Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P85517

- BGL2_PASFU

UniProt

P85517 - BGL2_PASFU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Beta-glucosidase 2

Gene
N/A
Organism
Passalora fulva (Tomato leaf mold) (Cladosporium fulvum)
Status
Reviewed - 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

  1. beta-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
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

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

ProtoNeti Search...

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