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P12614 (BGLS_AGRSA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

EC=3.2.1.21
Alternative name(s):
Amygdalase
Beta-D-glucoside glucohydrolase
Cellobiase
Gentiobiase
Gene names
Name:abg
OrganismAgrobacterium sp. (strain ATCC 21400)
Taxonomic identifier74562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacterium

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Molecular functionGlycosidase
Hydrolase
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

Chain1 – 459459Beta-glucosidase
PRO_0000063869

Sites

Active site1711Proton donor Potential
Active site3591Nucleophile Ref.2

Sequences

Sequence LengthMass (Da)Tools
P12614 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: AAB799153493A682

FASTA45951,170
        10         20         30         40         50         60 
MTDPNTLAAR FPGDFLFGVA TASFQIEGST KADGRKPSIW DAFCNMPGHV FGRHNGDIAC 

        70         80         90        100        110        120 
DHYNRWEEDL DLIKEMGVEA YRFSLAWPRI IPDGFGPINE KGLDFYDRLV DGCKARGIKT 

       130        140        150        160        170        180 
YATLYHWDLP LTLMGDGGWA SRSTAHAFQR YAKTVMARLG DRLDAVATFN EPWCAVWLSH 

       190        200        210        220        230        240 
LYGVHAPGER NMEAALAAMH HINLAHGFGV EASRHVAPKV PVGLVLNAHS AIPASDGEAD 

       250        260        270        280        290        300 
LKAAERAFQF HNGAFFDPVF KGEYPAEMME ALGDRMPVVE AEDLGIISQK LDWWGLNYYT 

       310        320        330        340        350        360 
PMRVADDATP GVEFPATMPA PAVSDVKTDI GWEVYAPALH TLVETLYERY DLPECYITEN 

       370        380        390        400        410        420 
GACYNMGVEN GQVNDQPRLD YYAEHLGIVA DLIRDGYPMR GYFAWSLMDN FEWAEGYRMR 

       430        440        450 
FGLVHVDYQT QVRTVKNSGK WYSALASGFP KGNHGVAKG 

« Hide

References

[1]"Structure and transcription analysis of the gene encoding a cellobiase from Agrobacterium sp. strain ATCC 21400."
Wakarchuk W.W., Greenberg N.M., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
J. Bacteriol. 170:301-307(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a 'retaining' glycosidase."
Withers S.G., Warren R.A.J., Street I.P., Rupitz K., Kempton J.B., Aebersold R.
J. Am. Chem. Soc. 112:5887-5889(1990)
Cited for: ACTIVE SITE GLU-359.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19033 Genomic DNA. Translation: AAA22085.1.
PIRGLAG. A28673.

3D structure databases

ProteinModelPortalP12614.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL1075038.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR017736. Glyco_hydro_1_beta-glucosidase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10353. PTHR10353. 1 hit.
PfamPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
SUPFAMSSF51445. SSF51445. 1 hit.
TIGRFAMsTIGR03356. BGL. 1 hit.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGLS_AGRSA
AccessionPrimary (citable) accession number: P12614
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: December 11, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries