<p>This entry represents a structural domain with a beta-Grasp fold that is found in molybdopterinsynthase subunit MoaD [<cite idref="PUB00036720"/>], as well as in the thiamin biosynthesis sulphur carrier protein ThiS [<cite idref="PUB00034477"/>].</p><p>ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer. ThiS is coded in the thiCEFSGH operon in <taxon tax_id="562">Escherichia coli</taxon>. ThiS proteins have two conserved Glycines at the COOH terminus. Thiocarboxylate is formed at the last G in the activation process. Sulphur is transferred from ThiI to ThiS in a reaction catalysed by IscS [<cite idref="PUB00007564"/>]. MoaD, a protein involved in sulphur transfer during molybdopterin synthesis, is about the same length and shows limited sequence similarity to ThiS. Both have the conserved GG at the COOH end.</p>