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Database: UniProt
Entry: A0A1G1THK4_9BACT
LinkDB: A0A1G1THK4_9BACT
Original site: A0A1G1THK4_9BACT 
ID   A0A1G1THK4_9BACT        Unreviewed;       799 AA.
AC   A0A1G1THK4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=BEN49_06830 {ECO:0000313|EMBL:OGX90376.1};
OS   Hymenobacter coccineus.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1908235 {ECO:0000313|EMBL:OGX90376.1, ECO:0000313|Proteomes:UP000177506};
RN   [1] {ECO:0000313|EMBL:OGX90376.1, ECO:0000313|Proteomes:UP000177506}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 8649 {ECO:0000313|EMBL:OGX90376.1,
RC   ECO:0000313|Proteomes:UP000177506};
RA   Sedlacek I., Kralova S., Kyrova K., Maslanova I., Stankova E., Vrbovska V.,
RA   Nemec M., Bartak M., Svec P., Busse H.-J., Pantucek R.;
RT   "Hymenobacter coccineus sp. nov., Hymenobacter lapidarius sp. nov. and
RT   Hymenobacter glacialis sp. nov., isolated from Antarctic soil.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:OGX90376.1}.
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DR   EMBL; MDZA01000155; OGX90376.1; -; Genomic_DNA.
DR   RefSeq; WP_070743105.1; NZ_MDZA01000155.1.
DR   AlphaFoldDB; A0A1G1THK4; -.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000177506; 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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..799
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009579494"
FT   DOMAIN          709..778
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   799 AA;  85008 MW;  A0C56E33105786F1 CRC64;
     MTKYLALGLG LFSATALAQP TGPPLYKNAR APTETRVQDL LGRMTREEKV GQLSTLLGWK
     MYDKQGPRVA VSAAYRKAVD ERHIGMLWAT LRADPWTQKT LLTGLNPTLA AEATNALQKY
     AREHTRLGIP LLLAEECPHG HMAIGTTVFP TSIGQSSTWD PALIEQMAGA IAAEARAQGA
     HVGYGPVLDL AREPRWSRVE ETYGEDPVLN SAMGVAMVRG FQGPNPGPVS GPHIISTLKH
     FTAYGVPEGG HNGGSISTGP RELYQSFLPP FRAAVKAGAL SVMTAYNSVD GVPCSANEFL
     LTDLLRKQWG FQGFTVSDLG SISGLVGGHR VAATPAAAAA LAINAGLDTD LSGYGYDKDL
     LAAVADGSVS GAVLDRAVGR LLRQKFEMGL FENPYVVVKN AAKQVRTPAH VQLARRVAQE
     SVVLLKNERD LLPLSKTLKT IAVIGPNADN IYNQLGDYTA PQPDDNIVTV LEGIRTKVAA
     TTKVTYVKGC AIRDTTSADI AGAVAAARGA QVAVVVVGGS SARDFKTEYQ STGAATVTAA
     AGGQVVSDME SGEGFDRATL DLLGKQLQLV QAVVATGTPT VVVLIKGRPL NLNWLAAHVP
     AVLDAWYPGQ EGGNAVADVL FGDVNPAGRL PISVPKSVGQ LPIYYNYKTP ARHDYVEMDA
     KPLYAFGYGL SYAKFVYADL RTAVVESAGT VQVKVSFKVK NTSARAGDEV AQLYLRDNVS
     SVVTPAKQLK KFQRFALKAG EEKTVEFTLG PDDLMLLGPQ MQWVVEPGAF TAMVGAASDD
     IRLEQQFTLR NGLNLPVGQ
//
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