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Protein

Beta-glucosidase 2

Gene
N/A
Organism
Passalora fulva (Tomato leaf mold) (Cladosporium fulvum)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.1 Publication

Kineticsi

  1. KM=0.18 mM for pNPG1 Publication

    pH dependencei

    Optimum pH is 5.5.1 Publication

    Temperature dependencei

    Optimum temperature is 45 degrees Celsius.1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-glucosidase 2 (EC:3.2.1.21)
    Alternative name(s):
    Beta-D-glucoside glucohydrolase
    Cellobiase
    Gentiobiase
    OrganismiPassalora fulva (Tomato leaf mold) (Cladosporium fulvum)
    Taxonomic identifieri5499 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesDothideomycetidaeCapnodialesMycosphaerellaceaePassalora

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›39›39Beta-glucosidase 2PRO_0000370228Add
    BLAST

    Sequencei

    Sequence statusi: Fragments.

    P85517-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30 
    GVDVLLGQGL LAPRTPFTGE GPSQKSYGTE LLSKPNDGK
    Length:39
    Mass (Da):4,029
    Last modified:April 14, 2009 - v1
    Checksum:i419ECD2D7582085B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-adjacent residuesi14 – 152Curated
    Non-adjacent residuesi25 – 262Curated
    Non-terminal residuei39 – 391

    Cross-referencesi

    3D structure databases

    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Family and domain databases

    ProtoNetiSearch...

    Publicationsi

    1. "A novel ginsenoside rb1-hydrolyzing beta-D-glucosidase from Cladosporium fulvum."
      Zhao X., Gao L., Wang J., Bi H., Gao J., Du X., Zhou Y., Tai G.
      Process Biochem. 44:612-618(2009)
      Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiBGL2_PASFU
    AccessioniPrimary (citable) accession number: P85517
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: April 14, 2009
    Last modified: October 1, 2014
    This is version 9 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries

    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.