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
//