A0A0N8NMH0 · A0A0N8NMH0_9FIRM

Function

function

Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Pathway

tRNA modification; tRNA-queuosine biosynthesis.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site94Proton acceptor
Binding site94-98substrate
Binding site148substrate
Binding site191substrate
Binding site218substrate
Active site268Nucleophile
Binding site306Zn2+ (UniProtKB | ChEBI)
Binding site308Zn2+ (UniProtKB | ChEBI)
Binding site311Zn2+ (UniProtKB | ChEBI)
Binding site337Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionmetal ion binding
Molecular FunctiontRNA-guanosine(34) queuine transglycosylase activity
Biological Processqueuosine biosynthetic process
Biological ProcesstRNA wobble guanine modification
Biological ProcesstRNA-guanine transglycosylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Queuine tRNA-ribosyltransferase
  • EC number
  • Alternative names
    • Guanine insertion enzyme
    • tRNA-guanine transglycosylase

Gene names

    • Name
      tgt
    • ORF names
      TR13x_01275

Organism names

  • Taxonomic identifier
  • Strain
    • TR13
  • Taxonomic lineage
    Bacteria > Bacillota > Tissierellia > Tissierellales > Thermohalobacteraceae > Caloranaerobacter

Accessions

  • Primary accession
    A0A0N8NMH0

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer. Within each dimer, one monomer is responsible for RNA recognition and catalysis, while the other monomer binds to the replacement base PreQ1.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain15-369tRNA-guanine15 transglycosylase-like
Region249-255RNA binding
Region273-277RNA binding; important for wobble base 34 recognition

Sequence similarities

Belongs to the queuine tRNA-ribosyltransferase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    373
  • Mass (Da)
    42,662
  • Last updated
    2016-01-20 v1
  • Checksum
    5F8A00D0652849D9
MMAVKYELIKESTECKARLGKLHTPHGIIETPIFMPVGTRATVKTMTPEELKDLGAQIILSNTYHLYLRPGHELIKEAGGLHKFMNWDKPILTDSGGFQVFSLGDLRKITEEGVEFRSHIDGSRHFISPEKSIEIQNALGSDIIMAFDECAPYPSDRDYVKHSLERTTRWAKRCKEAHRNPETQALFGIVQGGMYRDLREQSAKEIIDLDFPGYAIGGLSVGEPKELMYEVLDYTAPLLPKNKPRYLMGVGSPDCLFEGVIRGIDMFDCVLPTRIARNGTVMTSQGKVVIRNAKYARDFGKLDPECDCYTCQNYSRAYIRHLFNVNEILGARLTTIHNLYFLLKLMENIRLAIKEDRLLQYKEEFFKKYGYIK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JXLL01000001
EMBL· GenBank· DDBJ
KPU28008.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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