ID BGL47_ARATH Reviewed; 535 AA.
AC Q9SVS1;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 2.
DT 24-JAN-2024, entry version 125.
DE RecName: Full=Beta-glucosidase 47 {ECO:0000303|PubMed:15604686};
DE Short=AtBGLU47 {ECO:0000303|PubMed:15604686};
DE EC=3.2.1.21 {ECO:0000250|UniProtKB:O64879};
DE Flags: Precursor;
GN Name=BGLU47 {ECO:0000303|PubMed:15604686};
GN OrderedLocusNames=At4g21760 {ECO:0000312|Araport:AT4G21760};
GN ORFNames=F17L22.220 {ECO:0000312|EMBL:CAB36820.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15604686; DOI=10.1007/s11103-004-0790-1;
RA Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R.,
RA Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E., Esen A.;
RT "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase
RT family 1.";
RL Plant Mol. Biol. 55:343-367(2004).
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:0000250|UniProtKB:O64879};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36820.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81283.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035527; CAB36820.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161555; CAB81283.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84500.1; -; Genomic_DNA.
DR PIR; T05851; T05851.
DR RefSeq; NP_193907.2; NM_118296.4.
DR AlphaFoldDB; Q9SVS1; -.
DR SMR; Q9SVS1; -.
DR STRING; 3702.Q9SVS1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR GlyCosmos; Q9SVS1; 4 sites, No reported glycans.
DR PaxDb; 3702-AT4G21760-1; -.
DR ProteomicsDB; 240425; -.
DR EnsemblPlants; AT4G21760.1; AT4G21760.1; AT4G21760.
DR GeneID; 828264; -.
DR Gramene; AT4G21760.1; AT4G21760.1; AT4G21760.
DR KEGG; ath:AT4G21760; -.
DR Araport; AT4G21760; -.
DR TAIR; AT4G21760; BGLU47.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9SVS1; -.
DR PhylomeDB; Q9SVS1; -.
DR PRO; PR:Q9SVS1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SVS1; baseline and differential.
DR Genevisible; Q9SVS1; AT.
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; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353:SF27; BETA-GLUCOSIDASE 47; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Signal.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..535
FT /note="Beta-glucosidase 47"
FT /id="PRO_0000390319"
FT ACT_SITE 221
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT ACT_SITE 426
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT BINDING 73
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 175
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 220..221
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 363
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 426
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT BINDING 470
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 477..478
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 486
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 240..247
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT DISULFID 371..376
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
SQ SEQUENCE 535 AA; 61962 MW; 399BF7E254501870 CRC64;
MKKSIVYEIM ETKSSMYLSQ FRLWLCFIIT TLVSLSSSTR WYDDHISLKE IHAEETFHFP
KNFLFGTASS AYQYEGAYLT DGKTLSNWDV FTNISGKIAD GSHGKVAVDH YHRYPGDLDL
MEDLGVNSYR LSLSWARILP KGRFGDVNMG GIDHYNRMIN DILKTGIEPF VTLTHYDIPQ
ELEYRYGSWL NPQIREDFEH YANICFRHFG DRVKFWSTFN EPNVQVILGY RTGTYPPSRC
SKPFGNCSCG DSYIEPLVAA HNIILSHLAA VNLYRTKFQE QQRGQIGIVM NTIWFEPISD
SLADRLAADR AQAFYLTWFL DPVVFGRYPR EMREILGDDL PEFTKDDLKS SKNALDFIGI
NQYTSRYAKD CLHSVCEPGK GGSRAEGFVY ANALKDGLRL GEPVGMEEML MYATERYKNI
TLYVTENGFG ENNTGVLLND YQRVKFMSNY LDALKRAMRK GADVRGYFAW SLLDNFEWIS
GYTIRFGMYH VDFSTQERTP RLSASWYKNF IFQHRALSKD DWCLKQKEDT NFFLI
//
