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   27-MAR-2024, entry version 93.
DE   RecName: Full=Beta-glucosidase 11 {ECO:0000303|PubMed:15604686};
DE            Short=AtBGLU11 {ECO:0000303|PubMed:15604686};
DE            EC=3.2.1.21 {ECO:0000250|UniProtKB:O64879};
DE   Flags: Precursor;
GN   Name=BGLU11 {ECO:0000303|PubMed:15604686};
GN   OrderedLocusNames=At1g02850 {ECO:0000312|Araport:AT1G02850};
GN   ORFNames=F22D16.15 {ECO:0000312|EMBL:AAF02882.1};
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=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         Evidence={ECO:0000250|UniProtKB:O64879};
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.B3H5Q1; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; B3H5Q1; 4 sites, No reported glycans.
DR   PaxDb; 3702-AT1G02850-4; -.
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; AT1G02850; BGLU11.
DR   eggNOG; KOG0626; Eukaryota.
DR   InParanoid; B3H5Q1; -.
DR   OMA; LKDSYFW; -.
DR   OrthoDB; 3373839at2759; -.
DR   PhylomeDB; B3H5Q1; -.
DR   BioCyc; ARA:AT1G02850-MONOMER; -.
DR   PRO; PR:B3H5Q1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; B3H5Q1; baseline and differential.
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; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF29; BETA-GLUCOSIDASE 11; 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; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
DR   Genevisible; B3H5Q1; AT.
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|UniProtKB:Q7XSK0"
FT   ACT_SITE        422
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         45
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         144
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         189..190
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         356
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         422
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   BINDING         466
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         482
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        388
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        209..217
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
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
//