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trmA tRNA m(5)U54 methyltransferase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947143, updated on 3-Dec-2024

Summary

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Official Symbol
trmA
Official Full Name
tRNA m(5)U54 methyltransferase
Primary source
ECOCYC:EG11022
Locus tag
b3965
See related
ASAP:ABE-0012983
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
ECK3957; rT; rumT
Summary
The trmA gene is essential. [More information is available at EcoGene: EG11022]. trmA encodes the methyltransferase that is responsible for methylation of U54 in all tRNAs. [More information is available at EcoCyc: EG11022].
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Genomic context

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Sequence:
NC_000913.3 (4162170..4163270, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene DNA-binding transcriptional dual regulator OxyR Neighboring gene soluble pyridine nucleotide transhydrogenase Neighboring gene DNA-binding transcriptional repressor FabR Neighboring gene DUF1422 domain-containing inner membrane protein YijD Neighboring gene cobalamin outer membrane transporter Neighboring gene glutamate racemase Neighboring gene 16S ribosomal RNA

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. Purification of transfer RNA (m5U54)-methyltransferase from Escherichia coli. Association with RNA. Ny T, et al. Eur J Biochem, 1988 Nov 15. PMID 2461858
  2. Enzymatic mechanism of tRNA (m5U54)methyltransferase. Kealey JT, et al. Biochimie, 1994. PMID 7748948
  3. Stereochemistry of tRNA(m5U54)-methyltransferase catalysis: 19F NMR spectroscopy of an enzyme-FUraRNA covalent complex. Kealey JT, et al. Biochemistry, 1995 Feb 28. PMID 7532997
  4. The methyltransferase TrmA facilitates tRNA folding through interaction with its RNA-binding domain. Keffer-Wilkes LC, et al. Nucleic Acids Res, 2020 Aug 20. PMID 32597953, Free PMC Article
  5. Cloning and restriction mapping of the trmA gene coding for transfer ribonucleic acid (5-methyluridine)-methyltransferase in Escherichia coli K-12. Ny T, et al. J Bacteriol, 1980 May. PMID 6247318, Free PMC Article

See all (50) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The methyltransferase TrmA facilitates tRNA folding through interaction with its RNA-binding domain.
    Title: The methyltransferase TrmA facilitates tRNA folding through interaction with its RNA-binding domain.
  2. findings show that m (5)U formation in tmRNAs is exclusively due to TrmA and should be considered as a dual-specific enzyme
    Title: RNA-methyltransferase TrmA is a dual-specific enzyme responsible for C5-methylation of uridine in both tmRNA and tRNA.
  3. N-terminus verified by Edman degradation on complete protein
    Title: Purification of transfer RNA (m5U54)-methyltransferase from Escherichia coli. Association with RNA.
  4. A mutagenesis study to determine which amino acids are important for the formation of the TrmA-tRNA intermediate and/or the enzymatic activity.
    Title: Amino acid residues of the Escherichia coli tRNA(m5U54)methyltransferase (TrmA) critical for stability, covalent binding of tRNA and enzymatic activity.
Submit: New GeneRIF Correction

General gene information

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Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables RNA methyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables S-adenosylmethionine-dependent methyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables methyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables rRNA binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables rRNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent IBA
Inferred from Biological aspect of Ancestor
more info
  
enables tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent IDA
Inferred from Direct Assay
more info
 PubMed 
enables tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent 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 
Process Evidence Code Pubs
involved_in RNA modification IEA
Inferred from Electronic Annotation
more info
  
involved_in RNA processing IEA
Inferred from Electronic Annotation
more info
  
involved_in methylation IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within tRNA folding IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in tRNA methylation IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within tRNA methylation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in tRNA processing IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
tRNA m(5)U54 methyltransferase
NP_418400.1

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
    4162170..4163270 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_418400.1 tRNA m(5)U54 methyltransferase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_418400.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A376L3L6, W1F562
    Conserved Domains (1) summary
    PRK05031
    Location:1 → 366
    PRK05031; tRNA (uracil-5-)-methyltransferase; Validated
Nucleotide Protein
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