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Protein

Laccase-2d

Gene
N/A
Organism
Cerrena unicolor (Canker rot fungus) (Daedalea unicolor)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 PublicationCurated

Catalytic activityi

4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.By similarity1 Publication

Cofactori

Cu cationBy similarityNote: Binds 4 Cu cations per monomer.By similarity

Enzyme regulationi

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+.1 Publication

Kineticsi

  1. KM=54.1 µM for ABTS (at 70 degrees Celsius)1 Publication
  2. KM=57.1 µM for ABTS (at 30 degrees Celsius)1 Publication
  3. KM=19.2 µM for syringaldizine (at 30 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 3.0 at 70 degrees Celsius with ABTS as substrate, and 6.0 with guaiacol and syringaldazine as substrate.1 Publication

Temperature dependencei

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 9.0.1 Publication

GO - Molecular functioni

  1. hydroquinone:oxygen oxidoreductase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. lignin catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lignin degradation

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Laccase-2d1 Publication (EC:1.10.3.2)
Alternative name(s):
Benzenediol:oxygen oxidoreductaseBy similarity
Diphenol oxidaseBy similarity
Laccase-IId1 Publication
Short name:
Lac-IId1 Publication
Urishiol oxidaseBy similarity
OrganismiCerrena unicolor (Canker rot fungus) (Daedalea unicolor)
Taxonomic identifieri90312 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPolyporaceaeCerrena

Subcellular locationi

Secreted Curated

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›47›47Laccase-2dPRO_0000320022Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated; contains 17% carbohydrates.1 Publication

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homodimer.By similarity

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini? – ›47Plastocyanin-like 3Sequence Analysis
Domaini2 – ?Plastocyanin-like 1Sequence Analysis

Sequence similaritiesi

Belongs to the multicopper oxidase family.Sequence Analysis
Contains 3 plastocyanin-like domains.Sequence Analysis

Keywords - Domaini

Repeat

Sequencei

Sequence statusi: Fragments.

P85430-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
GTGPVADLHI INKDLSPDGF QRPTVVAGGG RDVVSIGRAG DNVTIRF
Length:47
Mass (Da):4,846
Last modified:September 2, 2008 - v2
Checksum:iDFC1942A188FC2B9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-adjacent residuesi30 – 3121 Publication
Non-terminal residuei47 – 4711 Publication

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "A thermostable metal-tolerant laccase with bioremediation potential from a marine-derived fungus."
    D'Souza-Ticlo D., Sharma D., Raghukumar C.
    Mar. Biotechnol. 11:725-737(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION.
    Strain: MTCC 51591 Publication.

Entry informationi

Entry nameiLAC2D_CERUI
AccessioniPrimary (citable) accession number: P85430
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: September 2, 2008
Last modified: January 7, 2015
This is version 25 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

On the 2D-gel the determined pI of this protein is: 5.3, its MW is: 59 kDa.1 Publication

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.