AROQ_HELPY
ID AROQ_HELPY Reviewed; 167 AA.
AC Q48255;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 140.
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=HP_1038;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487;
RX PubMed=8912695; DOI=10.1042/bj3190559;
RA Bottomley J.R., Clayton C.L., Chalk P.A., Kleanthous C.;
RT "Cloning, sequencing, expression, purification and preliminary
RT characterization of a type II dehydroquinase from Helicobacter pylori.";
RL Biochem. J. 319:559-565(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 10-167 IN COMPLEX WITH SUBSTRATE,
RP AND SUBUNIT.
RX PubMed=12784220; DOI=10.1002/prot.10415;
RA Lee B.I., Kwak J.E., Suh S.W.;
RT "Crystal structure of the type II 3-dehydroquinase from Helicobacter
RT pylori.";
RL Proteins 51:616-617(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS,
RP AND SUBUNIT.
RX PubMed=16480265; DOI=10.1021/jm0505361;
RA Robinson D.A., Stewart K.A., Price N.C., Chalk P.A., Coggins J.R.,
RA Lapthorn A.J.;
RT "Crystal structures of Helicobacter pylori type II dehydroquinase inhibitor
RT complexes: new directions for inhibitor design.";
RL J. Med. Chem. 49:1282-1290(2006).
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 -!- 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:12784220,
CC ECO:0000269|PubMed:16480265}.
CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC {ECO:0000305}.
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DR EMBL; AE000511; AAD08081.1; -; Genomic_DNA.
DR EMBL; X98878; CAA67380.1; -; Genomic_DNA.
DR PIR; S72447; S72447.
DR RefSeq; NP_207828.1; NC_000915.1.
DR RefSeq; WP_000699284.1; NC_018939.1.
DR PDB; 1J2Y; X-ray; 2.60 A; A=1-167.
DR PDB; 2C4V; X-ray; 2.50 A; A=1-167.
DR PDB; 2C4W; X-ray; 1.55 A; A=1-167.
DR PDB; 2C57; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-167.
DR PDB; 2WKS; X-ray; 2.95 A; A/B/C/D/E/F=1-167.
DR PDB; 2XB9; X-ray; 2.75 A; A/B/C=1-167.
DR PDB; 2XD9; X-ray; 1.95 A; A/B/C=1-167.
DR PDB; 2XDA; X-ray; 1.85 A; A=1-167.
DR PDB; 4B6R; X-ray; 2.00 A; A/B/C=1-167.
DR PDB; 4B6S; X-ray; 1.90 A; A/B/C=1-167.
DR PDBsum; 1J2Y; -.
DR PDBsum; 2C4V; -.
DR PDBsum; 2C4W; -.
DR PDBsum; 2C57; -.
DR PDBsum; 2WKS; -.
DR PDBsum; 2XB9; -.
DR PDBsum; 2XD9; -.
DR PDBsum; 2XDA; -.
DR PDBsum; 4B6R; -.
DR PDBsum; 4B6S; -.
DR AlphaFoldDB; Q48255; -.
DR SMR; Q48255; -.
DR DIP; DIP-3328N; -.
DR IntAct; Q48255; 2.
DR MINT; Q48255; -.
DR STRING; 85962.C694_05370; -.
DR BindingDB; Q48255; -.
DR ChEMBL; CHEMBL4680; -.
DR DrugBank; DB03868; 3-Dehydroquinic Acid.
DR DrugBank; DB04698; N-(1,4-dihydro-5H-tetrazol-5-ylidene)-9-oxo-9H-xanthene-2-sulfonamide.
DR DrugCentral; Q48255; -.
DR PaxDb; Q48255; -.
DR EnsemblBacteria; AAD08081; AAD08081; HP_1038.
DR KEGG; hpy:HP_1038; -.
DR PATRIC; fig|85962.47.peg.1117; -.
DR eggNOG; COG0757; Bacteria.
DR OMA; AYTHYSY; -.
DR PhylomeDB; Q48255; -.
DR BRENDA; 4.2.1.10; 2604.
DR UniPathway; UPA00053; UER00086.
DR EvolutionaryTrace; Q48255; -.
DR PRO; PR:Q48255; -.
DR Proteomes; UP000000429; 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 CHAIN 1..167
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000159905"
FT ACT_SITE 22
FT /note="Proton acceptor"
FT ACT_SITE 102
FT /note="Proton donor"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12784220"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12784220"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12784220"
FT BINDING 103..104
FT /ligand="substrate"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12784220"
FT SITE 17
FT /note="Transition state stabilizer"
FT CONFLICT 156
FT /note="K -> Q (in Ref. 1; CAA67380)"
FT /evidence="ECO:0000305"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:2C4W"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:2C4W"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:2C4W"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2C4W"
FT HELIX 27..40
FT /evidence="ECO:0007829|PDB:2C4W"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:2C4W"
FT HELIX 55..66
FT /evidence="ECO:0007829|PDB:2C4W"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2C4W"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:2C4W"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:2C4W"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:2C4W"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2C4W"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:2C4W"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:2C4W"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2C4W"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:2C4W"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:2C4W"
FT HELIX 132..151
FT /evidence="ECO:0007829|PDB:2C4W"
FT TURN 152..156
FT /evidence="ECO:0007829|PDB:2C4W"
SQ SEQUENCE 167 AA; 18483 MW; 1AEC60B924987F07 CRC64;
MKILVIQGPN LNMLGHRDPR LYGMVTLDQI HEIMQTFVKQ GNLDVELEFF QTNFEGEIID
KIQESVGSDY EGIIINPGAF SHTSIAIADA IMLAGKPVIE VHLTNIQARE EFRKNSYTGA
ACGGVIMGFG PLGYNMALMA MVNILAEMKA FQEAQKNNPN NPINNQK
