EzCatDB: S00382
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DB codeS00382
CATH domainDomain 13.40.50.9100 : Rossmann foldCatalytic domain
E.C.4.2.1.10
MACiEM0055


Enzyme Name
UniProtKBKEGG

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
RefSeqNP_626225.1 (Protein)
NC_003888.3 (DNA/RNA sequence)
NP_217053.1 (Protein)
NC_000962.3 (DNA/RNA sequence)
NP_337108.1 (Protein)
NC_002755.2 (DNA/RNA sequence)
YP_006515978.1 (Protein)
NC_018143.1 (DNA/RNA sequence)
NP_390327.1 (Protein)
NC_000964.3 (DNA/RNA sequence)
PfamPF01220 (DHquinase_II)
[Graphical view]
PF01220 (DHquinase_II)
[Graphical view]
PF01220 (DHquinase_II)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00400Phenylalanine, tyrosine and tryptophan biosynthesis

UniProtKB: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



Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00944C02637C00001
Compound3-Dehydroquinate3-DehydroshikimateH2O
Typecarbohydrate,carboxyl groupcarbohydrate,carboxyl groupH2O
ChEBI17947
30918
15377
PubChem439351
439774
962
22247451
           
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
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