ID A0A0M8YE84_9PSEU Unreviewed; 717 AA.
AC A0A0M8YE84;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=ADK67_20020 {ECO:0000313|EMBL:KOX23715.1};
OS Saccharothrix sp. NRRL B-16348.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX23715.1, ECO:0000313|Proteomes:UP000037722};
RN [1] {ECO:0000313|EMBL:KOX23715.1, ECO:0000313|Proteomes:UP000037722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX23715.1,
RC ECO:0000313|Proteomes:UP000037722};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOX23715.1}.
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DR EMBL; LGED01000197; KOX23715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8YE84; -.
DR STRING; 1415542.ADK67_20020; -.
DR PATRIC; fig|1415542.3.peg.4323; -.
DR Proteomes; UP000037722; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.290; -; 1.
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 InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
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 PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326}.
FT DOMAIN 615..717
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 587..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 717 AA; 75287 MW; 8336DCD7BA2BC90C CRC64;
MVPHLRPVAT AQVAAQADPR VEQLLARMSL DDKVGQMTQV DRGALDSTAD LATYRIGSLL
SGGGSAPTPN TPQSWADMYD NFQRTALSTP LGIPLIYGVD AVHGHNNVRG ATIFPHNIGL
GATRDPELVK RIGEVTAKEV AGTGIDWNFA PCLCVARDDR WGRTYESFGE VPEIPTAMTT
YVDGLQGATL GGTPSSVLAT AKHYIGDGGT AAGDDQGDAR ITEQELRTVH LPPFRAAVDR
GVGSVMISYS SWNGVKAHGH RYLITDVLKT ELGFTGFVVS DWAGVDQIDG ATGFTGAEVA
AAVNAGIDMV MVPTDYRRFI SLLKAEVQAG RVPMARIDDA NRRILTKKFE LGLFERPLTD
RSLTSTVGSA AHRDLARQAV RQSQVLLRND GVLPLAKSGR YFVAGKSADD IGHQSGGWTI
SWQGGSGNVT PGTTILQGIR DLVGNGAAIT HDRYGAGVDG SYDAAIAVVG ETPYAEGQGD
RPYGLGMDRE DLETINRLRS AGIPVVVVLV SGRPIDFIGQ EGHWNALLAS WLPGTEGRGV
ADVLFGDHNP TGKLPVTWMN SGAQQPLNAG DGKAALYPLG HGLSYRPITT STTPTSTTSS
TTTTTPTSTS TTTTTAPPPG GCVATARLTG SWQGGFQVEV TVTNAGAARL NGWTVTWAKL
GGQTINSLWN GKVTETGTSV SVDDVGWNGT LAPGTSGSFG YTATGSAATP ELTCRAR
//
