A9QW82 · A9QW82_HORVU

  • Protein
    Glucose-1-phosphate adenylyltransferase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

Function

function

This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.

Catalytic activity

Pathway

Glycan biosynthesis; starch biosynthesis.

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
Cellular Componentchloroplast
Molecular FunctionATP binding
Molecular Functionglucose-1-phosphate adenylyltransferase activity
Biological Processglycogen biosynthetic process
Biological Processstarch biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glucose-1-phosphate adenylyltransferase
  • EC number
  • Alternative names
    • ADP-glucose pyrophosphorylase

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Pooideae > Triticodae > Triticeae > Hordeinae > Hordeum

Accessions

  • Primary accession
    A9QW82

Subcellular Location

Keywords

Expression

Gene expression databases

Interaction

Subunit

Heterotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain86-358Nucleotidyl transferase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    513
  • Mass (Da)
    56,215
  • Last updated
    2008-02-05 v1
  • Checksum
    130A5718072EB92A
MAMAAAASPSKILIPPHRASAVTAAASTSCDSLRLLCAPRGRRQRPRGLVARPVPRRPFFFSPRAVSDSKSSQTCLDPDASTNVLGIILGGGAGTRLYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYGSNIGGYKNEGFVEVLAAQQSPDNPDWFQGTADAVRQYLWPFEEHNVMEYLILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEERAAFGLMKIDEEGRIIEFAEKPKGEQLKAMMVDTTILGLEDARAKEMPYIASMGIYVISKHVMLQLLREQFPGANDFGSEVIPGATSTGMRVQAYLYDGYWEDIGTIEAFYNANLGITKKPIPDFSFYDRSAPIYTQPRHLPPSKVLDADVTDSVIGVGCVIKNCKIHHSVVGLRSCISEGAIIEDTLLMGADYYETEADKKLLAEKGGIPIGIGKNSHIKRAIIDKNARIGDNVMIINVDNVQEAARETDGYFIKSGIVTVIKDALLPSGTVI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
EU275212
EMBL· GenBank· DDBJ
ABX72229.1
EMBL· GenBank· DDBJ
mRNA

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