E6X4P3 · QUEG_CELAD
- ProteinEpoxyqueuosine reductase
- GenequeG
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids306 (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 | 131 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 185 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 188 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 191 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 195 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 211 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 238 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 241 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 245 | [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 > Bacteroidota > Flavobacteriia > Flavobacteriales > Flavobacteriaceae > Cellulophaga
Accessions
- Primary accessionE6X4P3
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000416067 | 1-306 | Epoxyqueuosine reductase | |||
Sequence: MNTKEKHSDLIKAEAIRLGFLSCGISKANFLEEEAPRLEKWLKNNMNGEMQYMENHFDKRLDPRLLVDDAKSVISLTLNYYPEEQQADGTYKISKYAYGHDYHHVIKGKLKQLQEFISEEIGEVGGRAFVDSAPVLDKAWAAKSGLGWIGKHSNLLTQKTGSFYFIAELIVDLDLTYDHPVTDHCGTCTACIDACPTQAIVQPYVVDGSKCISYFTIELKNEIPQEFQGKFDDWAFGCDVCQDVCPWNRFSKPHSEPLFNPHPDLLSLTKKDWEEITDDVFKKVFQKSAVKRTKYAGLKRNIDFLK |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 173-205 | 4Fe-4S ferredoxin-type | ||||
Sequence: LDLTYDHPVTDHCGTCTACIDACPTQAIVQPYV |
Sequence similarities
Belongs to the QueG family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length306
- Mass (Da)34,962
- Last updated2011-03-08 v1
- Checksum9E6D5E0B88CC90DD
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002453 EMBL· GenBank· DDBJ | ADV49368.1 EMBL· GenBank· DDBJ | Genomic DNA |