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Database: UniProt
Entry: A0A0G1X953_9BACT
LinkDB: A0A0G1X953_9BACT
Original site: A0A0G1X953_9BACT 
ID   A0A0G1X953_9BACT        Unreviewed;       406 AA.
AC   A0A0G1X953;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:KKW27703.1};
GN   ORFNames=UY71_C0039G0008 {ECO:0000313|EMBL:KKW27703.1};
OS   Parcubacteria group bacterium GW2011_GWB1_52_7.
OC   Bacteria.
OX   NCBI_TaxID=1618885 {ECO:0000313|EMBL:KKW27703.1, ECO:0000313|Proteomes:UP000034383};
RN   [1] {ECO:0000313|EMBL:KKW27703.1, ECO:0000313|Proteomes:UP000034383}
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:KKW27703.1}.
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DR   EMBL; LCRC01000039; KKW27703.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1X953; -.
DR   PATRIC; fig|1618885.3.peg.766; -.
DR   Proteomes; UP000034383; 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; 2.
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        320
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   406 AA;  48778 MW;  2FFE5C2F8A16AF66 CRC64;
     MRFEFPKKFL WGAATSAHQV EGGNHNDWTE WEKSPKRIAD LKRRGLNPEE YISGKAADHY
     HRFREDFDIA RSLGHNAHRF SIEWSRVEPE EGKFNEKEIE HYREVIKALR ERGMEPFVTL
     WHWTLPIWFA QKGGWLHKDA EKDFIRFVSK VVSELKLEVH YWITGNELET YARHGYFLGD
     RPPNRRNFIF SYLVLRKLLK AHKAAYKEIK RIASEAEVGF TESVVYFEPF NQWPHNLLLL
     RLVKWWRNNL FFEEFAASSD FIGLQHYFHS RIRLSPKSNW WIQFNENKKV SDFGWEIYPE
     GIYRVLKELG RYNKPIYITE NGLADAKDRY RADYIRDHIA CMGRALDEGV DVRGYFYWSL
     LDNFEWQEGY WPRFGLVEVN YKTLERKIRP SALEYKKIIA MNSIEL
//
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