| IED ID | IndEnz0015000002 |
| Enzyme Type ID | laccase000002 |
| Protein Name |
Laccase-1 EC 1.10.3.2 Benzenediol:oxygen oxidoreductase 1 Diphenol oxidase 1 Ligninolytic phenoloxidase Urishiol oxidase 1 |
| Gene Name | LAC1 |
| Organism | Melanocarpus albomyces |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Chaetomiaceae Melanocarpus Melanocarpus albomyces |
| Enzyme Sequence | MKTFTSALALVVGMLAPGAVVAAPPSTPAQRDLVELREARQEGGKDLRPREPTCNTPSNRACWSDGFDINTDYEVSTPDTGVTQSYVFNLTEVDNWMGPDGVVKEKVMLINGNIMGPNIVANWGDTVEVTVINNLVTNGTSIHWHGIHQKDTNLHDGANGVTECPIPPKGGQRTYRWRARQYGTSWYHSHFSAQYGNGVVGTIQINGPASLPYDIDLGVFPITDYYYRAADDLVHFTQNNAPPFSDNVLINGTAVNPNTGEGQYANVTLTPGKRHRLRILNTSTENHFQVSLVNHTMTVIAADMVPVNAMTVDSLFLAVGQRYDVVIDASRAPDNYWFNVTFGGQAACGGSLNPHPAAIFHYAGAPGGLPTDEGTPPVDHQCLDTLDVRPVVPRSVPVNSFVKRPDNTLPVALDLTGTPLFVWKVNGSDINVDWGKPIIDYILTGNTSYPVSDNIVQVDAVDQWTYWLIENDPEGPFSLPHPMHLHGHDFLVLGRSPDVPAASQQRFVFDPAVDLARLNGDNPPRRDTTMLPAGGWLLLAFRTDNPGAWLFHCHIAWHVSGGLSVDFLERPADLRQRISQEDEDDFNRVCDEWRAYWPTNPYPKIDSGLKRRRWVEESEWLVR |
| Enzyme Length | 623 |
| Uniprot Accession Number | Q70KY3 |
| Absorption | BIOPHYSICOCHEMICAL PROPERTIES: Absorption: Abs(max)=280 nm {ECO:0000269|PubMed:12111146, ECO:0000269|PubMed:12118243}; Note=Exhibits a shoulder at 360 nm, a smaller absorption peak at 450 nm, and a second, larger peak at 590 nm. {ECO:0000269|PubMed:12118243}; |
| 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:12111146}; |
| DNA Binding | |
| EC Number | 1.10.3.2 |
| Enzyme Function | FUNCTION: Lignin degradation and detoxification of lignin-derived products. {ECO:0000269|PubMed:15474046, ECO:0000305}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60-70 degrees Celsius. {ECO:0000269|PubMed:12111146, ECO:0000269|PubMed:12118243}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.5 with 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulphonate) as substrate, 5.0-7.5 with guiacol as substrate, and 6.0-7.0 with syringaldazine as substrate. {ECO:0000269|PubMed:12111146, ECO:0000269|PubMed:12118243}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (36); Chain (1); Disulfide bond (3); Glycosylation (8); Helix (14); Metal binding (11); Propeptide (2); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Copper;Direct protein sequencing;Disulfide bond;Glycoprotein;Lignin degradation;Metal-binding;Oxidoreductase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (9) |
| Cross Reference PDB | 1GW0; 2IH8; 2IH9; 2Q9O; 3DKH; 3FU7; 3FU8; 3FU9; 3QPK; |
| Mapped Pubmed ID | 17045575; 18249560; 19563811; 19780817; 21524088; |
| Motif | |
| Gene Encoded By | |
| Mass | 68,958 |
| Kinetics | |
| Metal Binding | METAL 143; /note=Copper 1; type 2; /evidence=ECO:0000269|PubMed:12118243; METAL 145; /note=Copper 2; type 3; /evidence=ECO:0000269|PubMed:12118243; METAL 188; /note=Copper 2; type 3; /evidence=ECO:0000269|PubMed:12118243; METAL 190; /note=Copper 3; type 3; /evidence=ECO:0000269|PubMed:12118243; METAL 481; /note=Copper 4; type 1; /evidence=ECO:0000269|PubMed:12118243; METAL 484; /note=Copper 1; type 2; /evidence=ECO:0000269|PubMed:12118243; METAL 486; /note=Copper 3; type 3; /evidence=ECO:0000269|PubMed:12118243; METAL 552; /note=Copper 3; type 3; /evidence=ECO:0000269|PubMed:12118243; METAL 553; /note=Copper 4; type 1; /evidence=ECO:0000269|PubMed:12118243; METAL 554; /note=Copper 2; type 3; /evidence=ECO:0000269|PubMed:12118243; METAL 558; /note=Copper 4; type 1; /evidence=ECO:0000269|PubMed:12118243 |
| Rhea ID | RHEA:11276 |
| Cross Reference Brenda | 1.10.3.2; |