InterPro domain: IPR038987

Eukaryotic and prokaryotic molybdoenzymes require a molybdopterin cofactor(MoCF or Moco) for their activity. The biosynthesis of this cofactor involves acomplex multistep enzymatic pathway. In bacteria, The final step in MoCF synthesis is the attachment of mononuclear Mo to MPT, a process that requires MoeA and which is enhanced by MogA in an Mg2 ATP-dependent manner [ 1 ].

In eukaryotes, MogA and MoeA are fused into a single polypeptide chain, such as in Drosophila protein cinnamon [ 2 ]. The corresponding mammalian protein gephyrin has also been implicated in the anchoring of glycinergic receptors to the cytoskeleton at inhibitory synapses [ 3 , 4 ].

1. Mutational analysis of Escherichia coli MoeA: two functional activities map to the active site cleft. Biochemistry 46, 78-86
2. The Drosophila molybdenum cofactor gene cinnamon is homologous to three Escherichia coli cofactor proteins and to the rat protein gephyrin. Genetics 137, 791-801
3. Simultaneous impairment of neuronal and metabolic function of mutated gephyrin in a patient with epileptic encephalopathy. EMBO Mol Med 7, 1580-94
4. The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin. Structure 9, 299-310