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InterPro: IPR001381 Dehydroquinase class I

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UniProtKB

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728 proteins

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

Accession

IPR001381 DHquinase_I

Type

Domain

Signatures Help

Database	ID	Name	Proteins
HAMAP	MF_00214	DHquinase_I	546
Pfam	PF01487	DHquinase_I	719
TIGRFAMs	TIGR01093	aroD	565
Signatures in BioMart

InterPro Relationships Help

Parent

IPR013785 Aldolase-type TIM barrel

Found in

IPR008289 Pentafunctional AroM protein

Contains

IPR018508 3-dehydroquinate dehydratase, active site

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. A histidine [1] is involved in the catalytic mechanism.

Structural links Help

PDB - click here

SCOP: c.1.10.1

CATH: 3.20.20.70

Database links Help

PDBe-motif: PS01028

Enzyme: EC:4.2.1.10

PROSITE doc: PDOC00788

PANDIT: PF01487

Blocks: IPB001381

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001381

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O30011 3-dehydroquinate dehydratase

O66440 3-dehydroquinate dehydratase

P07547 Pentafunctional AROM polypeptide

P08566 Pentafunctional AROM polypeptide

Q9SQT8 Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic

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
IPR011342	Quinate/shikimate 5-dehydrogenase
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
	Nichols CE, Lockyer M, Hawkins AR, Stammers DK. Crystal structures of Staphylococcus aureus type I dehydroquinase from enzyme turnover experiments. Proteins 56 2004 625-8 [PubMed: 15229896] http://dx.doi.org/10.1002/prot.20165
	Hawkins AR, Lamb HK. The molecular biology of multidomain proteins. Selected examples. Eur. J. Biochem. 232 1995 7-18 [PubMed: 7556173] http://dx.doi.org/10.1111/j.1432-1033.1995.tb20775.x
	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