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P22073 (BGLA_PAEPO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 87. 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 A

Short name=BGA
EC=3.2.1.21
Alternative name(s):
Amygdalase
Beta-D-glucoside glucohydrolase
Cellobiase
Gentiobiase
Gene names
Name:bglA
OrganismPaenibacillus polymyxa (Bacillus polymyxa)
Taxonomic identifier1406 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

BglA is intracellular and cleaves cellobiose probably through inorganic phosphate mediated hydrolysis.

Catalytic activity

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

Subunit structure

Homooctamer.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
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 – 448448Beta-glucosidase A
PRO_0000063871

Sites

Active site1661Proton donor Potential
Active site3521Nucleophile By similarity

Secondary structure

.................................................................................. 448
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22073 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: D971D2E61B6627C1

FASTA44851,649
        10         20         30         40         50         60 
MTIFQFPQDF MWGTATAAYQ IEGAYQEDGR GLSIWDTFAH TPGKVFNGDN GNVACDSYHR 

        70         80         90        100        110        120 
YEEDIRLMKE LGIRTYRFSV SWPRIFPNGD GEVNQEGLDY YHRVVDLLND NGIEPFCTLY 

       130        140        150        160        170        180 
HWDLPQALQD AGGWGNRRTI QAFVQFAETM FREFHGKIQH WLTFNEPWCI AFLSNMLGVH 

       190        200        210        220        230        240 
APGLTNLQTA IDVGHHLLVA HGLSVRRFRE LGTSGQIGIA PNVSWAVPYS TSEEDKAACA 

       250        260        270        280        290        300 
RTISLHSDWF LQPIYQGSYP QFLVDWFAEQ GATVPIQDGD MDIIGEPIDM IGINYYSMSV 

       310        320        330        340        350        360 
NRFNPEAGFL QSEEINMGLP VTDIGWPVES RGLYEVLHYL QKYGNIDIYI TENGACINDE 

       370        380        390        400        410        420 
VVNGKVQDDR RISYMQQHLV QVHRTIHDGL HVKGYMAWSL LDNFEWAEGY NMRFGMIHVD 

       430        440 
FRTQVRTPKE SYYWYRNVVS NNWLETRR 

« Hide

References

[1]"Sequences and homology analysis of two genes encoding beta-glucosidases from Bacillus polymyxa."
Gonzalez-Candelas L., Ramon D., Polaina J.
Gene 95:31-38(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Crystal structure of beta-glucosidase A from Bacillus polymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases."
Sanz-Aparicio J., Hermoso J.A., Martinez-Ripoll M., Lequerica J.L., Polaina J.
J. Mol. Biol. 275:491-502(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Strain: ATCC 842 / DSM 36 / JCM 2507 / NBRC 15309 / NCIMB 8158 / NCTC 10343 / NRRL B-4317 / VKM B-514.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60210 Genomic DNA. Translation: AAA22263.1.
PIRJW0037.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BGAX-ray2.40A/B/C/D2-448[»]
1BGGX-ray2.30A/B/C/D1-448[»]
1E4IX-ray2.00A2-448[»]
1TR1X-ray2.20A/B/C/D2-448[»]
1UYQX-ray2.20A2-448[»]
ProteinModelPortalP22073.
SMRP22073. Positions 2-448.
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...

Other

EvolutionaryTraceP22073.

Entry information

Entry nameBGLA_PAEPO
AccessionPrimary (citable) accession number: P22073
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: October 16, 2013
This is version 87 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries