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Protein

6-phospho-beta-glucosidase BglB

Gene

bglB

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 and phosphorylated salicin), and a low affinity for phosphorylated beta-methyl-glucoside.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 sitei172 – 1721Proton donorSequence Analysis
Active sitei361 – 3611NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciEcoCyc:EG10114-MONOMER.
ECOL316407:JW3699-MONOMER.
MetaCyc:EG10114-MONOMER.
SABIO-RKP11988.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phospho-beta-glucosidase BglB (EC:3.2.1.86)
Alternative name(s):
Phospho-beta-glucosidase B
Gene namesi
Name:bglB
Ordered Locus Names:b3721, JW3699
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10114. bglB.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4704706-phospho-beta-glucosidase BglBPRO_0000063898Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriP11988.

Interactioni

Protein-protein interaction databases

DIPiDIP-9214N.
IntActiP11988. 3 interactions.
STRINGi511145.b3721.

Structurei

3D structure databases

ProteinModelPortaliP11988.
SMRiP11988. Positions 4-462.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.Curated

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088631.
InParanoidiP11988.
KOiK01223.
OMAiSMVPNPH.
OrthoDBiEOG6F81PM.
PhylomeDBiP11988.

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.

P11988-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAFPETFLW GGATAANQVE GAWQEDGKGI STSDLQPHGV MGKMEPRILG
60 70 80 90 100
KENIKDVAID FYHRYPEDIA LFAEMGFTCL RISIAWARIF PQGDEVEPNE
110 120 130 140 150
AGLAFYDRLF DEMAQAGIKP LVTLSHYEMP YGLVKNYGGW ANRAVIDHFE
160 170 180 190 200
HYARTVFTRY QHKVALWLTF NEINMSLHAP FTGVGLAEES GEAEVYQAIH
210 220 230 240 250
HQLVASARAV KACHSLLPEA KIGNMLLGGL VYPLTCQPQD MLQAMEENRR
260 270 280 290 300
WMFFGDVQAR GQYPGYMQRF FRDHNITIEM TESDAEDLKH TVDFISFSYY
310 320 330 340 350
MTGCVSHDES INKNAQGNIL NMIPNPHLKS SEWGWQIDPV GLRVLLNTLW
360 370 380 390 400
DRYQKPLFIV ENGLGAKDSV EADGSIQDDY RIAYLNDHLV QVNEAIADGV
410 420 430 440 450
DIMGYTSWGP IDLVSASHSQ MSKRYGFIYV DRDDNGEGSL TRTRKKSFGW
460 470
YAEVIKTRGL SLKKITIKAP
Length:470
Mass (Da):53,161
Last modified:July 1, 1993 - v2
Checksum:i2B8422B20D7E5C98
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471D → G in AAA23511 (PubMed:3034860).Curated
Sequence conflicti449 – 4513GWY → RMVC in AAA23511 (PubMed:3034860).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16487 Genomic DNA. Translation: AAA23511.1.
L10328 Genomic DNA. Translation: AAA62072.1.
U00096 Genomic DNA. Translation: AAC76744.1.
AP009048 Genomic DNA. Translation: BAE77567.1.
M15746 Genomic DNA. Translation: AAA83838.1.
PIRiB65175.
RefSeqiNP_418177.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76744; AAC76744; b3721.
BAE77567; BAE77567; BAE77567.
GeneIDi948234.
KEGGiecj:Y75_p3447.
eco:b3721.
PATRICi32122937. VBIEscCol129921_3844.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16487 Genomic DNA. Translation: AAA23511.1.
L10328 Genomic DNA. Translation: AAA62072.1.
U00096 Genomic DNA. Translation: AAC76744.1.
AP009048 Genomic DNA. Translation: BAE77567.1.
M15746 Genomic DNA. Translation: AAA83838.1.
PIRiB65175.
RefSeqiNP_418177.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP11988.
SMRiP11988. Positions 4-462.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9214N.
IntActiP11988. 3 interactions.
STRINGi511145.b3721.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76744; AAC76744; b3721.
BAE77567; BAE77567; BAE77567.
GeneIDi948234.
KEGGiecj:Y75_p3447.
eco:b3721.
PATRICi32122937. VBIEscCol129921_3844.

Organism-specific databases

EchoBASEiEB0112.
EcoGeneiEG10114. bglB.

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088631.
InParanoidiP11988.
KOiK01223.
OMAiSMVPNPH.
OrthoDBiEOG6F81PM.
PhylomeDBiP11988.

Enzyme and pathway databases

BioCyciEcoCyc:EG10114-MONOMER.
ECOL316407:JW3699-MONOMER.
MetaCyc:EG10114-MONOMER.
SABIO-RKP11988.

Miscellaneous databases

PROiP11988.

Gene expression databases

GenevestigatoriP11988.

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. "Beta-glucoside (bgl) operon of Escherichia coli K-12: nucleotide sequence, genetic organization, and possible evolutionary relationship to regulatory components of two Bacillus subtilis genes."
    Schnetz K., Toloczyki C., Rak B.
    J. Bacteriol. 169:2579-2590(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CRYPTIC OPERON.
    Strain: K12.
  2. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
    Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
    Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Nucleotide sequence of bglC, the gene specifying enzymeIIbgl of the PEP:sugar phosphotransferase system in Escherichia coli K12, and overexpression of the gene product."
    Bramley H.F., Kornberg H.L.
    J. Gen. Microbiol. 133:563-573(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
    Strain: K12.
  6. "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.

Entry informationi

Entry nameiBGLB_ECOLI
AccessioniPrimary (citable) accession number: P11988
Secondary accession number(s): P78124, Q2M839
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 1, 1993
Last modified: May 27, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Part of the cryptic bglGFBH operon.

Keywords - Technical termi

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. 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.