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P85149 (LAC2_CERUI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Laccase-2

EC=1.10.3.2
Alternative name(s):
Benzenediol:oxygen oxidoreductase 2
Diphenol oxidase 2
Lac II
Urishiol oxidase 2
OrganismCerrena unicolor (Canker rot fungus) (Daedalea unicolor)
Taxonomic identifier90312 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaHomobasidiomycetesAphyllophoralesCerrena

Protein attributes

Sequence length10 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lignin degradation and detoxification of lignin-derived products Probable. UniProtKB Q12718

Catalytic activity

4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O. Ref.1

Cofactor

Binds 4 copper ions per monomer By similarity. UniProtKB Q12718

Subcellular location

Secreted By similarity UniProtKB Q12718.

Post-translational modification

Glycosylated; contains 8.47% carbohydrates. Ref.1

Miscellaneous

On the 2D-gel the determined pI of this protein is: 4.56, its MW is: 62.03 kDa. Ref.1

Sequence similarities

Belongs to the multicopper oxidase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.166 mM for syringaldazine Ref.1

pH dependence:

Optimum pH is 5.3. Ref.1

Temperature dependence:

Optimum temperature is 60 degrees Celsius. Ref.1

Ontologies

Keywords
   Biological processLignin degradation
   Cellular componentSecreted
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processlignin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhydroquinone:oxygen oxidoreductase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›10›10Laccase-2
PRO_0000288803

Experimental info

Non-terminal residue101

Sequences

Sequence LengthMass (Da)Tools
P85149 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 212CE22AADC2D768

FASTA101,005
        10 
AIGPVADLHI 

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References

[1]"Purification of Cerrena unicolor laccase."
Janusz G., Rogalski J.M.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION.

Cross-references

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

PROSITEPS00079. MULTICOPPER_OXIDASE1. Partial match.
PS00080. MULTICOPPER_OXIDASE2. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLAC2_CERUI
AccessionPrimary (citable) accession number: P85149
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: November 16, 2011
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families