W7LXK0 · W7LXK0_GIBM7

Function

Catalytic activity

Pathway

Amino-acid biosynthesis.

Features

Showing features for active site, binding site, site.

157950100150200250300350400450500550
TypeIDPosition(s)Description
Active site2For GATase activity
Binding site98L-glutamine (UniProtKB | ChEBI)
Binding site234ATP (UniProtKB | ChEBI)
Binding site301ATP (UniProtKB | ChEBI)
Binding site375-376ATP (UniProtKB | ChEBI)
Site377Important for beta-aspartyl-AMP intermediate formation

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosol
Molecular Functionasparagine synthase (glutamine-hydrolyzing) activity
Molecular FunctionATP binding
Biological Processasparagine biosynthetic process
Biological Processglutamine metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    asparagine synthase (glutamine-hydrolyzing)
  • EC number

Gene names

    • ORF names
      FVEG_02650

Organism names

Accessions

  • Primary accession
    W7LXK0

Proteomes

Organism-specific databases

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain2-187Glutamine amidotransferase type-2
Region560-579Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    579
  • Mass (Da)
    65,535
  • Last updated
    2014-04-16 v1
  • Checksum
    1BE807ACC2226462
MCGIFACHRHPDVEKFKPTALKLAKQIRHRGPDWSGSVIANHTILCHERLSIVGVESGAQPLTNADDSIILAVNGEIYNHRHIRKNLKEQYHFKTTSDCEVIIPLYTEFDTDCPNHLDGMFSFVLYDKKQDRTIAARDPIGITTFYQGWSSKEPGTVYFASELKCLHSVCDKIVAFPPGHVYDSKTGETTRYFNPSWWDPKKVPSNPVDYKVLRHALEKAVRKRLMAEVPFGVLLSGGLDSSLTASIAQREVTRLRKQALEANGNVLPVENPDTGEGLVGVDDDDHLDTLTYLPQLNSFSIGLPGSPDNKAALEVAKFLGTKHHVMTFTIEDGLNALSDVIFHLETYDVTTIRASTPMYLLSRKIKAMGIKMVLSGEGSDEIFGGYLYFHAAPDKEAFHEETVRRVKNLHLADCLRANKSTSAWGLEARVPFLDKEFLETSMNIDPQEKMITKDRLEKYIIRKAFDTSDEPDEQPYLPDNILWRQKEQFSDGVGYGWIDALKDNAEKQVTDEMMKNPKPEWGNDIPDTKEAYWYRCMFDEHFPPHCASTVMRWTPTWSKQTDPSGRAISTHNAKYDNAA

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
W7LNQ1W7LNQ1_GIBM7FVEG_02650490
W7LL55W7LL55_GIBM7FVEG_02650457
W7M5F4W7M5F4_GIBM7FVEG_02650486
W7LXB7W7LXB7_GIBM7FVEG_02650449
W7LXB2W7LXB2_GIBM7FVEG_02650546

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS022244
EMBL· GenBank· DDBJ
EWG40119.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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