A5I0T6 · SYE_CLOBH

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).

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

148550100150200250300350400450
TypeIDPosition(s)Description
Binding site108Zn2+ (UniProtKB | ChEBI)
Binding site110Zn2+ (UniProtKB | ChEBI)
Binding site135Zn2+ (UniProtKB | ChEBI)
Binding site137Zn2+ (UniProtKB | ChEBI)
Binding site255ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular Functionglutamate-tRNA ligase activity
Molecular Functionglutamine-tRNA ligase activity
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological Processglutaminyl-tRNA aminoacylation
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
    • Ordered locus names
      CBO1094, CLC_1146

Organism names

Accessions

  • Primary accession
    A5I0T6
  • Secondary accessions
    • A7G2J8

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003309621-485Glutamate--tRNA ligase

Interaction

Subunit

Monomer.

Structure

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif11-21'HIGH' region
Motif252-256'KMSKS' region

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    485
  • Mass (Da)
    55,743
  • Last updated
    2007-06-26 v1
  • Checksum
    4D4264727F64BBB2
MTNKVRTRFAPSPTGYMHVGNLRTALYAYLIAKHDNGDFILRIEDTDQERLVEGALDVIYNTLKITGLSHDEGPDIGGPVGPYVQSERRNIYIEYAEKLIEKGEAYYCFCSKERLDMLRANSEALKRPFRYDKHCIDLSKEEIDKKIAEGVPYVIRQKNPTTGSTSFHDEIYGDISVDNSELDDMILIKSDGLPTYNFANVVDDHLMGITHVVRGSEYLSSSPKYNRLYEAFGWDVPIYVHCPPIMKDEHHKLSKRNGDASFEDLMAKGYLKEAILNYIALLGWNPGGEKEVFSMEELIEAFNYRNINKAPAVFDTKKLKWMNGEYIRALSLDKFHEMALPYYEEALTRDLDTKKISELLHTRVEVLNEIPEQLDFFNNLLEYSPEMYIHKKMKTTYENSLKSLEEVLPKLEALENWTFENIKEVCMNLVKELEVKNGVVLWPIRTAVSGKQFTPGGAFEIADILGKEETLERIKIGIDKLKALQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000727
EMBL· GenBank· DDBJ
ABS38569.1
EMBL· GenBank· DDBJ
Genomic DNA
AM412317
EMBL· GenBank· DDBJ
CAL82647.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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