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InterPro: IPR001086 Prephenate dehydratase

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UniProtKB

Matches:

1737 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
Matches in BioMart

Accession

IPR001086 Preph_deHydtase

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00800	PDT	1735
PROSITE profile	PS51171	PREPHENATE_DEHYDR_3	1713
Signatures in BioMart

InterPro Relationships Help

Found in

IPR008242 Bifunctional P-protein, chorismate mutase/prephenate dehydratase

Contains

IPR018528 Prephenate dehydratase, conserved site

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].

Structural links Help

PDB - click here

SCOP: c.94.1.1

CATH: 3.40.190.10

Database links Help

PDBe-motif: PS00857 , PS00858

Enzyme: EC:4.2.1.51

PROSITE doc: PDOC00671

PANDIT: PF00800

Blocks: IPB001086

CluSTr: ALLvsALL:31905:45.4

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001086

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O14361 Putative prephenate dehydratase

O22241 Arogenate dehydratase 4, chloroplastic

P0A9J8 P-protein

P32452 Putative prephenate dehydratase

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
IPR001273	Aromatic amino acid hydroxylase
IPR020822	Chorismate mutase, type II
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

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, 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 2000 4722-8 [PubMed: 10769128] http://dx.doi.org/10.1021/bi9926680
	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
	Tan K, Li H, Zhang R, Gu M, Clancy ST, Joachimiak A. Structures of open (R) and close (T) states of prephenate dehydratase (PDT)--implication of allosteric regulation by L-phenylalanine. J. Struct. Biol. 162 2008 94-107 [PubMed: 18171624] http://dx.doi.org/10.1016/j.jsb.2007.11.009

InterPro 23.1