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Q46829

- BGLA_ECOLI

UniProt

Q46829 - BGLA_ECOLI

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
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    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

    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 – 234
    Turni36 – 394
    Helixi62 – 654
    Helixi69 – 8315
    Beta strandi86 – 916
    Helixi94 – 974
    Beta strandi98 – 1014
    Helixi108 – 12316
    Beta strandi127 – 1359
    Helixi139 – 1446
    Helixi147 – 1493
    Helixi152 – 16716
    Turni168 – 1714
    Beta strandi174 – 1785
    Turni179 – 1824
    Helixi183 – 1853
    Helixi192 – 1976
    Helixi201 – 2033
    Beta strandi204 – 2063
    Helixi207 – 23226
    Beta strandi236 – 2438
    Beta strandi247 – 2526
    Helixi254 – 26310
    Helixi265 – 27612
    Helixi281 – 29010
    Helixi300 – 3067
    Beta strandi310 – 3156
    Beta strandi320 – 3223
    Beta strandi324 – 3263
    Helixi355 – 36915
    Beta strandi373 – 3775
    Helixi395 – 41319
    Beta strandi419 – 4224
    Beta strandi433 – 4353
    Beta strandi438 – 4414
    Beta strandi444 – 4474
    Beta strandi459 – 4613
    Helixi463 – 47311
    Turni474 – 4763

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XHYX-ray2.30A/B/C/D1-479[»]
    ProteinModelPortaliQ46829.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Phylogenomic databases

    eggNOGiCOG2723.
    HOGENOMiHOG000088631.
    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

    MIVKKLTLPK DFLWGGAVAA HQVEGGWNKG GKGPSICDVL TGGAHGVPRE    50
    ITKEVLPGKY YPNHEAVDFY GHYKEDIKLF AEMGFKCFRT SIAWTRIFPK 100
    GDEAQPNEEG LKFYDDMFDE LLKYNIEPVI TLSHFEMPLH LVQQYGSWTN 150
    RKVVDFFVRF AEVVFERYKH KVKYWMTFNE INNQRNWRAP LFGYCCSGVV 200
    YTEHENPEET MYQVLHHQFV ASALAVKAAR RINPEMKVGC MLAMVPLYPY 250
    SCNPDDVMFA QESMRERYVF TDVQLRGYYP SYVLNEWERR GFNIKMEDGD 300
    LDVLREGTCD YLGFSYYMTN AVKAEGGTGD AISGFEGSVP NPYVKASDWG 350
    WQIDPVGLRY ALCELYERYQ RPLFIVENGF GAYDKVEEDG SINDDYRIDY 400
    LRAHIEEMKK AVTYDGVDLM GYTPWGCIDC VSFTTGQYSK RYGFIYVNKH 450
    DDGTGDMSRS RKKSFNWYKE VIASNGEKL 479
    Length:479
    Mass (Da):55,361
    Last modified:November 1, 1997 - v2
    Checksum:iAA493EDAB0E95A56
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2XHY X-ray 2.30 A/B/C/D 1-479 [» ]
    ProteinModelPortali Q46829.
    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.
    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

    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: October 1, 2014
    This is version 109 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