| IED ID | IndEnz0015000070 |
| Enzyme Type ID | laccase000070 |
| Protein Name |
Laccase-1 EC 1.10.3.2 Diphenol oxidase 1 |
| Gene Name | LAC1 CNAG_03465 |
| Organism | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
| 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. grubii (Filobasidiella neoformans var. grubii) Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
| Enzyme Sequence | MRGVVKLFFLSCSLVSLVSSEETGKSPTANYDHYMPKATATIDPSVFALSNDFEITDVPTTREYTFDITKALASPDGYEREVYVVNNMFPGPVIEANTGDTIIVHVNNHLEEGQSIHWHGLRQLGTAFMDGVPGITQCPIPPGSSFTYQFTVSHQSGTFWWHSHYSNSMADGIWGPLIIHSPNEPLQRGRDYDEDRIVFITDWVHDNSEVVIAALATPEGYKGSPAPPQGDAILINGRGQTNCTATGSSSCTYPPPPEIHVPVNCRVRLRFISATAHPMYRITIDNHPLEVVETDGTAVYGPTVHEISIAPGERYSAIINTSEGKEGDAFWLRTSVALGCMFGGIDQVGLAVVRYTGNGMVSTEEPQTTAWSDLAGATTPCAGLDQTYTLSPRESFSAPREFSQSHVFNSQRGAFVNVYGNTFQGYGFNNISYQNQIFNPLLSIVQRGGSCESTLVASTTFPDLGSGNIIINNLDGVIDHPYHLHGNEFQVIGRGTGALSLDNLTNIDFNLDNPVRKDTLWIQGGSWVVLRITTDNPGVWALHCHIGWHLTEGKLAVVVIQPGAIGHMEGPESWTNLCANTDPNAFGPARRSPSPSIQSSKTSTFQYLREVKGKVVKRRGAREA |
| Enzyme Length | 624 |
| Uniprot Accession Number | J9VY90 |
| 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:12581355}; |
| 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 (By similarity). 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 (By similarity). Plays an important role in virulence (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q55P57, ECO:0000303|PubMed:15381117}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (1); Domain (3); Glycosylation (4); Metal binding (11); Region (1); Signal peptide (1) |
| Keywords | Cell wall;Copper;Disulfide bond;Glycoprotein;Metal-binding;Oxidoreductase;Repeat;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Induced by copper (PubMed:12581355). Transcriptional induction by copper is dependent on enhancer region II, at position -1792 to -1614 within the 5'-untranslated region (PubMed:12581355). {ECO:0000269|PubMed:12581355}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11500433, ECO:0000269|PubMed:12581355}. Secreted, cell wall {ECO:0000269|PubMed:11500433, ECO:0000269|PubMed:12581355, ECO:0000269|PubMed:16524904}. Note=Does not associate with the cell membrane. {ECO:0000269|PubMed:16524904}. |
| 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 | 68,107 |
| 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 |