ID Card:
| Full name: |
tRNA uridine(34) hydroxylase |
| Synonym: |
yegQ |
| UniProt: |
P76403 |
| Enzyme type: |
|
| Position of modification - modification: |
t:None - ho5U
|
| Level of experimental evidence: |
2 |
| Level of experimental reliability: |
2 |
Protein sequence:
MFKPELLSPAGTLKNMRYAFAYGADAVYAGQPRYSLRVRNNEFNHENLQLGINEAHALGKKFYVVVNIAPHNAKLKTFIRDLKPVVEMGPDALIMSDPGLIMLVREHFPEMPIHLSVQANAVNWATVKFWQQMGLTRVILSRELSLEEIEEIRNQVPDMEIEIFVHGALCMAYSGRCLLSGYINKRDPNQGTCTNACRWEYNVQEGKEDDVGNIVHKYEPIPVQNVEPTLGIGAPTDKVFMIEEAQRPGEYMTAFEDEHGTYIMNSKDLRAIAHVERLTKMGVHSLKIEGRTKSFYYCARTAQVYRKAIDDAAAGKPFDTSLLETLEGLAHRGYTEGFLRRHTHDDYQNYEYGYSVSDRQQFVGEFTGERKGDLAAVAVKNKFSVGDSLELMTPQGNINFTLEHMENAKGEAMPIAPGDGYTVWLPVPQDLELNYALLMRNFSGETTRNPHGK
Comments:
Involved in prephenate-dependent formation of 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs, the first step in 5-carboxymethoxyuridine (cmo5U) biosynthesis. Involved differently in ho5U formation in each tRNA; tRNA(Leu3) and tRNA(Pro3) are major targets of TrhP.
| Reaction |
Substrate |
SubstrateType |
Position |
(Anti)Codon |
Modified (Anti)Codon |
Amino Acid Change |
Transcript Name |
Transcript Region |
Cellular Localization |
References |
|
U:ho5U
|
tRNA (t) |
tRNA/tRNA/prokaryotic cytosol |
34 |
|
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Publications:
| Title |
Authors |
Journal |
Details |
PubMed Id |
DOI |
| Dual pathways of tRNA hydroxylation ensure efficient translation by expanding decoding capability. |
Sakai Y; Kimura S; Suzuki T |
Nat Commun |
[details]
|
31253794
|
10.1038/s41467-019-10750-8
|