A0A090WIX7 · A0A090WIX7_9FLAO

  • Protein
    Multifunctional fusion protein
  • Gene
    gatB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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).
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Features

Showing features for site, binding site.

TypeIDPosition(s)Description
Site548Important for tRNA non-discrimination
Binding site692L-aspartate (UniProtKB | ChEBI)
Binding site738L-aspartate (UniProtKB | ChEBI)
Binding site738-740ATP (UniProtKB | ChEBI)
Binding site747ATP (UniProtKB | ChEBI)
Binding site969L-aspartate (UniProtKB | ChEBI)
Binding site1007ATP (UniProtKB | ChEBI)
Binding site1014L-aspartate (UniProtKB | ChEBI)
Binding site1059-1062ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionaspartate-tRNA ligase activity
Molecular Functionaspartate-tRNA(Asn) ligase activity
Molecular FunctionATP binding
Molecular Functionglutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
Molecular Functionnucleic acid binding
Molecular Functiontransferase activity
Biological Processaspartyl-tRNA aminoacylation
Biological Processglutaminyl-tRNAGln biosynthesis via transamidation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    Aspartate--tRNA(Asp/Asn) ligase
  • EC number
  • Alternative names
    • Aspartyl-tRNA synthetase
    • Non-discriminating aspartyl-tRNA synthetase
      (AspRS
      ; ND-AspRS
      )
  • Recommended name
    Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
  • EC number
  • Short names
    Asp/Glu-ADT subunit B

Gene names

    • Name
      gatB
    • Synonyms
      aspS
    • ORF names
      JCM19301_410
      , JCM19538_1214

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • JCM 19301
    • JCM 19538
  • Taxonomic lineage
    Bacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Flavobacteriaceae > Jejuia

Accessions

  • Primary accession
    A0A090WIX7

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Heterotrimer of A, B and C subunits.
Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain662-1080Aminoacyl-transfer RNA synthetases class-II family profile
Region716-719Aspartate

Sequence similarities

Belongs to the GatB/GatE family. GatB subfamily.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,111
  • Mass (Da)
    125,888
  • Last updated
    2014-11-26 v1
  • Checksum
    F42C9CFF7FA2C61F
MELEQLNEQLKKHELELVIGLETHVRLNTKTKLFCSCPNQEIETPNQNICSVCTGQMGVLPAINKEAIKKAIYFGKAVKSTFENEIISWDRKHYEYPDNPKNIQITQFHHPIIPDGQVSCFRNDGSQFTVNLTQVHIEEDAAKLMHEKKVSLVDFNKAGVPLIEIVTEPCIRHIEDASIYAQYIQRIVQNLGISEANLEKGEFKSDVSVSLRKRRSYKLNPRTEIKNLNSFKFMVEALKEEVEKQLNYFLEHKEFRPDQTTVLFDADLKQTKTMRKKEFEADYRFISEPDLPFVNIKDVVDNISVDISSLPFAVESILIKGGVLPQDAKFFTADAVRSKTFVAINDVIKDPSFVAKTLVNNIGAEEYGNIHRIEHLIEIFQMFKAEKITSVLVQNAITAYLKDRTFDYNKYFEDNTISQSQIDEAIAKVISENEAIANDIKSGNQGKAGILVGKVIGIIGKGAPGKVIRESILAQLAADSLATTHAETASKQSAKSSAEKQAAEEETLPQIPIVIKEQYRSHKASELSEASISQKVTLAGWVSSVRDHGELIFIDLRDSSHEIFQVRLSRESFPNLDELVKLKPESVITVTGEVVQRKADDYNPALRTGTIELETSELDILNLSKTLPFEIKRAHKSNETVRFKYKYLDHRNDDVRRAIINRHKVIKLMRDLLDEQEFLEVETPILTAGTDEGAREFIVPTRKKAGSFYTLPQAPQQFKQILMVSGYEKYFQIARCFRDEDSRGDRQPEFTQLDIEMAYASMQDIIDLSTNMFNEIVTRIYGKKWILHPFEVLTYKEAMDYYGCDRPDLRFGLKLQDITNIVKDTTFQVFSKPIDEGGIVKCIRVSVEEQGKKRLSKGQIEKLTGIAQEHGLGGLAYIIVNENDLQSPIIKFLGEDIAKNIIKTTNAQVGDIVFFSAADYETANKALDAVRQELGSMLKLINPKELRPAWVVDFPMFEKTEEGNWTFTHNPFSMPAVKDIEKHINGKEEEIGSIIAQQYDLILNGFEIGGGSVRAHKPEILEATYKNMGYNKEDMMKSVGTMYNAFHYGAPPHGGIAWGVDRLMMILEKKASIREVMAFPKTGTSEDLLFGSPSPLSDKKVEEMNVKVIRN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BBNR01000010
EMBL· GenBank· DDBJ
GAL67437.1
EMBL· GenBank· DDBJ
Genomic DNA
BBNY01000004
EMBL· GenBank· DDBJ
GAL88779.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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