D2NPM3 · D2NPM3_ROTMD

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

Lacks conserved residue(s) required for the propagation of feature annotation.

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 site148Proton acceptor
Binding site148-152substrate
Binding site235substrate
Binding site285substrate
Binding site312substrate
Active site359Nucleophile
Binding site397Zn2+ (UniProtKB | ChEBI)
Binding site399Zn2+ (UniProtKB | ChEBI)
Binding site402Zn2+ (UniProtKB | ChEBI)
Binding site428Zn2+ (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
    • Ordered locus names
      RMDY18_17590

Organism names

Accessions

  • Primary accession
    D2NPM3

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 region, domain.

Type
IDPosition(s)Description
Region1-20Disordered
Domain71-158tRNA-guanine15 transglycosylase-like
Domain193-461tRNA-guanine15 transglycosylase-like
Region364-368RNA 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
    466
  • Mass (Da)
    51,371
  • Last updated
    2010-03-02 v1
  • Checksum
    D80AECC5B94CCDA7
MRTPPPAKEAGFSGRLGCRHSDGKQTIERRMSVLDNSFPTEDFGFTITSRLADTASPSAERVEANGGQFRGRTGVITTPHGQIQTPAFTPVGTKATVKAVLPESMKELGAQALLSNAYHLYLQPGPEILDAAGGLGAFMNWDGPTFTDSGGFQVMSLGSGFKKVIDMGTVADAKGADGRPLGDDDVAKGKERLAHIDDDGVNFKSHIDGSIHRFTPEVSMQVQHQIGADVMFAFDELTTLYNSRGYQEEALERTRLWALRCIAEHQRLTAERVGKPYQALFGVIQGAQYEDLRRKACQDLGSMPFDGFGIGGALEKENLGTIVRWCAEELPESKPRHLLGISEPDDIFVGIENGVDTFDCVSPTRVARNAAVYSPTGRYNITNARFKADFSPIYEGCDCYTCTHYTRAYLRHLFKADERLAATLASIHNERFIVRMVDDAREAIKDGTYFEYRDEFLGNYYSGKKP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP011540
EMBL· GenBank· DDBJ
BAI65591.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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