ID E9DKW6_9STRE Unreviewed; 479 AA.
AC E9DKW6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:EFX55675.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:EFX55675.1};
GN ORFNames=HMPREF0848_01272 {ECO:0000313|EMBL:EFX55675.1};
OS Streptococcus sp. C150.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=435842 {ECO:0000313|EMBL:EFX55675.1, ECO:0000313|Proteomes:UP000005993};
RN [1] {ECO:0000313|EMBL:EFX55675.1, ECO:0000313|Proteomes:UP000005993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C150 {ECO:0000313|EMBL:EFX55675.1,
RC ECO:0000313|Proteomes:UP000005993};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S., Surette M.G.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptococcus sp. C150.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR EMBL; GL698449; EFX55675.1; -; Genomic_DNA.
DR RefSeq; WP_008535420.1; NZ_GL698449.1.
DR AlphaFoldDB; E9DKW6; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_0_2_9; -.
DR Proteomes; UP000005993; Unassembled WGS sequence.
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:EFX55675.1}.
FT ACT_SITE 376
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 479 AA; 54877 MW; 340CF5A407E73F7F CRC64;
MTKKLTFPDG FLWGGATAAN QCEGAYDADG RGLANVDVVP IGKDRLSIIT GHRKMFDFED
GYFYPAKESI DMYHRYKEDI ALFGEMGFKT YRLSIAWSRI FPKGDEAEPN EAGLAFYEDL
FKECHKYGIE PLVTITHFDC PMHLITEYGG WRNRKMLGFY ENLCRTLFTR YKGLVKYWLT
FNEINMILHA PFMGAGLCFE EGENEEQVKY QAAHHELVAS AMATKLAHEI DPDNKVGCML
AAGQYYPNTA HPRDYWSAMQ EDRSSYFFID VQARGEYPNY AKKQWERDGI ELEMTEEDLT
LLKEHTVDFI SFSYYASRVA SGDPEVNEKT AGNIFASIKN PYLEASEWGW QIDPLGLRIT
LNAIWDRYQK PMFIVENGLG AVDRPDENGY VEDDYRIDYL AAHIKAMRDA INEDGVVLWG
YTTWGCIDLV SAGTGEMKKR YGFIYVDRDN DGNGSLKRSK KKSFNWYKEV IASNGASVE
//
