Q7NKL3 · QUEG_GLOVI
- ProteinEpoxyqueuosine reductase
- GenequeG
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids319 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic activity
- AH2 + epoxyqueuosine34 in tRNA = A + H2O + queuosine34 in tRNA
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 [4Fe-4S] clusters per monomer.
Pathway
tRNA modification; tRNA-queuosine biosynthesis.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 128 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 182 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 185 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 188 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 192 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 208 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 236 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 239 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 243 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | epoxyqueuosine reductase activity | |
Molecular Function | metal ion binding | |
Biological Process | queuosine biosynthetic process | |
Biological Process | tRNA modification |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEpoxyqueuosine reductase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Gloeobacterales > Gloeobacteraceae > Gloeobacter
Accessions
- Primary accessionQ7NKL3
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000416072 | 1-319 | Epoxyqueuosine reductase | |||
Sequence: MAPTAAQIKSRARALGFHKVGIARADALDGEAAERLGGWLAAGYAGEMRWMHDPRRRDIQQVLPGVRSVICVALSYNTAQGEPAPGQARISRYALGRDYHKVLGKPLKELARWIEASDPGCRAVAYVDTGPVQEKAWAEAAGLGWIGKNACLITLEYGSWVFLGEILTTLDLEANDPHPNYCGTCTRCLSACPTAALVEPAVVDARKCLAYHTIENRAPELPEAIAEHQHGWVVGCDLCQTCCPFNLRAERWGRYSEVADFAPRDPWNEITLDQLADLSDAEFERWSEGSAIRRVKASGLRRNARSALGASGDSLAQAH |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 173-202 | 4Fe-4S ferredoxin-type | ||||
Sequence: EANDPHPNYCGTCTRCLSACPTAALVEPAV |
Sequence similarities
Belongs to the QueG family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length319
- Mass (Da)34,806
- Last updated2003-12-15 v1
- ChecksumBC2D8254709A608C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BA000045 EMBL· GenBank· DDBJ | BAC89405.1 EMBL· GenBank· DDBJ | Genomic DNA |