| IED ID | IndEnz0018000939 |
| Enzyme Type ID | peroxidase000939 |
| Protein Name |
Dye-decolorizing peroxidase EglDyP EC 1.11.1.19 EC 1.11.1.7 |
| Gene Name | dyp1 |
| Organism | Exidia glandulosa (Black witch's butter) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Auriculariales Exidiaceae Exidia Exidia glandulosa (Black witch's butter) |
| Enzyme Sequence | MRLSPSFLSLALVIFVGEVVARNVVARASNPASVTGTRKVSLLKNVAGLPAVPTAQQVAVSSLNTDDIQGDILVGMHKQQQRFYFFTINDAATFKTHLAADIAPVVASVTQLSSVSTQPLVALNIAFSQTGLNALGVTDNVGDALFTAGQASNTVGNLKETTDNWVAQFKTPGIHGVILLASDDKSLIDQQEASIQSTFGAAISKVYSLDGAIRPGAEAGHEMFGFLDGIAQPAISGLGTPLPGQLVVDEGVIIVGGTNDPIARPADGWMTGGSFLAFRQLEQLVPEFNKYLLDNAPAVDGKSLQDRADLLGARMVGRWKSGAPIDLTPLADDPALGADPQRNNNFDFTHANFSITTDQTHCPFSAHIRKTRPRADLVAPANSIIRSGIPYGSEVSAAEAAANATTNERGLAFVSYQSQLNKGFQFLQNTWANNPGFIFGKNVQPGQDPIIGQNSGAIRSVVGLDPANPTGALSMGQFVVSRGGEYFFSPPISALTGKLAA |
| Enzyme Length | 501 |
| Uniprot Accession Number | I2DBY2 |
| Absorption | BIOPHYSICOCHEMICAL PROPERTIES: Absorption: Abs(max)=405 nm {ECO:0000269|PubMed:23111597}; |
| Active Site | ACT_SITE 228; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:I2DBY1 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 H2O2 + Reactive Blue 5 = 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H(+) + 2 H2O + phthalate; Xref=Rhea:RHEA:28086, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:17563, ChEBI:CHEBI:63950, ChEBI:CHEBI:63955, ChEBI:CHEBI:64278; EC=1.11.1.19; Evidence={ECO:0000269|PubMed:23111597}; 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:23111597}; |
| DNA Binding | |
| EC Number | 1.11.1.19; 1.11.1.7 |
| Enzyme Function | FUNCTION: Manganese-independent peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known. In addition to classic peroxidase substrates (e.g. 2,6-dimethoxyphenol), oxidizes dyes such as Reactive Blue 5 and Reactive Black 5. {ECO:0000269|PubMed:23111597}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. Retains 50%-90% of its activity after heating for 2 hours at 60 degrees Celsius, while no decrease in activity is observed within the same time at 30 or 40 degrees Celsius. {ECO:0000269|PubMed:23111597}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5 with 2,6-dimethoxyphenol as substrate. Retains more than 50% of its activity after 4 hours at pH 2.5. {ECO:0000269|PubMed:23111597}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Glycosylation (2); Metal binding (1); Propeptide (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;Glycoprotein;Heme;Iron;Metal-binding;Oxidoreductase;Peroxidase;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23111597}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,641 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14 uM for H(2)O(2) {ECO:0000269|PubMed:23111597}; |
| Metal Binding | METAL 367; /note=Iron (heme axial ligand); via tele nitrogen; /evidence=ECO:0000250|UniProtKB:I2DBY1 |
| Rhea ID | RHEA:28086; RHEA:56136 |
| Cross Reference Brenda | 1.11.1.19; |