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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//