Home  |  Contact
PROSITE documentation PDOC00141 [for PROSITE entry PS00156]

Orotidine 5'-phosphate decarboxylase active site


Orotidine 5'-phosphate decarboxylase (EC (OMPdecase) [1,2] catalyzes the last step in the de novo biosynthesis of pyrimidines, the decarboxylation of OMP into UMP. In higher eukaryotes OMPdecase is part, with orotate phosphoribosyltransferase, of a bifunctional enzyme, while the prokaryotic and fungal OMPdecases are monofunctional protein.

Some parts of the sequence of OMPdecase are well conserved across species. The best conserved region is located in the N-terminal half of OMPdecases and is centered around a lysine residue which is essential for the catalytic function of the enzyme. We have used this region as a signature pattern.

Last update:

January 2002 / Pattern and text revised.

Technical section

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

OMPDECASE, PS00156; Orotidine 5'-phosphate decarboxylase active site  (PATTERN)


1AuthorsJacquet M. Guilbaud R. Garreau H.
TitleSequence analysis of the DdPYR5-6 gene coding for UMP synthase in Dictyostelium discoideum and comparison with orotate phosphoribosyl transferases and OMP decarboxylases.
SourceMol. Gen. Genet. 211:441-445(1988).
PubMed ID2835631

2AuthorsKimsey H.H. Kaiser D.
TitleThe orotidine-5'-monophosphate decarboxylase gene of Myxococcus xanthus. Comparison to the OMP decarboxylase gene family.
SourceJ. Biol. Chem. 267:819-824(1992).
PubMed ID1730672

PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)