A0A7Z2QC22 · A0A7Z2QC22_9BACI

  • Protein
    asparagine synthase (glutamine-hydrolyzing)
  • Gene
    asnB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    2/5

Function

Catalytic activity

Pathway

Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1.

Features

Showing features for active site, binding site, site.

161350100150200250300350400450500550600
TypeIDPosition(s)Description
Active site2For GATase activity
Binding site102L-glutamine (UniProtKB | ChEBI)
Binding site292ATP (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
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

    • Name
      asnB
    • ORF names
      GNK04_08810

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • N1-1
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus

Accessions

  • Primary accession
    A0A7Z2QC22

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-214Glutamine amidotransferase type-2

Sequence similarities

Belongs to the asparagine synthetase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    613
  • Mass (Da)
    69,790
  • Last updated
    2021-06-02 v1
  • Checksum
    1FB174B46E27E034
MCGITGWVDWKKNLTGEEKVLQDMAQTLSKRGPDASNDWVDGHCGFGHTRLVVVDPAGGSQPMTRKHGDINYTICYNGELYNTEDLRKVLLGKGYTFQSHSDTEVLLTCYVEWGEQCVDHLNGIFAFGIWDGERLFLARDRLGVKPLFYRQSGSSLQFGSELKAILAHPDVKKEIDRGGLQEIFGLGPSRTPGHGVFRGISELRPGFAMKFDRSGLRIWRYWNVVSNEHTDNLDTTVEKVGDLLKDSIKRQLVADVPVCTFLSGGVDSSAITSVARSAFQDDGKGTLRSFSVDYVDNDKYFKSSEFQPNSDAPWIKKVSAELATDHTNCVIDTAQLVHHLKEAIECRDLPGMADVDSSLLWFSKEIKKHATVALSGECADEIFGGYPWFHKPELLDQEQFPWMRSTLERQAMLKEDVRNKLKLEDYVIERYRESIKETPALDGESEIEAKRRALFYLNLNWFMTTLLERKDRMSMGASLEVRVPFSDHRIIEYVWNVPWEMKMLDGREKGLLRKAMTGTLSHDVLYRKKSPYPKTYNPAYTKAVSSWLQDTLNNKQAPLLELIDQKVVQEIIDSEGKAFKVPWFGQLMAGPQLIAHLAQINYWMEHHNVNLVD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP046564
EMBL· GenBank· DDBJ
QHA91515.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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