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A0A7S6RVP7 · A0A7S6RVP7_9PROT

  • 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).

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 site89Proton acceptor
Binding site89-93substrate
Binding site143substrate
Binding site185substrate
Binding site212substrate
Active site262Nucleophile
Binding site300Zn2+ (UniProtKB | ChEBI)
Binding site302Zn2+ (UniProtKB | ChEBI)
Binding site305Zn2+ (UniProtKB | ChEBI)
Binding site331Zn2+ (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
      HRU73_05290

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • H1_AOB3
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Nitrosomonadales > Nitrosomonadaceae > Nitrosomonas

Accessions

  • Primary accession
    A0A7S6RVP7

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
Domain11-360tRNA-guanine15 transglycosylase-like
Region243-249RNA binding
Region267-271RNA 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
    371
  • Mass (Da)
    41,443
  • Last updated
    2021-09-29 v1
  • MD5 Checksum
    F810F6BDFAB5246B913F1BEBD4BD779A
MKFQLHCRDHEARRGTLTLAHGTVETPAFMPVGTYGAVKGLSPDELHTLGAGIILGNTFHLWLRPGLEVIGAHGGLHRFMHWDRPILTDSGGFQVFSLGALRKICEEGVRFRSPVNGDTCFLTPEESMRIQQVLNSDIVMIFDECTPYPVDMQIAESSMQLSLRWAERSKAAHAGNPNALFGIVQGGMYESLRDRSAAGLCAIGFDGYAIGGLSVGEPKADMQRILRHTAPQLPADKPRYLMGVGTPEDIVHAVAQGIDLFDCVLPTRNARNGWLYTSQGILKLRNSRYRLDISPPDEHCDCYTCRHFTRAYLHHLQRTGEMLGARLNSLHNLHYYQRLMANIRKAIETGQFEQFARKFSGQDFMLKCASV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP054389
EMBL· GenBank· DDBJ
QOJ08937.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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