A0A0Q8U9H6 · A0A0Q8U9H6_9ACTN

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 site572Zn2+ (UniProtKB | ChEBI)
Binding site576Zn2+ (UniProtKB | ChEBI)
Binding site676Zn2+ (UniProtKB | ChEBI)
Binding site680Zn2+ (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

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
      ASE24_22255

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Root224
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Propionibacteriales > Nocardioidaceae > Nocardioides

Accessions

  • Primary accession
    A0A0Q8U9H6

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-719Alanyl-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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    891
  • Mass (Da)
    96,536
  • Last updated
    2016-01-20 v1
  • MD5 Checksum
    7E71F72C053FF9B6D0DD9D9CC3D7A602
MDTAEIRRRFVAHFERDGHTPVPSASLLLDDPNLLFVNAGMVPFKPYFLGQETPPYDRATSVQKCVRTPDIEDVGKTTRHGTFFEMCGNFSFGDYFKEHAIELAWDLVTKPVADGGWGFDEAKLYPSVYVDDPEAVALWRKITGLPDDRIARLGKSENYWSMGVPGPGGPCSEILIDRGPAYGADGDFSAEDRYLEFWNLVFMQDELSAVRSKEDFDISGSLPKKNIDTGMGLERVAFMTQGVENMYEIDVMFPVIQMAEQLTGRRYGADHEDDVRFRVVADHVRSSMMLIGDGVTPGNEARGYVLRRLLRRAVRSMRLLGYEDPALPELFPVSRDKMGETYTDLHTDWERISRVAYAEEETFRKTLQAGTQIFDLAAQGVKKSGGSTLSGDEAFALHDTYGFPIDLTLEMASEAGLAVDEQGFRSLMAEQRERAKADARAKRGQHADTGAYRTILDEHGPTEWLAYETLETESNALALLVGGSPAPVLVAGDVGELVLDRTPFYAESGGQAADAGTIEFDGGRLEVLDVQRPVRGLVVHQVRVVDGEFTPGDHLLHAQVDPEWRTGARQAHSGTHVVHAALREVLGPSALQSGSYNRPGYLRLDFGWTTGLSPEQVRDIEQVSNEALRADLPVGWQYMTLSEAKDWGAIALFGETYDNTKVRVVEIGGPWSRELCGGTHVDHSSQIGTIVVTGEASVGSGNRRIEAFTGVEGFRYLARERDVVAQLTGLLKTQPDDLVGRVGDLVERLRTAEKEIEKVRVGQLLAAGGSLASGAARIGPVNVVAHRADGAGGGDVRTLALDVRGRLPKGEPGVVVIIGAADGKVAVVAAVNDEARARGLSANDLVRAVGPLVGGKGGGKDDVAQGGGTDMSRIDEALAVVAAEVGRVAAG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LMIN01000014
EMBL· GenBank· DDBJ
KRC41925.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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