| IED ID | IndEnz0015000096 |
| Enzyme Type ID | laccase000096 |
| Protein Name |
Laccase-2 EC 1.10.3.2 Benzenediol:oxygen oxidoreductase 2 Diphenol oxidase 2 Urishiol oxidase 2 |
| Gene Name | POX2 |
| Organism | Pleurotus ostreatus (Oyster mushroom) (White-rot fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetidae Agaricales Pleurotaceae Pleurotus Pleurotus ostreatus (Oyster mushroom) (White-rot fungus) |
| Enzyme Sequence | MFPGARILATLTLALHLLHGAHAAIGPAGNMYIVNEDVSPDGFARSAVVARSVPATDPTPATASIPGVLVQGNKGDNFQLNVVNQLSDTTMLKTTSIHWHGFFQAGSSWADGPAFVTQCPVASGDSFLYNFNVPDQAGTFWYHSHLSTQYCDGLRGPFVVYDPSDPHLSLYDIDNADTVITLEDWYHIVAPQNAAIPTPDSTLINGKGRYAGGPTSPLAIINVESNKRYRFRLVSMSCDPNFTFSIDGHSLLVIEADAVNIVPITVDSIQIFAGQRYSFVLTANQAVDNYWIRANPNLGSTGFVGGINSAILRYAGATEDDPTTTSSTSTPLLETNLVPLENPGAPGPPVPGGADININLAMAFDFTTFELTINGVPFLPPTAPVLLQILSGASTAASLLPSGSIYELEANKVVEISMPALAVGGPHPFHLHGHTFDVIRSAGSTTYNFDTPARRDVVNTGTGANDNVTIRFVTDNPGPWFLHCHIDWHLEIGLAVVFAEDVTSISAPPAAWDDLCPIYNALSDNDKGGIVPS |
| Enzyme Length | 533 |
| Uniprot Accession Number | Q12739 |
| 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 (1); 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 | PTM: N-glycosylated at Asn-467; contains a high-mannose glycan with a varying number of mannose residues. {ECO:0000269|PubMed:8654395}. |
| Signal Peptide | SIGNAL 1..23 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 56,767 |
| Kinetics | |
| Metal Binding | METAL 98; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 100; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 143; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 145; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 427; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 430; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 432; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 483; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 484; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 485; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 489; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3 |
| Rhea ID | RHEA:11276 |
| Cross Reference Brenda | 1.10.3.2; |