ID   AROQ_LEGPA              Reviewed;         145 AA.
AC   Q5X7S5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00169};
DE            Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00169};
DE            EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00169};
DE   AltName: Full=Type II DHQase {ECO:0000255|HAMAP-Rule:MF_00169};
GN   Name=aroQ {ECO:0000255|HAMAP-Rule:MF_00169}; OrderedLocusNames=lpp0530;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
CC   -!- FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate.
CC       {ECO:0000255|HAMAP-Rule:MF_00169}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00169};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       3/7. {ECO:0000255|HAMAP-Rule:MF_00169}.
CC   -!- SUBUNIT: Homododecamer. {ECO:0000255|HAMAP-Rule:MF_00169}.
CC   -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00169}.
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DR   EMBL; CR628336; CAH11678.1; -; Genomic_DNA.
DR   RefSeq; WP_011213103.1; NC_006368.1.
DR   AlphaFoldDB; Q5X7S5; -.
DR   SMR; Q5X7S5; -.
DR   KEGG; lpp:lpp0530; -.
DR   LegioList; lpp0530; -.
DR   HOGENOM; CLU_090968_1_0_6; -.
DR   OMA; AYTHYSY; -.
DR   UniPathway; UPA00053; UER00086.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
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   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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase.
FT   CHAIN           1..145
FT                   /note="3-dehydroquinate dehydratase"
FT                   /id="PRO_1000077045"
FT   ACT_SITE        23
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   ACT_SITE        101
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         102..103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   SITE            18
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
SQ   SEQUENCE   145 AA;  15775 MW;  887883265458F9FD CRC64;
     MKKILVLHGP NLNLLGSREP SIYGHASLTE INGDLIQEAD NAGIRLSCFQ SNAEAELIQA
     VHQAGIDKIN YIIINPAAFT HTSIALRDAL SAVAIPFIEV HLSNIFSRET FRHHSYFSDI
     AVGVISGLGT KGYLLALQAI IKELK