IED ID | IndEnz0018001353 |
Enzyme Type ID | peroxidase001353 |
Protein Name |
Ligninase-3 EC 1.11.1.14 Diarylpropane peroxidase Lignin peroxidase Ligninase III |
Gene Name | |
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 | MAFKQLLSAVTLALAASAASVTRRATCPDGTQLMNAECCALLAVRDDLQNNMFNNECGDEAHEALRLTFHDAIAISPAMEATGQFGGGGADGSIMIFSDIETKFHPNIGLDEVVESFRPFQQRSGMGVADFIQFSGAVGTSNCPGAPTLNAFIGRKDATQAAPDGLVPEPFHDVNTILARFNDAGDFDELETVWFLIAHSVAAQNDIDPAVSHAPFDSTPSVMDGQFFIETQLRGVEFIGSGGIEGVAESPVKGEFRLMSDQQIARDNRTACEWQSFGTDQAKLQNRFQFIFEAMGQLGTDPTTLIDCSDVLPVPPPLSTVPHFPAGITINDVEPACAETPFPTLPTDPGPATAVAAVPRD |
Enzyme Length | 361 |
Uniprot Accession Number | P20010 |
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=1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + glycolaldehyde + guaiacol + H2O; Xref=Rhea:RHEA:48004, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17071, ChEBI:CHEBI:17098, ChEBI:CHEBI:28591, ChEBI:CHEBI:86963; EC=1.11.1.14; Evidence={ECO:0000250|UniProtKB:P06181}; CATALYTIC ACTIVITY: Reaction=2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O; Xref=Rhea:RHEA:30271, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:62150, ChEBI:CHEBI:88143; EC=1.11.1.14; Evidence={ECO:0000250|UniProtKB:P06181}; |
DNA Binding | |
EC Number | 1.11.1.14 |
Enzyme Function | FUNCTION: Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin. {ECO:0000250|UniProtKB:P06181}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Secondary metabolite metabolism; lignin degradation. |
nucleotide Binding | |
Features | Active site (1); Chain (1); Glycosylation (1); Metal binding (10); Region (1); Signal peptide (1); Site (1) |
Keywords | Calcium;Glycoprotein;Heme;Hydrogen peroxide;Iron;Lignin degradation;Metal-binding;Oxidoreductase;Peroxidase;Signal |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 38,439 |
Kinetics | |
Metal Binding | METAL 71; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 89; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 91; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 93; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 199; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 200; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 217; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 219; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 222; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 224; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
Rhea ID | RHEA:48004; RHEA:30271 |
Cross Reference Brenda |