P85517 (BGL2_CLAFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Beta-glucosidase 2 EC=3.2.1.21 Alternative name(s): Beta-D-glucoside glucohydrolase Cellobiase Gentiobiase
Organism	Cladosporium fulvum (Fulvia fulva)
Taxonomic identifier	5499 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Dothideomycetes › Dothideomycetidae › Capnodiales › Mycosphaerellaceae › mitosporic Mycosphaerellaceae › Passalora

Protein attributes

Sequence length	39 AA.
Sequence status	Fragments.
Protein existence	Evidence 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 process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	beta-glucosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›39	›39	Beta-glucosidase 2		PRO_0000370228
Experimental info
	Non-adjacent residues	14 – 15	2
	Non-adjacent residues	25 – 26	2
	Non-terminal residue	1	1
	Non-terminal residue	39	1

Sequences

	Sequence		Length	Mass (Da)
	P85517 [UniParc]. Last modified April 14, 2009. Version 1. Checksum: 419ECD2D7582085B	FASTA	39	4,029
	10 20 30 GVDVLLGQGL LAPRTPFTGE GPSQKSYGTE LLSKPNDGK

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
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

BGL2_CLAFU

Accession

Primary (citable) accession number: P85517

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	April 14, 2009
Last modified:	November 2, 2010
This is version 5 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program