ID   A0A1H9QHF8_9PSEU        Unreviewed;       775 AA.
AC   A0A1H9QHF8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:SER59289.1};
GN   ORFNames=SAMN04488000_110144 {ECO:0000313|EMBL:SER59289.1};
OS   Lentzea albida.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=65499 {ECO:0000313|EMBL:SER59289.1, ECO:0000313|Proteomes:UP000199503};
RN   [1] {ECO:0000313|EMBL:SER59289.1, ECO:0000313|Proteomes:UP000199503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44437 {ECO:0000313|EMBL:SER59289.1,
RC   ECO:0000313|Proteomes:UP000199503};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; FOFV01000010; SER59289.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9QHF8; -.
DR   STRING; 65499.SAMN04488000_110144; -.
DR   OrthoDB; 3187421at2; -.
DR   Proteomes; UP000199503; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 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   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; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-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}.
FT   DOMAIN          702..763
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   775 AA;  81654 MW;  1E7A54288BC7BE5B CRC64;
     MDIEKAIARL DLPRKVRLLT GSALFALHDE PEIGLASLKL SDGPTGVRGA ELRGGTIACV
     LPNATLLAQH WDTALAREVG EVLADEAAAQ QVHVVLGPTI NLHRTALGGR LFEAYSEDPL
     LTAAIAAAYV RGLQDKGIAA TPKHYVANES ETERRTASMV LDEKTLREIY LLPFEIVVED
     SSPWAIMAAY NNVNGVPATE HAELVEGVLR GEWGFDGLLM SDWFATKSTA ASANGGLDLA
     MPGPGGPWED KLVAAVEAGE VAESTIDDHV ARLLLLASRT GAFGEQRAWP RDLPAPDSTL
     RREQLRRFAA GGMTVLKNSG VLPLRDDSVA LIGRHAIDTV AQGGGSAGVR PPHVISIADG
     LTSRLGNAVS VVDGVEVRLR YAAPGAGVLT AVRATTFDAD GEVLATRDME IAELAAYGGW
     AQGATSIEVS GEVVLDEPTR MLIGVRGFGE WTVEVGGKQH ATLLAWADGI VEEALLKPPH
     WTAEVLLSPG DRITARVRGA SALVGLITQP VPRSPADAIG AAVRAAREAD VAVVVVGLTE
     EQETEGFDKT TLALPGEQDA LVAAVAAAAR RTVVVVNAAT PVLMPWLDQV DAVLWAGLPG
     QEAGDAVAAA LLGDVEPAGR LVTTFPRADA DALNLVPSDG ELVYSEGTAI GYRGATDPLF
     WFGHGLGYTT WEYGTAQLSV VDGLVGSVSA EVMNTGDRTG REVVQVYLRP RDEPVRLIGF
     AVADLAPGET ARVEVPCDPR VQRVWQDGWH PLTGGEVLIA RGLGDVRVTL PADQE
//