ID A0A1F5BVV9_9BACT Unreviewed; 426 AA.
AC A0A1F5BVV9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Beta-glucosidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2988_04580 {ECO:0000313|EMBL:OGD34741.1};
OS Candidatus Azambacteria bacterium RIFCSPLOWO2_01_FULL_46_25.
OC Bacteria; Candidatus Azambacteria.
OX NCBI_TaxID=1797298 {ECO:0000313|EMBL:OGD34741.1, ECO:0000313|Proteomes:UP000176650};
RN [1] {ECO:0000313|EMBL:OGD34741.1, ECO:0000313|Proteomes:UP000176650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGD34741.1}.
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DR EMBL; MEYS01000001; OGD34741.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5BVV9; -.
DR STRING; 1797298.A2988_04580; -.
DR Proteomes; UP000176650; 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 340
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 426 AA; 50750 MW; 8955FAD38B84B5B2 CRC64;
MNSNNFEKHK NLGGFPKGFL WGSATSSHQV EGGTRNDWSE WEKQNAERLA QEAEKKFNHL
SNWTDIKAQA QNPANYISGR ACDHYNRYEE DFDIAQSLGH NVHRFSIEWS RIEPEEGKWD
EKEIEHYRKV IRALHERGME PFVTLWHWCI PLWMRDKGGV TSKEFPRYFA RYAERMAQEL
GNDVKFWMTL NEPTSVIINS FMLGVWPPQK KSVFFTLRAY KTLAQAHREA YYAIRAVQKN
AQIGFGNILK FCEPMRKNFF DGLIARIADF WLNRYFLKLT GDTHDYYALQ YYFHMRIAFP
GKIKNENERL SDLGWELYPE GIYHLLKRPE YSKKPVYITE NGLADARDAQ REWFIKEHLR
WVHKAMQEGV DVRGYFYWSL LDNFEWDKGF WPRFGLVEID YKTLERKIRP SAHEYAKIIK
SNSLES
//
