A0A1G2MK77 · A0A1G2MK77_9BACT

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.

Type
IDPosition(s)Description
Active site93Proton acceptor
Binding site93-97substrate
Binding site190substrate
Binding site248substrate
Binding site275substrate
Active site322Nucleophile
Binding site360Zn2+ (UniProtKB | ChEBI)
Binding site362Zn2+ (UniProtKB | ChEBI)
Binding site365Zn2+ (UniProtKB | ChEBI)
Binding site391Zn2+ (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
      A3D50_02255

Organism names

Accessions

  • Primary accession
    A0A1G2MK77

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.

Type
IDPosition(s)Description
Domain14-103tRNA-guanine15 transglycosylase-like
Domain146-420tRNA-guanine15 transglycosylase-like
Region303-309RNA binding
Region327-331RNA 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
    421
  • Mass (Da)
    46,131
  • Last updated
    2017-02-15 v1
  • MD5 Checksum
    5A22902164669B0D643B5DD2FB1CE11B
MPKFHIQKGDVKSRARAGTIVTAHGIIETPAFIPVATKATVKSLTPEMVGQAVQAQAVLANTYHLYLQPGTEIIQKAGGLGKFMNWSGPTFTDSGGFQAFSLGAAFGRRMGKVWGAEERSRNNELWIGTNTNVIPPNSLFIIPNSDSLASIDDDGVTFRSVLDGSTHRFTPEISIDIQHAIGADIIFAFDECAAPDADYQYQKRAMDRTHDWAERCTRQHEAGIMNKELGGNKNTSSLSPQALFGIVQGGRHKDLRQESARIIGSMDFDGFGIGGSFDKDDIATAVGWVTAILPEEKPRHLLGIGEPMDLVLGIEQGIDTFDCVAPTRLGRFGTAYTASGRINLLNLRFVADMSPLDHDCHCYSCSNFTRAYIAHLFRAKEMLAATLASIHNLHFLIDITNRAREAILNGSFQEFKEKLLK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MHRM01000006
EMBL· GenBank· DDBJ
OHA24335.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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