| IED ID | IndEnz0018000449 | 
| Enzyme Type ID | peroxidase000449 | 
| Protein Name | 
                        
                            
                                Ligninase C  EC 1.11.1.14 Diarylpropane peroxidase Lignin peroxidase  | 
                    
| Gene Name | |
| Organism | Trametes versicolor (White-rot fungus) (Coriolus versicolor) | 
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Polyporales Polyporaceae (bracket fungi) Trametes Trametes versicolor (White-rot fungus) (Coriolus versicolor) | 
| Enzyme Sequence | MAFKSLLSFVSVIGALQGANAALTRRVACPDGVNTATNAACCQLFAVREDLQQNLFHGGLCTAEAHESLRLTFHDAIAISPALEAQGIFGGGGADGSIAIFPEIETNFHPNIGLDEIIELQKPFIARHNISVADFIQFAGAIGASNCAGAPQLAAFVGRKDATQPAPDGLVPEPFHTPDQIFDRLADASQGEFDPILTVWLLTAHTVAAANDVDPTKSGLPFDSTPELWDTQFFLETQLRGTSFPGSGGNQGEVESPLAGEMRLQSDHTIARDSRTACEWQSFVDNQPKAQQMFQFVFHDLSIFGQDINTLVDCTEVVPIPADPQGHTHFPAGLSNADIEQACAETPFPTFPTDPGPKTAVAPVPKPPAARK | 
| Enzyme Length | 372 | 
| Uniprot Accession Number | P20013 | 
| Absorption | |
| Active Site | ACT_SITE 74; /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:0000269|PubMed:2707445}; 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:0000269|PubMed:2707445}; | 
| 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); Compositional bias (1); Glycosylation (1); Metal binding (10); Region (1); Signal peptide (1); Site (1) | 
| Keywords | Calcium;Direct protein sequencing;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..26; /evidence=ECO:0000269|PubMed:2707445 | 
| Structure 3D | |
| Cross Reference PDB | - | 
| Mapped Pubmed ID | - | 
| Motif | |
| Gene Encoded By | |
| Mass | 39,625 | 
| Kinetics | |
| Metal Binding | METAL 75; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 93; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 95; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 97; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 205; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 206; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 223; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 225; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 228; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 230; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 | 
| Rhea ID | RHEA:48004; RHEA:30271 | 
| Cross Reference Brenda |