| IED ID | IndEnz0015000021 |
| Enzyme Type ID | laccase000021 |
| Protein Name |
Laccase EC 1.10.3.2 Benzenediol:oxygen oxidoreductase Diphenol oxidase Ligninolytic phenoloxidase Urishiol oxidase |
| Gene Name | LCC3-1 LAC3 LCC1 |
| Organism | Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Polyporales Polyporaceae (bracket fungi) Trametes Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina) |
| Enzyme Sequence | MSRFQSLLSFVLVSLAAVANAAIGPVADLTLTNAAVSPDGFSREAVVVNGITPAPLIAGQKGDRFQLNVIDNLTNHTMLKTTSIHWHGFFQHGTNWADGVSFVNQCPIASGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYDPNDPQASLYDIDNDDTVITLADWYHVAAKLGPRFPLGADATLINGLGRSPGTTTADLAVIKVTQGKRYRFRLVSLSCDPNHTFSIDGHTMTVIEADSVNTQPLEVDSIQIFAAQRYSFVLDASQPVDNYWIRANPAFGNVGFAGGINSAILRYDGAPEVEPTTTQTTSTKPLNEADLHPLTPMPVPGRPEAGGVDKPLNMVFNFNGTNFFINNHSFVPPSVPVLLQILSGAQAAQDLVPDGSVYVLPSNSSIEISFPATANAPGTPHPFHLHGHTFAVVRSAGSSEYNYDNPIFRDVVSTGQPGDNVTIRFQTNNPGPWFLHCHIDFHLEAGFAVVLAEDTPDTAAVNPVPQSWSDLCPIYDALDPSDL |
| Enzyme Length | 518 |
| Uniprot Accession Number | O59896 |
| 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 (By similarity). Cleaves the C-C and C-O bonds of some phenolic lignin model compounds (such as O- and P-quinols, aminophenols and phenylenediamine) (PubMed:8919775). May also be involved in synthesis of phenoxazinone pigments (PubMed:9572949). {ECO:0000250|UniProtKB:Q70KY3, ECO:0000269|PubMed:8919775, ECO:0000303|PubMed:9572949}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Disulfide bond (2); Domain (3); Glycosylation (6); Metal binding (11); Region (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Copper;Direct protein sequencing;Disulfide bond;Glycoprotein;Lignin degradation;Metal-binding;Oxidoreductase;Repeat;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: By lignosulfonate, veratryl alcohol and 2,5-xylidine. {ECO:0000269|PubMed:8919775}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q70KY3}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000269|PubMed:8919775 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 55,986 |
| Kinetics | |
| Metal Binding | METAL 85; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 87; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 130; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 132; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 416; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 419; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 421; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 471; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 472; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 473; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 477; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3 |
| Rhea ID | RHEA:11276 |
| Cross Reference Brenda |