ID   BGL33_ARATH             Reviewed;         614 AA.
AC   O48779; Q8H7F9;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   24-JAN-2024, entry version 132.
DE   RecName: Full=Beta-glucosidase 33 {ECO:0000303|PubMed:15604686};
DE            Short=AtBGLU33 {ECO:0000303|PubMed:15604686};
DE            EC=3.2.1.21 {ECO:0000250|UniProtKB:O64879};
DE   Flags: Precursor;
GN   Name=BGLU33 {ECO:0000303|PubMed:15604686};
GN   OrderedLocusNames=At2g32860 {ECO:0000312|Araport:AT2G32860};
GN   ORFNames=T21L14.20 {ECO:0000312|EMBL:AAB91979.1};
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=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 [MRNA] OF 134-614 (ISOFORM 2).
RA   Stracke R., Palme K.;
RT   "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT   and guard cells.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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=2;
CC       Name=1;
CC         IsoId=O48779-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O48779-2; Sequence=VSP_038464, VSP_038465;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN60253.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAN60253.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC003033; AAB91979.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08753.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08754.1; -; Genomic_DNA.
DR   EMBL; AF083694; AAN60253.1; ALT_FRAME; mRNA.
DR   PIR; T01121; T01121.
DR   RefSeq; NP_180845.2; NM_128846.4. [O48779-2]
DR   RefSeq; NP_973587.1; NM_201858.1. [O48779-1]
DR   AlphaFoldDB; O48779; -.
DR   SMR; O48779; -.
DR   STRING; 3702.O48779; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; O48779; 5 sites, No reported glycans.
DR   PaxDb; 3702-AT2G32860-2; -.
DR   ProteomicsDB; 240334; -. [O48779-1]
DR   EnsemblPlants; AT2G32860.1; AT2G32860.1; AT2G32860. [O48779-2]
DR   EnsemblPlants; AT2G32860.2; AT2G32860.2; AT2G32860. [O48779-1]
DR   GeneID; 817847; -.
DR   Gramene; AT2G32860.1; AT2G32860.1; AT2G32860. [O48779-2]
DR   Gramene; AT2G32860.2; AT2G32860.2; AT2G32860. [O48779-1]
DR   KEGG; ath:AT2G32860; -.
DR   Araport; AT2G32860; -.
DR   TAIR; AT2G32860; BGLU33.
DR   eggNOG; KOG0626; Eukaryota.
DR   InParanoid; O48779; -.
DR   OMA; HNTFEDD; -.
DR   OrthoDB; 639953at2759; -.
DR   PhylomeDB; O48779; -.
DR   BioCyc; ARA:AT2G32860-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-19205; -.
DR   PRO; PR:O48779; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O48779; 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:SF320; BETA-GLUCOSIDASE 33; 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; O48779; AT.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..614
FT                   /note="Beta-glucosidase 33"
FT                   /id="PRO_0000389595"
FT   ACT_SITE        263
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   ACT_SITE        479
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         113
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         217
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         262..263
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         407
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         479
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   BINDING         529
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         536..537
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         545
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   CARBOHYD        344
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   CARBOHYD        439
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        491
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        282..290
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   VAR_SEQ         323..324
FT                   /note="VE -> CQE (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_038464"
FT   VAR_SEQ         435..446
FT                   /note="VITNNLSLPDLQ -> DSQNNSPHLK (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_038465"
FT   CONFLICT        291
FT                   /note="P -> S (in Ref. 3; AAN60253)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   614 AA;  70190 MW;  D1ACCE2438151D29 CRC64;
     MATATLTLFL GLLALTSTIL SFNADARPQP SDEDLGTIIG PHQTSFDDEI GIVIGPHATV
     DDEDIDMDMG TTVGPQTNLN DDDLGTIIGP EFEIHKQDFP ADFIFGTSVS AYQVEGAKKG
     SGRGLTSWDE FTHMFPEKVQ QNGDGDEGVD FYTRYKDDIK LMKELNTNGF RFSISWTRIL
     PYGTIKKGVN EEGVKFYNDL INELLANGIQ PSVTLFHWES PLALEMEYGG FLNERIVEDF
     REFANFCFKE FGDRVKNWAT FNEPSVYSVA GYSKGKKAPG RCSKWQAPKC PTGDSSEEPY
     IVAHNQILAH LAAVDEFRNC KKVEGGGKIG IVLVSHWFEP KDPNSSEDVK AARRSLEYQL
     GWFLRPLTYG QYPAEMLEDV NIRLREFTPE ESEKLRKSLD FVGLNYYGAF FSTPLAKVNS
     SQLNYETDLR VNWTVITNNL SLPDLQTTSM GIVIYPAGLK NILKHIKDEY MDPEIYIMEN
     GMDEIDYGTK NITEATNDYG RKEFIKSHIL IMGKSIRMDK VRLKGYYIWS LMDNFEWDKG
     YKVRFGLYYV DYNDNMKRYI RSSGKWLSEF LDSKETLHKC YFEGHREKGY APKLFDVEYL
     EPENSQLSYR SDFM
//