D2NPM3 · D2NPM3_ROTMD
- ProteinQueuine tRNA-ribosyltransferase
- Genetgt
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids466 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
- 7-aminomethyl-7-carbaguanine + guanosine34 in tRNA = 7-aminomethyl-7-carbaguanosine34 in tRNA + guanine
Cofactor
Note: Binds 1 zinc ion per subunit.
Pathway
tRNA modification; tRNA-queuosine biosynthesis.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 148 | Proton acceptor | |||
Binding site | 148-152 | substrate | |||
Binding site | 235 | substrate | |||
Binding site | 285 | substrate | |||
Binding site | 312 | substrate | |||
Active site | 359 | Nucleophile | |||
Binding site | 397 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 399 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 402 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 428 | Zn2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | metal ion binding | |
Molecular Function | tRNA-guanosine(34) queuine transglycosylase activity | |
Biological Process | queuosine biosynthetic process | |
Biological Process | tRNA wobble guanine modification | |
Biological Process | tRNA-guanine transglycosylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameQueuine tRNA-ribosyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Rothia
Accessions
- Primary accessionD2NPM3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-20 | Disordered | |||
Domain | 71-158 | tRNA-guanine15 transglycosylase-like | |||
Domain | 193-461 | tRNA-guanine15 transglycosylase-like | |||
Region | 364-368 | RNA binding; important for wobble base 34 recognition | |||
Sequence similarities
Belongs to the queuine tRNA-ribosyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length466
- Mass (Da)51,371
- Last updated2010-03-02 v1
- ChecksumD80AECC5B94CCDA7
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP011540 EMBL· GenBank· DDBJ | BAI65591.1 EMBL· GenBank· DDBJ | Genomic DNA |