BGL17_ARATH
ID BGL17_ARATH Reviewed; 517 AA.
AC O64882; B3H6D8; Q8GY78;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Beta-glucosidase 17;
DE Short=AtBGLU17;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU17; OrderedLocusNames=At2g44480; ORFNames=F4I1.29;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O64882-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O64882-2; Sequence=VSP_038456;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; AC004521; AAC16094.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10426.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10427.1; -; Genomic_DNA.
DR EMBL; AK117809; BAC42451.1; -; mRNA.
DR EMBL; AY074629; AAL69445.1; -; mRNA.
DR PIR; T02403; T02403.
DR RefSeq; NP_001118525.1; NM_001125053.1. [O64882-2]
DR RefSeq; NP_181976.1; NM_130011.3. [O64882-1]
DR AlphaFoldDB; O64882; -.
DR SMR; O64882; -.
DR STRING; 3702.AT2G44480.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; O64882; -.
DR PRIDE; O64882; -.
DR ProteomicsDB; 240788; -. [O64882-1]
DR EnsemblPlants; AT2G44480.1; AT2G44480.1; AT2G44480. [O64882-1]
DR EnsemblPlants; AT2G44480.2; AT2G44480.2; AT2G44480. [O64882-2]
DR GeneID; 819055; -.
DR Gramene; AT2G44480.1; AT2G44480.1; AT2G44480. [O64882-1]
DR Gramene; AT2G44480.2; AT2G44480.2; AT2G44480. [O64882-2]
DR KEGG; ath:AT2G44480; -.
DR Araport; AT2G44480; -.
DR TAIR; locus:2050512; AT2G44480.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; O64882; -.
DR PhylomeDB; O64882; -.
DR PRO; PR:O64882; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64882; baseline and differential.
DR Genevisible; O64882; AT.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..517
FT /note="Beta-glucosidase 17"
FT /id="PRO_0000389580"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 417
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 466
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 473..474
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 223..230
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038456"
FT CONFLICT 259
FT /note="E -> V (in Ref. 3; BAC42451)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 59121 MW; 1A9E4DD65EE1A760 CRC64;
MAIKSIFIII IISIITSISE LYALDPSFLR LSTSLQRSSF PQDFRFGAAS SAYQSEGAAN
VDGREPSIWD TFTKQYPEKI SDGSNGDVAD EFYYRFKEDV AHMKEIGLDS FRFSISWSRI
LPRGTVAGGV NQAGINFYNH LINELISNGI RPLVTLFHWD TPQALEDEYG GFLNPQIVKD
FVEYVDICFK EFGDRVKEWI TINEPNMFAV LGYNVGNIAP GRCSSYVQNC TVGNSATEPY
LVAHYLILSH AATVQLYREK YQSFHGGTIG MTIQTYWMIP KYNTPACREA AKRALDFFFG
WFADPITYGD YPKTMRELVG NRLPKFTKKQ SKMVRGSFDF FGLNYYTSRY VEDVMFYANT
NLSYTTDSRV NQTTEKNGVP VGEPTSADWL FICPEGFQDV LLYIKSKFQN PVILVTENGM
PSENDKSLSV NIALNDEAKI KYHQLHLTAL LEAVSQGADV RGYYIWSLMD DFEWEFGYKY
RYGLVYVDFQ DGLKRHLKSS ALWYHHFLSN SSSYQMD
