A0A564VZX4 · A0A564VZX4_9BIFI

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.

1892100200300400500600700800
TypeIDPosition(s)Description
Binding site573Zn2+ (UniProtKB | ChEBI)
Binding site577Zn2+ (UniProtKB | ChEBI)
Binding site677Zn2+ (UniProtKB | ChEBI)
Binding site681Zn2+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
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
      BCJG468_00343

Organism names

  • Taxonomic identifier
  • Strain
    • Bifidobacterium_catenulatum_JG_Bg468
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A564VZX4

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-720Alanyl-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
    892
  • Mass (Da)
    97,462
  • Last updated
    2019-10-16 v1
  • Checksum
    A8D0A1BE0DF1FB41
MRTSEIAKRYLDYFEKHGHLIVPSASLISPNPTTLFTIAGMVPFIPYLMGEQTPPKSRMASNQKCVRTLDIDEVGKTTRHGTFFQMLGNFSFGDYFKEEAIHYAYELLTTPQDKGGYGFDPEKLWMTTFTDDEEARSMWKNEGVDPEHIQIMGMEDNFWTTGGPGPGGPCSEIYVDRGPEYGVEGGPIADENRYIEIWDLVFENYEVDNVKSKTDLHIVGELENKNIDTGAGLERLAYLMQGKQNIYETDEVFPVIEAAQKLSGRTYGDDEAMDVRFRIVADHVRSALMIMSDGVRPSNNGRGYVLRRLLRRTVKAMRELGVPGPVMPTLLPTSKAAMEPSYPELNNTFHDVSEAAYGEEDAFRRTLESGTEIFDLAVAKAKESGSDAVSGEDAFKLHDTYGFPIEITLEMAADQGVKVDEAKFRELMAEQKSRARADALKKRHNVDLSVYDDFKKTLVQPIDFLGYTDMSARAKVLGIMQEGKGSVPAVTGPANVEVILDRTPFYAQAGGQLADQGEILSDDGAVLEVDDVQKPIKDLIVHQCRLTEGTLVVGAEVNANIDLDRRGAIARSHTATHMVHKALREELGPQATQRGSEDAPNRLRFDFQWSSAPSKDAMNSVEARVNEKLRENLAVTTQEMKFDDAIALGAMHLFGEKYGDVVRVVSIGEDGWSRELCGGTHVDHVGKIGAVNIMSEASIGSGVRRVDAVVGESAYEFNAREHALVSQLSDMVNARPDELADRVNALLAKLKESDRRLAAMYESQLSASVPALVAEAKASQTPVKVAAKNVEHFGSFDALRKTVLDVRGQLGEETPVVVALAGVNEEGKPMVAVATNEAARKQGIKAGDLVRGASKILGGGGGGKPDFAQGGGADATKIDEALEALAHQAMKG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CABHNV010000075
EMBL· GenBank· DDBJ
VUX38284.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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