AROQ_STRCO
ID AROQ_STRCO Reviewed; 157 AA.
AC P15474; O33608;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=3-dehydroquinate dehydratase;
DE Short=3-dehydroquinase;
DE EC=4.2.1.10;
DE AltName: Full=Type II DHQase;
GN Name=aroQ; OrderedLocusNames=SCO1961; ORFNames=SCC54.21c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RA Hunter I.S.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [3]
RP PROTEIN SEQUENCE OF 2-35.
RX PubMed=2306211; DOI=10.1042/bj2650735;
RA White P.J., Young J., Hunter I.S., Nimmo J.G., Coggins J.R.;
RT "The purification and characterization of 3-dehydroquinase from
RT Streptomyces coelicolor.";
RL Biochem. J. 265:735-738(1990).
RN [4]
RP ENZYME KINETICS, AND MUTAGENESIS OF ARG-24.
RX PubMed=8798709; DOI=10.1074/jbc.271.40.24492;
RA Krell T., Horsburgh M.J., Cooper A., Kelly S.M., Coggins J.R.;
RT "Localization of the active site of type II dehydroquinases. Identification
RT of a common arginine-containing motif in the two classes of
RT dehydroquinases.";
RL J. Biol. Chem. 271:24492-24497(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-24 IN
RP COMPLEX WITH SUBSTRATE ANALOG, AND SUBUNIT.
RX PubMed=11937054; DOI=10.1016/s0969-2126(02)00747-5;
RA Roszak A.W., Robinson D.A., Krell T., Hunter I.S., Fredrickson M.,
RA Abell C., Coggins J.R., Lapthorn A.J.;
RT "The structure and mechanism of the type II dehydroquinase from
RT Streptomyces coelicolor.";
RL Structure 10:493-503(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, AND
RP SUBUNIT.
RX PubMed=15162210; DOI=10.1039/b404535a;
RA Frederickson M., Roszak A.W., Coggins J.R., Lapthorn A.J., Abell C.;
RT "(1R,4S,5R)-3-Fluoro-1,4,5-trihydroxy-2-cyclohexene-1-carboxylic acid: the
RT fluoro analogue of the enolate intermediate in the reaction catalyzed by
RT type II dehydroquinases.";
RL Org. Biomol. Chem. 2:1592-1596(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, AND
RP SUBUNIT.
RX PubMed=16106291; DOI=10.1039/b507156a;
RA Toscano M.D., Stewart K.A., Coggins J.R., Lapthorn A.J., Abell C.;
RT "Rational design of new bifunctional inhibitors of type II
RT dehydroquinase.";
RL Org. Biomol. Chem. 3:3102-3104(2005).
CC -!- FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:32364; EC=4.2.1.10;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1100 uM for 3-dehydroquinate (at pH 8 and 25 degrees Celsius);
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7.
CC -!- SUBUNIT: Homododecamer. {ECO:0000269|PubMed:11937054,
CC ECO:0000269|PubMed:15162210, ECO:0000269|PubMed:16106291}.
CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC {ECO:0000305}.
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DR EMBL; AJ001493; CAA04787.1; -; Genomic_DNA.
DR EMBL; AL939110; CAB38151.1; -; Genomic_DNA.
DR PIR; S08196; S08196.
DR PIR; T35990; T35990.
DR RefSeq; NP_626225.1; NC_003888.3.
DR RefSeq; WP_003976858.1; NZ_VNID01000001.1.
DR PDB; 1D0I; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L=2-157.
DR PDB; 1GTZ; X-ray; 1.60 A; A/B/C/D/E/F/G/H/I/J/K/L=2-157.
DR PDB; 1GU0; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=2-157.
DR PDB; 1GU1; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L=2-157.
DR PDB; 1V1J; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=2-157.
DR PDB; 2BT4; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-157.
DR PDB; 2CJF; X-ray; 1.95 A; A/B/C/D/E/F/G/H/I/J/K/L=1-157.
DR PDBsum; 1D0I; -.
DR PDBsum; 1GTZ; -.
DR PDBsum; 1GU0; -.
DR PDBsum; 1GU1; -.
DR PDBsum; 1V1J; -.
DR PDBsum; 2BT4; -.
DR PDBsum; 2CJF; -.
DR AlphaFoldDB; P15474; -.
DR SMR; P15474; -.
DR STRING; 100226.SCO1961; -.
DR BindingDB; P15474; -.
DR ChEMBL; CHEMBL5276; -.
DR DrugBank; DB08485; (1S,4S,5S)-1,4,5-TRIHYDROXY-3-[3-(PHENYLTHIO)PHENYL]CYCLOHEX-2-ENE-1-CARBOXYLIC ACID.
DR DrugBank; DB04656; 1,3,4-TRIHYDROXY-5-(3-PHENOXYPROPYL)-CYCLOHEXANE-1-CARBOXYLIC A CID.
DR DrugBank; DB02801; 2,3-Anhydro-quinic acid.
DR DrugBank; DB02786; 2-Anhydro-3-Fluoro-Quinic Acid.
DR DrugBank; DB04347; 3-Dehydroshikimate.
DR DrugCentral; P15474; -.
DR GeneID; 1097395; -.
DR KEGG; sco:SCO1961; -.
DR PATRIC; fig|100226.15.peg.1987; -.
DR eggNOG; COG0757; Bacteria.
DR HOGENOM; CLU_090968_2_0_11; -.
DR InParanoid; P15474; -.
DR OMA; CAGIVIN; -.
DR PhylomeDB; P15474; -.
DR BRENDA; 4.2.1.10; 5998.
DR SABIO-RK; P15474; -.
DR UniPathway; UPA00053; UER00086.
DR EvolutionaryTrace; P15474; -.
DR PRO; PR:P15474; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IBA:GO_Central.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019631; P:quinate catabolic process; IBA:GO_Central.
DR CDD; cd00466; DHQase_II; 1.
DR Gene3D; 3.40.50.9100; -; 1.
DR HAMAP; MF_00169; AroQ; 1.
DR InterPro; IPR001874; DHquinase_II.
DR InterPro; IPR018509; DHquinase_II_CS.
DR InterPro; IPR036441; DHquinase_II_sf.
DR PANTHER; PTHR21272; PTHR21272; 1.
DR Pfam; PF01220; DHquinase_II; 1.
DR PIRSF; PIRSF001399; DHquinase_II; 1.
DR SUPFAM; SSF52304; SSF52304; 1.
DR TIGRFAMs; TIGR01088; aroQ; 1.
DR PROSITE; PS01029; DEHYDROQUINASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Direct protein sequencing; Lyase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2306211"
FT CHAIN 2..157
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000159930"
FT ACT_SITE 29
FT /note="Proton acceptor"
FT ACT_SITE 107
FT /note="Proton donor"
FT BINDING 80
FT /ligand="substrate"
FT BINDING 86
FT /ligand="substrate"
FT BINDING 93
FT /ligand="substrate"
FT BINDING 108..109
FT /ligand="substrate"
FT BINDING 118
FT /ligand="substrate"
FT SITE 24
FT /note="Transition state stabilizer"
FT MUTAGEN 24
FT /note="R->A: Reduces kcat 30000-fold. Reduces KM for 3-
FT dehydroquinate 6-fold."
FT /evidence="ECO:0000269|PubMed:8798709"
FT MUTAGEN 24
FT /note="R->K: Reduces kcat 2700-fold. Reduces KM for 3-
FT dehydroquinate 4-fold."
FT /evidence="ECO:0000269|PubMed:8798709"
FT MUTAGEN 24
FT /note="R->Q: Reduces kcat 3100-fold. Reduces KM for 3-
FT dehydroquinate 8-fold."
FT /evidence="ECO:0000269|PubMed:8798709"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:1GTZ"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:1GTZ"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:1GTZ"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:1GTZ"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:1GTZ"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:1GTZ"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1GTZ"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:1GTZ"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:1GTZ"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:1GTZ"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:1GTZ"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:1GTZ"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:1GTZ"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1GTZ"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1GTZ"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1GTZ"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:1GTZ"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:1GTZ"
SQ SEQUENCE 157 AA; 16682 MW; 61D9F95C7E2C67EB CRC64;
MPRSLANAPI MILNGPNLNL LGQRQPEIYG SDTLADVEAL CVKAAAAHGG TVDFRQSNHE
GELVDWIHEA RLNHCGIVIN PAAYSHTSVA ILDALNTCDG LPVVEVHISN IHQREPFRHH
SYVSQRADGV VAGCGVQGYV FGVERIAALA GAGSARA
