IED ID | IndEnz0017000005 |
Enzyme Type ID | manganese peroxidase000005 |
Protein Name |
Manganese peroxidase 2 MnP2 EC 1.11.1.13 Manganese peroxidase isozyme 2 |
Gene Name | mnp2 |
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 | MAFNFAAILAFVSLAAVTSAAPSKTTCSNGVVVPDAVCCDFVPLASALQSEVLMGDCGEDAHELVRLIFHDAIAISQSMGPSAGGGADGSMLIFPTVEPAFFPNLGIADSVNNLIPFLSQFPTISAGDLVQFAGAVAISNCPGAPQLEFLAGRPNATAPAIDGLIPEPQDDVTKILARFKDAGNFSPAEVVALLASHSIARADHVDPTLDAAPFDSTPFDFDTQIFLEVLLKGVGFPGLANNTGEVSSPLPVTDGTDVGELRLQSDFALARDERTACAWQSFVNEQEAMATAFKNAVKKLAVLGHNRNDLVDCSAVVPVPKPATGTPATFPASTGPQDLELTCTTEPFPTLSTAPGAQQTLIPHCSDGTMTCNSVQFDGPATNFGGADDS |
Enzyme Length | 390 |
Uniprot Accession Number | Q70LM3 |
Absorption | |
Active Site | ACT_SITE 70; /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. {ECO:0000269|Ref.2}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Disulfide bond (5); Glycosylation (2); Metal binding (12); Sequence conflict (2); Signal peptide (1); Site (1) |
Keywords | Calcium;Direct protein sequencing;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..23; /evidence=ECO:0000269|PubMed:15809005 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 40,326 |
Kinetics | |
Metal Binding | METAL 59; /note=Manganese; /evidence=ECO:0000250; METAL 63; /note=Manganese; /evidence=ECO:0000250; METAL 71; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 86; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 88; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 90; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 197; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 198; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 203; /note=Manganese; /evidence=ECO:0000250; METAL 215; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 217; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 222; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
Rhea ID | RHEA:22776 |
Cross Reference Brenda |