A0A0A1U8W0 · A0A0A1U8W0_ENTIV
- ProteinQueuine tRNA-ribosyltransferase catalytic subunit 1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids397 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). 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 queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product.
Catalytic activity
- guanosine34 in tRNA + queuine = guanine + queuosine34 in tRNA
Cofactor
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 92 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 92-96 | substrate | ||||
Sequence: DSGGF | ||||||
Binding site | 146 | substrate | ||||
Sequence: D | ||||||
Binding site | 190 | substrate | ||||
Sequence: Q | ||||||
Binding site | 217 | substrate | ||||
Sequence: G | ||||||
Active site | 267 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 305 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 307 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 310 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 342 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | metal ion binding | |
Molecular Function | tRNA-guanosine(34) queuine transglycosylase activity | |
Biological Process | tRNA-guanine transglycosylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameQueuine tRNA-ribosyltransferase catalytic subunit 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Amoebozoa > Evosea > Archamoebae > Mastigamoebida > Entamoebidae > Entamoeba
Accessions
- Primary accessionA0A0A1U8W0
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Subunit
Heterodimer of a catalytic subunit and an accessory subunit.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-373 | tRNA-guanine15 transglycosylase-like | ||||
Sequence: RARQCTLHLPHGEVETPVFMPVGTKGSVKSLTYEQVTEMGCQILLANTYHMYLHPGVTVLKKSGGLHNYTKWNGNILTDSGGFQMVSLSETMSVSEEGVVFESIVDKKQINLPPEESIHIQQAIGSDIMMQLDDVVSSLTTGPRVSEAMERSVRWLGRCKKVYEETKDKQNLFGIIQGGLNADLRKKCLEGMVAVDTPGYAIGGLSGGEAKDDFWRMVDVSAQGLPETKPRYLMGVGYPVEMILCVLFGVDMFDCVYPTRTARFGTVFSDDGMVALKVNKYKDQYEVIDKNCDCLCCQKGNGLTKSALHFMFVNGAEEGTPVAQYLTHHNITYLFNLMRKYRVAIREKKAKVFAKEYIMR | ||||||
Region | 248-254 | RNA binding | ||||
Sequence: GVGYPVE | ||||||
Region | 272-276 | RNA binding; important for wobble base 34 recognition | ||||
Sequence: TRTAR |
Sequence similarities
Belongs to the queuine tRNA-ribosyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length397
- Mass (Da)44,202
- Last updated2015-02-04 v1
- Checksum819C4CE0DE0AFB5B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KB206604 EMBL· GenBank· DDBJ | ELP89561.1 EMBL· GenBank· DDBJ | Genomic DNA |