Pathways & interactions
MoaB/Mog-like domain superfamily (IPR036425)
Short name: MoaB/Mog-like_dom_sf
- MoaB/Mog domain (IPR001453)
- Competence-induced protein CinA (IPR008135)
- Bifunctional molybdenum cofactor biosynthesis MobB/MoeA (IPR012182)
- FAD synthetase with the MoaB/Mog domain (IPR012183)
- Bifunctional molybdopterin binding protein /nucleotidyl transferase, putative (IPR012184)
- Molybdenum cofactor biosynthesis protein MoaB (IPR012245)
- Bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA (IPR012247)
- Molybdenum cofactor biosynthesis protein B, proteobacteria (IPR013484)
- Putative competence-damage inducible protein, Archaea (IPR023055)
- Molybdopterin biosynthesis protein MoeA-like (IPR038987)
MoaB/Mog domain, also known as Cnx1G domain, is found in the bacterial molybdenum cofactor (Moco) biosynthesis protein MoaB/Mog and N-terminal of the eukaryotic MoCF biosynthesis proteins, such as the Drosophila protein cinnamon, the Arabidopsis protein cnx1 and the mammal protein gephyrin [PMID: 19675644]. These proteins are involved in the final steps of Moco synthesis. In E. coli two proteins, MogA and MoeA are essential for Mo insertion into molybdopterin, while in plants and animals one fusion protein with two domains (G and E domains) fulfils this function. The G domain of Cnx1 and gephyrin shares similarity with MoaB/Mog, while their E domain displays similarities to the sulfurtransferase rhodanese (homologous to E. coli MoeA/chlE) [PMID: 15073332]. Structurally, MogA is folded into a compact molecule with alpha/beta/alpha architecture and forms a trimer [PMID: 10636880]. The Cnx1G domain has been shown to bind molybdopterin [PMID: 12590921].
This domain is also found in N-terminal of the FAD synthases belonging to the COG1058 family that catalyses the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme [PMID: 23776507]. The COG1058 family member CinA from Thermus thermophilus is shown to have both nicotinamide mononucleotide deamidase and ADP-ribose pyrophosphatase activities, with ADP-ribose pyrophosphatase activity attributed to the N-termminal domain [PMID: 25313401].
The structure of the MoaB/Mog domain has three layers (alpha/beta/alpha) with mixed beta-sheet of five strands where the strand 5 is antiparallel to the rest.