ID Q8DU50_STRMU Unreviewed; 478 AA.
AC Q8DU50;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:AAN58797.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:AAN58797.1};
GN Name=ascB {ECO:0000313|EMBL:AAN58797.1};
GN OrderedLocusNames=SMU_1102 {ECO:0000313|EMBL:AAN58797.1};
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN58797.1, ECO:0000313|Proteomes:UP000002512};
RN [1] {ECO:0000313|EMBL:AAN58797.1, ECO:0000313|Proteomes:UP000002512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR EMBL; AE014133; AAN58797.1; -; Genomic_DNA.
DR RefSeq; NP_721491.1; NC_004350.2.
DR RefSeq; WP_002262239.1; NC_004350.2.
DR AlphaFoldDB; Q8DU50; -.
DR STRING; 210007.SMU_1102; -.
DR KEGG; smu:SMU_1102; -.
DR PATRIC; fig|210007.7.peg.986; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_0_2_9; -.
DR OrthoDB; 1637462at2; -.
DR PhylomeDB; Q8DU50; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU004468};
KW Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:AAN58797.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002512}.
FT ACT_SITE 376
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 478 AA; 55110 MW; 2662777888970DBB CRC64;
MIKLKPFPQG FLWGGATAAN QCEGAYNVDG RGLANVDVVP IGEDRFPIIA GKKKMFDFEE
GYFYPAKDSI DMYHHFKEDI ALFGEMGFKT YRLSIAWTRI FPQGDELEPN EAGLQFYEDL
FKECHKYGIE PLVTITHFDC PMHLIEEYGG WRNRKMLEFY ERLCRTLFTR FKGLVKYWLT
FNEINMILHA PFMGAGLYFE EGENEEEVKY QSAHHELVAS AIATKLAHEI DAENQVGCML
AAGQYYPNTC NPNDYWKAMK EDRSNYFFID VQARGEYPNY AKKQFERDGL NIIMTQEDLQ
LLKENTVDFV SFSYYSSRVA SADPKINDET QGNIFASIKN PYLSSSEWGW QIDPLGLRIT
LNTIWDRYQK PMFIVENGLG AIDKPDKNGY VEDDYRIDYL REHIKAMNAA INEDGVQLLG
YTTWGCIDLV SAGTGEMKKR YGFIYVDRDN AGNGTLKRSK KKSFDWYKKV IASNGTDL
//
