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BGLA_ECOLI
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   03-AUG-2022, entry version 152.
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; Proteobacteria; 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_JACEFS010000009.1.
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; Q46829; -.
DR   PRIDE; Q46829; -.
DR   EnsemblBacteria; AAC75939; AAC75939; b2901.
DR   EnsemblBacteria; BAE76966; BAE76966; BAE76966.
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; VEACDRK; -.
DR   PhylomeDB; Q46829; -.
DR   BioCyc; EcoCyc:G495-MON; -.
DR   BioCyc; MetaCyc:G495-MON; -.
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   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; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 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
 
 
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