| IED ID | IndEnz0015000005 |
| Enzyme Type ID | laccase000005 |
| Protein Name |
Laccase EC 1.10.3.2 Benzenediol:oxygen oxidoreductase Diphenol oxidase Urishiol oxidase |
| Gene Name | |
| Organism | Trametes maxima (White-rot fungus) (Cerrena maxima) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Polyporales Polyporaceae (bracket fungi) Trametes Trametes maxima (White-rot fungus) (Cerrena maxima) |
| Enzyme Sequence | AVGPVADNTITDAATSPDGFSRQAVVVNGVTPGPLVAGNIGDRFQLNVIDNLTNHTMLKTTSVHWHGFFQQGTNWADGPAFINQCPISPGHSFLYDFQVPNQAGTFWYHSHLSTQYCDGLRGPFVVYDPNDPHASRYDVDNDDTVITLADWYHTAAKLGPRFPAGADATLINGKGRAPSDTSAELSVIKVTKGKRYRFRLVSLSCDPNFTFSIDGHNLTIIEVDSSNSQPLSVDSIQIFAAQRYSFVLNANQAVDNYWIRANPNFGNVGFNGGINSAILRYDGAPAVEPTTNQTTSVKPLNEVNLHPLVSTPVPGSPSSGGVDKAINMAFNFNGSNFFINGASFVPPSVPVLLQILSGAQTAQDLLPSGSVYVLPSNASIEISFPATAAAPGAPHPFHLHGHTFAVVRSAGSTVYNYSNPIFRDVVSTGTPAAGDNVTIRFLTNNPGPWFLHCHIDFHLEGGFAVVQAEDVPDVKATNPVPQAWSDLCPTYDANAPSDQ |
| Enzyme Length | 499 |
| Uniprot Accession Number | D0VWU3 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O; Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2; Evidence={ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782}; |
| DNA Binding | |
| EC Number | 1.10.3.2 |
| Enzyme Function | FUNCTION: Lignin degradation and detoxification of lignin-derived products. {ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (34); Chain (1); Disulfide bond (2); Domain (3); Glycosylation (9); Helix (14); Metal binding (11); Modified residue (2); Turn (4) |
| Keywords | 3D-structure;Copper;Disulfide bond;Glycoprotein;Lignin degradation;Metal-binding;Nitration;Oxidoreductase;Repeat;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782}. |
| Modified Residue | MOD_RES 196; /note="3'-nitrotyrosine"; /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782, ECO:0000269|Ref.3"; MOD_RES 372; /note="3'-nitrotyrosine"; /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782, ECO:0000269|Ref.3" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 2H5U; 3DIV; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,451 |
| Kinetics | |
| Metal Binding | METAL 64; /note="Copper 1; type 2"; /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3, ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"; METAL 66; /note="Copper 2; type 3"; /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3, ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"; METAL 109; /note="Copper 2; type 3"; /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3, ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"; METAL 111; /note="Copper 3; type 3"; /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3, ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"; METAL 395; /note="Copper 4; type 1"; /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3, ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"; METAL 398; /note="Copper 1; type 2"; /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3, ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"; METAL 400; /note="Copper 3; type 3"; /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3, ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"; METAL 452; /note="Copper 3; type 3"; /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3, ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"; METAL 453; /note="Copper 4; type 1"; /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3, ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"; METAL 454; /note="Copper 2; type 3"; /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3, ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"; METAL 458; /note="Copper 4; type 1"; /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3, ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV" |
| Rhea ID | RHEA:11276 |
| Cross Reference Brenda |