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Protein

6-phospho-beta-glucosidase BglA

Gene

bglA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei180 – 1801Proton donorSequence Analysis
Active sitei377 – 3771NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  1. 6-phospho-beta-glucosidase activity Source: UniProtKB-EC
  2. glucosidase activity Source: EcoCyc

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

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

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phospho-beta-glucosidase BglA (EC:3.2.1.86)
Alternative name(s):
Phospho-beta-glucosidase A
Gene namesi
Name:bglA
Synonyms:bglD, yqfC
Ordered Locus Names:b2901, JW2869
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13079. bglA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4794796-phospho-beta-glucosidase BglAPRO_0000063897Add
BLAST

Proteomic databases

PaxDbiQ46829.
PRIDEiQ46829.

Expressioni

Inductioni

Constituvely expressed.1 Publication

Gene expression databases

GenevestigatoriQ46829.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

DIPiDIP-9213N.
IntActiQ46829. 5 interactions.
MINTiMINT-1322539.
STRINGi511145.b2901.

Structurei

Secondary structure

1
479
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 234Combined sources
Turni36 – 394Combined sources
Helixi62 – 654Combined sources
Helixi69 – 8315Combined sources
Beta strandi86 – 916Combined sources
Helixi94 – 974Combined sources
Beta strandi98 – 1014Combined sources
Helixi108 – 12316Combined sources
Beta strandi127 – 1359Combined sources
Helixi139 – 1446Combined sources
Helixi147 – 1493Combined sources
Helixi152 – 16716Combined sources
Turni168 – 1714Combined sources
Beta strandi174 – 1785Combined sources
Turni179 – 1824Combined sources
Helixi183 – 1853Combined sources
Helixi192 – 1976Combined sources
Helixi201 – 2033Combined sources
Beta strandi204 – 2063Combined sources
Helixi207 – 23226Combined sources
Beta strandi236 – 2438Combined sources
Beta strandi247 – 2526Combined sources
Helixi254 – 26310Combined sources
Helixi265 – 27612Combined sources
Helixi281 – 29010Combined sources
Helixi300 – 3067Combined sources
Beta strandi310 – 3156Combined sources
Beta strandi320 – 3223Combined sources
Beta strandi324 – 3263Combined sources
Helixi355 – 36915Combined sources
Beta strandi373 – 3775Combined sources
Helixi395 – 41319Combined sources
Beta strandi419 – 4224Combined sources
Beta strandi433 – 4353Combined sources
Beta strandi438 – 4414Combined sources
Beta strandi444 – 4474Combined sources
Beta strandi459 – 4613Combined sources
Helixi463 – 47311Combined sources
Turni474 – 4763Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XHYX-ray2.30A/B/C/D1-479[»]
ProteinModelPortaliQ46829.
SMRiQ46829. Positions 4-479.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.Curated

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088631.
InParanoidiQ46829.
KOiK01223.
OMAiFIHVNKN.
OrthoDBiEOG6F81PM.
PhylomeDBiQ46829.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q46829-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVKKLTLPK DFLWGGAVAA HQVEGGWNKG GKGPSICDVL TGGAHGVPRE
60 70 80 90 100
ITKEVLPGKY YPNHEAVDFY GHYKEDIKLF AEMGFKCFRT SIAWTRIFPK
110 120 130 140 150
GDEAQPNEEG LKFYDDMFDE LLKYNIEPVI TLSHFEMPLH LVQQYGSWTN
160 170 180 190 200
RKVVDFFVRF AEVVFERYKH KVKYWMTFNE INNQRNWRAP LFGYCCSGVV
210 220 230 240 250
YTEHENPEET MYQVLHHQFV ASALAVKAAR RINPEMKVGC MLAMVPLYPY
260 270 280 290 300
SCNPDDVMFA QESMRERYVF TDVQLRGYYP SYVLNEWERR GFNIKMEDGD
310 320 330 340 350
LDVLREGTCD YLGFSYYMTN AVKAEGGTGD AISGFEGSVP NPYVKASDWG
360 370 380 390 400
WQIDPVGLRY ALCELYERYQ RPLFIVENGF GAYDKVEEDG SINDDYRIDY
410 420 430 440 450
LRAHIEEMKK AVTYDGVDLM GYTPWGCIDC VSFTTGQYSK RYGFIYVNKH
460 470
DDGTGDMSRS RKKSFNWYKE VIASNGEKL
Length:479
Mass (Da):55,361
Last modified:November 1, 1997 - v2
Checksum:iAA493EDAB0E95A56
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28375 Genomic DNA. Translation: AAA83082.1.
U00096 Genomic DNA. Translation: AAC75939.1.
AP009048 Genomic DNA. Translation: BAE76966.1.
PIRiE65074.
RefSeqiNP_417377.1. NC_000913.3.
YP_491102.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75939; AAC75939; b2901.
BAE76966; BAE76966; BAE76966.
GeneIDi12934286.
947378.
KEGGiecj:Y75_p2833.
eco:b2901.
PATRICi32121216. VBIEscCol129921_2996.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28375 Genomic DNA. Translation: AAA83082.1.
U00096 Genomic DNA. Translation: AAC75939.1.
AP009048 Genomic DNA. Translation: BAE76966.1.
PIRiE65074.
RefSeqiNP_417377.1. NC_000913.3.
YP_491102.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XHYX-ray2.30A/B/C/D1-479[»]
ProteinModelPortaliQ46829.
SMRiQ46829. Positions 4-479.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9213N.
IntActiQ46829. 5 interactions.
MINTiMINT-1322539.
STRINGi511145.b2901.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbiQ46829.
PRIDEiQ46829.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75939; AAC75939; b2901.
BAE76966; BAE76966; BAE76966.
GeneIDi12934286.
947378.
KEGGiecj:Y75_p2833.
eco:b2901.
PATRICi32121216. VBIEscCol129921_2996.

Organism-specific databases

EchoBASEiEB2889.
EcoGeneiEG13079. bglA.

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088631.
InParanoidiQ46829.
KOiK01223.
OMAiFIHVNKN.
OrthoDBiEOG6F81PM.
PhylomeDBiQ46829.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ46829.

Gene expression databases

GenevestigatoriQ46829.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiBGLA_ECOLI
AccessioniPrimary (citable) accession number: Q46829
Secondary accession number(s): Q2M9U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 1, 2015
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.