| IED ID | IndEnz0017000006 |
| Enzyme Type ID | manganese peroxidase000006 |
| Protein Name |
Manganese peroxidase 3 MnP3 EC 1.11.1.13 Manganese peroxidase isozyme 3 |
| Gene Name | mnp3 |
| Organism | Phlebia radiata (White-rot fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Polyporales Meruliaceae Phlebia Phlebia radiata (White-rot fungus) |
| Enzyme Sequence | MAFKQLLTAISIVSVANAALTRRVACPDGVNTATNAVCCSLFAVRDLIQDQLFDGGECGEEVHESLRLTFHDAIGISPTIASTGVFGGGGADGSIAIFAEIETNFHANNGVDEIIGEQAPFIQMTNMTTADFIQFAGAVGVSNCPGAPALPVFVGRPDATQPAPDKTVPEPFDTVDSILARFADAGGFSSAEVVALLASHTIAAADHVDPSIPGTPFDSTPEIFDTQFFIETQLRGILFPGTGGNQGEVESPLHGEIRLQSDSELARDSRTACEWQSFVNNQAKIQSAFKAAFRKMTILGHSESSLIECSEVIQTPPALEGNAHLPAGQTMNDIEQACATTPFPSLSADPGPATSVAPVPPS |
| Enzyme Length | 362 |
| Uniprot Accession Number | Q96TS6 |
| Absorption | |
| Active Site | ACT_SITE 71; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O2 + 2 Mn(2+) = 2 H2O + 2 Mn(3+); Xref=Rhea:RHEA:22776, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:29035, ChEBI:CHEBI:29041; EC=1.11.1.13; |
| DNA Binding | |
| EC Number | 1.11.1.13 |
| Enzyme Function | FUNCTION: Catalyzes the oxidation of Mn(2+) to Mn(3+). The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin compounds. This isozyme is also able to oxidize phenols and amines in the absence of Mn(2+), similar to versatile peroxidases. {ECO:0000269|Ref.2}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (4); Glycosylation (1); Metal binding (13); Propeptide (1); Region (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Lignin degradation;Manganese;Metal-binding;Oxidoreductase;Peroxidase;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: By a combination of high manganese and malonate levels. {ECO:0000269|Ref.2}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 37,815 |
| Kinetics | |
| Metal Binding | METAL 60; /note=Manganese; /evidence=ECO:0000250; METAL 64; /note=Manganese; /evidence=ECO:0000250; METAL 72; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 90; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 92; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 94; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 200; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 201; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 206; /note=Manganese; /evidence=ECO:0000250; METAL 218; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 220; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 223; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 225; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
| Rhea ID | RHEA:22776 |
| Cross Reference Brenda |