PROSITE documentation PDOC00828
Molybdenum 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.


Technical section

PROSITE methods (with tools and information) covered by this documentation:

MOCF_BIOSYNTHESIS_1, PS01078; Molybdenum cofactor biosynthesis proteins signature 1  (PATTERN)

MOCF_BIOSYNTHESIS_2, PS01079; Molybdenum cofactor biosynthesis proteins signature 2  (PATTERN)


1AuthorsKamdar K.P. Shelton M.E. Finnerty V.
TitleThe Drosophila molybdenum cofactor gene cinnamon is homologous to three Escherichia coli cofactor proteins and to the rat protein gephyrin.
SourceGenetics 137:791-801(1994).
PubMed ID8088525

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