Reviewed,
UniProtKB/Swiss-Prot P85430 (LAC2D_CERUI)
Last modified
June 16, 2009.
Version 8.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Laccase-2d EC=1.10.3.2 Alternative name(s): Laccase-IId Short name=Lac-IId Benzenediol:oxygen oxidoreductase Urishiol oxidase Diphenol oxidase |
| Organism | Cerrena unicolor (Canker rot fungus) (Daedalea unicolor) |
| Taxonomic identifier | 90312 [NCBI] |
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Aphyllophorales › Cerrena |
Protein attributes
| Sequence length | 47 AA. |
| Sequence status | Fragments. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Lignin degradation and detoxification of lignin-derived products Probable. Has highest activity towards ABTS, also active towards ferulic acid and guaiacol, but is not active towards tyrosine, vanillic acid, 2,5-dimethyl aniline, p-anisidine or violuric acid. |
| Catalytic activity | 4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O. UniProtKB Q99044 |
| Cofactor | Binds 4 copper ions per monomer By similarity. UniProtKB Q12718 |
| Enzyme regulation | Inhibited by sodium azide, SDS and mercaptoethanol, but not by 4-hexyl resocinol, L-cysteine and dithiothreitol. Activity is inhibited by the heavy metal ions Cr, W, Sn, Ag+ and Hg2+, but not by Pb2+, Fe3+, Ni2+, Li2+, Co2+ or Cd2+. |
| Subunit structure | Homodimer By similarity. UniProtKB Q99044 |
| Subcellular location | |
| Post-translational modification | N-glycosylated; contains 17% carbohydrates. |
| Miscellaneous | On the 2D-gel the determined pI of this protein is: 5.3, its MW is: 59 kDa. |
| Sequence similarities | Belongs to the multicopper oxidase family. Contains 3 plastocyanin-like domains. |
| biophysicochemical properties | Kinetic parameters: KM=54.1 µM for ABTS (at 70 degrees Celsius) KM=57.1 µM for ABTS (at 30 degrees Celsius) KM=19.2 µM for syringaldizine (at 30 degrees Celsius) pH dependence: Optimum pH is 3.0 at 70 degrees Celsius with ABTS as substrate, and 6.0 with guaiacol and syringaldazine as substrate. Temperature dependence: Optimum temperature is 70 degrees Celsius at pH 3.0 with ABTS as substrate. Retains 100% of its activity after 1 hour at 30 degrees Celsius at pH 9.0. Retains more than 60% of its activity after 180 minutes at 60 degrees Celsius at pH 9.0. Retains approximately 50% of its activity after 90 minutes at 70 degrees Celsius at pH 9.0. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lignin degradation |
| Cellular component | Secreted |
| Domain | Repeat |
| Ligand | Copper Metal-binding |
| Molecular function | Oxidoreductase |
| PTM | Glycoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | lignin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW laccase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›47 | ›47 | Laccase-2d | PRO_0000320022 | |||||
Regions | |||||||||
| Domain | 2 – ? | Plastocyanin-like 1 | |||||||
| Domain | ? – ›47 | Plastocyanin-like 3 | |||||||
Amino acid modifications | |||||||||
| Glycosylation | 42 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Non-adjacent residues | 30 – 31 | 2 | |||||||
| Non-terminal residue | 47 | 1 | |||||||
Sequences
References
| [1] | "A thermostable metal-tolerant laccase with bioremediation potential from a marine-derived fungus." D'Souza-Ticlo D., Sharma D., Raghukumar C. Mar. Biotechnol. 0:0-0(2009) [PubMed: 19283431] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION. Strain: MTCC 5159. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR002355. Cu_oxidase_Cu_BS. [Graphical view] |
| PROSITE | PS00079. MULTICOPPER_OXIDASE1. Partial match. PS00080. MULTICOPPER_OXIDASE2. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LAC2D_CERUI | ||||||||
| Accession | Primary (citable) accession number: P85430 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

Clusters with


