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Q8TWY1 · SYA_METKA

Function

function

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

1915100200300400500600700800900
TypeIDPosition(s)Description
Binding site605Zn2+ (UniProtKB | ChEBI)
Binding site609Zn2+ (UniProtKB | ChEBI)
Binding site709Zn2+ (UniProtKB | ChEBI)
Binding site713Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionalanine-tRNA ligase activity
Molecular Functionaminoacyl-tRNA editing activity
Molecular FunctionATP binding
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological Processalanyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alanine--tRNA ligase
  • EC number
  • Alternative names
    • Alanyl-tRNA synthetase
      (AlaRS
      )

Gene names

    • Name
      alaS
    • Ordered locus names
      MK0900

Organism names

Accessions

  • Primary accession
    Q8TWY1

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000752651-915Alanine--tRNA ligase

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region882-901Disordered

Domain

Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    915
  • Mass (Da)
    103,908
  • Last updated
    2002-08-02 v2
  • MD5 Checksum
    B52E634201414010BEB65CC34DA8E8F8
MKVDPSEFELEFFEEIGFERKRCPECGEYFWGPPEAEVCNETPCVEYSFIGDPPASVKLDVWEAGEEFFRFFERHDHEVLDRYPVVARWRDDIHLTIASIACFQPWVTSGEVPPPANPLVINQPCIRLNDIDNVGRTGRHFTLFHMGGHHAFNNHPHDRRDIYWKEETVRLCYEFTVEKLGIPEEKIAFKESWWEGGGNAGPCFEVVVDGLELATLVFMQYEQVGGEYRELPQKIVDTGYGIERYAWITTGEPTAYDAVFGDLVDATARDLGVEIDGEAREILGELARVAGLMDVETESDLRVLRNRVARRLDLDVNELVRVAEPVEFVYGILDHARCLAFMLGDGVVPSNAGEGYLARLVIRRALRLLDGLDAEREYLLEVVERVLEDLRGTYPELAEREEYIQDALECEIDRYTRALKRGKKEVRKRLEEKGELSFEDLVELYDSHGIPPEVAREIAEDEGVEVEVPDDFYSRVAERHEGPEEVEEGLEELERIAVEEELPETELAFYDDEKRLEFKAEVIGTYEVNGDAWVVLDRTYFYPEGGGQEADRGTMRWKDGEAEVKDVQKVRGVVFHRIDGDVPPEGAEVECEVDGERRMRLTRNHTATHVILEAARRVLGDHVWQAGAHKSTDEARLDVTHHRRISDEELREIERLANEIVMKDLPVNKRFMDRNEAERRYGFELYQGGVVPGREIRVVEIEGWNVQACAGTHCDSTGEIGPIKIVGRERIQDGVERIRFAAGEAALERIWETEDLLRETCEVLRVNPENLPKTVKRFFEEWKEQRKRIERLERELVEAKLRAAPAEGRRVGDFTVTLVELEDVEVGSVAGTVEELVKEHENLVLVAKIVSNGSCQVVVGSGESAPPAGELMREIGKLIEGGGGGDERLAQGGGRNPDGLTEDRLVEIVEDLAGG

Sequence caution

The sequence AAM02113.1 differs from that shown. Reason: Erroneous initiation

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE009439
EMBL· GenBank· DDBJ
AAM02113.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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