| IED ID | IndEnz0015000124 |
| Enzyme Type ID | laccase000124 |
| Protein Name |
Laccase EC 1.10.3.2 Benzenediol:oxygen oxidoreductase Diphenol oxidase Urishiol oxidase |
| Gene Name | LAC-1 |
| Organism | Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Diaporthales Cryphonectriaceae Cryphonectria-Endothia species complex Cryphonectria Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica) |
| Enzyme Sequence | MPSFFRALFSGLIASQLSWAAPSLLHPLEPRQQPNCNTASNRACWISGSYDITTDYEVKTPLTGVVRQYDLTLTQAENWLGPDGVVKEDVMLVNGNILGPVIHAQWGDTISVTVTNNLKYNGTTIHWHGIRQLNTNLQDGVNGITECPIPPNGGSKTYTFIAHQYGTSWYHSHFSAQYGNGIVGAIQIDGPASLPYDIDLGPLVLSDYYYKTADELVVYTQSNAPPASDNVLFNGTNINPANTTQGQYKTITLTPGKRHRLRIINTSVENNFQVSIVGHSMTVIESDFVPVDSFTTDSLFVGIGQRYDVTIDASQATDNYWMNVTFGGGGFCGKSNNPYPAAIIHYNGASNSHPTNKGVAPADHECLDLLNLVPVVPRSIPTSGFVAASDNTLDVQLSTTTRKWTINGSTLDVDWGHPITQYVINKSTAWPSTDNVWLVEEANQWAYWLIENDPTATGNALPHPIHLHGHDFVVLGRSPNVSPTAQTPYTFTSSDVSSLNGNNPIRRDVVMLPPKGWLLIAFQTTNPGAWLMHCHIAWHVSAGLGNTFLEQPSAFVAGLNTNDVNQLNSQCKSWNAYYPSKDIFKQDDSGV |
| Enzyme Length | 591 |
| Uniprot Accession Number | Q03966 |
| 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:0000250|UniProtKB:Q70KY3}; |
| DNA Binding | |
| EC Number | 1.10.3.2 |
| Enzyme Function | FUNCTION: Lignin degradation and detoxification of lignin-derived products. {ECO:0000250|UniProtKB:Q70KY3}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (2); Domain (3); Glycosylation (7); Metal binding (11); Signal peptide (1) |
| Keywords | Copper;Disulfide bond;Glycoprotein;Lignin degradation;Metal-binding;Oxidoreductase;Repeat;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q70KY3}. |
| 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 | 64,696 |
| Kinetics | |
| Metal Binding | METAL 126; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 128; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 171; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 173; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 463; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 466; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 468; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 533; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 534; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 535; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 539; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3 |
| Rhea ID | RHEA:11276 |
| Cross Reference Brenda |