Q93ZI4 · BGL10_ARATH

Function

Catalytic activity

  • Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
    EC:3.2.1.21 (UniProtKB | ENZYME | Rhea)

Features

Showing features for binding site, active site.

150850100150200250300350400450500
TypeIDPosition(s)Description
Binding site42a beta-D-glucoside (UniProtKB | ChEBI)
Binding site142a beta-D-glucoside (UniProtKB | ChEBI)
Binding site187-188a beta-D-glucoside (UniProtKB | ChEBI)
Active site188Proton donor
Binding site331a beta-D-glucoside (UniProtKB | ChEBI)
Active site398Nucleophile
Binding site398a beta-D-glucoside (UniProtKB | ChEBI)
Binding site441a beta-D-glucoside (UniProtKB | ChEBI)
Binding site457a beta-D-glucoside (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentplant-type vacuole
Molecular Functionbeta-glucosidase activity
Molecular Functionscopolin beta-glucosidase activity
Biological Processanthocyanin-containing compound metabolic process
Biological Processcarbohydrate metabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

    • GH1Glycoside Hydrolase Family 1

Names & Taxonomy

Protein names

  • Recommended name
    Beta-glucosidase 10
  • EC number
  • Short names
    AtBGLU10

Gene names

    • Name
      BGLU10
    • ORF names
      T27E11.70
    • Ordered locus names
      At4g27830

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q93ZI4
  • Secondary accessions
    • Q9STP3

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-22
ChainPRO_000038957223-508Beta-glucosidase 10
Disulfide bond207↔215
Glycosylation214N-linked (GlcNAc...) asparagine
Glycosylation219N-linked (GlcNAc...) asparagine
Glycosylation365N-linked (GlcNAc...) asparagine
Glycosylation431N-linked (GlcNAc...) asparagine
Glycosylation463N-linked (GlcNAc...) asparagine
Glycosylation485N-linked (GlcNAc...) asparagine
Glycosylation501N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    508
  • Mass (Da)
    57,078
  • Last updated
    2001-12-01 v1
  • Checksum
    47458C35740A6D20
MKLYSLLSVFLVILLATSDSDAFTRNNFPKDFLFGAATSAYQWEGAVAEDGRTPSVWDTFSHTYNRGNLGNGDITSDGYHKYKEDVKLMAEMGLESFRFSISWSRLIPNGRGLINPKGLLFYKNLIKELISHGIEPHVTLYHYDLPQSLEDEYGGWINRKIIEDFTAYADVCFREFGEDVKLWTTINEATIFAIGSYDQGISPPGHCSPNKFINCTSGNSSTEPYLAGHNILLAHASASKLYKLKYKSTQKGSIGLSIFAFGLSPYTNSKDDEIATQRAKAFFYGWMLKPLVFGDYPDEMKRTVGSRLPVFSEEESEQLKGSSDFIGIIHYTTFYVTNKPSPSIFPSMNEGFFKDMGVYMISAANSSFLLWEATPWGLEGILEYIKQSYNNPPIYILENGMPMGRDSTLQDTQRIEFIQAYIGAMLNAIKNGSDTRGYFVWSMIDLYELLSGYTTSFGMYYVNFSDPGRKRTPKLSASWYTGFLNGTIDVATQDTIQLQSNISGSSSL

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1P8B4J5A0A1P8B4J5_ARATHBGLU10420

Sequence caution

The sequence CAB43971.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence CAB81432.1 differs from that shown. Reason: Erroneous gene model prediction

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL078579
EMBL· GenBank· DDBJ
CAB43971.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AL161571
EMBL· GenBank· DDBJ
CAB81432.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002687
EMBL· GenBank· DDBJ
AEE85398.1
EMBL· GenBank· DDBJ
Genomic DNA
AY057518
EMBL· GenBank· DDBJ
AAL09758.1
EMBL· GenBank· DDBJ
mRNA
BT002654
EMBL· GenBank· DDBJ
AAO11570.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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