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InterPro: IPR001874 Dehydroquinase, class II

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UniProtKB

Matches:

1381 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
Matches in BioMart

Accession

IPR001874 DHquinase_II

Type

Family

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.40.50.9100	DHquinase_II	1313
HAMAP	MF_00169	AroQ	978
ProDom	PD004527	DHquinase_II	1377
Pfam	PF01220	DHquinase_II	1362
PIRSF	PIRSF001399	DHquinase_II	1320
PANTHER	PTHR21272	DHquinase_II	1338
SuperFamily	SSF52304	DHquinase_II	1351
TIGRFAMs	TIGR01088	aroQ	1231
Signatures in BioMart

InterPro Relationships Help

Contains

IPR018509 Dehydroquinase, class II, conserved 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. Class-II enzymes are homododecameric enzymes of about 17 kDa. They are found in some bacteria such as actinomycetales [1, 2] and some fungi where they act in a catabolic pathway that allows the use of quinic acid as a carbon source.

Structural links Help

PDB - click here

SCOP: c.23.13.1

CATH: 3.40.50.9100

Database links Help

PDBe-motif: PS01029

Enzyme: EC:4.2.1.10

PROSITE doc: PDOC00789

PANDIT: PF01220

Blocks: IPB001874

PRIAM: PRI000430

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001874

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P05147 Catabolic 3-dehydroquinase

P0A4Z6 3-dehydroquinate dehydratase

P73367 3-dehydroquinate dehydratase

Q5M936 Torsin-3A

Q9ER38 Torsin-3A

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR018509	Dehydroquinase, class II, conserved site
IPR001874	Dehydroquinase, class II
IPR001270	Chaperonin clpA/B
IPR010448	Torsin
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Garbe T, Servos S, Hawkins A, Dimitriadis G, Young D, Dougan G, Charles I. The Mycobacterium tuberculosis shikimate pathway genes: evolutionary relationship between biosynthetic and catabolic 3-dehydroquinases. Mol. Gen. Genet. 228 385-92 1991 [PubMed: 1910148] http://dx.doi.org/10.1007/BF00260631
2.	Lalonde G, O'Hanley PD, Stocker BA, Denich KT. Characterization of a 3-dehydroquinase gene from Actinobacillus pleuropneumoniae with homology to the eukaryotic genes qa-2 and QUTE. Mol. Microbiol. 11 273-80 1994 [PubMed: 8170389] http://dx.doi.org/10.1111/j.1365-2958.1994.tb00307.x

Additional Reading Open in usermanual
	Toscano MD, Stewart KA, Coggins JR, Lapthorn AJ, Abell C. Rational design of new bifunctional inhibitors of type II dehydroquinase. Org. Biomol. Chem. 3 2005 3102-4 [PubMed: 16106291] http://dx.doi.org/10.1039/b507156a
	Payne RJ, Riboldi-Tunnicliffe A, Kerbarh O, Abell AD, Lapthorn AJ, Abell C. Design, synthesis, and structural studies on potent biaryl inhibitors of type II dehydroquinases. 2 2007 1010-3 [PubMed: 17487901] http://dx.doi.org/10.1002/cmdc.200700062
	Robinson DA, Stewart KA, Price NC, Chalk PA, Coggins JR, Lapthorn AJ. Crystal structures of Helicobacter pylori type II dehydroquinase inhibitor complexes: new directions for inhibitor design. J. Med. Chem. 49 2006 1282-90 [PubMed: 16480265] http://dx.doi.org/10.1021/jm0505361
	Maes D, Gonzalez-Ramirez LA, Lopez-Jaramillo J, Yu B, De Bondt H, Zegers I, Afonina E, Garcia-Ruiz JM, Gulnik S. Structural study of the type II 3-dehydroquinate dehydratase from Actinobacillus pleuropneumoniae. Acta Crystallogr. D Biol. Crystallogr. 60 2004 463-71 [PubMed: 14993670] http://dx.doi.org/10.1107/S090744490302969X
	Frederickson M, Roszak AW, Coggins JR, Lapthorn AJ, Abell C. (1R,4S,5R)-3-Fluoro-1,4,5-trihydroxy-2-cyclohexene-1-carboxylic acid: the fluoro analogue of the enolate intermediate in the reaction catalyzed by type II dehydroquinases. Org. Biomol. Chem. 2 2004 1592-6 [PubMed: 15162210] http://dx.doi.org/10.1039/b404535a

InterPro 24.0