D9SAE5 · D9SAE5_FIBSS

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.

1882100200300400500600700800
TypeIDPosition(s)Description
Binding site564Zn2+ (UniProtKB | ChEBI)
Binding site568Zn2+ (UniProtKB | ChEBI)
Binding site670Zn2+ (UniProtKB | ChEBI)
Binding site674Zn2+ (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
      FSU_1489

Organism names

Accessions

  • Primary accession
    D9SAE5

Proteomes

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain5-713Alanyl-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
    882
  • Mass (Da)
    97,706
  • Last updated
    2010-10-05 v1
  • Checksum
    0D42CB0C848DF74A
MSEKMTSAQVRESFIKFFESKGHLFVRSSPVVPHDDPTLMFTNAGMNQFKAIFLGDNPKGWKRACNSQKCLRVSGKHNDLDVVGRDNYHHTFFEMLGNWSFGDYYKKEAISWAWELLTEVWKLPKERLFATVYQDDDEAWQIWKDVSGLPDDRIMRFDAHSNFWEMGDTGPCGPCSEIHYDRGDLATQAETFKDPIKGVNGENDRYIEIWNNVFMQYERVSDGSLIPLKAKNVDTGMGFERICAILQGKTSNYDTDVFTPIIAKIAELSGVPYNDGEAGTPHRVIADHIRAISFAIADGALPSNEGRGYVLRRILRRASRFARLLGQKKPFICQLVQVLADTMGDAFPEIRERKEFVASVIKSEEESFIRTLDAGLERFAAISAELKKGDKIPGDKVFLLYDTYGFPPDLTGILAEEKGLLIDEEGYEKCMNEQKERARANMKQGINTMGTEGWTQYSEASTNFVGYELSACETKVVRWREDKGVLSIVLETSPFYAEMGGQVGDKGTLVSADLEIQVFDTVKVNDTALCRGKVVKGEANEKTMGAVFMATVDNDRRADIRKNHSATHLLQAALREVLGTHVQQQGSFVSNELLRFDFSHFNAMTAEEIQKVEDIVNAKIMECLPVHTDVMDVDEAKASGAMALFGEKYGDKVRVVKMGDAGVEFSRELCGGLHVQNTGNIGMVKIVSESSVSAGVRRIEAVSGRGALSLLRAGTQILNALREQLRCKDAEVLDRIQQTFAKTQNLEKSLQFVKLELATLAAAELLNGGINVMGVNLFVRELSLPDEKYKNLLDGVQNKLDVDSVAVIANKDNGSGSIAVMVGKNVQAKGIKAGDIVRDLAKACNGKGGGRPDRAQAGTREPEKIAEAIANANNWIRAKLGA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002158
EMBL· GenBank· DDBJ
ADL27021.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp