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    tsaC L-threonylcarbamoyladenylate synthase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947783, updated on 3-Dec-2024

    Summary

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    Official Symbol
    tsaC
    Official Full Name
    L-threonylcarbamoyladenylate synthase
    Primary source
    ECOCYC:G7698
    Locus tag
    b3282
    See related
    ASAP:ABE-0010766
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    ECK3269; rimN; yrdC
    Summary
    RimN(YrdC) but not paralog YciO is required for synthesis of t(6)A37 (threonylcarbamoyladenosine) of ANN decoding tRNAs (El Yacoubi, 2009). [More information is available at EcoGene: EG12840]. RimN is a putative ribosome maturation factor. [More information is available at EcoCyc: G7698].
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    Genomic context

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    Sequence:
    NC_000913.3 (3430843..3431415, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene hexapeptide repeat-containing protein YrdA Neighboring gene DUF1488 domain-containing protein YrdB Neighboring gene shikimate dehydrogenase Neighboring gene putative DNA topoisomerase Neighboring gene DUF494 domain-containing protein Smg Neighboring gene protein Smf

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Specificity in the biosynthesis of the universal tRNA nucleoside N(6)-threonylcarbamoyl adenosine (t(6)A)-TsaD is the gatekeeper. Swinehart W, et al. RNA, 2020 Sep. PMID 32385138, Free PMC Article
    2. N-(purin-6-ylcarbamoyl)threonine: biosynthesis in vitro in transfer RNA by an enzyme purified from Escherichia coli. Körner A, et al. FEBS Lett, 1974 Mar 1. PMID 4604806
    3. The enzymatic synthesis of N-(purin-6-ylcarbamoyl)threonine, an anticodon-adjacent base in transfer ribonucleic acid. Elkins BN, et al. Biochemistry, 1974 Oct 22. PMID 4609459
    4. Mechanism of N6-threonylcarbamoyladenonsine (t(6)A) biosynthesis: isolation and characterization of the intermediate threonylcarbamoyl-AMP. Lauhon CT. Biochemistry, 2012 Nov 6. PMID 23072323
    5. Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography. Fountoulakis M, et al. Electrophoresis, 1999 Aug. PMID 10493123

    See all (18) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Pathways from PubChem

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    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables ATP binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables L-threonylcarbamoyladenylate synthase IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables L-threonylcarbamoyladenylate synthase IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables double-stranded RNA binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables double-stranded RNA binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables nucleotidyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables nucleotidyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables nucleotidyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables tRNA binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables tRNA binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables tRNA binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in rRNA processing IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in regulation of translational fidelity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in ribosome biogenesis IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tRNA processing IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within tRNA threonylcarbamoyladenosine modification EXP
    Inferred from Experiment
    more info
    		 PubMed 
    acts_upstream_of_or_within tRNA threonylcarbamoyladenosine modification IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in tRNA threonylcarbamoyladenosine modification IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    L-threonylcarbamoyladenylate synthase
    NP_417741.1

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      3430843..3431415 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417741.1 L-threonylcarbamoyladenylate synthase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417741.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A1X3JBL4
      Conserved Domains (1) summary
      PRK10634
      Location:1 → 190
      PRK10634; L-threonylcarbamoyladenylate synthase type 1 TsaC
    Nucleotide Protein
    Heading Accession and Version

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