ID BGLA_ECOLI Reviewed; 479 AA.
AC Q46829; Q2M9U0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 27-MAR-2024, entry version 159.
DE RecName: Full=6-phospho-beta-glucosidase BglA;
DE EC=3.2.1.86;
DE AltName: Full=Phospho-beta-glucosidase A;
GN Name=bglA; Synonyms=bglD, yqfC; OrderedLocusNames=b2901, JW2869;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION AS A GLUCOSIDASE, SUBSTRATE SPECIFICITY, AND INDUCTION.
RX PubMed=4576407; DOI=10.1128/jb.114.3.909-915.1973;
RA Prasad I., Young B., Schaefler S.;
RT "Genetic determination of the constitutive biosynthesis of phospho-
RT glucosidase A in Escherichia coli K-12.";
RL J. Bacteriol. 114:909-915(1973).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SUBUNIT.
RX PubMed=22393408; DOI=10.1371/journal.pone.0032498;
RA Totir M., Echols N., Nanao M., Gee C.L., Moskaleva A., Gradia S.,
RA Iavarone A.T., Berger J.M., May A.P., Zubieta C., Alber T.;
RT "Macro-to-micro structural proteomics: native source proteins for high-
RT throughput crystallization.";
RL PLoS ONE 7:E32498-E32498(2012).
CC -!- FUNCTION: Catalyzes the hydrolysis of phosphorylated beta-glucosides
CC into glucose-6-phosphate (G-6-P) and aglycone. It has a high affinity
CC for phosphorylated aromatic beta-glucosides (p-nitrophenyl-beta-
CC glucoside, phenyl beta-glucoside, arbutin), with the exception of
CC phosphorylated salicin, and a low affinity for phosphorylated beta-
CC methyl-glucoside. Apparently, it has only a very limited role in the
CC utilization of external beta-glucosides. {ECO:0000269|PubMed:4576407}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose +
CC D-glucose 6-phosphate; Xref=Rhea:RHEA:10772, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58312, ChEBI:CHEBI:61548; EC=3.2.1.86;
CC -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:22393408}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:4576407}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; U28375; AAA83082.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75939.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76966.1; -; Genomic_DNA.
DR PIR; E65074; E65074.
DR RefSeq; NP_417377.1; NC_000913.3.
DR RefSeq; WP_001295376.1; NZ_JACEFQ010000008.1.
DR PDB; 2XHY; X-ray; 2.30 A; A/B/C/D=1-479.
DR PDBsum; 2XHY; -.
DR AlphaFoldDB; Q46829; -.
DR SMR; Q46829; -.
DR BioGRID; 4263280; 25.
DR DIP; DIP-9213N; -.
DR IntAct; Q46829; 5.
DR STRING; 511145.b2901; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR jPOST; Q46829; -.
DR PaxDb; 511145-b2901; -.
DR EnsemblBacteria; AAC75939; AAC75939; b2901.
DR GeneID; 947378; -.
DR KEGG; ecj:JW2869; -.
DR KEGG; eco:b2901; -.
DR PATRIC; fig|511145.12.peg.2996; -.
DR EchoBASE; EB2889; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_0_2_6; -.
DR InParanoid; Q46829; -.
DR OMA; HGSNDFY; -.
DR PhylomeDB; Q46829; -.
DR BioCyc; EcoCyc:G495-MONOMER; -.
DR BioCyc; MetaCyc:G495-MONOMER; -.
DR BRENDA; 3.2.1.86; 2026.
DR PRO; PR:Q46829; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0015926; F:glucosidase activity; IDA:EcoCyc.
DR GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353:SF348; 6-PHOSPHO-BETA-GLUCOSIDASE ASCB-RELATED; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..479
FT /note="6-phospho-beta-glucosidase BglA"
FT /id="PRO_0000063897"
FT ACT_SITE 180
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 377
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:2XHY"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 69..83
FT /evidence="ECO:0007829|PDB:2XHY"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:2XHY"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 108..123
FT /evidence="ECO:0007829|PDB:2XHY"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 152..167
FT /evidence="ECO:0007829|PDB:2XHY"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:2XHY"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:2XHY"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:2XHY"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 207..232
FT /evidence="ECO:0007829|PDB:2XHY"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:2XHY"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 265..276
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 281..290
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 300..306
FT /evidence="ECO:0007829|PDB:2XHY"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:2XHY"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:2XHY"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 355..369
FT /evidence="ECO:0007829|PDB:2XHY"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 395..413
FT /evidence="ECO:0007829|PDB:2XHY"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:2XHY"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:2XHY"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:2XHY"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:2XHY"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:2XHY"
FT HELIX 463..473
FT /evidence="ECO:0007829|PDB:2XHY"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:2XHY"
SQ SEQUENCE 479 AA; 55361 MW; AA493EDAB0E95A56 CRC64;
MIVKKLTLPK DFLWGGAVAA HQVEGGWNKG GKGPSICDVL TGGAHGVPRE ITKEVLPGKY
YPNHEAVDFY GHYKEDIKLF AEMGFKCFRT SIAWTRIFPK GDEAQPNEEG LKFYDDMFDE
LLKYNIEPVI TLSHFEMPLH LVQQYGSWTN RKVVDFFVRF AEVVFERYKH KVKYWMTFNE
INNQRNWRAP LFGYCCSGVV YTEHENPEET MYQVLHHQFV ASALAVKAAR RINPEMKVGC
MLAMVPLYPY SCNPDDVMFA QESMRERYVF TDVQLRGYYP SYVLNEWERR GFNIKMEDGD
LDVLREGTCD YLGFSYYMTN AVKAEGGTGD AISGFEGSVP NPYVKASDWG WQIDPVGLRY
ALCELYERYQ RPLFIVENGF GAYDKVEEDG SINDDYRIDY LRAHIEEMKK AVTYDGVDLM
GYTPWGCIDC VSFTTGQYSK RYGFIYVNKH DDGTGDMSRS RKKSFNWYKE VIASNGEKL
//
