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Reviewed, UniProtKB/Swiss-Prot P85430 (LAC2D_CERUI)

Last modified June 16, 2009. Version 8. 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-2d
    EC=1.10.3.2
Alternative name(s):
    Laccase-IId
      Short name=Lac-IId
    Benzenediol:oxygen oxidoreductase
    Urishiol oxidase
    Diphenol oxidase
OrganismCerrena unicolor (Canker rot fungus) (Daedalea unicolor)
Taxonomic identifier90312 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaHomobasidiomycetesAphyllophoralesCerrena

Protein attributes

Sequence length47 AA.
Sequence statusFragments.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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

Secreted.

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 processLignin degradation
   Cellular componentSecreted
   DomainRepeat
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMGlycoprotein
   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 – ›47›47Laccase-2d
PRO_0000320022

Regions

Domain2 – ?Plastocyanin-like 1
Domain? – ›47Plastocyanin-like 3

Amino acid modifications

Glycosylation421N-linked (GlcNAc...) Potential

Experimental info

Non-adjacent residues30 – 312
Non-terminal residue471

Sequences

Sequence LengthMass (Da)Tools
P85430-1 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: DFC1942A188FC2B9

FASTA474,846
        10         20         30         40 
GTGPVADLHI INKDLSPDGF QRPTVVAGGG RDVVSIGRAG DNVTIRF 

« Hide

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

ModBaseSearch...

Family and domain databases

InterProIPR002355. Cu_oxidase_Cu_BS.
[Graphical view]
PROSITEPS00079. MULTICOPPER_OXIDASE1. Partial match.
PS00080. MULTICOPPER_OXIDASE2. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLAC2D_CERUI
AccessionPrimary (citable) accession number: P85430
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: September 2, 2008
Last modified: June 16, 2009
This is version 8 of the entry and version 2 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