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InterPro: IPR018508 3-dehydroquinate dehydratase, active site

Protein matches Help

UniProtKB

Matches:

250 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
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Accession

IPR018508 3-dehydroquinate_DH_AS

Type

Active_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS01028	DEHYDROQUINASE_I	250
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001381 Dehydroquinase class I
IPR008289 Pentafunctional AroM protein
IPR013785 Aldolase-type TIM barrel

GO Term annotation Help

Function

GO:0003855 3-dehydroquinate dehydratase activity

InterPro annotation

Entry Details in BioMart

Abstract

3-dehydroquinate dehydratase (EC:4.2.1.10), or dehydroquinase, catalyzes the conversion of 3-dehydroquinate into 3-dehydroshikimate. It is the third step in the shikimate pathway for the biosynthesis of aromatic amino acids from chorismate. Two classes of dehydroquinases exist, known as types I and II.

The best studied type I enzyme is from Escherichia coli (gene aroD) and related bacteria where it is a homodimeric protein. In fungi, dehydroquinase is part of a multifunctional enzyme which catalyzes five consecutive steps in the shikimate pathway. This conserved signature pattern contains the histidine that is involved in the catalytic mechanism [1].

Structural links Help

PDB - click here

SCOP: c.1.10.1

CATH: 3.20.20.70

Database links Help

Enzyme: EC:4.2.1.10

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018508

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A4FWC6 3-dehydroquinate dehydratase

O66440 3-dehydroquinate dehydratase

P07547 Pentafunctional AROM polypeptide

P08566 Pentafunctional AROM polypeptide

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013785	Aldolase-type TIM barrel
IPR013792	RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta
IPR002658	3-dehydroquinate synthase AroB
IPR013708	Shikimate dehydrogenase substrate binding, N-terminal
IPR010110	Shikimate-5-dehydrogenase
IPR008289	Pentafunctional AroM protein
IPR016037	3-dehydroquinate synthase AroB, subgroup
IPR000623	Shikimate kinase
IPR001381	Dehydroquinase class I
IPR018508	3-dehydroquinate dehydratase, active site
IPR016040	NAD(P)-binding domain
IPR006151	Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
IPR006264	3-phosphoshikimate 1-carboxyvinyltransferase, subgroup
IPR001986	3-phosphoshikimate 1-carboxyvinyltransferase, core
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Deka RK, Kleanthous C, Coggins JR. Identification of the essential histidine residue at the active site of Escherichia coli dehydroquinase. J. Biol. Chem. 267 22237-42 1992 [PubMed: 1429576] http://intl.jbc.org/cgi/content/abstract/267/31/22237

Additional Reading Open in usermanual
	Lee WH, Perles LA, Nagem RA, Shrive AK, Hawkins A, Sawyer L, Polikarpov I. Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity. Acta Crystallogr. D Biol. Crystallogr. 58 2002 798-804 [PubMed: 11976491] http://dx.doi.org/10.1107/S0907444902003918
	Gourley DG, Shrive AK, Polikarpov I, Krell T, Coggins JR, Hawkins AR, Isaacs NW, Sawyer L. The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction. Nat. Struct. Biol. 6 1999 521-5 [PubMed: 10360352] http://dx.doi.org/10.1038/9287

InterPro 23.1