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Database: UniProt
Entry: A0A1E5GVK6_9ENTE
LinkDB: A0A1E5GVK6_9ENTE
Original site: A0A1E5GVK6_9ENTE 
ID   A0A1E5GVK6_9ENTE        Unreviewed;       463 AA.
AC   A0A1E5GVK6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:OEG16733.1};
GN   ORFNames=BCR25_03800 {ECO:0000313|EMBL:OEG16733.1};
OS   Enterococcus termitis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=332950 {ECO:0000313|EMBL:OEG16733.1, ECO:0000313|Proteomes:UP000095094};
RN   [1] {ECO:0000313|EMBL:OEG16733.1, ECO:0000313|Proteomes:UP000095094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 8895 {ECO:0000313|EMBL:OEG16733.1,
RC   ECO:0000313|Proteomes:UP000095094};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OEG16733.1}.
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DR   EMBL; MIJY01000012; OEG16733.1; -; Genomic_DNA.
DR   RefSeq; WP_069663130.1; NZ_MIJY01000012.1.
DR   AlphaFoldDB; A0A1E5GVK6; -.
DR   PATRIC; fig|332950.4.peg.1546; -.
DR   OrthoDB; 9765195at2; -.
DR   Proteomes; UP000095094; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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:SF136; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLC; 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}.
FT   ACT_SITE        363
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   463 AA;  53947 MW;  E099BDC5CD96EE82 CRC64;
     MTHTFPENFL WGASISAHQT EGAYNAEGKG LSVQDTRQRD NHDIADFTVA VDHYHRYKED
     IRLLAEMGIK VFRFSIAWTR IFPNGRGKVN DLGIQHYSDV IDELLKYDIQ PYITLNHFDL
     PQALEDEGGW GVRTTVDAFV HYAETVFKAY GDRVKHWLTI NEPNIMLLVD KKILGKEIPL
     REKYQQFHHL MISEKYAFKR CHELIEGGKI GPVPNISLVY PATSKPLDNQ AALYFNSVRN
     WAYLDFSCFG RYNTVFKDYL NRNDVSITFA SEDQELMEKH FPDFVAMNFY TTVTVEKPTE
     RDGMANGISD QQSEDIMEWG FYKGFTNPFL KKNQFNWTID PDGLKTTLQT LYDRYHLPII
     ITENGLGAKD ELTEDGKIHD DYRIDYLEQH IDQCRQAIEA GVDLIGYSPW SAIDLISVHE
     GISKRYGFIY VDRNEHDEKE MHRYKKDSFY WYQSLIKANQ LPS
//
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