O04931 · AGLU_BETVU

Function

function

High activity for alpha-glucan.

Catalytic activity

  • Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.
    EC:3.2.1.20 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

1913100200300400500600700800900
TypeIDPosition(s)Description
Active site469
Active site472
Active site568Proton donor

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
Molecular Functionalpha-1,4-glucosidase activity
Molecular Functioncarbohydrate binding
Biological Processcarbohydrate metabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Alpha-glucosidase
  • EC number
  • Alternative names
    • Maltase

Organism names

  • Taxonomic identifier
  • Strain
    • cv. NK-152
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > Caryophyllales > Chenopodiaceae > Betoideae > Beta

Accessions

  • Primary accession
    O04931

Phenotypes & Variants

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-28
ChainPRO_000001858229-913Alpha-glucosidase
Glycosylation54N-linked (GlcNAc...) asparagine
Glycosylation404N-linked (GlcNAc...) asparagine
Glycosylation495N-linked (GlcNAc...) asparagine
Glycosylation517N-linked (GlcNAc...) asparagine
Glycosylation728N-linked (GlcNAc...) asparagine
Glycosylation823N-linked (GlcNAc...) asparagine

Post-translational modification

The N-terminus is blocked.

Keywords

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region106-142Disordered
Compositional bias109-128Pro residues

Sequence similarities

Belongs to the glycosyl hydrolase 31 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    913
  • Mass (Da)
    102,117
  • Last updated
    1997-07-01 v1
  • Checksum
    02AC4F0B505369CC
MERSKLPRYICPTLAVVLPLVLCMVVEGATTSKNDNQGEAIGYGYQVKNAKVDNSTGKSLTALLQLIRNSPVYGPDIHFLSFTASFEEDDTLRIRFTDANNRRWEIPNEVLPRPPPPPSPPPLSSLQHLPKPIPQNQPTTTVLSHPHSDLAFTLFHTTPFGFTIYRKSTHDVLFDATPIPSNPTTFLIYKDQYLQLSSSLPAQQAHLYGLGEHTKPTFQLAHNQILTLWNADIASFNRDLNLYGSHPFYMDVRSSPMVGSTHGVFLLNSNGMDVEYTGDRITYKVIGGIIDLYIFAGRTPEMVLDQYTKLIGRPAPMPYWAFGFHQCRWGYRDVNEIETVVDKYAEARIPLEVMWTDIDYMDAFKDFTLDPVHFPLDKMQQFVTKLHRNGQRYVPILDPGINTNKSYGTFIRGMQSNVFIKRNGNPYLGSVWPGPVYYPDFLDPAARSFWVDEIKRFRDILPIDGIWIDMNEASNFITSAPTPGSTLDNPPYKINNSGGRVPINSKTIPATAMHYGNVTEYNAHNLYGFLESQATREALVRPATRGPFLLSRSTFAGSGKYTAHWTGDNAARWDDLQYSIPTMLNFGLFGMPMIGADICGFAESTTEELCCRWIQLGAFYPFSRDHSARDTTHQELYLWESVAASARTVLGLRYELLPYYYTLMYDANLRGSPIARPLSFTFPDDVATYGISSQFLIGRGIMVSPVLQPGSSIVNAYSPRGNWVSLSNYTSSVSVSAGTYVSLSAPPDHINVHIHEGNIVAMQGEAMTTQAARSTPFHLLVVMSDHVASTGELFLDNGIEMDIGGPGGKWTLVRFFAESGINNLTISSEVVNRGYAMSQRWVMDKITILGLKRRVKIKEYTVQKDAGAIKVKGLGRRTSSHNQGGFFVSVISDLRQLVGQAFKLELEFEGATR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias109-128Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D89615
EMBL· GenBank· DDBJ
BAA20343.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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