ID A0A445DIN3_ARAHY Unreviewed; 681 AA.
AC A0A445DIN3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=Ahy_A04g020854 {ECO:0000313|EMBL:RYR63065.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR63065.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR63065.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738}, and
RC GDAAS-fuhuasheng2018 {ECO:0000313|EMBL:RYR63065.1};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR63065.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) 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 -!- 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:RYR63065.1}.
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DR EMBL; SDMP01000004; RYR63064.1; -; Genomic_DNA.
DR EMBL; SDMP01000004; RYR63065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445DIN3; -.
DR STRING; 3818.A0A445DIN3; -.
DR Proteomes; UP000289738; Chromosome a04.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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:SF35; GLYCOSYL HYDROLASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..681
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036353968"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..388
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 427..636
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
SQ SEQUENCE 681 AA; 73960 MW; 400273DE675D4DE6 CRC64;
MNRALIRFLV SLWLCCCCWL VSIGEAQAQG GEYMKYKDPK QPVAVRVKDL LDRMTLEEKI
GQMVQIDRSV ANAEVMKNSF IGSVLSGGGS EPLPKATAQD WVNMINEFQR GSLASRLGIP
MMYGIDAVHG HNNVYNATIF PHNVGLGCTR QVEILIVDPD LAQKIGAATA LEVRATGIPY
VFAPCIAVCR DPRWGRCYES YSEDPKIVEQ MTEIIPGLQG SLPANAKKGF PYVGGKTKVA
ACAKHFVGDG GTTKGVNENN TVIDWHGLLS LHMPAYSDSI IKGVSTVMVS YSSWNGVKMH
ANRDLVTGFL KNTLKFKGFV ISDWQGIDKI TSPPDSNYTY SVQASIQAGV DMVMVPYKFD
EFIQDLNLLV KNNVIPMDRI DDAVARILLV KFTMGLFENP LADFSLVDQL GSQGHRDLAR
EAVRKSLVLL KNGKNGSAPL LPLSKNVPKI LVAGTHADNL GYQCGGWTIK WQGFSGNMDT
SGTTILSAIK SAVDPSTEVV FRENPDSEFV KSNNFDYAIV AVGELPYAET AGDSTTLTMT
DPGPNIINNV CGNVKCVVII VSGRPIVIEP YVSSIDALVA AWLPGTEGQG VTDALFGDYG
FSGKLARTWF KSVDQLPMNV GDPHYDPLFP FGFGLTTESV KDLVARSTSS VASVRACIFT
ILVTLIISLY LIGEAQFIGA Y
//
