ID D7LN94_ARALL Unreviewed; 609 AA.
AC D7LN94;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=ARALYDRAFT_485079 {ECO:0000313|EMBL:EFH53795.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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}.
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DR EMBL; GL348717; EFH53795.1; -; Genomic_DNA.
DR RefSeq; XP_002877536.1; XM_002877490.1.
DR AlphaFoldDB; D7LN94; -.
DR STRING; 81972.D7LN94; -.
DR EnsemblPlants; fgenesh2_kg.5__1071__AT3G47000.1; fgenesh2_kg.5__1071__AT3G47000.1; fgenesh2_kg.5__1071__AT3G47000.1.
DR GeneID; 9311891; -.
DR Gramene; fgenesh2_kg.5__1071__AT3G47000.1; fgenesh2_kg.5__1071__AT3G47000.1; fgenesh2_kg.5__1071__AT3G47000.1.
DR KEGG; aly:9311891; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_9_3_1; -.
DR OrthoDB; 1208905at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; 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; 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:SF33; BETA-D-GLUCAN EXOHYDROLASE-LIKE PROTEIN-RELATED; 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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 30..358
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 397..605
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
SQ SEQUENCE 609 AA; 66500 MW; 75A82F115D20360B CRC64;
MVVKEESSCV YKNQDAPVEV RVKDLLSRMT LPEKIGQMTQ IERRVASHAA FTDFFIGSVL
NAGGSVPFED AKSSDWADMI DGFQRSALAS RLGIPIIYGT DAVHGNNNVY GATVFPHNIG
LGATRDADLV RRIGAATALE VRASGAHWAF APCVAVLRDP RWGRCYESYG EDPGLVCEMA
SLVSGLQGVP PEEHLNGYPF VAGRNNVVAC VKHFVGDGGT DKGINEGNTI ASYEDLEKIH
IPPYLNCLAQ GVSTVMASYS SWNGTRLHAD RFLLTEILKE KLGFKGFLVS DWEGLDRLSE
PQGSNYRYCI KTAVNAGIDM VMVPFKYEQF IQDMTDLVKS GEISMARVND AVERILRVKF
VSGLFEYPLT DRSLLPTVGC KEHRELAQEA VRKSLALLKN GKNADKPFLP LDRNAKRILV
TGTHADDLGY QCGGWTKTWF GLSGRITIGT TLLDAIKEAV GDETEVIYEK TPSKETLASS
EGFSYAIVAV GEPPYAETMG DNSELKISFN GSDIVTAVAE TIPTLVILIS GRPVVLEPTV
LEKTEALVAA WLPGTEGQGM ADVIFGDYDF EGKLPVSWFK RVEHLPLDAQ TNSYDPLFPF
GFGLTSKPV
//
