Reviewed,
UniProtKB/Swiss-Prot Q96UM2 (LAC3_BOTFU)
Last modified
January 19, 2010.
Version 35.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Laccase-3 EC=1.10.3.2 Alternative name(s): Benzenediol:oxygen oxidoreductase 3 Urishiol oxidase 3 Diphenol oxidase 3 | ||
| Gene names |
| ||
| Organism | Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea) | ||
| Taxonomic identifier | 40559 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Leotiomycetes › Helotiales › Sclerotiniaceae › Botryotinia |
Protein attributes
| Sequence length | 454 AA. |
| Sequence status | Fragment. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Lignin degradation and detoxification of lignin-derived products By similarity. |
| Catalytic activity | 4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O. |
| Cofactor | Binds 4 copper ions per monomer By similarity. |
| Subcellular location | Secreted Potential. |
| Sequence similarities | Belongs to the multicopper oxidase family. Contains 3 plastocyanin-like domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lignin degradation |
| Cellular component | Secreted |
| Domain | Repeat |
| Ligand | Copper Metal-binding |
| Molecular function | Oxidoreductase |
| PTM | Glycoprotein |
| 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 – ›454 | ›454 | Laccase-3 | PRO_0000267639 | |||||
Regions | |||||||||
| Domain | ‹1 – 95 | ›95 | Plastocyanin-like 1 | ||||||
| Domain | 101 – 252 | 152 | Plastocyanin-like 2 | ||||||
| Domain | 319 – 454 | 136 | Plastocyanin-like 3 | ||||||
Sites | |||||||||
| Metal binding | 29 | 1 | Copper 1; type 2 By similarity | ||||||
| Metal binding | 31 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 73 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 75 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 375 | 1 | Copper 4; type 1 By similarity | ||||||
| Metal binding | 378 | 1 | Copper 1; type 2 By similarity | ||||||
| Metal binding | 380 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 437 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 438 | 1 | Copper 4; type 1 By similarity | ||||||
| Metal binding | 439 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 443 | 1 | Copper 4; type 1 By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 24 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 138 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 169 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 218 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 314 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 334 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 395 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 454 | 1 | |||||||
Sequences
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References
| [1] | "Resveratrol acts as a natural profungicide and induces self-intoxication by a specific laccase." Schouten A., Wagemakers L., Stefanato F.L., van der Kaaij R.M., van Kan J.A.L. Mol. Microbiol. 43:883-894(2002) [PubMed: 11929539] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SAS56. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY047482 Genomic DNA. Translation: AAL06114.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GW0 based on UniProtKB Q70KY3. |
| SMR | Q96UM2. Positions 1-453. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.10.3.2. 290409. |
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. 1 hit. PS00080. MULTICOPPER_OXIDASE2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LAC3_BOTFU | ||||||||
| Accession | Primary (citable) accession number: Q96UM2 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

Clusters with


