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A0A9N8RRE0 · A0A9N8RRE0_9BURK

  • Protein
    Queuine tRNA-ribosyltransferase
  • Gene
    tgt
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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 site106Proton acceptor
Binding site106-110substrate
Binding site160substrate
Binding site209substrate
Binding site236substrate
Active site286Nucleophile
Binding site324Zn2+ (UniProtKB | ChEBI)
Binding site326Zn2+ (UniProtKB | ChEBI)
Binding site329Zn2+ (UniProtKB | ChEBI)
Binding site355Zn2+ (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
      LMG31841_00168

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • LMG 31841
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Paraburkholderia

Accessions

  • Primary accession
    A0A9N8RRE0

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.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain28-388tRNA-guanine15 transglycosylase-like
Region267-273RNA binding
Region291-295RNA 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
    395
  • Mass (Da)
    44,063
  • Last updated
    2023-09-13 v1
  • MD5 Checksum
    28B9B5F6BA9E00C661CA8DC0A5AED3ED
MTDGHQHATQTGRPDNGLKFELLTTDGQARRGRVTLNHGVVETPIFMPVGTYGTVKAVQPRELEEMHAQIILGNTFHLWLRPGLETIGAHGGLHAFMGWKKPILTDSGGFQVFSLGDLRKITEDGVTFASPINGDKLFLSPEVSMQIQKVLNSDIVMQFDECTPYATNNVPTSHQEAADSMRMSMRWAKRSIDEFNRLGNPNALFGIVQGGMFEDLRDESLAGLAEIDFHGFAIGGLSVGEPKEDMMRVLNHIGPKLPANKPHYLMGVGTPEDLVAGVAAGVDMFDCVMPTRNARNGWLFTRFGDVKIRNAVHKNSLRPLDEQCGCYTCRNFTRGYLHHLHRVGEILGAQLNTIHNLHYYLELMQEMRDAIEAHMFDAFRKQFHENRARGVEGPA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CAJQZC010000001
EMBL· GenBank· DDBJ
CAG4886315.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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