Reviewed,
UniProtKB/Swiss-Prot Q12541 (LAC1_AGABI)
Last modified
November 25, 2008.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Laccase-1 EC=1.10.3.2 Alternative name(s): Laccase I Benzenediol:oxygen oxidoreductase 1 Urishiol oxidase 1 Diphenol oxidase 1 | ||
| Gene names |
| ||
| Organism | Agaricus bisporus (Common mushroom) | ||
| Taxonomic identifier | 5341 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Agaricomycetidae › Agaricales › Agaricaceae › Agaricus |
Protein attributes
| Sequence length | 520 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Lignin degradation and detoxification of lignin-derived products By similarity. |
| Catalytic activity | 4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O. |
| Cofactor | Binds 4 copper ions per monomer By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the multicopper oxidase family. Contains 3 plastocyanin-like domains. |
Ontologies
Keywords | |
|---|---|
| Biological process | Lignin degradation |
| Cellular component | Secreted |
| Domain | Repeat Signal |
| 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-KW |
| Molecular function | copper ion binding Inferred from electronic annotation. Source: InterPro 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | |||||||
| Chain | 20 – 520 | 501 | Laccase-1 | PRO_0000002918 | |||||
Regions | |||||||||
| Domain | 21 – 145 | 125 | Plastocyanin-like 1 | ||||||
| Domain | 157 – 305 | 149 | Plastocyanin-like 2 | ||||||
| Domain | 375 – 488 | 114 | Plastocyanin-like 3 | ||||||
Sites | |||||||||
| Metal binding | 82 | 1 | Copper 1; type 2 By similarity | ||||||
| Metal binding | 84 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 127 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 129 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 417 | 1 | Copper 4; type 1 By similarity | ||||||
| Metal binding | 420 | 1 | Copper 1; type 2 By similarity | ||||||
| Metal binding | 422 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 470 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 471 | 1 | Copper 4; type 1 By similarity | ||||||
| Metal binding | 472 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 476 | 1 | Copper 4; type 1 By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 108 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 239 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 299 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 454 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 492 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Identification of two laccase genes in the cultivated mushroom Agaricus bisporus." Perry C.R., Smith M., Britnell C.H., Wood D.A., Thurston C.F. J. Gen. Microbiol. 139:1209-1218(1993) [PubMed: 8360614] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: D649. Tissue: Mycelium. |
Cross-references
Sequence databases | |
|---|---|
| L10664 Genomic DNA. Translation: AAC18877.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1HFU based on UniProtKB Q9Y780. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR001117. Cu-oxidase. IPR011706. Cu-oxidase_2. IPR011707. Cu-oxidase_3. IPR002355. Cu_oxidase_Cu_BS. IPR008972. Cupredoxin. [Graphical view] |
| Gene3D | G3DSA:2.60.40.420. Cupredoxin. 3 hits. |
| Pfam | PF00394. Cu-oxidase. 1 hit. PF07731. Cu-oxidase_2. 1 hit. PF07732. Cu-oxidase_3. 1 hit. [Graphical view] |
| PROSITE | PS00079. MULTICOPPER_OXIDASE1. 2 hits. PS00080. MULTICOPPER_OXIDASE2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LAC1_AGABI | ||||||||
| Accession | Primary (citable) accession number: Q12541 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

Clusters with


