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Q46829

- BGLA_ECOLI

UniProt

Q46829 - BGLA_ECOLI

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Protein

6-phospho-beta-glucosidase BglA

Gene

bglA

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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. single-organism carbohydrate catabolic process Source: EcoCyc
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: Chromosome, UP000000625: 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.
OMAiREGCADY.
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 .
PIRi E65074.
RefSeqi NP_417377.1. NC_000913.3.
YP_491102.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XHY X-ray 2.30 A/B/C/D 1-479 [» ]
ProteinModelPortali Q46829.
SMRi Q46829. Positions 4-479.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9213N.
IntActi Q46829. 5 interactions.
MINTi MINT-1322539.
STRINGi 511145.b2901.

Protein family/group databases

CAZyi GH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbi Q46829.
PRIDEi Q46829.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75939 ; AAC75939 ; b2901 .
BAE76966 ; BAE76966 ; BAE76966 .
GeneIDi 12934286.
947378.
KEGGi ecj:Y75_p2833.
eco:b2901.
PATRICi 32121216. VBIEscCol129921_2996.

Organism-specific databases

EchoBASEi EB2889.
EcoGenei EG13079. bglA.

Phylogenomic databases

eggNOGi COG2723.
HOGENOMi HOG000088631.
InParanoidi Q46829.
KOi K01223.
OMAi REGCADY.
OrthoDBi EOG6F81PM.
PhylomeDBi Q46829.

Enzyme and pathway databases

BioCyci EcoCyc:G495-MONOMER.
ECOL316407:JW2869-MONOMER.
MetaCyc:G495-MONOMER.

Miscellaneous databases

PROi Q46829.

Gene expression databases

Genevestigatori Q46829.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR10353. PTHR10353. 1 hit.
Pfami PF00232. Glyco_hydro_1. 1 hit.
[Graphical view ]
PRINTSi PR00131. GLHYDRLASE1.
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 111 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