BGL13_ARATH
ID BGL13_ARATH Reviewed; 507 AA.
AC Q9LU02;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Beta-glucosidase 13;
DE Short=AtBGLU13;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU13; OrderedLocusNames=At5g44640; ORFNames=K15C23.9;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
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].
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2008) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; AB024024; BAA98117.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95142.1; -; Genomic_DNA.
DR EMBL; BT033043; ACE79745.1; -; mRNA.
DR RefSeq; NP_199277.1; NM_123831.2.
DR AlphaFoldDB; Q9LU02; -.
DR SMR; Q9LU02; -.
DR STRING; 3702.AT5G44640.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q9LU02; -.
DR PRIDE; Q9LU02; -.
DR ProteomicsDB; 240785; -.
DR EnsemblPlants; AT5G44640.1; AT5G44640.1; AT5G44640.
DR GeneID; 834493; -.
DR Gramene; AT5G44640.1; AT5G44640.1; AT5G44640.
DR KEGG; ath:AT5G44640; -.
DR Araport; AT5G44640; -.
DR TAIR; locus:2152160; AT5G44640.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9LU02; -.
DR OMA; SEWGWTI; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q9LU02; -.
DR BioCyc; ARA:AT5G44640-MON; -.
DR PRO; PR:Q9LU02; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LU02; baseline and differential.
DR Genevisible; Q9LU02; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
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 Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..507
FT /note="Beta-glucosidase 13"
FT /id="PRO_0000389576"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 414
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 459
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 466..467
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 219..227
FT /evidence="ECO:0000250"
SQ SEQUENCE 507 AA; 56957 MW; 83AC8DC0DC7AC434 CRC64;
MRTKYFSLLV FIIVLASNEV IAKKHSSTPK LRRSDFPKDF IFGAATSAYQ VEGAAHEDGR
GPSIWDTFSE KYPEKIKDGT NGSIASDSYH LYKEDVGLLH QIGFGAYRFS ISWSRILPRG
NLKGGINQAG IDYYNNLINE LLSKGIKPFA TIFHWDTPQS LEDAYGGFFG AEIVNDFRDY
ADICFKNFGD RVKHWMTLNE PLTVVQQGYV AGVMAPGRCS KFTNPNCTAG NGATEPYIVG
HNLILAHGEA VKVYREKYKA SQKGQVGIAL NAGWNLPYTE SAEDRLAAAR AMAFTFDYFM
EPLVTGKYPV DMVNNVKDGR LPTFTAKQSK MLKGSYDFIG INYYSSSYAK DVPCSSENVT
LFSDPCASVT GEREGVPIGP KAASDWLLIY PKGIRDLLLY AKYKFKDPVM YITENGRDEA
STGKIDLKDS ERIDYYAQHL KMVQDAISIG ANVKGFFAWS LLDNFEWATG YSVRFGLVYV
DFNDGRKRYP KKSAKWFRKL LSEKKRN
