<p>This putative domain is found in the MoeZ protein and the MoeB protein. The domain has twoCXXC motifs that are only partly conserved. MoeZ is necessary for the synthesis of pyridine-2,6-bis(thiocarboxylic acid), a small secreted metabolite that has a high affinity for transitionmetals, increases iron uptake efficiency by 20% in <taxon tax_id="316">Pseudomonas stutzeri</taxon>, has the ability to reduce both soluble and mineral forms ofiron, and has antimicrobial activity towards several species of bacteria. MoeB is the molybdopterin synthase activating enzyme in the molybdopterin cofactor biosynthesis pathway.Both these enzymes are members of a superfamily consisting of related but structurally distinct proteins that are members of pathways involved in thetransfer of sulphur-containing moieties to metabolites [<cite idref="PUB00010435"/>] and both also contain the UBA/THIF-type NAD/FAD binding fold (<db_xref db="INTERPRO" dbkey="IPR000594"/>). </p> MoeZ/MoeB