PROSITE documentation PDOC00828Molybdenum cofactor biosynthesis proteins signatures
Eukaroytic and prokaryotic molybdoenzymes require a molybdopterin cofactor (MoCF) for their activity. The biosynthesis of this cofactor involves a complex multistep enzymatic pathway. One of the eukaryotic proteins involved in this pathway is the Drosophila protein cinnamon [1] which is highly similar to gephyrin, a rat microtubule-associated protein which was thought to anchor the glycine receptor to subsynaptic microtubules. Cinnamon and gephyrin are evolutionary related, in their N-terminal half, to the Escherichia coli MoCF biosynthesis proteins mog/chlG and moaB/chlA2 and, in their C-terminal half, to Escherichia coli moeA/chlE.
As signature patterns, we selected two conserved regions: one located in the N-terminal half, the other in the C-terminal half.
Last update:December 2004 / Pattern and text revised.
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| 1 | Authors | Kamdar K.P. Shelton M.E. Finnerty V. |
| Title | The Drosophila molybdenum cofactor gene cinnamon is homologous to three Escherichia coli cofactor proteins and to the rat protein gephyrin. | |
| Source | Genetics 137:791-801(1994). | |
| PubMed ID | 8088525 |
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