ID Q9HGX2_AGABI Unreviewed; 861 AA.
AC Q9HGX2;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN Name=bg1 {ECO:0000313|EMBL:CAC03462.1};
OS Agaricus bisporus (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX NCBI_TaxID=5341 {ECO:0000313|EMBL:CAC03462.1};
RN [1] {ECO:0000313|EMBL:CAC03462.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D649 {ECO:0000313|EMBL:CAC03462.1};
RA Morales-Almora P., Thurston C.F.;
RT "Molecular analysis of the cellulolytic genes in Agaricus bisporus.";
RL Submitted (AUG-2000) 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}.
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DR EMBL; AJ293760; CAC03462.1; -; mRNA.
DR AlphaFoldDB; Q9HGX2; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
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; 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 InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF28; 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 Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS51820; PA14; 1.
PE 2: Evidence at transcript level;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:CAC03462.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAC03462.1}.
FT DOMAIN 413..577
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 861 AA; 94354 MW; 8B52C0A18DB39AB3 CRC64;
MPPSDFANAD IDKIVDALTT DEAILLSAGV GFWHTHAIER LQIPAVKVSD GPNGIRGNHF
FMGTPAKCLP SSTAMGATFD RDLLEEVGLK LLAREAKLRS ASVILAPTCN IQRNPLGGRS
FESFSEDPFL SGMLCSAYIN GIQKGGIGAT IKHFVGNDKE DDRTGYDSIH YRTTSSGDLS
PSVHAGSRNM PLHGAIMTAY NRVNGIHVCE NPELLQKILR DEWKSDVMIM SDWFGTYSVD
VGLNAGLDLE MPGLNKWRSL ESVNRSIQSR KVTAKKVKER ARKVLELVKK CAQGAPEILD
GDGLERTLDS DEDNALMRKF AAESIVLLKN DKKVLPLDRK SLKKVAIVGG NAKAAVLSGG
GSAALKPSYF VARPAGLVKA LKEVNPNIEV TYSEGARAAK TLPTLDFDLF TESGQRGWTG
SWHAHENDDS LVALPTPIKT QYVDETRMFI SSSSPAGITK KWTLRMKGYL KPRERDCKFE
FGLTAAGRAK LFVDGKLVID NWTRQRRGVE FFGCGSEEET GVVELKAGVK HEIYVDFCNV
RGPADGDETE TIMDSNPGIR LGGAEVEDPD ELLNSAVSIA KDADAVIIVV GLNGDWETEG
NDRTTLALPG RTDELVQKVV AANPRAVVVT QAGSAITMPW VDQVSSLLHT WYLGNATGDA
IADVIFGNHN PSGKLSLTFP KRLEDVPAHG YFHSEKGKVT YAEGLYVGYK HYQHRNIEPL
FAFGHGLSYT SFNISDLRLS QPIVSGDQFD LKATVKLTNT GNITGSQVVQ LYIGLPKTSE
LTHPRWQLRG FKKMRDVKPG ESREVELVMD RLSVSYWDKE WVVENGAYDV RVAFTSEEGV
GEGQELLGRF NVEKGFGWRG L
//
