ID   A0A0G1W747_9BACT        Unreviewed;       381 AA.
AC   A0A0G1W747;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Beta-glucosidase A {ECO:0000313|EMBL:KKU86173.1};
GN   ORFNames=UY15_C0014G0015 {ECO:0000313|EMBL:KKU86173.1};
OS   Parcubacteria group bacterium GW2011_GWA2_47_9.
OC   Bacteria.
OX   NCBI_TaxID=1618849 {ECO:0000313|EMBL:KKU86173.1, ECO:0000313|Proteomes:UP000034427};
RN   [1] {ECO:0000313|EMBL:KKU86173.1, ECO:0000313|Proteomes:UP000034427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00000448};
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:KKU86173.1}.
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DR   EMBL; LCOX01000014; KKU86173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1W747; -.
DR   PATRIC; fig|1618849.3.peg.432; -.
DR   Proteomes; UP000034427; 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; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 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|RuleBase:RU004468};
KW   Hydrolase {ECO:0000256|RuleBase:RU004468}.
FT   ACT_SITE        295
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   381 AA;  45402 MW;  44945780A94FB986 CRC64;
     MKFPPGFLWG SATSAYQVEG GIENSDWSKG YRAGLACDHY NRYEEDFDLL QKLNQNGYRF
     SIEWSRVEPE SGLFDEQELE HYRRILFSLR RRNIQTFVTL HHFTSPDWFA KAGGWTNAKA
     PYYFSRFAER LLEEYKGLVD FWITINEPMI YAAKGYLDGT WLPRKKNPIL FLKVLHNQTL
     AHKKIYELFH KKAEVRVGIA KNNQFFESYN RKSFLDRAVV KLADYFMNRW FLNRIAGHLD
     FIGLNYYFHQ KIAFPWGTRN ENKKISDIGW EVYPEGIYHV LSGLKKYQKT VYVTENGVAD
     NRDLLRRDFI RGHLYWIHKA IQGGVDVRGY LHWSLIDNFE WEKGFEPRFG LVEVDYKTLE
     RKIRPSAYYY SEICRNNGFE H
//