TIGR00177

molybdenum cofactor biosynthesis domain

NCBIfam entry
Member databaseNCBIfam (includes TIGRFAMs)
NCBIfam typedomain
Short namemolyb_syn

Description

The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this HMM. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.

References

1. The functional principle of eukaryotic molybdenum insertases. Krausze J, Hercher TW, Zwerschke D, Kirk ML, Blankenfeldt W, Mendel RR, Kruse T. Biochem J 475, 1739-1753, (2018). View articlePMID: 29717023

2. The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin. Xiang S, Nichols J, Rajagopalan KV, Schindelin H. Structure 9, 299-310, (2001). View articlePMID: 11525167

3. Structure of the molybdenum-cofactor biosynthesis protein MoaB of Escherichia coli. Bader G, Gomez-Ortiz M, Haussmann C, Bacher A, Huber R, Fischer M. Acta Crystallogr. D Biol. Crystallogr. 60, 1068-75, (2004). View articlePMID: 15159566

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