O28029 · SYA_ARCFU

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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

1906100200300400500600700800900
TypeIDPosition(s)Description
Binding site600Zn2+ (UniProtKB | ChEBI)
Binding site604Zn2+ (UniProtKB | ChEBI)
Binding site703Zn2+ (UniProtKB | ChEBI)
Binding site707Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionalanine-tRNA ligase activity
Molecular Functionaminoacyl-tRNA editing activity
Molecular FunctionATP binding
Molecular Functionidentical protein 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
      AF_2255

Organism names

Accessions

  • Primary accession
    O28029

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis703Loss of tRNA editing activity.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000752601-906Alanine--tRNA ligase

Proteomic databases

Interaction

Subunit

Homodimer.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY O28029alaS O280293EBI-15779415, EBI-15779415

Protein-protein interaction databases

Family & Domains

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    906
  • Mass (Da)
    102,536
  • Last updated
    1998-01-01 v1
  • Checksum
    2AD39B7B65C72C8B
MTLDEEYLDITFLTENGFVRKRCPKCGKHFWTADPEREICGDPPCESYSFIGNPVFKKPFELDEMREYYLNFFERRGHGRIERYPVVARWRTDIYLTIASIADFQPFVTSGVAPPPANPLTISQPCIRLDDLDSVGRTGRHLTLFEMMAHHAFNYPGKEIYWKNETVAYCTELLNELGVKKEDIVYKEEPWAGGGNAGPCLEAIVGGLEVATLVFMNLEEHPEGDIEIKGARYRKMDNYIVDTGYGLERFVWASKGTPTVYDAIFPEVVDTIIDNSNVSFNREDERVRRIVAESSKLAGIMGELRGERLNQLRKSVADTVGVSVEELEGIVVPLEKVYSLADHTRCILFMLGDGLVPSNAGAGYLARLMIRRSLRLAEELELGLDLYDLVEMHKKILGFEFDVPLSTVQEILELEKERYRTTVSKGTRLVERLVERKKKLEKDDLIELYDSHGIPVELAVGIAAEKGAEVEMPKDIYAELAKRHSKAEKVQEKKITLQNEYPATEKLYYDDPTLLEFEAEVIGVEGDFVILNRSAFYPESGGQDNDVGYLIANGGKFEVVDVLEADGVVLHVVKGAKPEVGTKVKGVIDSDVRWRHMRHHSATHVLLYSLQKVLGNHVWQAGARKEFSKARLDVTHFRRPSEEEIKEIEMLANREILANKPIKWEWMDRIEAERKFGFRLYQGGVPPGRKIRVVQVGDDVQACGGTHCRSTGEIGMLKILKVESIQDGVIRFEFAAGEAAIEAVEEMERLLREASSILRVEPAKLPKTVERFFEEWKDQRKEIERLKSVIADLWADILMERAEEFDSMKVVAEVVDADMQALQKLAERLAEKGAVGCLMAKGEGKVFVVTFSGQKYDARELLREIGRVAKGSGGGRKDVAQGAVQQLLDREEMLDVIFRFLSEHEG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE000782
EMBL· GenBank· DDBJ
AAB89002.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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