BGL15_ARATH
ID BGL15_ARATH Reviewed; 506 AA.
AC O64879;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Beta-glucosidase 15;
DE Short=AtBGLU15;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU15; OrderedLocusNames=At2g44450; ORFNames=F4I1.26;
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 [LARGE SCALE MRNA] OF 3-506.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX PubMed=25468534; DOI=10.1016/j.phytochem.2014.10.028;
RA Roepke J., Bozzo G.G.;
RT "Arabidopsis thaliana beta-glucosidase BGLU15 attacks flavonol 3-O-beta-
RT glucoside-7-O-alpha-rhamnosides.";
RL Phytochemistry 109:14-24(2014).
CC -!- FUNCTION: Beta-glucosidase involved in the rapid degradation of
CC flavonol 3-O-beta-glucoside-7-O-alpha-rhamnosides during abiotic stress
CC recovery. No activity with quercetin 3-O-alpha-rhamnoside, quercetin 3-
CC O-beta-galactoside and rutin. {ECO:0000269|PubMed:25468534}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=51 uM for kaempferol 3-O-beta-glucoside-7-O-alpha-rhamnoside
CC {ECO:0000269|PubMed:25468534};
CC KM=36 uM for quercetin 3-O-beta-glucoside-7-O-alpha-rhamnoside
CC {ECO:0000269|PubMed:25468534};
CC KM=60 uM for kaempferol 3-O-beta-glucoside
CC {ECO:0000269|PubMed:25468534};
CC KM=52 uM for quercetin 3-O-beta-glucoside
CC {ECO:0000269|PubMed:25468534};
CC KM=2592 uM for p-nitrophenyl beta-D-glucoside
CC {ECO:0000269|PubMed:25468534};
CC Vmax=1.08 umol/min/mg enzyme with kaempferol 3-O-beta-glucoside-7-O-
CC alpha-rhamnoside as substrate {ECO:0000269|PubMed:25468534};
CC Vmax=0.89 umol/min/mg enzyme with quercetin 3-O-beta-glucoside-7-O-
CC alpha-rhamnoside as substrate {ECO:0000269|PubMed:25468534};
CC Vmax=0.76 umol/min/mg enzyme with kaempferol 3-O-beta-glucoside as
CC substrate {ECO:0000269|PubMed:25468534};
CC Vmax=0.47 umol/min/mg enzyme with quercetin 3-O-beta-glucoside as
CC substrate {ECO:0000269|PubMed:25468534};
CC Vmax=3.37 umol/min/mg enzyme with p-nitrophenyl beta-D-glucoside as
CC substrate {ECO:0000269|PubMed:25468534};
CC Note=kcat is 1.30 sec(-1) with kaempferol 3-O-beta-glucoside-7-O-
CC alpha-rhamnoside as substrate. kcat is 1.10 sec(-1) with quercetin 3-
CC O-beta-glucoside-7-O-alpha-rhamnoside as substrate. kcat is 0.92
CC sec(-1) with kaempferol 3-O-beta-glucoside as substrate. kcat is 0.57
CC sec(-1) with quercetin 3-O-beta-glucoside as substrate. kcat is 4.08
CC sec(-1) with p-nitrophenyl beta-D-glucoside as substrate.
CC {ECO:0000269|PubMed:25468534};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:25468534};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000305|PubMed:25468534}.
CC -!- INDUCTION: Up-regulated during abiotic stress recovery.
CC {ECO:0000269|PubMed:25468534}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX818939; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC004521; AAC16091.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10421.1; -; Genomic_DNA.
DR EMBL; BX818939; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T02400; T02400.
DR RefSeq; NP_181973.1; NM_130008.3.
DR AlphaFoldDB; O64879; -.
DR SMR; O64879; -.
DR STRING; 3702.AT2G44450.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; O64879; -.
DR PRIDE; O64879; -.
DR ProteomicsDB; 240471; -.
DR EnsemblPlants; AT2G44450.1; AT2G44450.1; AT2G44450.
DR GeneID; 819052; -.
DR Gramene; AT2G44450.1; AT2G44450.1; AT2G44450.
DR KEGG; ath:AT2G44450; -.
DR Araport; AT2G44450; -.
DR TAIR; locus:2050605; AT2G44450.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; O64879; -.
DR OMA; PERITDH; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; O64879; -.
DR BioCyc; ARA:AT2G44450-MON; -.
DR PRO; PR:O64879; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64879; baseline and differential.
DR Genevisible; O64879; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
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:0033329; P:kaempferol O-glucoside metabolic process; IDA:UniProtKB.
DR GO; GO:0033302; P:quercetin O-glucoside metabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Apoplast; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..506
FT /note="Beta-glucosidase 15"
FT /id="PRO_0000389578"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 413
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 343
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 465..466
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 DISULFID 219..227
FT /evidence="ECO:0000250"
SQ SEQUENCE 506 AA; 56905 MW; 82FDFB3B52946DF9 CRC64;
MRGNYLSLLV VLIVLASNDV LANNNSSTPK LRRSDFPEDF IFGSATSAYQ VEGGAHEDGR
GPSIWDTFSE KYPEKIKDGS NGSVADNSYH LYKEDVALLH QIGFNAYRFS ISWSRILPRG
NLKGGINQAG IDYYNNLINE LLSKGIKPFA TMFHWDTPQA LEDAYGGFRG AEIVNDFRDY
ADICFKNFGD RVKHWMTLNE PLTVVQQGYV AGVMAPGRCS KFTNPNCTDG NGATEPYIVG
HNLILSHGAA VQVYREKYKA SQQGQVGIAL NAGWNLPYTE SPKDRLAAAR AMAFTFDYFM
EPLVTGKYPV DMVNNVKGRL PIFTAQQSKM LKGSYDFIGI NYYSSTYAKD VPCSTKDVTM
FSDPCASVTG ERDGVPIGPK AASDWLLIYP KGIRDLVLYA KYKFKDPVMY ITENGRDEFS
TNKIFLKDGD RIDYYARHLE MVQDAISVGA NVKGFFAWSL LDNFEWAMGY TVRFGLVYVD
FKDGCKRYPK KSAEWFRKLL NEKKND
