ASCB_ECOLI
ID ASCB_ECOLI Reviewed; 474 AA.
AC P24240; P78104; Q2MAB3; Q59375;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=6-phospho-beta-glucosidase AscB;
DE EC=3.2.1.86;
GN Name=ascB; OrderedLocusNames=b2716, JW2686;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630307; DOI=10.1093/oxfordjournals.molbev.a040753;
RA Hall B.G., Xu L.;
RT "Nucleotide sequence, function, activation, and evolution of the cryptic
RT asc operon of Escherichia coli K12.";
RL Mol. Biol. Evol. 9:688-706(1992).
RN [2]
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 [3]
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).
CC -!- FUNCTION: Can hydrolyze salicin, cellobiose, and probably arbutin.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69226.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M73326; AAA16430.1; -; Unassigned_DNA.
DR EMBL; U29579; AAA69226.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75758.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76793.1; -; Genomic_DNA.
DR PIR; H65051; H65051.
DR RefSeq; NP_417196.1; NC_000913.3.
DR RefSeq; WP_000110363.1; NZ_STEB01000027.1.
DR AlphaFoldDB; P24240; -.
DR SMR; P24240; -.
DR BioGRID; 4259428; 18.
DR IntAct; P24240; 5.
DR STRING; 511145.b2716; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; P24240; -.
DR PRIDE; P24240; -.
DR EnsemblBacteria; AAC75758; AAC75758; b2716.
DR EnsemblBacteria; BAE76793; BAE76793; BAE76793.
DR GeneID; 947460; -.
DR KEGG; ecj:JW2686; -.
DR KEGG; eco:b2716; -.
DR PATRIC; fig|1411691.4.peg.4025; -.
DR EchoBASE; EB0083; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_0_2_6; -.
DR InParanoid; P24240; -.
DR OMA; FEEGYFY; -.
DR PhylomeDB; P24240; -.
DR BioCyc; EcoCyc:EG10085-MON; -.
DR BioCyc; MetaCyc:EG10085-MON; -.
DR PRO; PR:P24240; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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: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 GO; GO:2000892; P:cellobiose catabolic process; IMP:EcoCyc.
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 3: Inferred from homology;
KW Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..474
FT /note="6-phospho-beta-glucosidase AscB"
FT /id="PRO_0000063895"
FT ACT_SITE 180
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 372
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT CONFLICT 405..406
FT /note="EA -> GT (in Ref. 1; AAA16430)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="S -> C (in Ref. 1; AAA16430)"
FT /evidence="ECO:0000305"
FT CONFLICT 455..456
FT /note="RK -> HR (in Ref. 1; AAA16430)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 53935 MW; 02ACE6BEBF211011 CRC64;
MSVFPESFLW GGALAANQSE GAFREGDKGL TTVDMIPHGE HRMAVKLGLE KRFQLRDDEF
YPSHEATDFY HRYKEDIALM AEMGFKVFRT SIAWSRLFPQ GDEITPNQQG IAFYRSVFEE
CKKYGIEPLV TLCHFDVPMH LVTEYGSWRN RKLVEFFSRY ARTCFEAFDG LVKYWLTFNE
INIMLHSPFS GAGLVFEEGE NQDQVKYQAA HHQLVASALA TKIAHEVNPQ NQVGCMLAGG
NFYPYSCKPE DVWAALEKDR ENLFFIDVQA RGTYPAYSAR VFREKGVTIN KAPGDDEILK
NTVDFVSFSY YASRCASAEM NANNSSAANV VKSLRNPYLQ VSDWGWGIDP LGLRITMNMM
YDRYQKPLFL VENGLGAKDE FAANGEINDD YRISYLREHI RAMGEAIADG IPLMGYTTWG
CIDLVSASTG EMSKRYGFVF VDRDDAGNGT LTRTRKKSFW WYKKVIASNG EDLE
