A0A0G9LIH2 · A0A0G9LIH2_9CLOT
- ProteinQueuine tRNA-ribosyltransferase
- Genetgt
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids380 (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 | 93 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 93-97 | substrate | ||||
Sequence: DSGGF | ||||||
Binding site | 147 | substrate | ||||
Sequence: D | ||||||
Binding site | 198 | substrate | ||||
Sequence: Q | ||||||
Binding site | 225 | substrate | ||||
Sequence: G | ||||||
Active site | 275 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 313 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 315 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 318 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 344 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | tRNA-guanosine(34) queuine transglycosylase activity | |
Biological Process | queuosine biosynthetic process | |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Clostridium
Accessions
- Primary accessionA0A0G9LIH2
Proteomes
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 domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 13-376 | tRNA-guanine15 transglycosylase-like | ||||
Sequence: GEARRGRFETPHGTIETPVFMNVGTLAVIKGAVSTMDLKEIGCQVELSNTYHLHLRPSDKVVASLGGLHNFMNWDRPILTDSGGFQVFSLSGMRKIKEEGVYFSSHIDGKKIFMGPEESMQIQSNLASTIAMAFDECIPNPSTRDYVEKSVARTTRWLERCKKEMDRLNSLPETINKEQMLFGINQGGCYEDIRIEHAKTITKMDLDGYAIGGLAVGETHEEMYRIIDAVVPYLPEDKPIYLMGVGTPSNILEAVDRGVDFFDCVLPARNGRHGHVFTKEGKINLMNAKFELDTRPIDEGCQCPACRSYTRAYIRHLFKAKEMLAMRLCVLHNLYFYNKLMEDIRSAIDGGYFKEFKDEKLKEW | ||||||
Region | 256-262 | RNA binding | ||||
Sequence: GVGTPSN | ||||||
Region | 280-284 | RNA binding; important for wobble base 34 recognition | ||||
Sequence: ARNGR |
Sequence similarities
Belongs to the queuine tRNA-ribosyltransferase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length380
- Mass (Da)43,182
- Last updated2015-09-16 v1
- ChecksumF8813298E2E2FBCC
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LBMX01000049 EMBL· GenBank· DDBJ | KLE16108.1 EMBL· GenBank· DDBJ | Genomic DNA |