IED ID | IndEnz0015000016 |
Enzyme Type ID | laccase000016 |
Protein Name |
Laccase-1 EC 1.10.3.2 Diphenol oxidase 1 |
Gene Name | LAC1 CNBG3550 |
Organism | Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) (Filobasidiella neoformans) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Tremellomycetes Tremellales (jelly fungi) Cryptococcaceae Cryptococcus Cryptococcus neoformans species complex Cryptococcus neoformans (Filobasidiella neoformans) Cryptococcus neoformans var. neoformans Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) (Filobasidiella neoformans) |
Enzyme Sequence | MRGLAKLFFLSCSFVSLVSSEKTDESPTAVSDNYMPKATATIDPSVFALSNDFEITDVPTTREYTFDIAKAFASPDGYEREVYVVNNMFPGPVIEANTGDTIIVHVNNHLDEGQSLHWHGLRQLGTAFMDGVPGITQCPIPPGGSFTYNFTVSHQSGTYWWHSHYSNSMADGIWGPLIVHSPNEPLQRGRDYDEDRIVFITDWMHDNSEIIIAALATPEGYKGNIAPPQGDAILINGRGQTNCTATGSSSCFYPPPPEIQVPVNCRVRLRFISATAHPMYRISIDNHPMEVVEADGTAVYGPTVHEISVAPGERYSAIINTNEGKEGDAFWLRTSVALSCMFGAVSQEGLAVVRYTGNGMVSTEEPQTSAWSDLAGVTVPCTGLDQTYTLSPRDSLSAPREPLQSHFFNSERGAFVNVLGNTFQGYGFNNISYQNQIFNPLLSIVQRGGSCENTLVSSRTFPDFGPGNIIINNLDTVIDHPYHLHGNEFQVIGRGTGALSIDNLTNIDFTLDNPVRKDTLWIQGGSWAVLRITADNPGVWALHCHIGWHLTEGKLAVIVVQPSAIGHMESPESWTNLCANTDPNAFGPAKRSSSPSIQSSKTSSFQYLREVKGKVVKRRGAREA |
Enzyme Length | 624 |
Uniprot Accession Number | Q55P57 |
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:0000269|PubMed:8300520}; |
DNA Binding | |
EC Number | 1.10.3.2 |
Enzyme Function | FUNCTION: Laccase that catalyzes the oxidation of certain aromatic compounds, including L-dopa, to quinones, which then polymerize to melanin (PubMed:1100669, PubMed:6807845, PubMed:6804444, PubMed:8760791). Able to oxidize a wide variety of aromatic diphenol and diamino groups in the ortho, meta, and para positions but not monophenolic groups such as in phenol, tyramine, or tyrosine (PubMed:8300520). Plays an important role in virulence (PubMed:8760791). Plays a role in dissemination to extrapulmonary sites but is not involved in pulmonary growth or in elicitation of cellular immune responses in the lung (PubMed:14977977). {ECO:0000269|PubMed:1100669, ECO:0000269|PubMed:14977977, ECO:0000269|PubMed:6804444, ECO:0000269|PubMed:6807845, ECO:0000269|PubMed:8300520, ECO:0000269|PubMed:8760791}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (1); Domain (3); Glycosylation (4); Metal binding (11); Mutagenesis (1); Region (1); Signal peptide (1) |
Keywords | Cell wall;Copper;Direct protein sequencing;Disulfide bond;Glycoprotein;Metal-binding;Oxidoreductase;Repeat;Secreted;Signal |
Interact With | |
Induction | INDUCTION: Expressed during infection of host (PubMed:8760791). Expression is repressed by glucose (PubMed:8300520). {ECO:0000269|PubMed:8300520, ECO:0000269|PubMed:8760791}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11500433}. Secreted, cell wall {ECO:0000269|PubMed:11500433}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000269|PubMed:8300520 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 68,270 |
Kinetics | |
Metal Binding | METAL 117; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 119; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 162; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 164; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 480; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 483; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 485; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 543; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 544; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 545; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:D0VWU3; METAL 549; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:D0VWU3 |
Rhea ID | RHEA:11276 |
Cross Reference Brenda |