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InterPro: IPR018528 Prephenate dehydratase, conserved site

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UniProtKB

Matches:

1301 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
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Accession

IPR018528 Preph_deHydtase_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00857	PREPHENATE_DEHYDR_1	783
PROSITE pattern	PS00858	PREPHENATE_DEHYDR_2	1034
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001086 Prephenate dehydratase
IPR002912 Amino acid-binding ACT
IPR008242 Bifunctional P-protein, chorismate mutase/prephenate dehydratase

GO Term annotation Help

Process

GO:0009094 L-phenylalanine biosynthetic process

Function

GO:0004664 prephenate dehydratase activity

InterPro annotation

Entry Details in BioMart

Abstract

Prephenate dehydratase (EC:4.2.1.51, 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:5.4.99.5) while in other bacteria it is a monofunctional enzyme. The sequence of monofunctional PDT aligns well with the C-terminal part of P-proteins [1].

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 [2]. The second region is located in the regulatory (Phe binding) region in the part C-terminal to PDT and this includes a conserved glutamate.

Database links Help

Enzyme: EC:4.2.1.51

CluSTr: ALLvsALL:31905:45.4

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018528

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O22241 Arogenate dehydratase 4, chloroplastic

P0A9J8 P-protein

Q54XS1 Probable phenylalanine-4-hydroxylase

Q58054 Prephenate dehydratase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001086	Prephenate dehydratase
IPR002912	Amino acid-binding ACT
IPR018528	Prephenate dehydratase, conserved site
IPR019773	Tyrosine 3-monooxygenase-like
IPR019774	Aromatic amino acid hydroxylase, C-terminal
IPR001273	Aromatic amino acid hydroxylase
IPR020822	Chorismate mutase, type II
IPR018301	Aromatic amino acid hydroxylase, iron/copper binding site
IPR010952	Chorismate mutase, gammaproteobacteria
IPR008242	Bifunctional P-protein, chorismate mutase/prephenate dehydratase
IPR002701	Chorismate mutase
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Schnappauf G, Krappmann S, Braus GH. Tyrosine and tryptophan act through the same binding site at the dimer interface of yeast chorismate mutase. J. Biol. Chem. 273 17012-7 1998 [PubMed: 9642265] http://dx.doi.org/10.1074/jbc.273.27.17012
2.	Zhang S, Wilson DB, Ganem B. Probing the catalytic mechanism of prephenate dehydratase by site-directed mutagenesis of the Escherichia coli P-protein dehydratase domain. Biochemistry 39 4722-8 2000 [PubMed: 10769128] http://dx.doi.org/10.1021/bi9926680

Additional Reading Open in usermanual
	Prakash P, Pathak N, Hasnain SE. pheA (Rv3838c) of Mycobacterium tuberculosis encodes an allosterically regulated monofunctional prephenate dehydratase that requires both catalytic and regulatory domains for optimum activity. J. Biol. Chem. 280 2005 20666-71 [PubMed: 15753077] http://dx.doi.org/10.1074/jbc.M502107200
	Fischer RS, Zhao G, Jensen RA. Cloning, sequencing, and expression of the P-protein gene (pheA) of Pseudomonas stutzeri in Escherichia coli: implications for evolutionary relationships in phenylalanine biosynthesis. J. Gen. Microbiol. 137 1991 1293-301 [PubMed: 1919506]
	Zhang S, Pohnert G, Kongsaeree P, Wilson DB, Clardy J, Ganem B. Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins. J. Biol. Chem. 273 1998 6248-53 [PubMed: 9497350] http://dx.doi.org/10.1074/jbc.273.11.6248

InterPro 23.1