A0A926NWX1 · A0A926NWX1_9HYPH

  • Protein
    Glutamate--tRNA ligase
  • Gene
    gltX
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).

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 binding site.

147450100150200250300350400450
TypeIDPosition(s)Description
Binding site243ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular Functionglutamate-tRNA ligase activity
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological Processglutamyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glutamate--tRNA ligase
  • EC number
  • Alternative names
    • Glutamyl-tRNA synthetase
      (GluRS
      )

Gene names

    • Name
      gltX
    • ORF names
      HK439_21570

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • PHM038
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Stappiaceae > Roseibium

Accessions

  • Primary accession
    A0A926NWX1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain, motif, compositional bias, region.

TypeIDPosition(s)Description
Domain5-307Glutamyl/glutaminyl-tRNA synthetase class Ib catalytic
Motif11-21'HIGH' region
Compositional bias113-135Basic and acidic residues
Region113-137Disordered
Motif240-244'KMSKS' region
Domain342-471Aminoacyl-tRNA synthetase class I anticodon-binding

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    474
  • Mass (Da)
    52,581
  • Last updated
    2023-02-22 v1
  • Checksum
    65D0469459CD0374
MAQDVVTRFAPSPTGYLHIGGARTALFNWLFSRHHGGKMLLRIEDTDRARSTQEAVDAILDGLTWLGLDWDGEPISQASRVDRHKEVVEQMLAQGKAYRCYATQEDLAAMREKARAEGRPPRYDGTWRDRDPSEAPEGVAPAIRLKAPLEGETVVDDLVQGRVTFPNKDLDDLVLMRSDGTPTYMLAVVVDDHDMGITHIIRGDDHLTNAARQTLIFQAMGWDVPVMAHIPLIHGPDGAKLSKRHGALGAEAYRAMGYLPEAMRNYLARLGWSHGDEEIMSTDDMIKWFGMEAVGKSPARFDFKKLENLNGHYMRATADAELLQHWKTCLEHIDGGQDVLAWLAEADHEATALAALPGLKERAKTLVELTESASYLWRQRPLDCDEKAANILNDEARALLSGLHETLSAVPTWEAEALEVSVKAFAEEKELKLGKVAQPLRAALTGRGTSPGIYDVLVALGREESLNRIRDQAI

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias113-135Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABFCZ010000027
EMBL· GenBank· DDBJ
MBD1548862.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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