BGL11_ARATH
ID BGL11_ARATH Reviewed; 521 AA.
AC B3H5Q1; A8MRZ0; Q3EDK1; Q94A86; Q9SRX8;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Beta-glucosidase 11;
DE Short=AtBGLU11;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU11; OrderedLocusNames=At1g02850; ORFNames=F22D16.15;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 5).
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 [4]
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=5;
CC Name=1;
CC IsoId=B3H5Q1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B3H5Q1-2; Sequence=VSP_038454;
CC Name=3;
CC IsoId=B3H5Q1-3; Sequence=VSP_038453, VSP_038454;
CC Name=4;
CC IsoId=B3H5Q1-4; Sequence=VSP_038452, VSP_038454;
CC Name=5;
CC IsoId=B3H5Q1-5; Sequence=VSP_038451, VSP_038454;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF02882.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009525; AAF02882.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27480.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27482.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27483.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27484.1; -; Genomic_DNA.
DR EMBL; AY049274; AAK83616.1; -; mRNA.
DR EMBL; AY062763; AAL32841.1; -; mRNA.
DR EMBL; BT001137; AAN64528.1; -; mRNA.
DR PIR; G86158; G86158.
DR RefSeq; NP_001117217.1; NM_001123745.2. [B3H5Q1-2]
DR RefSeq; NP_563666.1; NM_100166.4. [B3H5Q1-5]
DR RefSeq; NP_849578.5; NM_179247.6. [B3H5Q1-3]
DR RefSeq; NP_973746.3; NM_202017.3. [B3H5Q1-1]
DR AlphaFoldDB; B3H5Q1; -.
DR SMR; B3H5Q1; -.
DR STRING; 3702.AT1G02850.4; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; B3H5Q1; -.
DR PRIDE; B3H5Q1; -.
DR ProteomicsDB; 240784; -. [B3H5Q1-1]
DR EnsemblPlants; AT1G02850.1; AT1G02850.1; AT1G02850. [B3H5Q1-5]
DR EnsemblPlants; AT1G02850.2; AT1G02850.2; AT1G02850. [B3H5Q1-3]
DR EnsemblPlants; AT1G02850.4; AT1G02850.4; AT1G02850. [B3H5Q1-1]
DR EnsemblPlants; AT1G02850.5; AT1G02850.5; AT1G02850. [B3H5Q1-2]
DR GeneID; 839435; -.
DR Gramene; AT1G02850.1; AT1G02850.1; AT1G02850. [B3H5Q1-5]
DR Gramene; AT1G02850.2; AT1G02850.2; AT1G02850. [B3H5Q1-3]
DR Gramene; AT1G02850.4; AT1G02850.4; AT1G02850. [B3H5Q1-1]
DR Gramene; AT1G02850.5; AT1G02850.5; AT1G02850. [B3H5Q1-2]
DR KEGG; ath:AT1G02850; -.
DR Araport; AT1G02850; -.
DR TAIR; locus:2024685; AT1G02850.
DR eggNOG; KOG0626; Eukaryota.
DR InParanoid; B3H5Q1; -.
DR OMA; YFGCTAR; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; B3H5Q1; -.
DR BioCyc; ARA:AT1G02850-MON; -.
DR PRO; PR:B3H5Q1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; B3H5Q1; baseline and differential.
DR Genevisible; B3H5Q1; 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..521
FT /note="Beta-glucosidase 11"
FT /id="PRO_0000389574"
FT ACT_SITE 190
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 422
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 356
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 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 209..217
FT /evidence="ECO:0000250"
FT VAR_SEQ 250..299
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_038451"
FT VAR_SEQ 250..296
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038452"
FT VAR_SEQ 250..272
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038453"
FT VAR_SEQ 454
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_038454"
SQ SEQUENCE 521 AA; 58062 MW; F9A0B143B5E12C7E CRC64;
MKLLSNSLMF LPLLALALTA VSSLKYSRND FPPGFVFGSG TSAYQVEGAA DEDGRTPSIW
DVFAHAGHSG VAAGNVACDQ YHKYKEDVKL MADMGLEAYR FSISWSRLLP SGRGPINPKG
LQYYNNLIDE LITHGIQPHV TLHHFDLPQA LEDEYGGWLS QEIVRDFTAY ADTCFKEFGD
RVSHWTTINE VNVFALGGYD QGITPPARCS PPFGLNCTKG NSSIEPYIAV HNMLLAHASA
TILYKQQYKV LLSASLPSSI CIAFCYVLFI TQYKQHGSVG ISVYTYGAVP LTNSVKDKQA
TARVNDFYIG WILHPLVFGD YPETMKTNVG SRLPAFTEEE SEQVKGAFDF VGVINYMALY
VKDNSSSLKP NLQDFNTDIA VEMTLVGNTS IENEYANTPW SLQQILLYVK ETYGNPPVYI
LENGQMTPHS SSLVDTTRVK YLSSYIKAVL HSLSRKGSDV KGYFQWSLMD VFELFGGYER
SFGLLYVDFK DPSLKRSPKL SAHWYSSFLK GTLHHPSYAS S
