<p> Members of this family catalyse the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of tRNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 (<db_xref db="SWISSPROT" dbkey="P53759"/>) from <taxon tax_id="4932">Saccharomyces cerevisiae</taxon> (Baker's yeast) acts on pre-tRNA-Phe, while Dus 2 (<db_xref db="SWISSPROT" dbkey="P53720"/>) acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD [<cite idref="PUB00014304"/>]. Some family members may be targeted to the mitochondria and even have a role in mitochondria [<cite idref="PUB00014304"/>]. </p><p>The signature pattern used in this entry contains a conserved cysteine which could be one of the active site residues.</p> tRNA-dihydrouridine synthase, conserved site