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Reviewed, UniProtKB/Swiss-Prot P29090 (BGL3_ASPWE)

Last modified June 16, 2009. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Beta-glucosidase A-3
    EC=3.2.1.21
Alternative name(s):
    Gentiobiase
    Cellobiase
    Beta-D-glucoside glucohydrolase
OrganismAspergillus wentii
Taxonomic identifier5066 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length63 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
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.

Pathway

Glycan metabolism; cellulose degradation.

Sequence similarities

Belongs to the glycosyl hydrolase 3 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›63›63Beta-glucosidase A-3
PRO_0000210776

Sites

Active site121

Amino acid modifications

Glycosylation481N-linked (GlcNAc...)
Glycosylation561N-linked (GlcNAc...)

Experimental info

Non-terminal residue11
Non-terminal residue631

Sequences

Sequence LengthMass (Da)Tools
P29090-1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: B93EDF03B5AEA63A

FASTA636,689
        10         20         30         40         50         60 
AZLGFZGFVM SDWAAHHAGV SGALAGLBMG SMPGBVBYBS GTSYWGTNLT ISLWVNGTVP 


ZWR 

« Hide

References

[1]"Isolation and structure of a tryptic glycopeptide from the active site of beta-glucosidase A3 from Aspergillus wentii."
Bause E., Legler G.
Biochim. Biophys. Acta 626:459-465(1980) [PubMed: 6783081] [Abstract]
Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases

PIRA29171.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Enzyme and pathway databases

BRENDA3.2.1.21. 215346.

Family and domain databases

InterProIPR019800. Glyco_hydro_3_AS.
IPR001764. Glyco_hydro_3_N.
[Graphical view]
PfamPF00933. Glyco_hydro_3. 1 hit.
[Graphical view]
PROSITEPS00775. GLYCOSYL_HYDROL_F3. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGL3_ASPWE
AccessionPrimary (citable) accession number: P29090
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 16, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents