A number of proteins involved in the biosynthesis of metallo cofactors have
been shown [1,2] to be evolutionary related. These proteins are:
Bacterial and archebacterial protein moaA, which is involved in the
biosynthesis of the molybdenum cofactor (molybdopterin; MPT).
Arabidopsis thaliana cnx2, a protein involved in molybdopterin biosynthesis
and which is highlys similar to moaA.
Bacillus subtilis narA, which seems to be the moaA ortholog in that
Bacterial protein nifB (or fixZ) which is involved in the biosynthesis of
the nitrogenase iron-molybdenum cofactor.
Bacterial protein pqqE which is involved in the biosynthesis of the
cofactor pyrrolo-quinoline-quinone (PQQ).
Pyrococcus furiosus cmo, a protein involved in the synthesis of a
molybdopterin-based tungsten cofactor.
Caenorhabditis elegans hypothetical protein F49E2.1.
All these proteins share, in their N-terminal region, a conserved domain that
contains three cysteines. In moaA, these cysteines have been shown  to be
important for the biological activity. They could be inolved in the binding of
an iron-sulfur cluster.
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