ID A0A081BLU3_9BACT Unreviewed; 454 AA.
AC A0A081BLU3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
GN ORFNames=U14_02602 {ECO:0000313|EMBL:GAK51359.1};
OS Candidatus Moduliflexus flocculans.
OC Bacteria; Candidatus Moduliflexota; Candidatus Moduliflexia;
OC Candidatus Moduliflexales; Candidatus Moduliflexaceae.
OX NCBI_TaxID=1499966 {ECO:0000313|EMBL:GAK51359.1};
RN [1] {ECO:0000313|EMBL:GAK51359.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W.,
RA Hugenholtz P.;
RT "First genomic representation of candidate bacterial phylum KSB3 points to
RT enhanced environmental sensing as a trigger of wastewater bulking.";
RL PeerJ 3:e740-e740(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 ECO:0000256|RuleBase:RU361175};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|RuleBase:RU361175}.
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DR EMBL; DF820457; GAK51359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A081BLU3; -.
DR STRING; 1499966.U14_02602; -.
DR HOGENOM; CLU_001859_1_0_0; -.
DR Proteomes; UP000030700; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR NCBIfam; TIGR03356; BGL; 1.
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; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361175};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
KW Reference proteome {ECO:0000313|Proteomes:UP000030700}.
FT ACT_SITE 163
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 356
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 410..411
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 454 AA; 51882 MW; 28655705AF23DE20 CRC64;
MNFPENFVWG VAAAAYQIEG AAYDEGKGLS VWDMFCRKPG AVWNGHTGDV ACDHYHRYQE
DVALMKELGL PAYRLSVSWP RVLPQGVGAV NEKGLDFYDR LIDELLAANI TPYVTLFHWD
YPLELFRRGG WLNPDSPEWF ADYTRLMVER LSDRVRHWMT YNEPRVFVGL GHEIGRHAPG
LQFGLPDVLQ MCHHVMLSHG RGVQTIRAYS KTPSQVGCVV TTGFQQMPAT NRPEDIEAAR
EAMFSISTPN CFHTALWLDP ILLGRYPDTA YSTYGDAMPV IHDGDLATMH QPLDFIGLNI
YFGEQYAAGS DGRPEKVPFP AGHPQTAFRW FVTPEALYWG PKFVYERYGV PVMITENGLS
NLDWVSTDGK VHDPQRIDFL RRYLIELRRA CADGVDVRGY FQWSILDNFE WAEGYKERFG
LVHVDYQTQK RTPKDSAFWY KSIIASNGRA LDEI
//
