A0A9D1A9Z4 · A0A9D1A9Z4_9FIRM

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.
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 site194substrate
Binding site221substrate
Active site271Nucleophile
Binding site309Zn2+ (UniProtKB | ChEBI)
Binding site311Zn2+ (UniProtKB | ChEBI)
Binding site314Zn2+ (UniProtKB | ChEBI)
Binding site340Zn2+ (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
      IAB31_02535

Organism names

  • Taxonomic identifier
  • Strain
    • ChiSjej4B22-8148
  • Taxonomic lineage
    Bacteria > Bacillati > Bacillota > Clostridia > Lachnospirales > Lachnospiraceae > Lachnospiraceae incertae sedis > Candidatus Choladousia

Accessions

  • Primary accession
    A0A9D1A9Z4

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
Domain10-373tRNA-guanine15 transglycosylase-like
Region252-258RNA binding

Sequence similarities

Belongs to the queuine tRNA-ribosyltransferase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    377
  • Mass (Da)
    42,989
  • Last updated
    2023-05-03 v1
  • MD5 Checksum
    3C000DBC46B2CCBEFE2A10F3A919C69A
MYKILKKDGKAKRAEFSTVHGTVQTPVFMNVGTAAAIKGAVATTDLEEIGTQIELSNTYHLHVRPGDEIIKKLGGLHRFMNWHRPILTDSGGFQVFSLASLRKIQEEGVQFQSHIDGRRIFMGPEESMQIQSNLASTIAMAFDECPSSRADREYVQNSVDRTTRWLVRCKNEMERLNSLEDTINKKQLLFGINQGAVFDDIRIEHAKRIAELDLDGYAVGGLAVGETHEEMYRILDAVVPYLPEEKPTYLMGVGTPVNILEAVERGVDFFDCVYPSRNGRHGHVYTAEGKLNLFNAKYELDEKPIQEGCGCPACRNYSRAYIRHLLKAKEMLGMRLCVLHNLYFYNHLMEDIRQAIEAGNYREFKKNWISRYEGKQE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DVGK01000032
EMBL· GenBank· DDBJ
HIR12785.1
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.
Help