 34; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..33; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 20032108; 33238617; |
| Motif | |
| Gene Encoded By | |
| Mass | 38,355 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=61.9 umol/min/mg enzyme with guaiacol as substrate {ECO:0000269|PubMed:18603027}; Note=In the presence of H(2)O(2).; |
| Metal Binding | METAL 76; /note=Calcium 1; /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; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 83; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 85; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 202; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 203; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 259; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 262; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 267; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
| Rhea ID | RHEA:56136 |
| Cross Reference Brenda |