O65399 · E131_ARATH

Function

Catalytic activity

  • Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
    EC:3.2.1.39 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

151150100150200250300350400450500
TypeIDPosition(s)Description
Active site137Proton donor
Active site284Nucleophile

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 Componentextracellular region
Cellular Componentplasma membrane
Cellular Componentside of membrane
Molecular Functionglucan endo-1,3-beta-D-glucosidase activity
Biological Processcarbohydrate metabolic process
Biological Processdefense response

Keywords

Enzyme and pathway databases

Protein family/group databases

    • CBM43Carbohydrate-Binding Module Family 43
    • GH17Glycoside Hydrolase Family 17

Names & Taxonomy

Protein names

  • Recommended name
    Glucan endo-1,3-beta-glucosidase 1
  • EC number
  • Alternative names
    • (1->3)-beta-glucan endohydrolase 1 ((1->3)-beta-glucanase 1)
    • Beta-1,3-endoglucanase 1 (Beta-1,3-glucanase 1)

Gene names

    • ORF names
      F12F1.33, F25C20_1
    • Ordered locus names
      At1g11820

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
    O65399
  • Secondary accessions
    • F4IAH7
    • Q84W37

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

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

Type
IDPosition(s)Description
Signal1-28
ChainPRO_000001188429-485Glucan endo-1,3-beta-glucosidase 1
Glycosylation109N-linked (GlcNAc...) asparagine
Glycosylation192N-linked (GlcNAc...) asparagine
Glycosylation274N-linked (GlcNAc...) asparagine
Glycosylation374N-linked (GlcNAc...) asparagine
Glycosylation378N-linked (GlcNAc...) asparagine
Disulfide bond382↔445
Glycosylation407N-linked (GlcNAc...) asparagine
Glycosylation473N-linked (GlcNAc...) asparagine
Glycosylation480N-linked (GlcNAc...) asparagine
Lipidation485GPI-anchor amidated alanine
PropeptidePRO_0000011885486-511Removed in mature form

Post-translational modification

Contains two additional disulfide bonds.

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.

O65399-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    511
  • Mass (Da)
    55,630
  • Last updated
    2011-11-16 v3
  • Checksum
    1C29693D4F94E8C4
MAFTSMVSTVPVLFFFFTLLLISANSSSLSHNIKVQEQDKDPFVGFNIGTDVSNLLSPTELVKFLQAQKVNHVRLYDADPELLKALAKTKVRVIISVPNNQLLAIGSSNSTAASWIGRNVVAYYPETLITAISVGDEVLTTVPSSAPLLLPAIESLYNALVASNLHTQIKVSTPHAASIMLDTFPPSQAYFNQTWHSIMVPLLQFLSKTGSPLMMNLYPYYVYMQNKGVVPLDNCLFEPLTPSKEMVDPNTLLHYTNVLDAMVDAAYVSMKNLNVSDVAVLVTESGWPSKGDSKEPYATIDNADTYNSNLIKHVFDRTGTPLHPEMTSSVYIYELFNEDLRAPPVSEASWGLFYGNSTPVYLLHVSGSGTFLANDTTNQTYCIAMDGVDAKTLQAALDWACGPGRSNCSEIQPGESCYQPNNVKGHASFAFNSYYQKEGRASGSCDFKGVAMITTTDPSHGSCIFPGSKKVGNRTQTVVNSTEVAAGEATSRSLSRGFCVTIMILVTFSIL

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1P8AWX9A0A1P8AWX9_ARATHAt1g11820477
F4IAH8F4IAH8_ARATHAt1g11820384

Sequence caution

The sequence AAC17632.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence AAO42272.1 differs from that shown. Reason: Miscellaneous discrepancy Probable cloning artifact leading to a deletion into the sequence.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC002131
EMBL· GenBank· DDBJ
AAC17632.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AC007296
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CP002684
EMBL· GenBank· DDBJ
AEE28791.1
EMBL· GenBank· DDBJ
Genomic DNA
BT004271
EMBL· GenBank· DDBJ
AAO42272.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.

Genome annotation databases

Similar Proteins

Disclaimer

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