A0A2K2HBS3 · A0A2K2HBS3_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.

TypeIDPosition(s)Description
Active site98Proton acceptor
Binding site98-102substrate
Binding site152substrate
Binding site195substrate
Binding site222substrate
Active site272Nucleophile
Binding site310Zn2+ (UniProtKB | ChEBI)
Binding site312Zn2+ (UniProtKB | ChEBI)
Binding site315Zn2+ (UniProtKB | ChEBI)
Binding site341Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionmetal ion binding
Molecular FunctiontRNA-guanosine(34) queuine transglycosylase activity
Biological Processqueuosine biosynthetic process
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
      C2E25_05935

Organism names

  • Taxonomic identifier
  • Strain
    • HR-1
  • Taxonomic lineage
    Bacteria > Thermodesulfobacteriota > Desulfuromonadia > Desulfuromonadales > Geothermobacteraceae > Geothermobacter

Accessions

  • Primary accession
    A0A2K2HBS3

Proteomes

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.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain19-374tRNA-guanine15 transglycosylase-like
Region253-259RNA binding
Region277-281RNA binding; important for wobble base 34 recognition

Sequence similarities

Belongs to the queuine tRNA-ribosyltransferase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    379
  • Mass (Da)
    42,417
  • Last updated
    2018-03-28 v1
  • Checksum
    654FE7FD2578C85E
MQRTLKPFSFELLAGDPGCGARRGRMITRRGVIETPVFMPVGTQATVKGMLPEALDEIGAQIILGNTYHLYLRPGHDLIARLGGLHAFMHWSGPILTDSGGFQVFSLGELRKISEEGVAFQSHLDGSRHLLTPESSIAIQEALGADIIMAFDECIPHPAEREYVVDSTARSGRWARRCRQARRPDDGAALFGIVQGGMYRDLRRQSAEELREIGFEGYALGGLSVGESTELMYEVMDYSLPLLPEDAPRYVMGVGTPENLVEGIARGVDMFDCVMPTRNARNGVLFTRRGKLSIKQARYREDESPIDPRCDCYVCRHYSRAYLRHLFRANEILSSVLNTHHNLHYYLSLMAAARAAIEQGSFTAFRRDFYAQREQTVPA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PPFX01000009
EMBL· GenBank· DDBJ
PNU20755.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp