A0A4Y8UYX4 · A0A4Y8UYX4_9GAMM

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 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
      E3V39_10585

Organism names

Accessions

  • Primary accession
    A0A4Y8UYX4

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
Domain10-363tRNA-guanine15 transglycosylase-like
Region243-249RNA binding
Region267-271RNA 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
    372
  • Mass (Da)
    41,489
  • Last updated
    2019-09-18 v1
  • Checksum
    246EE52944672360
MEFKVHNTDGLARRATLSFPRGDVQTPAFMPVGTYGTVKGMTPQQINDIGAEIILGNTFHLMLRPGTDVIQKHGDLHDFMGWHKPILTDSGGFQVFSLGELRKINEQGVTFRSPIDGSKVFLGPESAIAVQQKLGSDIIMIFDECTPYPASEHEAKTSMELSLRWAKRCKDAHGDHPSALFGIVQGGMYDHLRQQSLDGLVALDFDGYAIGGLSVGEPKGEMIKVLDYVAHQMPADKPRYLMGVGTPGDIIEAVRRGIDMFDCVMPTRNARNAHLFTSQGVLKLRNARFKDDTRALDPACVCYTCQNFSRAYLHHLDKCNEMLGAQLNTIHNLHFYQHLMQGLRQALEQGRFTAFVEDFYREQSVLENNADA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SPIB01000002
EMBL· GenBank· DDBJ
TFH73632.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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