A0A220NV46 · A0A220NV46_9ROSI

Function

Catalytic activity

  • Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.
    EC:2.4.1.18 (UniProtKB | ENZYME | Rhea)

Pathway

Glycan biosynthesis; starch biosynthesis.

Features

Showing features for active site.

1865100200300400500600700800
TypeIDPosition(s)Description
Active site505Nucleophile
Active site560Proton 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
Cellular Componentamyloplast
Molecular Function1,4-alpha-glucan branching enzyme activity
Molecular Function1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis)
Molecular Functioncation binding
Molecular Functionhydrolase activity, hydrolyzing O-glycosyl compounds
Biological Processglycogen biosynthetic process
Biological Processstarch biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    1,4-alpha-glucan branching enzyme
  • EC number

Gene names

    • Name
      SBEII

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fagales > Fagaceae > Castanea

Accessions

  • Primary accession
    A0A220NV46

Subcellular Location

Keywords

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias72-88Polar residues
Region72-106Disordered
Region125-150Disordered
Domain362-722Glycosyl hydrolase family 13 catalytic

Sequence similarities

Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    865
  • Mass (Da)
    98,761
  • Last updated
    2017-10-25 v1
  • Checksum
    0ED4956BF90215F0
MVYTISGIRFPAVSPLCNRSRSNFVGNRCSNISLLPTKDSFSRKIFAGKSSPDSDSSSLTVAASNKILVPGSQGDGSLSLTDQLDNPETVLKDPQGLHDVDNQTMENDKKLKDEEHFVESIRGYNEVQHEQESAASSLVGDDSRAQGKKPSVHIAKTITIEKDEVRPRTIPPPGPGHGIYEIDPLLNNYREHLDYRYGQYKKLREAIDKNEGGLEVFSRGYEKFGFIRSDTGITYREWAPGAKSAALIGDFNNWNPNADVMTRNEFGVWEIFLPNNADGSPPIPHCSRVKIRMDTPSGIKDSIPAWIKFSVQAPGEIPYNGIYYDPPEEEKYVFKYPQPKRPKSLRIYEAHVGMSSTEPKINTYANFRDDVLPRIKKLGYNAVQIMAIQEHSYYASFGYHVTNFFAPSSRCGTPDDLKSLIDKAHELGLLVLMDIVHSHASNNVLDGLNLLDGTDSHYFHSGSRGYHWMWDSRLFNYGSWEVIRYLLSNARWWLEEYKFDGFRFDGVTSMMYTHHGLQVAFTGNYTEYFGLATDVDAVVYLMLVNDVIHGLFPEAVSIGEDVSGMPAFCIPVQDGGVGFDYRLHMAIADKWIELLKKKDEDWRMGDIVHTLTNRRWLEKCVSYAESHDQALVGDKTIAFWLMDKDMYDFMALDRPSTPLVDRGIALHKMIRLITMGLGGEGYLNFMGNEFGHPEWIDFPRGDQHLPDGRIILGNNNSYDKCRRRFDLGDAEYLRYHGMQEFDRAMQHIEETYCFMTSEHQYVSRKDEGDKVIVFERGNLVFVFNFHWTNSYSDYRVGCFKPGKYKIVLDSDDALFGGFNRIDHSAEYFSFDGWYDKRPRSFLVYAPCRTAVVYALVEDEPEPVKH

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias72-88Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KY429028
EMBL· GenBank· DDBJ
ASJ80803.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp