Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q46829 (BGLA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
6-phospho-beta-glucosidase BglA
EC=3.2.1.86
Alternative name(s):
Phospho-beta-glucosidase A
Gene names
Name:bglA
Synonyms:bglD, yqfC
Ordered Locus Names:b2901, JW2869
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolysis of phosphorylated beta-glucosides into glucose-6-phosphate (G-6-P) and aglycone. It has a high affinity for phosphorylated aromatic beta-glucosides (p-nitrophenyl-beta-glucoside, phenyl beta-glucoside, arbutin), with the exception of phosphorylated salicin, and a low affinity for phosphorylated beta-methyl-glucoside. Apparently, it has only a very limited role in the utilization of external beta-glucosides. Ref.3

Catalytic activity

6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate.

Subunit structure

Homotetramer Probable. Ref.4

Induction

Constituvely expressed. Ref.3

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Ontologies

Keywords
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_function6-phospho-beta-glucosidase activity

Inferred from direct assay Ref.3. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4794796-phospho-beta-glucosidase BglA
PRO_0000063897

Sites

Active site1801Proton donor Potential
Active site3771Nucleophile By similarity

Secondary structure

1 ........................................................................ 479
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q46829 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: AA493EDAB0E95A56

FASTA47955,361
        10         20         30         40         50         60 
MIVKKLTLPK DFLWGGAVAA HQVEGGWNKG GKGPSICDVL TGGAHGVPRE ITKEVLPGKY 

        70         80         90        100        110        120 
YPNHEAVDFY GHYKEDIKLF AEMGFKCFRT SIAWTRIFPK GDEAQPNEEG LKFYDDMFDE 

       130        140        150        160        170        180 
LLKYNIEPVI TLSHFEMPLH LVQQYGSWTN RKVVDFFVRF AEVVFERYKH KVKYWMTFNE 

       190        200        210        220        230        240 
INNQRNWRAP LFGYCCSGVV YTEHENPEET MYQVLHHQFV ASALAVKAAR RINPEMKVGC 

       250        260        270        280        290        300 
MLAMVPLYPY SCNPDDVMFA QESMRERYVF TDVQLRGYYP SYVLNEWERR GFNIKMEDGD 

       310        320        330        340        350        360 
LDVLREGTCD YLGFSYYMTN AVKAEGGTGD AISGFEGSVP NPYVKASDWG WQIDPVGLRY 

       370        380        390        400        410        420 
ALCELYERYQ RPLFIVENGF GAYDKVEEDG SINDDYRIDY LRAHIEEMKK AVTYDGVDLM 

       430        440        450        460        470 
GYTPWGCIDC VSFTTGQYSK RYGFIYVNKH DDGTGDMSRS RKKSFNWYKE VIASNGEKL

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Genetic determination of the constitutive biosynthesis of phospho--glucosidase A in Escherichia coli K-12."
Prasad I., Young B., Schaefler S.
J. Bacteriol. 114:909-915(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A GLUCOSIDASE, SUBSTRATE SPECIFICITY, INDUCTION.
[4]"Macro-to-micro structural proteomics: native source proteins for high-throughput crystallization."
Totir M., Echols N., Nanao M., Gee C.L., Moskaleva A., Gradia S., Iavarone A.T., Berger J.M., May A.P., Zubieta C., Alber T.
PLoS ONE 7:E32498-E32498(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U28375 Genomic DNA. Translation: AAA83082.1.
U00096 Genomic DNA. Translation: AAC75939.1.
AP009048 Genomic DNA. Translation: BAE76966.1.
PIRE65074.
RefSeqNP_417377.1. NC_000913.2.
YP_491102.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XHYX-ray2.30A/B/C/D1-479[»]
ProteinModelPortalQ46829.
SMRQ46829. Positions 4-479.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9213N.
IntActQ46829. 5 interactions.
MINTMINT-1322539.
STRING511145.b2901.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbQ46829.
PRIDEQ46829.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75939; AAC75939; b2901.
BAE76966; BAE76966; BAE76966.
GeneID12934286.
947378.
KEGGecj:Y75_p2833.
eco:b2901.
PATRIC32121216. VBIEscCol129921_2996.

Organism-specific databases

EchoBASEEB2889.
EcoGeneEG13079. bglA.

Phylogenomic databases

eggNOGCOG2723.
HOGENOMHOG000088631.
KOK01223.
OMANTTWRSK.
ProtClustDBPRK15014.

Enzyme and pathway databases

BioCycEcoCyc:G495-MONOMER.
ECOL316407:JW2869-MONOMER.
MetaCyc:G495-MONOMER.

Gene expression databases

GenevestigatorQ46829.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
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. Glyco_hydro_cat. 1 hit.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGLA_ECOLI
AccessionPrimary (citable) accession number: Q46829
Secondary accession number(s): Q2M9U0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents