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Database: UniProt
Entry: W6K116_9MICO
LinkDB: W6K116_9MICO
Original site: W6K116_9MICO 
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
//
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