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Reviewed, UniProtKB/Swiss-Prot P85308 (LAC1B_CERUI)

Last modified November 24, 2009. Version 10. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Laccase-1b
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 1b
    Urishiol oxidase 1b
    Diphenol oxidase 1b
    Lac Ib
OrganismCerrena unicolor (Canker rot fungus) (Daedalea unicolor)
Taxonomic identifier90312 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaHomobasidiomycetesAphyllophoralesCerrena

Protein attributes

Sequence length9 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.

Miscellaneous

On the 2D-gel the determined pI of this protein is: 4.27, its MW is: 54.49 kDa. Ref.1

Sequence similarities

Belongs to the multicopper oxidase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.153 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
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processlignin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

laccase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›9›9Laccase-1b
PRO_0000310833

Experimental info

Non-terminal residue91

Sequences

Sequence LengthMass (Da)Tools
P85308-1 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 1CE22AADC2D76870

FASTA9892
AIGPVADLH 

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References

[1]Checinska A., Janusz G., Rogalski J.M.
Submitted (OCT-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.10.3.2. 280017.

Family and domain databases

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

Entry information

Entry nameLAC1B_CERUI
AccessionPrimary (citable) accession number: P85308
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: November 24, 2009
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents