| IED ID | IndEnz0015000011 |
| Enzyme Type ID | laccase000011 |
| Protein Name |
Laccase-1 EC 1.10.3.2 Benzenediol:oxygen oxidoreductase 1 Conidial laccase Diphenol oxidase 1 Laccase I Urishiol oxidase 1 |
| Gene Name | yA AN6635 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MYLSTVLFPLLALNLGLSHARFVRETLELTWEYGSPNGGTPREMVFTNGEYPGPDLIFDEDDDVEVLVINNLPFNTTVHWHGLEMRETPEADGVPGLTQTPIEPGATFTYRFRAYPAGTFWYHSHYKGLMQDGQVGAMYIRRKPDALRPYAVITEDPRELAEIQYAEDNPYLMLATDWTYLTSAEYHNIEVESGYNVFCVDSLLINGRGSVYCPGYQYLEEVSDDGLTAVLEGTHLTEKGCLQPDLHNVQGDYGPWNLSAVPTEVVFNCTPSSVEPPVIYVDPEFNGWVSLNFIGGAAQKAITFSVDNHPMWVYEVDGQFVEPREVEMVGVYSGARYAVMIKLDQTPGDYAIRIAVNGGDQVMSVYAILSYVNQDWIHRENVPKAAIGPHTDTVGYMNYGGGNTSADVRQLLFTENLPAFGVPPPPPSSEVSTTLRTGMIRVNNSYSWSLGNNVLYEPEMTSSTPLLFEPDPLAVIAPKYALTTENNTWVDIVLEITADPRDLIHPPHPIHKHGNRAYIIGNGVGKFRWENVSAAEAEVPDLFYVNETAALRDTFVTDFFDSRLMDGAWIVIRYFVQDKFPSILHCHIASHQMGGMALALLDGVDVWDS |
| Enzyme Length | 609 |
| Uniprot Accession Number | P17489 |
| 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: Required for the conversion of the yellow polyketide pigment synthesized by wA to the conidial green pigment. {ECO:0000269|PubMed:2659435}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (3); Glycosylation (7); Metal binding (11); Sequence conflict (3); Signal peptide (1) |
| Keywords | Conidiation;Copper;Glycoprotein;Metal-binding;Oxidoreductase;Reference proteome;Repeat;Secreted;Signal;Sporulation |
| 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 | 67,981 |
| Kinetics | |
| Metal Binding | METAL 79; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 81; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 123; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 125; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 508; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 511; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 513; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 585; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 586; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 587; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 591; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3 |
| Rhea ID | RHEA:11276 |
| Cross Reference Brenda |