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tgt tRNA-guanine transglycosylase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 949130, updated on 4-Apr-2024

Summary

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Gene symbol
tgt
Gene description
tRNA-guanine transglycosylase
Primary source
ASAP:ABE-0001413
Locus tag
b0406
See related
ECOCYC:EG10996
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
ECK0400; vacC(S.f.)
Summary
Tgt forms a transient covalent linkage with the tRNA substrate. [More information is available at EcoGene: EG10996]. The tgt gene encodes tRNA-guanine transglycosylase . [More information is available at EcoCyc: EG10996].
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Genomic context

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Sequence:
NC_000913.3 (426137..427264)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene acyl carrier protein phosphodiesterase Neighboring gene tRNA preQ1(34) S-adenosylmethionine ribosyltransferase-isomerase Neighboring gene Sec translocon accessory complex subunit YajC Neighboring gene Sec translocon accessory complex subunit SecD

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. Identification of the rate-determining step of tRNA-guanine transglycosylase from Escherichia coli. Garcia GA, et al. Biochemistry, 2009 Dec 1. PMID 19874048, Free PMC Article
  2. Site-specific modification of Shigella flexneri virF mRNA by tRNA-guanine transglycosylase in vitro. Hurt JK, et al. Nucleic Acids Res, 2007. PMID 17626052, Free PMC Article
  3. Role of aspartate 143 in Escherichia coli tRNA-guanine transglycosylase: alteration of heterocyclic substrate specificity. Todorov KA, et al. Biochemistry, 2006 Jan 17. PMID 16401090, Free PMC Article
  4. Mechanism and substrate specificity of tRNA-guanine transglycosylases (TGTs): tRNA-modifying enzymes from the three different kingdoms of life share a common catalytic mechanism. Stengl B, et al. Chembiochem, 2005 Nov. PMID 16206323
  5. The role of aspartic acid 143 in E. coli tRNA-guanine transglycosylase: insights from mutagenesis studies and computational modeling. Todorov KA, et al. Biophys J, 2005 Sep. PMID 15951383, Free PMC Article

See all (50) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. mutation of key residues in the E. coli TGT active site can ''open up'' the site to allow for the binding of competitive pteridine inhibitors.
    Title: Differential heterocyclic substrate recognition by, and pteridine inhibition of E. coli and human tRNA-guanine transglycosylases.
  2. phylogenetic and kinetic analyses support the conclusion that all tRNA-guanine transglycosylases have divergently evolved to specifically recognize their cognate heterocyclic substrates.
    Title: Evolution of eukaryal tRNA-guanine transglycosylase: insight gained from the heterocyclic substrate recognition by the wild-type and mutant human and Escherichia coli tRNA-guanine transglycosylases.
  3. N-terminus verified by Edman degradation on complete protein
    Title: tRNA-guanine transglycosylase from Escherichia coli. Overexpression, purification and quaternary structure.
  4. The key role of aspartate 143 in maintaining the anticodon identities of TGT queuine-containing tRNAs is confirmed.
    Title: Role of aspartate 143 in Escherichia coli tRNA-guanine transglycosylase: alteration of heterocyclic substrate specificity.
Submit: New GeneRIF Correction

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables glycosyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables pentosyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables tRNA-guanosine(34) queuine transglycosylase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables tRNA-guanosine(34) queuine transglycosylase activity IEA
Inferred from Electronic Annotation
more info
  
enables transferase activity IEA
Inferred from Electronic Annotation
more info
  
enables zinc ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
involved_in queuosine biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in queuosine biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within queuosine biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in tRNA modification IEA
Inferred from Electronic Annotation
more info
  
involved_in tRNA processing IEA
Inferred from Electronic Annotation
more info
  
involved_in tRNA wobble guanine modification IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within tRNA wobble guanine modification IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in tRNA-guanine transglycosylation IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
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-guanine transglycosylase
NP_414940.1

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
    426137..427264
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_414940.1 tRNA-guanine transglycosylase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_414940.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A3W4JV99, A0A7A7FCP2
    Conserved Domains (1) summary
    PRK00112
    Location:1 → 364
    tgt; queuine tRNA-ribosyltransferase; Provisional
Nucleotide Protein
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Gene LinkOut

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Other Literature Sources
Molecular Biology Databases
Research Materials