ID W6K116_9MICO Unreviewed; 449 AA.
AC W6K116;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 Name=bglA {ECO:0000313|EMBL:CCH74715.1};
GN ORFNames=BN11_4730014 {ECO:0000313|EMBL:CCH74715.1};
OS Tetrasphaera australiensis Ben110.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1193182 {ECO:0000313|EMBL:CCH74715.1, ECO:0000313|Proteomes:UP000035763};
RN [1] {ECO:0000313|EMBL:CCH74715.1, ECO:0000313|Proteomes:UP000035763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ben110 {ECO:0000313|EMBL:CCH74715.1,
RC ECO:0000313|Proteomes:UP000035763};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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|RuleBase:RU361175};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|RuleBase:RU361175}.
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:CCH74715.1}.
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DR EMBL; CAJA01000416; CCH74715.1; -; Genomic_DNA.
DR RefSeq; WP_048700070.1; NZ_HG764815.1.
DR AlphaFoldDB; W6K116; -.
DR STRING; 1193182.BN11_4730014; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000035763; 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:InterPro.
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; LACTASE-LIKE PROTEIN; 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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:CCH74715.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:CCH74715.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000035763}.
FT ACT_SITE 164
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 355
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 402
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 409..410
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 449 AA; 49355 MW; F1FE12EC88CA52AC CRC64;
MPQLPQDFLF GVATAAYQIE GAVTEDGRGR SVWDDFCDRP GAIVDGSSGA SACDSYHLYK
EDVDLMAGLG IDAYRFSISW PRIQPDGFGA VNQAGLDYYD RLVDALLARG IRPAATLFHW
DLPSPLEAEG GWLQRETAEA FADYARIVAE RLADRVAMWT PVNEPNIVTS LGYSTGMHAP
GRTLGLYALP AAHHLLLGHG LAVGALRAAG AKSVGCAQNH TVVWPTSQEE SDVAAADLFD
TIVNRMYAEP ILHGTYPDGI AQMMPGPVEH DVKIIGAPLD FYGFNYYNPT LVGSPHAGER
IGAEIAVDLP FSRHEIQGYP MTDFGWPVVP EGLLAVMRQL RERYGDRLPP LFVTENGCAY
NTGPDDKGVV MDTERVTFYD GHLAAVSQAI AEGIDVRGYF AWSLMDNFEW AEGFTKRFGL
VYTDFETQQR IPKLSYDWYA DLIRRTKAG
//