ID A0A0G0G744_9BACT Unreviewed; 414 AA.
AC A0A0G0G744;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:KKQ21855.1};
GN ORFNames=US36_C0012G0014 {ECO:0000313|EMBL:KKQ21855.1};
OS Candidatus Wolfebacteria bacterium GW2011_GWC1_37_10.
OC Bacteria; Candidatus Wolfebacteria.
OX NCBI_TaxID=1619010 {ECO:0000313|EMBL:KKQ21855.1, ECO:0000313|Proteomes:UP000034044};
RN [1] {ECO:0000313|EMBL:KKQ21855.1, ECO:0000313|Proteomes:UP000034044}
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:KKQ21855.1}.
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DR EMBL; LBSR01000012; KKQ21855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0G744; -.
DR PATRIC; fig|1619010.3.peg.426; -.
DR Proteomes; UP000034044; 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; 2.
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 330
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 414 AA; 49315 MW; EF2DD230A634E3ED CRC64;
MKFQFPKGFY WGVATSAHQV EGGNHNDWSE WEKENAERLA KEAEKKFSHL KNWQEIKEQA
QNPQNYISGR ACDHYNRFEE DFDIAKSLSH NTHRFSIEWS RIEPEEGKFN EIEIEHYRNV
IKALRGRDIE PFVTLWHWTI PIWMRDKGGV INKYFPNYFS RYAERMAQEL PDVKFWITLN
EPTAVISMAY GIGEWPPQRR NPLAALKVYK TLARSHNDAF KKIHTVSPKA NVGFVNILSF
IEPYKKNSIL DKLTARIAKY FSNEKFLNLT KWNHDFLAVD YYFHNRLQFP GKMKNENKKV
SDMGWELYPE GIYYVLKDLK KCEKPIYITE NGLADAGDIH REWFIKETLK NVYKAIQEGV
DVRGYFYWSL LDNFEWDKGF WPRFGLVEID YKTMERKIRP SAYEYAKIIK NNGF
//