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3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10) (Type II DHQase)

 AROQ_STRCO              Reviewed;         157 AA.
P15474; O33608;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
10-OCT-2018, entry version 142.
RecName: Full=3-dehydroquinate dehydratase;
Short=3-dehydroquinase;
EC=4.2.1.10;
AltName: Full=Type II DHQase;
Name=aroQ; OrderedLocusNames=SCO1961; ORFNames=SCC54.21c;
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces; Streptomyces albidoflavus group.
NCBI_TaxID=100226;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=A3(2) / NRRL B-16638;
Hunter I.S.;
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-471 / A3(2) / M145;
PubMed=12000953; DOI=10.1038/417141a;
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
Hopwood D.A.;
"Complete genome sequence of the model actinomycete Streptomyces
coelicolor A3(2).";
Nature 417:141-147(2002).
[3]
PROTEIN SEQUENCE OF 2-35.
PubMed=2306211; DOI=10.1042/bj2650735;
White P.J., Young J., Hunter I.S., Nimmo J.G., Coggins J.R.;
"The purification and characterization of 3-dehydroquinase from
Streptomyces coelicolor.";
Biochem. J. 265:735-738(1990).
[4]
ENZYME KINETICS, AND MUTAGENESIS OF ARG-24.
PubMed=8798709; DOI=10.1074/jbc.271.40.24492;
Krell T., Horsburgh M.J., Cooper A., Kelly S.M., Coggins J.R.;
"Localization of the active site of type II dehydroquinases.
Identification of a common arginine-containing motif in the two
classes of dehydroquinases.";
J. Biol. Chem. 271:24492-24497(1996).
[5]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-24
IN COMPLEX WITH SUBSTRATE ANALOG, AND SUBUNIT.
PubMed=11937054; DOI=10.1016/S0969-2126(02)00747-5;
Roszak A.W., Robinson D.A., Krell T., Hunter I.S., Fredrickson M.,
Abell C., Coggins J.R., Lapthorn A.J.;
"The structure and mechanism of the type II dehydroquinase from
Streptomyces coelicolor.";
Structure 10:493-503(2002).
[6]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOG, AND SUBUNIT.
PubMed=15162210; DOI=10.1039/b404535a;
Frederickson M., Roszak A.W., Coggins J.R., Lapthorn A.J., 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. 2:1592-1596(2004).
[7]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOG, AND SUBUNIT.
PubMed=16106291; DOI=10.1039/b507156a;
Toscano M.D., Stewart K.A., Coggins J.R., Lapthorn A.J., Abell C.;
"Rational design of new bifunctional inhibitors of type II
dehydroquinase.";
Org. Biomol. Chem. 3:3102-3104(2005).
-!- FUNCTION: Catalyzes a trans-dehydration via an enolate
intermediate. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1100 uM for 3-dehydroquinate (at pH 8 and 25 degrees
Celsius);
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 3/7.
-!- SUBUNIT: Homododecamer. {ECO:0000269|PubMed:11937054,
ECO:0000269|PubMed:15162210, ECO:0000269|PubMed:16106291}.
-!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
{ECO:0000305}.
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EMBL; AJ001493; CAA04787.1; -; Genomic_DNA.
EMBL; AL939110; CAB38151.1; -; Genomic_DNA.
PIR; S08196; S08196.
PIR; T35990; T35990.
RefSeq; NP_626225.1; NC_003888.3.
RefSeq; WP_003976858.1; NC_003888.3.
PDB; 1D0I; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L=2-157.
PDB; 1GTZ; X-ray; 1.60 A; A/B/C/D/E/F/G/H/I/J/K/L=2-157.
PDB; 1GU0; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=2-157.
PDB; 1GU1; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L=2-157.
PDB; 1V1J; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=2-157.
PDB; 2BT4; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-157.
PDB; 2CJF; X-ray; 1.95 A; A/B/C/D/E/F/G/H/I/J/K/L=1-157.
PDBsum; 1D0I; -.
PDBsum; 1GTZ; -.
PDBsum; 1GU0; -.
PDBsum; 1GU1; -.
PDBsum; 1V1J; -.
PDBsum; 2BT4; -.
PDBsum; 2CJF; -.
ProteinModelPortal; P15474; -.
SMR; P15474; -.
STRING; 100226.SCO1961; -.
BindingDB; P15474; -.
ChEMBL; CHEMBL5276; -.
DrugBank; DB02786; 2-Anhydro-3-Fluoro-Quinic Acid.
DrugBank; DB04347; 3-Dehydroshikimate.
PRIDE; P15474; -.
EnsemblBacteria; CAB38151; CAB38151; CAB38151.
GeneID; 1097395; -.
KEGG; sco:SCO1961; -.
PATRIC; fig|100226.15.peg.1987; -.
eggNOG; ENOG4108Z38; Bacteria.
eggNOG; COG0757; LUCA.
HOGENOM; HOG000217278; -.
InParanoid; P15474; -.
KO; K03786; -.
OMA; CAGIVIN; -.
OrthoDB; POG091H03XJ; -.
PhylomeDB; P15474; -.
BRENDA; 4.2.1.10; 5998.
SABIO-RK; P15474; -.
UniPathway; UPA00053; UER00086.
EvolutionaryTrace; P15474; -.
PRO; PR:P15474; -.
Proteomes; UP000001973; Chromosome.
GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd00466; DHQase_II; 1.
Gene3D; 3.40.50.9100; -; 1.
HAMAP; MF_00169; AroQ; 1.
InterPro; IPR001874; DHquinase_II.
InterPro; IPR018509; DHquinase_II_CS.
InterPro; IPR036441; DHquinase_II_sf.
PANTHER; PTHR21272; PTHR21272; 1.
Pfam; PF01220; DHquinase_II; 1.
PIRSF; PIRSF001399; DHquinase_II; 1.
SUPFAM; SSF52304; SSF52304; 1.
TIGRFAMs; TIGR01088; aroQ; 1.
PROSITE; PS01029; DEHYDROQUINASE_II; 1.
1: Evidence at protein level;
3D-structure; Amino-acid biosynthesis;
Aromatic amino acid biosynthesis; Complete proteome;
Direct protein sequencing; Lyase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2306211}.
CHAIN 2 157 3-dehydroquinate dehydratase.
/FTId=PRO_0000159930.
REGION 108 109 Substrate binding.
ACT_SITE 29 29 Proton acceptor.
ACT_SITE 107 107 Proton donor.
BINDING 80 80 Substrate.
BINDING 86 86 Substrate.
BINDING 93 93 Substrate.
BINDING 118 118 Substrate.
SITE 24 24 Transition state stabilizer.
MUTAGEN 24 24 R->A: Reduces Kcat 30000-fold. Reduces KM
for 3-dehydroquinate 6-fold.
{ECO:0000269|PubMed:8798709}.
MUTAGEN 24 24 R->K: Reduces Kcat 2700-fold. Reduces KM
for 3-dehydroquinate 4-fold.
{ECO:0000269|PubMed:8798709}.
MUTAGEN 24 24 R->Q: Reduces Kcat 3100-fold. Reduces KM
for 3-dehydroquinate 8-fold.
{ECO:0000269|PubMed:8798709}.
TURN 5 7 {ECO:0000244|PDB:1GTZ}.
STRAND 10 14 {ECO:0000244|PDB:1GTZ}.
HELIX 18 20 {ECO:0000244|PDB:1GTZ}.
TURN 21 23 {ECO:0000244|PDB:1GTZ}.
HELIX 26 29 {ECO:0000244|PDB:1GTZ}.
HELIX 34 46 {ECO:0000244|PDB:1GTZ}.
TURN 47 49 {ECO:0000244|PDB:1GTZ}.
STRAND 52 56 {ECO:0000244|PDB:1GTZ}.
HELIX 60 73 {ECO:0000244|PDB:1GTZ}.
STRAND 75 80 {ECO:0000244|PDB:1GTZ}.
HELIX 84 87 {ECO:0000244|PDB:1GTZ}.
HELIX 89 96 {ECO:0000244|PDB:1GTZ}.
STRAND 103 109 {ECO:0000244|PDB:1GTZ}.
HELIX 111 113 {ECO:0000244|PDB:1GTZ}.
HELIX 116 118 {ECO:0000244|PDB:1GTZ}.
HELIX 123 125 {ECO:0000244|PDB:1GTZ}.
STRAND 128 134 {ECO:0000244|PDB:1GTZ}.
HELIX 137 150 {ECO:0000244|PDB:1GTZ}.
SEQUENCE 157 AA; 16682 MW; 61D9F95C7E2C67EB CRC64;
MPRSLANAPI MILNGPNLNL LGQRQPEIYG SDTLADVEAL CVKAAAAHGG TVDFRQSNHE
GELVDWIHEA RLNHCGIVIN PAAYSHTSVA ILDALNTCDG LPVVEVHISN IHQREPFRHH
SYVSQRADGV VAGCGVQGYV FGVERIAALA GAGSARA


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