EzCatDB: S00382

DB codeS00382
CATH domainDomain 13.40.50.9100Catalytic domain
E.C.4.2.1.10
MACiEM0055


Enzyme Name
Swiss-protKEGG

P15474P0A4Z6P54517
Protein name3-dehydroquinate dehydratase3-dehydroquinate dehydratase3-dehydroquinate dehydratase3-dehydroquinate dehydratase
3-dehydroquinate hydrolase
DHQase
dehydroquinate dehydratase
3-dehydroquinase
5-dehydroquinase
dehydroquinase
5-dehydroquinate dehydratase
5-dehydroquinate hydro-lyase
3-dehydroquinate hydro-lyase
Synonyms3-dehydroquinase
EC 4.2.1.10
Type II DHQase
3-dehydroquinase
EC 4.2.1.10
Type II DHQase
3-dehydroquinase
EC 4.2.1.10
Type II DHQase

KEGG pathways
MAP codePathways
MAP00400Phenylalanine, tyrosine and tryptophan biosynthesis

Swiss-prot:Accession NumberP15474P0A4Z6P54517
Entry nameAROQ_STRCOAROQ_MYCTUAROQ_BACSU
Activity3-dehydroquinate = 3-dehydroshikimate + H(2)O.3-dehydroquinate = 3-dehydroshikimate + H(2)O.3-dehydroquinate = 3-dehydroshikimate + H(2)O.
SubunitHomododecamer.Homododecamer.Homododecamer.
Subcellular location


Cofactor




SubstratesProducts
KEGG-idC00944C02637C00001
Compound3-Dehydroquinate3-DehydroshikimateH2O
Typecarbohydrate,carboxyl groupcarbohydrate,carboxyl groupH2O
1d0iAUnboundUnbound
1d0iBUnboundUnbound
1d0iCUnboundUnbound
1d0iDUnboundUnbound
1d0iEUnboundUnbound
1d0iFUnboundUnbound
1d0iGUnboundUnbound
1d0iHUnboundUnbound
1d0iIUnboundUnbound
1d0iJUnboundUnbound
1d0iKUnboundUnbound
1d0iLUnboundUnbound
1gu0AUnboundUnbound
1gu0BUnboundUnbound
1gu0CUnboundUnbound
1gu0DUnboundUnbound
1gu0EUnboundUnbound
1gu0FUnboundUnbound
1gu0GUnboundUnbound
1gu0HUnboundUnbound
1gu0IUnboundUnbound
1gu0JUnboundUnbound
1gu0KUnboundUnbound
1gu0LUnboundUnbound
1gu1AAnalogue:FA1Unbound
1gu1BAnalogue:FA1Unbound
1gu1CAnalogue:FA1Unbound
1gu1DAnalogue:FA1Unbound
1gu1EAnalogue:FA1Unbound
1gu1FAnalogue:FA1Unbound
1gu1GAnalogue:FA1Unbound
1gu1HAnalogue:FA1Unbound
1gu1IAnalogue:FA1Unbound
1gu1JAnalogue:FA1Unbound
1gu1KAnalogue:FA1Unbound
1gu1LAnalogue:FA1Unbound
1gtzAUnboundBound:DHK
1gtzBUnboundBound:DHK
1gtzCUnboundBound:DHK
1gtzDUnboundBound:DHK
1gtzEUnboundBound:DHK
1gtzFUnboundBound:DHK
1gtzGUnboundBound:DHK
1gtzHUnboundBound:DHK
1gtzIUnboundBound:DHK
1gtzJUnboundBound:DHK
1gtzKUnboundBound:DHK
1gtzLUnboundBound:DHK
1h05AUnboundUnbound
1h0rAAnalogue:FA1Unbound
1h0sAAnalogue:FA6Unbound
2dhqAUnboundUnbound
1gqoAUnboundUnbound
1gqoBUnboundUnbound
1gqoCUnboundUnbound
1gqoDUnboundUnbound
1gqoEUnboundUnbound
1gqoFUnboundUnbound
1gqoGUnboundUnbound
1gqoHUnboundUnbound
1gqoIUnboundUnbound
1gqoJUnboundUnbound
1gqoKUnboundUnbound
1gqoLUnboundUnbound
1gqoMUnboundUnbound
1gqoNUnboundUnbound
1gqoOUnboundUnbound
1gqoPUnboundUnbound
1gqoQUnboundUnbound
1gqoRUnboundUnbound
1gqoSUnboundUnbound
1gqoTUnboundUnbound
1gqoUUnboundUnbound
1gqoVUnboundUnbound
1gqoXUnboundUnbound
1gqoYUnboundUnbound

Active-site residues
resource
literature [4] & [12]
pdbCatalytic residuescomment
1d0iAASN 16;ARG 23;TYR 28;HIS 106

1d0iBASN 16;ARG 23;TYR 28;HIS 106

1d0iCASN 16;ARG 23;TYR 28;HIS 106

1d0iDASN 16;ARG 23;TYR 28;HIS 106

1d0iEASN 16;ARG 23;TYR 28;HIS 106

1d0iFASN 16;ARG 23;TYR 28;HIS 106

1d0iGASN 16;ARG 23;TYR 28;HIS 106

1d0iHASN 16;ARG 23;TYR 28;HIS 106

1d0iIASN 16;ARG 23;TYR 28;HIS 106

1d0iJASN 16;ARG 23;TYR 28;HIS 106

1d0iKASN 16;ARG 23;TYR 28;HIS 106

1d0iLASN 16;ARG 23;TYR 28;HIS 106

1gu0AASN 16;ARG 23;TYR 28;HIS 106

1gu0BASN 16;ARG 23;TYR 28;HIS 106

1gu0CASN 16;ARG 23;TYR 28;HIS 106

1gu0DASN 16;ARG 23;TYR 28;HIS 106

1gu0EASN 16;ARG 23;TYR 28;HIS 106

1gu0FASN 16;ARG 23;TYR 28;HIS 106

1gu0GASN 16;ARG 23;TYR 28;HIS 106

1gu0HASN 16;ARG 23;TYR 28;HIS 106

1gu0IASN 16;ARG 23;TYR 28;HIS 106

1gu0JASN 16;ARG 23;TYR 28;HIS 106

1gu0KASN 16;ARG 23;TYR 28;HIS 106

1gu0LASN 16;ARG 23;TYR 28;HIS 106

1gu1AASN 16;ARG 23;TYR 28;HIS 106

1gu1BASN 16;ARG 23;TYR 28;HIS 106

1gu1CASN 16;ARG 23;TYR 28;HIS 106

1gu1DASN 16;ARG 23;TYR 28;HIS 106

1gu1EASN 16;ARG 23;TYR 28;HIS 106

1gu1FASN 16;ARG 23;TYR 28;HIS 106

1gu1GASN 16;ARG 23;TYR 28;HIS 106

1gu1HASN 16;ARG 23;TYR 28;HIS 106

1gu1IASN 16;ARG 23;TYR 28;HIS 106

1gu1JASN 16;ARG 23;TYR 28;HIS 106

1gu1KASN 16;ARG 23;TYR 28;HIS 106

1gu1LASN 16;ARG 23;TYR 28;HIS 106

1gtzAASN 16;      ;TYR 28;HIS 106
mutant R23A
1gtzBASN 16;      ;TYR 28;HIS 106
mutant R23A
1gtzCASN 16;      ;TYR 28;HIS 106
mutant R23A
1gtzDASN 16;      ;TYR 28;HIS 106
mutant R23A
1gtzEASN 16;      ;TYR 28;HIS 106
mutant R23A
1gtzFASN 16;      ;TYR 28;HIS 106
mutant R23A
1gtzGASN 16;      ;TYR 28;HIS 106
mutant R23A
1gtzHASN 16;      ;TYR 28;HIS 106
mutant R23A
1gtzIASN 16;      ;TYR 28;HIS 106
mutant R23A
1gtzJASN 16;      ;TYR 28;HIS 106
mutant R23A
1gtzKASN 16;      ;TYR 28;HIS 106
mutant R23A
1gtzLASN 16;      ;TYR 28;HIS 106
mutant R23A
1h05AASN 12;ARG 19;      ;HIS 101
invisible 24Y
1h0rAASN 12;      ;TYR 24;HIS 101
invisible 19R
1h0sAASN 12;ARG 19;      ;HIS 101
invisible 24Y
2dhqAASN 12;ARG 19;      ;HIS 101
invisible 24Y
1gqoAASN 10;ARG 17;      ;HIS  99

1gqoBASN 10;ARG 17;      ;HIS  99

1gqoCASN 10;ARG 17;      ;HIS  99

1gqoDASN 10;ARG 17;      ;HIS  99

1gqoEASN 10;ARG 17;      ;HIS  99

1gqoFASN 10;ARG 17;      ;HIS  99

1gqoGASN 10;ARG 17;      ;HIS  99

1gqoHASN 10;ARG 17;      ;HIS  99

1gqoIASN 10;ARG 17;      ;HIS  99

1gqoJASN 10;ARG 17;      ;HIS  99

1gqoKASN 10;ARG 17;      ;HIS  99

1gqoLASN 10;ARG 17;      ;HIS  99

1gqoMASN 10;ARG 17;      ;HIS  99

1gqoNASN 10;      ;      ;HIS  99
invisible 16-24
1gqoOASN 10;ARG 17;      ;HIS  99

1gqoPASN 10;ARG 17;      ;HIS  99

1gqoQASN 10;ARG 17;      ;HIS  99

1gqoRASN 10;ARG 17;      ;HIS  99

1gqoSASN 10;ARG 17;      ;HIS  99

1gqoTASN 10;ARG 17;      ;HIS  99

1gqoUASN 10;ARG 17;      ;HIS  99

1gqoVASN 10;ARG 17;      ;HIS  99
invisible 18-23
1gqoXASN 10;      ;      ;HIS  99
invisible 17-23
1gqoYASN 10;ARG 17;      ;HIS  99


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[8]Fig. 1, p.5223
[12]Fig.8, p.497-4982

references
[1]
PubMed ID1554351
JournalBiochem J
Year1992
Volume282
Pages687-95
AuthorsKleanthous C, Deka R, Davis K, Kelly SM, Cooper A, Harding SE, Price NC, Hawkins AR, Coggins JR
TitleA comparison of the enzymological and biophysical properties of two distinct classes of dehydroquinase enzymes.
[2]
PubMed ID8064862
JournalJ Mol Biol
Year1994
Volume241
Pages488-91
AuthorsGourley DG, Coggins JR, Isaacs NW, Moore JD, Charles IG, Hawkins AR
TitleCrystallization of a type II dehydroquinase from Mycobacterium tuberculosis.
[3]
PubMed ID8870678
JournalBiochem J
Year1996
Volume319
Pages269-78
AuthorsBottomley JR, Hawkins AR, Kleanthous C
TitleConformational changes and the role of metals in the mechanism of type II dehydroquinase from Aspergillus nidulans.
[4]
PubMed ID8798709
JournalJ Biol Chem
Year1996
Volume271
Pages24492-7
AuthorsKrell T, Horsburgh MJ, Cooper A, Kelly SM, Coggins JR
TitleLocalization of the active site of type II dehydroquinases. Identification of a common arginine-containing motif in the two classes of dehydroquinases.
[5]
PubMed ID9147947
JournalBiochem Soc Trans
Year1997
Volume25
Pages348; replaces 93S
AuthorsBoam DJ, Price NC, Kelly SM, Krell T, Coggins JR
TitleEvidence that the active site in type II dehydroquinase from Streptomyces coelicolor is near the single tryptophan.
[6]
PubMed ID9473305
JournalArch Biochem Biophys
Year1998
Volume350
Pages298-306
AuthorsFlorova G, Denoya CD, Morgenstern MR, Skinner DD, Reynolds KA
TitleCloning, expression, and characterization of a type II 3-dehydroquinate dehydratase gene from Streptomyces hygroscopicus.
[7]
PubMed ID9931316
JournalBiochem J
Year1999
Volume338
Pages195-202
AuthorsPrice NC, Boam DJ, Kelly SM, Duncan D, Krell T, Gourley DG, Coggins JR, Virden R, Hawkins AR
TitleThe folding and assembly of the dodecameric type II dehydroquinases.
[8]
PubMed ID10360352
JournalNat Struct Biol
Year1999
Volume6
Pages521-5
AuthorsGourley DG, Shrive AK, Polikarpov I, Krell T, Coggins JR, Hawkins AR, Isaacs NW, Sawyer L
TitleThe two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction.
Related PDB2dhq
[9]
PubMed ID10698442
JournalBioorg Med Chem Lett
Year2000
Volume10
Pages231-4
AuthorsParker EJ, Gonzalez Bello C, Coggins JR, Hawkins AR, Abell C
TitleMechanistic studies on type I and type II dehydroquinase with (6R)- and (6S)-6-fluoro-3-dehydroquinic acids.
[10]
PubMed ID11173479
JournalActa Crystallogr D Biol Crystallogr
Year2001
Volume57
Pages279-80
AuthorsKwak JE, Lee JY, Han BW, Moon J J, Sohn SH, Suh SW
TitleCrystallization and preliminary X-ray crystallographic analysis of type II dehydroquinase from Helicobacter pylori.
[11]
PubMed ID12387860
JournalFEBS Lett
Year2002
Volume530
Pages24-30
AuthorsEvans LD, Roszak AW, Noble LJ, Robinson DA, Chalk PA, Matthews JL, Coggins JR, Price NC, Lapthorn AJ
TitleSpecificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions.
Related PDB1h05
[12]
CommentsX-ray crystallography
PubMed ID11937054
JournalStructure (Camb)
Year2002
Volume10
Pages493-503
AuthorsRoszak AW, Robinson DA, Krell T, Hunter IS, Fredrickson M, Abell C, Coggins JR, Lapthorn AJ
TitleThe structure and mechanism of the type II dehydroquinase from Streptomyces coelicolor.
Related PDB1d0i,1gu0,1gu1,1gtz
[13]
PubMed ID12784220
JournalProteins
Year2003
Volume51
Pages616-7
AuthorsLee BI, Kwak JE, Suh SW
TitleCrystal structure of the type II 3-dehydroquinase from Helicobacter pylori.


createdupdated
2004-04-102009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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