BGL33_ARATH
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 03-AUG-2022, entry version 125.
DE RecName: Full=Beta-glucosidase 33;
DE Short=AtBGLU33;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU33; OrderedLocusNames=At2g32860; ORFNames=T21L14.20;
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 -!- 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 CAUTION: [Isoform 2]:
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.AT2G32860.2; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; O48779; -.
DR PRIDE; O48779; -.
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; locus:2059385; AT2G32860.
DR eggNOG; KOG0626; Eukaryota.
DR InParanoid; O48779; -.
DR OMA; HNTFEDD; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; O48779; -.
DR BioCyc; ARA:AT2G32860-MON; -.
DR BioCyc; MetaCyc:MON-19205; -.
DR PRO; PR:O48779; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48779; baseline and differential.
DR Genevisible; O48779; 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 GO; GO:0019762; P:glucosinolate catabolic process; IBA:GO_Central.
DR GO; GO:0009651; P:response to salt stress; IBA:GO_Central.
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..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"
FT ACT_SITE 479
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 529
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 536..537
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 282..290
FT /evidence="ECO:0000250"
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
