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P85517 (BGL2_PASFU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 8. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-glucosidase 2

EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase
Cellobiase
Gentiobiase
OrganismPassalora fulva (Tomato leaf mold) (Cladosporium fulvum)
Taxonomic identifier5499 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesDothideomycetidaeCapnodialesMycosphaerellaceaePassalora

Protein attributes

Sequence length39 AA.
Sequence statusFragments.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Biophysicochemical properties

Kinetic parameters:

KM=0.18 mM for pNPG Ref.1

pH dependence:

Optimum pH is 5.5. Ref.1

Temperature dependence:

Optimum temperature is 45 degrees Celsius. Ref.1

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionbeta-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›39›39Beta-glucosidase 2
PRO_0000370228

Experimental info

Non-adjacent residues14 – 152
Non-adjacent residues25 – 262
Non-terminal residue11
Non-terminal residue391

Sequences

Sequence LengthMass (Da)Tools
P85517 [UniParc].

Last modified April 14, 2009. Version 1.
Checksum: 419ECD2D7582085B

FASTA394,029
        10         20         30 
GVDVLLGQGL LAPRTPFTGE GPSQKSYGTE LLSKPNDGK 

« Hide

References

[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.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameBGL2_PASFU
AccessionPrimary (citable) accession number: P85517
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 14, 2009
Last modified: October 16, 2013
This is version 8 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries