A0A4D7QPX3 · A0A4D7QPX3_9HYPH

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.

1885100200300400500600700800
TypeIDPosition(s)Description
Binding site564Zn2+ (UniProtKB | ChEBI)
Binding site568Zn2+ (UniProtKB | ChEBI)
Binding site675Zn2+ (UniProtKB | ChEBI)
Binding site679Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionalanine-tRNA ligase activity
Molecular Functionaminoacyl-tRNA editing activity
Molecular FunctionATP binding
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological Processalanyl-tRNA aminoacylation
Biological Processnegative regulation of DNA-templated transcription

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
    • ORF names
      E8L99_20830

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NMCR1094
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Phreatobacteraceae > Phreatobacter

Accessions

  • Primary accession
    A0A4D7QPX3

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain, coiled coil, region.

Type
IDPosition(s)Description
Domain2-718Alanyl-transfer RNA synthetases family profile
Coiled coil734-761
Region850-870Disordered

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.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    885
  • Mass (Da)
    94,135
  • Last updated
    2019-07-31 v1
  • MD5 Checksum
    020C6ECB1095D6FBC6F428B13D792634
MTGVNQIRKTFLDFFQTNGHAVVESSPLVPRNDPTLMFANSGMVQFKNVFTGVEKRPYSRATTAQKCVRAGGKHNDLDNVGYTARHHTFFEMLGNFSFGDYFKDRAIELAWNLITKEYELPVSRLLVTVYSEDDEAFGLWKKIAGLPDSKIIRIPTSDNFWRMGDTGPCGPCSEIFYDHGDKVWGGPPGSADADGDRFIEIWNLVFMQYEEQAGGIRTALPRPSIDTGMGLERVSAVLQGTHDNYEIDLMRALIGASAVATGVEPDGPHKVSHRVIADHLRASSFLVADGVLPSNEGRGYVLRRIMRRAMRHASLLGAKDPLMHKLVPVLVREMGQAYPELQRAEALIAETLQLEEQRFRRTLERGLAILDDGTRDLGEGAVFSGDTAFTLYDTYGFPLDLTQDALRPRGITVDTAAFDAAMQQQKAMARAAWAGSGEAATDTVWFGVKEKTGATDFLGYDTETAEGQVLALVKEGAEVSSLGVGETGLVVLNQTPFYGESGGQQGDRGLMTGEGVRATVTETQKKLGDLFVHVVTVDEGKLAVGQALQLDVDHGRRSAIRANHSATHLLHEALRLVLGDHVAQKGSLVAPERLRFDFAHPKPISDEDLAKVEDIANAIVLANGPVVTRLMGVDDAVASGARALFGEKYGDEVRVVSMGAPPAGSNSSGWSVELCGGTHVGRTGDIGLVTVVGESAVAAGVRRIEAMTGSAARHHLAAQARKLEQVAGLVKTSVADVEARVEALVEERRKLERELTDARKKLAMGGGAGGADPVKTVGSVKLLARSVSGVEMKDLKGLADAGKAQVGSGVVVLANTGADGKVGLVVGVTADLVGRFDAVQLVRVGSEALGGKGGGGRPDMAQAGGPEGASAEDALKAIEAALAAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP039865
EMBL· GenBank· DDBJ
QCK88023.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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