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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

    GO - Biological processi

    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

    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.