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Q03506 (BGLA_BACCI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:bglA
OrganismBacillus circulans
Taxonomic identifier1397 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct 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

Initiator methionine11Removed Ref.1
Chain2 – 450449Beta-glucosidase
PRO_0000063870

Sites

Active site1661Proton donor Potential
Active site3551Nucleophile By similarity

Secondary structure

............................................................................. 450
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q03506 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C52C1DB233B72790

FASTA45051,303
        10         20         30         40         50         60 
MSIHMFPSDF KWGVATAAYQ IEGAYNEDGR GMSIWDTFAH TPGKVKNGDN GNVACDSYHR 

        70         80         90        100        110        120 
VEEDVQLLKD LGVKVYRFSI SWPRVLPQGT GEVNRAGLDY YHRLVDELLA NGIEPFCTLY 

       130        140        150        160        170        180 
HWDLPQALQD QGGWGSRITI DAFAEYAELM FKELGGKIKQ WITFNEPWCM AFLSNYLGVH 

       190        200        210        220        230        240 
APGNKDLQLA IDVSHHLLVA HGRAVTLFRE LGISGEIGIA PNTSWAVPYR RTKEDMEACL 

       250        260        270        280        290        300 
RVNGWSGDWY LDPIYFGEYP KFMLDWYENL GYKPPIVDGD MELIHQPIDF IGINYYTSSM 

       310        320        330        340        350        360 
NRYNPGEAGG MLSSEAISMG APKTDIGWEI YAEGLYDLLR YTADKYGNPT LYITENGACY 

       370        380        390        400        410        420 
NDGLSLDGRI HDQRRIDYLA MHLIQASRAI EDGINLKGYM EWSLMDNFEW AEGYGMRFGL 

       430        440        450 
VHVDYDTLVR TPKDSFYWYK GVISRGWLDL 

« Hide

References

[1]"Purification, characterization, gene cloning, and sequencing of a new beta-glucosidase from Bacillus circulans subsp. alkalophilus."
Paavilainen S.K., Hellman J., Korpela T.
Appl. Environ. Microbiol. 59:927-932(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-29.
Strain: ATCC 21783 / subsp. Alkalophilus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96979 Genomic DNA. Translation: AAA22266.1.
PIRA48969.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QOXX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P2-450[»]
ProteinModelPortalQ03506.
SMRQ03506. Positions 2-450.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-8328760.

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...

Other

EvolutionaryTraceQ03506.

Entry information

Entry nameBGLA_BACCI
AccessionPrimary (citable) accession number: Q03506
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 84 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries