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Protein

Beta-glucosidase 15

Gene

BGLU15

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Beta-glucosidase involved in the rapid degradation of flavonol 3-O-beta-glucoside-7-O-alpha-rhamnosides during abiotic stress recovery. No activity with quercetin 3-O-alpha-rhamnoside, quercetin 3-O-beta-galactoside and rutin.1 Publication

Catalytic activityi

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

Kineticsi

kcat is 1.30 sec(-1) with kaempferol 3-O-beta-glucoside-7-O-alpha-rhamnoside as substrate. kcat is 1.10 sec(-1) with quercetin 3-O-beta-glucoside-7-O-alpha-rhamnoside as substrate. kcat is 0.92 sec(-1) with kaempferol 3-O-beta-glucoside as substrate. kcat is 0.57 sec(-1) with quercetin 3-O-beta-glucoside as substrate. kcat is 4.08 sec(-1) with p-nitrophenyl beta-D-glucoside as substrate.1 Publication

  1. KM=51 µM for kaempferol 3-O-beta-glucoside-7-O-alpha-rhamnoside1 Publication
  2. KM=36 µM for quercetin 3-O-beta-glucoside-7-O-alpha-rhamnoside1 Publication
  3. KM=60 µM for kaempferol 3-O-beta-glucoside1 Publication
  4. KM=52 µM for quercetin 3-O-beta-glucoside1 Publication
  5. KM=2592 µM for p-nitrophenyl beta-D-glucoside1 Publication

Vmax=1.08 µmol/min/mg enzyme with kaempferol 3-O-beta-glucoside-7-O-alpha-rhamnoside as substrate1 Publication

Vmax=0.89 µmol/min/mg enzyme with quercetin 3-O-beta-glucoside-7-O-alpha-rhamnoside as substrate1 Publication

Vmax=0.76 µmol/min/mg enzyme with kaempferol 3-O-beta-glucoside as substrate1 Publication

Vmax=0.47 µmol/min/mg enzyme with quercetin 3-O-beta-glucoside as substrate1 Publication

Vmax=3.37 µmol/min/mg enzyme with p-nitrophenyl beta-D-glucoside as substrate1 Publication

pH dependencei

Optimum pH is 5.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501SubstrateBy similarity
Binding sitei154 – 1541SubstrateBy similarity
Binding sitei199 – 1991SubstrateBy similarity
Active sitei200 – 2001Proton donorBy similarity
Binding sitei343 – 3431SubstrateBy similarity
Active sitei413 – 4131NucleophileBy similarity
Binding sitei458 – 4581SubstrateBy similarity

GO - Molecular functioni

  1. beta-glucosidase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. kaempferol O-glucoside metabolic process Source: UniProtKB
  3. quercetin O-glucoside metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciARA:AT2G44450-MONOMER.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-glucosidase 15 (EC:3.2.1.21)
Short name:
AtBGLU15
Gene namesi
Name:BGLU15
Ordered Locus Names:At2g44450
ORF Names:F4I1.26
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G44450.

Subcellular locationi

Secretedextracellular spaceapoplast 1 Publication

GO - Cellular componenti

  1. apoplast Source: UniProtKB-SubCell
  2. cell wall Source: TAIR
  3. Golgi apparatus Source: TAIR
  4. plant-type cell wall Source: TAIR
  5. plasmodesma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Apoplast, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 506484Beta-glucosidase 15PRO_0000389578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi24 – 241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi25 – 251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi219 ↔ 227By similarity
Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO64879.
PRIDEiO64879.

Expressioni

Inductioni

Up-regulated during abiotic stress recovery.1 Publication

Gene expression databases

GenevestigatoriO64879.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT2G44450.1-P.

Structurei

3D structure databases

ProteinModelPortaliO64879.
SMRiO64879. Positions 29-500.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni465 – 4662Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088630.
InParanoidiO64879.
KOiK01188.
OMAiYSSTYAK.
PhylomeDBiO64879.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O64879-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGNYLSLLV VLIVLASNDV LANNNSSTPK LRRSDFPEDF IFGSATSAYQ
60 70 80 90 100
VEGGAHEDGR GPSIWDTFSE KYPEKIKDGS NGSVADNSYH LYKEDVALLH
110 120 130 140 150
QIGFNAYRFS ISWSRILPRG NLKGGINQAG IDYYNNLINE LLSKGIKPFA
160 170 180 190 200
TMFHWDTPQA LEDAYGGFRG AEIVNDFRDY ADICFKNFGD RVKHWMTLNE
210 220 230 240 250
PLTVVQQGYV AGVMAPGRCS KFTNPNCTDG NGATEPYIVG HNLILSHGAA
260 270 280 290 300
VQVYREKYKA SQQGQVGIAL NAGWNLPYTE SPKDRLAAAR AMAFTFDYFM
310 320 330 340 350
EPLVTGKYPV DMVNNVKGRL PIFTAQQSKM LKGSYDFIGI NYYSSTYAKD
360 370 380 390 400
VPCSTKDVTM FSDPCASVTG ERDGVPIGPK AASDWLLIYP KGIRDLVLYA
410 420 430 440 450
KYKFKDPVMY ITENGRDEFS TNKIFLKDGD RIDYYARHLE MVQDAISVGA
460 470 480 490 500
NVKGFFAWSL LDNFEWAMGY TVRFGLVYVD FKDGCKRYPK KSAEWFRKLL

NEKKND
Length:506
Mass (Da):56,905
Last modified:August 1, 1998 - v1
Checksum:i82FDFB3B52946DF9
GO

Sequence cautioni

The sequence BX818939 differs from that shown.Sequencing errors.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC004521 Genomic DNA. Translation: AAC16091.1.
CP002685 Genomic DNA. Translation: AEC10421.1.
BX818939 mRNA. No translation available.
PIRiT02400.
RefSeqiNP_181973.1. NM_130008.2.
UniGeneiAt.43824.

Genome annotation databases

EnsemblPlantsiAT2G44450.1; AT2G44450.1; AT2G44450.
GeneIDi819052.
KEGGiath:AT2G44450.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC004521 Genomic DNA. Translation: AAC16091.1.
CP002685 Genomic DNA. Translation: AEC10421.1.
BX818939 mRNA. No translation available.
PIRiT02400.
RefSeqiNP_181973.1. NM_130008.2.
UniGeneiAt.43824.

3D structure databases

ProteinModelPortaliO64879.
SMRiO64879. Positions 29-500.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT2G44450.1-P.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbiO64879.
PRIDEiO64879.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G44450.1; AT2G44450.1; AT2G44450.
GeneIDi819052.
KEGGiath:AT2G44450.

Organism-specific databases

TAIRiAT2G44450.

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088630.
InParanoidiO64879.
KOiK01188.
OMAiYSSTYAK.
PhylomeDBiO64879.

Enzyme and pathway databases

BioCyciARA:AT2G44450-MONOMER.

Gene expression databases

GenevestigatoriO64879.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation."
    Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., Weissenbach J., Salanoubat M.
    Genome Res. 14:406-413(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-506.
    Strain: cv. Columbia.
  4. Cited for: GENE FAMILY, NOMENCLATURE.
  5. "Arabidopsis thaliana beta-glucosidase BGLU15 attacks flavonol 3-O-beta-glucoside-7-O-alpha-rhamnosides."
    Roepke J., Bozzo G.G.
    Phytochemistry 109:14-24(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.

Entry informationi

Entry nameiBGL15_ARATH
AccessioniPrimary (citable) accession number: O64879
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: August 1, 1998
Last modified: April 1, 2015
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.