A0A517PJ32 · A0A517PJ32_9PLAN

  • Protein
    Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
  • Gene
    gatB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).

Catalytic activity

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 Functionasparaginyl-tRNA synthase (glutamine-hydrolyzing) activity
Molecular FunctionATP binding
Molecular Functionglutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
Molecular Functiontransferase activity
Biological Processglutaminyl-tRNAGln biosynthesis via transamidation
Biological Processtranslation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
  • EC number
  • Short names
    Asp/Glu-ADT subunit B

Gene names

    • Name
      gatB
    • ORF names
      HG66A1_11440

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • HG66A1
  • Taxonomic lineage
    Bacteria > Planctomycetota > Planctomycetia > Planctomycetales > Planctomycetaceae > Gimesia

Accessions

  • Primary accession
    A0A517PJ32

Proteomes

Interaction

Subunit

Heterotrimer of A, B and C subunits.

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias128-145Basic and acidic residues
Region128-147Disordered
Domain341-491Asn/Gln amidotransferase

Sequence similarities

Belongs to the GatB/GatE family. GatB subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    492
  • Mass (Da)
    55,203
  • Last updated
    2019-10-16 v1
  • Checksum
    E0A1E13CBB27534E
MDYTVIIGLEVHVQLQTKTKLFCGCSTKFNPDQPNTQTCPVCLGLPGALPVLNREAFRLGMKTGLAINCEIPSFTKWDRKQYYYPDLPKAYQISQYDLPMSQNGWLEIEIDPETRETKKVGIIRAHLEEDAGKNSHDESGRGQDSKVDLNRCGTPLVEIVSEPDLRSAQEARKYLEELKLLLTYIDVSDCNMQEGSLRCDANVNLHIHQENGDAIATTIVEIKNLNSFRGVEQAIEYEVKRQWEEWQKTGLTLKEVFKETRGWDADRGITLGQRSKEDVADYRYFPDPDLAPVTVTDAEREEVMNELCERPANRRNRFQADYGLSTYDAAVIIDQGIAFADYFETVAQGCDNGKQAANWVTQDVQRELNERSCQIADFPIRPEVLAALLQKVEASEITIKSARTVFQVLLEEDASSVERIQAVIDEKGLGLVSDTGELEAIVETVVAKNEKAVADFQSGKQAAVGALIGQVMREIKGADAKVVRELLIKKMS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias128-145Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP036266
EMBL· GenBank· DDBJ
QDT19379.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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