A0A5C7F139 · A0A5C7F139_9ACTN

  • 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

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site108Zn2+ (UniProtKB | ChEBI)
Binding site110Zn2+ (UniProtKB | ChEBI)
Binding site136Zn2+ (UniProtKB | ChEBI)
Binding site138Zn2+ (UniProtKB | ChEBI)
Binding site257ATP (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
      E4J93_04070

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • BA40
  • Taxonomic lineage
    Bacteria > Actinomycetota > Coriobacteriia > Coriobacteriales > Coriobacteriaceae > Collinsella

Accessions

  • Primary accession
    A0A5C7F139

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain4-323Glutamyl/glutaminyl-tRNA synthetase class Ib catalytic
Motif11-21'HIGH' region
Motif254-258'KMSKS' region
Domain357-486Aminoacyl-tRNA synthetase class I anticodon-binding

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    491
  • Mass (Da)
    53,801
  • Last updated
    2019-11-13 v1
  • Checksum
    A9E656F240A4C795
MSSNVRVRFAPSPTGKLHIGGARTAIYNWAFARANGGTFILRIDDTDPTRSTDENTQIILRAMRWLGLDWDEGPEVGGDFGPYSQTERLGLYKQTAERLLAEGKAYPCFCTPEQLAADREAAQARKDPFQGYQRRCRDLSPEEAQARIDAGEPYVLRIKVPQDRGNVVINDAVHGEVTFDAKELDDFVIFRSDGTPTYNFATVVDDALMGITHVIRGDDHLSNTPRQVIVYEAMGAPVPTFAHISMILGADGKKLSKRHGATSVEEYRDAGYLSDAFVNYLALLGWSLDGETTVIPRDVLASQFSLERISKNPATFDPKKLDWMNAEYINAMDDATFADEIMLPELLEAGLIDEGFEADEAWVDALAAIVRPRTKMPADAAAVAAPVFMTAETLEYDEKSVSKGLAKEGMGAVLDAARAALEAVTEWTPAHIDAALEPLPEALDVKKRLVFGAVRVAECGNMVSPPLGETMALIGRDDCLARIDRARPMAL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VOWY01000010
EMBL· GenBank· DDBJ
TXF36773.1
EMBL· GenBank· DDBJ
Genomic DNA

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