A0A3D9D9X1 · A0A3D9D9X1_9FLAO

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.

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 site564Zn2+ (UniProtKB | ChEBI)
Binding site568Zn2+ (UniProtKB | ChEBI)
Binding site666Zn2+ (UniProtKB | ChEBI)
Binding site670Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionalanine-tRNA ligase 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
    • ORF names
      DRF60_16830

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • KCTC 22547
  • Taxonomic lineage
    Bacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Weeksellaceae > Chryseobacterium group > Chryseobacterium

Accessions

  • Primary accession
    A0A3D9D9X1

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-709Alanyl-transfer RNA synthetases family profile

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
    867
  • Mass (Da)
    97,312
  • Last updated
    2019-01-16 v1
  • Checksum
    0606827DDB799335
MTSQEIRQKFLDYFKSKDHLIVPSAPIVLKDDPTLMFSNSGMTQFKDFFLGYKTPTAPRIADTQKCLRVSGKHNDLDDVGRDTYHHTMFEMLGNWSFGDYFKKDAIAFAWELLTEVFGIPKENLYVTIFEGDASENLERDQDAYNFWKSHISEDRIINGNKKDNFWEMGESGPCGPCSEIHVDLRTEEEKAKVSGLDLVNNDHPQVVEVWNLVFMEFNRKADKSLEKLPQQHVDTGMGFERLCMALQGKSSNYDTDVFTPLIAKVEELSGKKYTGILEDEKDIAIRVVVDHIRAVAFAIADGQLPSNGGAGYVIRRILRRGISYSYRFLGMKEPFLYKLVAVLQEQMGTFFPEIEKQGKLVSEVIKSEEDSFLKTIENGLIRVEKLIQQTIADNSKVLPSEEVFELYDTYGFPDDLTRIIAEEKGLTIDEAGFKVEMEKQKLRSKADSAQKVYDWVTLETKPENFVGYDQIESETYITRYRKVENKDGEFYQVVLSSSPFYPEGGGQVGDKGVLENAVESFEVLETKKENGLIISLINGLPKDAGAVFYAKVDATDRRNSQANHSVTHLLHEALREVLGTHVEQKGSYVGPDYLRFDFSHFNKMTEEELTLVEEKVNAKIKESIALQEFRSIPIQEALDKGAMALFGEKYGDSVRMIQFGSSKELCGGTHVKNTIEIGHFKITSESSAAAGIRRIEAISGDKSEEYFKNLENQIHELSQLLKSKDVVRSTEKLIEENISLKSEVEALKKEKAKGEIGEWKNAYEQKGNKQLLVKKTSLDAGSVKDIVFQLKREIPTSVTIILSDADGKPMITVGVSDDLAADYQAGAIVKDLAKEIQGGGGGNPGFATAGGKNLDGLENAYQKALNI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QNUH01000018
EMBL· GenBank· DDBJ
REC74783.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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