| IED ID | IndEnz0017000002 |
| Enzyme Type ID | manganese peroxidase000002 |
| Protein Name |
Dye-decolorizing peroxidase AauDyP1 EC 1.11.1.19 EC 1.11.1.7 AjP I Manganese-independent peroxidase I Cleaved into: Dye-decolorizing peroxidase AauDyP2 EC 1.11.1.19 EC 1.11.1.7 AjP II Manganese-independent peroxidase II |
| Gene Name | dyp1 |
| Organism | Auricularia auricula-judae (Judas ear fungus) (Tremella auricula-judae) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Auriculariales Auriculariaceae Auricularia Auricularia auricula-judae (Judas ear fungus) (Tremella auricula-judae) |
| Enzyme Sequence | MRLSPVFVALLSGLLAADLGLARSVAPRVADSPAAVTGTRKTSLLKNVAGLPPVPSAAQVAATSLNTDDIQGDILVGMHKQKQLFYFFAINDPATFKTHLASDIAPVVASVTQLSNVATQPLVALNIAFSNTGLLALGVTDNLGDSLFANGQAKDATSFKESTSSWVPQFAGTGIHGVIILASDTTDLIDQQVASIESTFGSSISKLYSLSASIRPGNEAGHEMFGFLDGIAQPAINGFNTPLPGQNIVDAGVIITGATNDPITRPSWAVGGSFLAFRQLEQLVPEFNKYLLDNAPAGSGSLQARADLLGARMVGRWKSGAPIDLTPTADDPALGADAQRNNNFTYSHAGFDLGSDQSHCPFSAHIRKTRPRADLGGSLTPPNLSAGANSIMRSGIPYGPEVTSAESASNTTTQERGLAFVAYQAQLSQGFHFLQQTWADNANFPPGKTPATVGLDPIIGQNNGQPRVVNGLLPSNSSASLSIPQFVVSHGGEYFFSPPISAIGGRLSA |
| Enzyme Length | 509 |
| Uniprot Accession Number | I2DBY1 |
| Absorption | BIOPHYSICOCHEMICAL PROPERTIES: Absorption: Abs(max)=405 nm; Note=Dye-decolorizing peroxidase AauDyP1. The value for Dye-decolorizing peroxidase AauDyP2 is 406 nm.; |
| Active Site | ACT_SITE 229; /note=Proton acceptor; /evidence=ECO:0000269|PubMed:23235158 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by imidazole. {ECO:0000269|PubMed:25542606}. |
| 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:19756587, ECO:0000269|PubMed:23111597, ECO:0000269|PubMed:25153532, ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606}; 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:19756587, ECO:0000269|PubMed:23111597, ECO:0000269|PubMed:25153532, ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606}; |
| DNA Binding | |
| EC Number | 1.11.1.19; 1.11.1.7; 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:19756587, ECO:0000269|PubMed:23111597, ECO:0000269|PubMed:25153532, ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Retains >80% activity after incubation at temperatures up to 60 degrees Celsius for 10 minutes. Retains 50% activity after incubation at 65.5 degrees Celsius for 10 minutes. Activity is lost after incubation at 70 degrees Celsius for 10 minutes. {ECO:0000269|PubMed:25153532}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5 for oxidation of 2,6-dimethoxyphenol (PubMed:23111597). Retains 100% activity after incubation at pH 2.5 for 4 hours (PubMed:23111597, PubMed:19756587, PubMed:25153532). Retains >60% activity after incubation at pH 2-11 at 4 degrees Celsius (PubMed:25153532). Retains >60% activity after incubation at pH 3-9 at room temperature (PubMed:25153532). {ECO:0000269|PubMed:19756587, ECO:0000269|PubMed:23111597, ECO:0000269|PubMed:25153532}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (18); Chain (2); Glycosylation (4); Helix (27); Metal binding (1); Mutagenesis (12); Propeptide (1); Signal peptide (1); Turn (7) |
| Keywords | 3D-structure;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..22; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (12) |
| Cross Reference PDB | 4AU9; 4UZI; 4W7J; 4W7K; 4W7L; 4W7M; 4W7N; 4W7O; 5AG0; 5AG1; 5IKD; 5IKG; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,992 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS) (Dye-decolorizing peroxidase AauDyP1, at pH 4.5) {ECO:0000269|PubMed:19756587}; KM=283 uM for ABTS (Dye-decolorizing peroxidase AauDyP1, at pH 3) {ECO:0000269|PubMed:25153532}; KM=20 uM for ABTS (Dye-decolorizing peroxidase AauDyP2, at pH 4.5) {ECO:0000269|PubMed:19756587}; KM=10 uM for H(2)O(2) (Dye-decolorizing peroxidase AauDyP1) {ECO:0000269|PubMed:19756587}; KM=5 uM for H(2)O(2) (Dye-decolorizing peroxidase AauDyP2) {ECO:0000269|PubMed:19756587}; KM=23 uM for Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP1, at pH 3) {ECO:0000269|PubMed:19756587}; KM=3.1 uM for Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP1, at pH 3) {ECO:0000269|PubMed:25495127}; KM=15 uM for Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP2, at pH 3) {ECO:0000269|PubMed:19756587}; KM=27 uM for 2,6-Dimethoxyphenol (DMP)(Dye-decolorizing peroxidase AauDyP1, at pH 4.5) {ECO:0000269|PubMed:19756587}; KM=27 uM for DMP (Dye-decolorizing peroxidase AauDyP1, at pH 5) {ECO:0000269|PubMed:25542606}; KM=23 uM for DMP (Dye-decolorizing peroxidase AauDyP2, at pH 4.5) {ECO:0000269|PubMed:19756587}; Vmax=134 umol/min/mg enzyme toward Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP1, at pH 3) {ECO:0000269|PubMed:19756587}; Vmax=375 umol/min/mg enzyme toward Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP2, at pH 3) {ECO:0000269|PubMed:19756587}; Vmax=331 umol/min/mg enzyme toward ABTS (Dye-decolorizing peroxidase AauDyP1, at pH 4.5) {ECO:0000269|PubMed:19756587}; Vmax=471 umol/min/mg enzyme toward ABTS (Dye-decolorizing peroxidase AauDyP2, at pH 4.5) {ECO:0000269|PubMed:19756587}; Vmax=105 umol/min/mg enzyme toward DMP (Dye-decolorizing peroxidase AauDyP1, at pH 4.5) {ECO:0000269|PubMed:19756587}; Vmax=130 umol/min/mg enzyme toward DMP (Dye-decolorizing peroxidase AauDyP2, at pH 4.5) {ECO:0000269|PubMed:19756587}; Vmax=315 umol/min/mg enzyme toward H(2)O(2) (Dye-decolorizing peroxidase AauDyP1, at pH 4.5) {ECO:0000269|PubMed:19756587}; Vmax=348 umol/min/mg enzyme toward H(2)O(2) (Dye-decolorizing peroxidase AauDyP2, at pH 4.5) {ECO:0000269|PubMed:19756587}; |
| Metal Binding | METAL 365; /note="Iron (heme axial ligand); via tele nitrogen"; /evidence="ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606, ECO:0000269|Ref.7, ECO:0000269|Ref.8, ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI, ECO:0007744|PDB:4W7J, ECO:0007744|PDB:4W7K, ECO:0007744|PDB:4W7L, ECO:0007744|PDB:4W7M, ECO:0007744|PDB:4W7N, ECO:0007744|PDB:4W7O, ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5IKD, ECO:0007744|PDB:5IKG" |
| Rhea ID | RHEA:28086; RHEA:56136 |
| Cross Reference Brenda | 1.11.1.19; |