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InterPro: IPR018509 Dehydroquinase, class II, conserved site

Protein matchesHelp
UniProtKB
Matches:
1191 proteins
AccessionHelp IPR018509 DHquinase_II_CS
TypeHelp Conserved_site
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR001874 Dehydroquinase, class II
GO Term annotationHelp
Function GO:0003855 3-dehydroquinate dehydratase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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. This conserved signature pattern is located in the N-terminal region.

Structural linksHelp
SCOP: c.23.13.1
CATH: 3.40.50.9100
Database linksHelp
Enzyme: EC:4.2.1.10

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR018509 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
A2BPL5 3-dehydroquinate dehydratase

P05147 Catabolic 3-dehydroquinase

P0A4Z6 3-dehydroquinate dehydratase

P73367 3-dehydroquinate dehydratase

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
SWISS-MODEL
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp
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 ReadingHelp
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
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InterPro 23.1