Conserved Site

Prephenate dehydratase, conserved site (IPR018528)

Short name: Preph_deHydtase_CS


Prephenate dehydratase (EC:, PDT) catalyses the decarboxylation of prephenate to phenylpyruvate. In microorganisms it is part of the terminal pathway of phenylalanine biosynthesis. In some bacteria such as Escherichia coli PDT is part of a bifunctional enzyme (P-protein) that also catalyses the transformation of chorismate into prephenate (chorismate mutase, IPR002701, EC: while in other bacteria it is a monofunctional enzyme. In the archaea Archaeoglobus fulgidus is part of a trifunctional enzyme [PMID: 19082689]. The sequence of monofunctional PDT aligns well with the C-terminal part of P-proteins [PMID: 9642265].

This entry represents two conserved regions. The first contains a conserved threonine which appears to be essential for the activity of the enzyme in E. coli [PMID: 10769128]. The second region is located in the regulatory (Phe binding) region in the part C-terminal to PDT and this includes a conserved glutamate.

GO terms

Biological Process

GO:0009094 L-phenylalanine biosynthetic process

Molecular Function

GO:0004664 prephenate dehydratase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns
PROSITE patterns