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Protein

Beta-glucosidase 1

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 6.0.1 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 1 (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 – ›40›40Beta-glucosidase 1PRO_0000370227Add
    BLAST

    Sequencei

    Sequence statusi: Fragments.

    P85516-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40
    LVAHEENVRV GKDEGFAKAG GLSRLPLEAG ESGTATFNVR
    Length:40
    Mass (Da):4,184
    Last modified:April 14, 2009 - v1
    Checksum:i9B7085022AB31854
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-adjacent residuesi9 – 102Curated
    Non-adjacent residuesi24 – 252Curated
    Non-terminal residuei40 – 401

    Cross-referencesi

    3D structure databases

    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Family and domain databases

    ProtoNetiSearch...

    Publicationsi

    1. Zhao X.S., Gao L., Wang J., Du X.L., Gao J., Zhou Y.F., Tai G.H.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiBGL1_PASFU
    AccessioniPrimary (citable) accession number: P85516
    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.