| IED ID | IndEnz0015000012 |
| Enzyme Type ID | laccase000012 |
| Protein Name |
Laccase-2 EC 1.10.3.2 Benzenediol:oxygen oxidoreductase 2 Diphenol oxidase 2 Laccase C Laccase II Urishiol oxidase 2 |
| Gene Name | LAC2 |
| Organism | Podospora anserina (Pleurage anserina) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Podosporaceae Podospora Podospora anserina (Pleurage anserina) |
| Enzyme Sequence | MMKSFFSAAALLLGLVAPSAVLAAPSLPGVPREVTRDLLRPVEERQSSCHTAANRACWAPGFDINTDYEVSTPNTGVTRTYTLTLTEVDNWLGPDGVVKQKVMLVNGDIFGPTITANWGDWIQVNVINNLRTNGTSIHWHGLHQKGTNMHDGANGVTECPIPPKGGSRIYRFRAQQYGTSWYHSHFSAQYGNGVVGTIVVNGPASVPYDIDLGVFPITDYYHKPADVLVEETMNGGPPPSDTVLFKGHGKNPQTGAGKFANVTLTPGKRHRLRIINTSTHDHFQLKLQNHTMTIIAADMVPVQAQTVDSLFLAVGQRYDVTIDANKSVGNYWFNATFGGGLACGASLNPHPAAVFRYQGAPNTLPTNIGTPAADANCMDLNNLTPVVSRSVPTSGFTPRPNNTLPVSLTLGGTPLFVWKVNGSSINVDWDKPIVDYVIAQNTSYPPQANVITVNSVNQWTYWLIENDPTGPFSIPHPMHLHGHDFLVVGRSPDQPAGVPQTRYRFNPATDMALLKSSNPVRRDVAMLPANGWLLIAFKSDNPGAWLFHCHIAWHVSGGLSVQYLERPNDLRNGFSQADKNQHNNNCNAWRAYWPTNPFPKIDSGLKVKKWVGEHPDWYIKN |
| Enzyme Length | 621 |
| Uniprot Accession Number | P78722 |
| 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: Probably involved in lignin degradation and in the detoxification of lignin-derived products in its natural habitat (herbivorous dung), which is rich in lignin of grasses and straw. Probably involved in melanin synthesis and in perithecia development. {ECO:0000303|PubMed:8914515}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (3); Domain (3); Glycosylation (9); Metal binding (11); Propeptide (2); Signal peptide (1) |
| Keywords | Copper;Disulfide bond;Glycoprotein;Lignin degradation;Melanin biosynthesis;Metal-binding;Oxidoreductase;Repeat;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Under oxidative stress on the mycelium by aromatic xenobiotics (guaiacol, hydroquinone, benzoquinone), and by copper salt at a concentration of 1 mM (growing mycelium). {ECO:0000269|PubMed:8914515}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q70KY3}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically processed at both its N-terminus and its C-terminus. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 68,129 |
| Kinetics | |
| Metal Binding | METAL 138; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 140; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 183; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 185; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 476; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 479; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 481; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 548; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 549; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 550; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 554; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3 |
| Rhea ID | RHEA:11276 |
| Cross Reference Brenda |