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Protein

Laccase-1b

Gene
N/A
Organism
Cerrena unicolor (Canker rot fungus) (Daedalea unicolor)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Lignin degradation and detoxification of lignin-derived products.By similarityCurated

Catalytic activityi

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

Cofactori

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

Kineticsi

  1. KM=0.153 mM for syringaldazine1 Publication

pH dependencei

Optimum pH is 5.3.1 Publication

Temperature dependencei

Optimum temperature is 60 degrees Celsius.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-1b (EC:1.10.3.2)
Alternative name(s):
Benzenediol:oxygen oxidoreductase 1b
Diphenol oxidase 1b
Lac Ib
Urishiol oxidase 1b
OrganismiCerrena unicolor (Canker rot fungus) (Daedalea unicolor)
Taxonomic identifieri90312 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPolyporaceaeCerrena

Subcellular locationi

Secreted By similarity

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 – ›9›9Laccase-1bPRO_0000310833

Family & Domainsi

Sequence similaritiesi

Belongs to the multicopper oxidase family.Sequence Analysis

Sequencei

Sequence statusi: Fragment.

Length:9
Mass (Da):892
Last modified:November 13, 2007 - v1
Checksum:i1CE22AADC2D76870
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei9 – 91

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiLAC1B_CERUI
AccessioniPrimary (citable) accession number: P85308
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: January 7, 2015
This is version 24 of the entry and version 1 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: 4.27, its MW is: 54.49 kDa.

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.