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P38645 (BGLB_THEBI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 72. 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:
Thermostable beta-glucosidase B

EC=3.2.1.21
Alternative name(s):
Amygdalase
Beta-D-glucoside glucohydrolase
Cellobiase
Gentiobiase
Gene names
Name:bglB
OrganismThermobispora bispora (Microbispora bispora)
Taxonomic identifier2006 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeThermobispora

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
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.

Subcellular location

Cytoplasm.

Miscellaneous

Shows greater activity against cellobiose than against aryl-beta-D-glucosides.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Biophysicochemical properties

Temperature dependence:

Thermostable, retains about 70% of its activity at 60 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 473473Thermostable beta-glucosidase B
PRO_0000063878

Sites

Active site1961Proton donor Potential
Active site3781Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
P38645 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 8F2188F1C93007CA

FASTA47352,228
        10         20         30         40         50         60 
MTESAMTSRA GRGRGADLVA AVVQGHAAAS DAAGDLSFPD GFIWGAATAA YQIEGAWRED 

        70         80         90        100        110        120 
GRGLWDVFSH TPGKVASGHT GDIACDHYHR YADDVRLMAG LGDRVYRFSV AWPRIVPDGS 

       130        140        150        160        170        180 
GPVNPAGLDF YDRLVDELLG HGITPYPTLY HWDLPQTLED RGGWAARDTA YRFAEYALAV 

       190        200        210        220        230        240 
HRRLGDRVRC WITLNEPWVA AFLATHRGAP GAADVPRFRA VHHLLLGHGL GLRLRSAGAG 

       250        260        270        280        290        300 
QLGLTLSLSP VIEARPGVRG GGRRVDALAN RQFLDPALRG RYPEEVLKIM AGHARLGHPG 

       310        320        330        340        350        360 
RDLETIHQPV DLLGVNYYSH VRLAAEGEPA NRLPGSEGIR FERPTAVTAW PGDRPDGLRT 

       370        380        390        400        410        420 
LLLRLSRDYP GVGLIITENG AAFDDRADGD RVHDPERIRY LTATLRAVHD AIMAGADLRG 

       430        440        450        460        470 
YFVWSVLDNF EWAYGYHKRG IVYVDYTTMR RIPRESALWY RDVVRRNGLR NGE 

« Hide

References

[1]"Cloning, characterization, and nucleotide sequence of a gene encoding Microbispora bispora BglB, a thermostable beta-glucosidase expressed in Escherichia coli."
Wright R.M., Yablonsky M.D., Shalita Z.P., Goyal A.K., Eveleigh D.E.
Appl. Environ. Microbiol. 58:3455-3465(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NRRL 15568.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97265 Genomic DNA. Translation: AAA25311.1.
PIRA48949.

3D structure databases

ProteinModelPortalP38645.
SMRP38645. Positions 40-467.
ModBaseSearch...
MobiDBSearch...

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 nameBGLB_THEBI
AccessionPrimary (citable) accession number: P38645
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 16, 2013
This is version 72 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