Enzymes
| UniProtKB help_outline | 3 proteins |
Reaction participants Show >> << Hide
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Namehelp_outline
5-methyluridine54 in tRNA
Identifier
RHEA-COMP:10167
Reactive part
help_outline
- Name help_outline 5-methyluridine 5'-phosphate residue Identifier CHEBI:74447 Charge -1 Formula C10H12N2O8P Positionhelp_outline 54 SMILEShelp_outline [C@@H]1(N2C(NC(=O)C(=C2)C)=O)O[C@H](COP(*)(=O)[O-])[C@H]([C@H]1O)O* 2D coordinates Mol file for the small molecule Search links Involved in 11 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,280 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline hydrogen sulfide Identifier CHEBI:29919 (CAS: 15035-72-0) help_outline Charge -1 Formula HS InChIKeyhelp_outline RWSOTUBLDIXVET-UHFFFAOYSA-M SMILEShelp_outline [S-][H] 2D coordinates Mol file for the small molecule Search links Involved in 56 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
5-methyl-2-thiouridine54 in tRNA
Identifier
RHEA-COMP:13344
Reactive part
help_outline
- Name help_outline 5-methyl-2-thiouridine 5'-phosphate residue Identifier CHEBI:136799 Charge -1 Formula C10H12N2O7PS SMILEShelp_outline C1=C(C(NC(N1[C@@H]2O[C@H](COP(*)(=O)[O-])[C@H]([C@H]2O)O*)=S)=O)C 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline AMP Identifier CHEBI:456215 Charge -2 Formula C10H12N5O7P InChIKeyhelp_outline UDMBCSSLTHHNCD-KQYNXXCUSA-L SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 508 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline diphosphate Identifier CHEBI:33019 (Beilstein: 185088) help_outline Charge -3 Formula HO7P2 InChIKeyhelp_outline XPPKVPWEQAFLFU-UHFFFAOYSA-K SMILEShelp_outline OP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,129 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:55188 | RHEA:55189 | RHEA:55190 | RHEA:55191 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Nonredox thiolation in tRNA occurring via sulfur activation by a [4Fe-4S] cluster.
Arragain S., Bimai O., Legrand P., Caillat S., Ravanat J.L., Touati N., Binet L., Atta M., Fontecave M., Golinelli-Pimpaneau B.
Sulfur is present in several nucleosides within tRNAs. In particular, thiolation of the universally conserved methyl-uridine at position 54 stabilizes tRNAs from thermophilic bacteria and hyperthermophilic archaea and is required for growth at high temperature. The simple nonredox substitution of ... >> More
Sulfur is present in several nucleosides within tRNAs. In particular, thiolation of the universally conserved methyl-uridine at position 54 stabilizes tRNAs from thermophilic bacteria and hyperthermophilic archaea and is required for growth at high temperature. The simple nonredox substitution of the C2-uridine carbonyl oxygen by sulfur is catalyzed by tRNA thiouridine synthetases called TtuA. Spectroscopic, enzymatic, and structural studies indicate that TtuA carries a catalytically essential [4Fe-4S] cluster and requires ATP for activity. A series of crystal structures shows that (<i>i</i>) the cluster is ligated by only three cysteines that are fully conserved, allowing the fourth unique iron to bind a small ligand, such as exogenous sulfide, and (<i>ii</i>) the ATP binding site, localized thanks to a protein-bound AMP molecule, a reaction product, is adjacent to the cluster. A mechanism for tRNA sulfuration is suggested, in which the unique iron of the catalytic cluster serves to bind exogenous sulfide, thus acting as a sulfur carrier. << Less
Proc. Natl. Acad. Sci. U.S.A. 114:7355-7360(2017) [PubMed] [EuropePMC]