ID   AROQ_BLOPB              Reviewed;         152 AA.
AC   Q493B0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=BPEN_301;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPEN;
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ40932.1; -; Genomic_DNA.
DR   RefSeq; WP_011282839.1; NC_007292.1.
DR   AlphaFoldDB; Q493B0; -.
DR   SMR; Q493B0; -.
DR   STRING; 291272.BPEN_301; -.
DR   EnsemblBacteria; AAZ40932; AAZ40932; BPEN_301.
DR   KEGG; bpn:BPEN_301; -.
DR   eggNOG; COG0757; Bacteria.
DR   HOGENOM; CLU_090968_1_0_6; -.
DR   OMA; AYTHYSY; -.
DR   BioCyc; CBLO291272:BPEN_RS01480-MON; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000007794; Chromosome.
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..152
FT                   /note="3-dehydroquinate dehydratase"
FT                   /id="PRO_1000077028"
FT   ACT_SITE        26
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   ACT_SITE        103
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         104..105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   SITE            21
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
SQ   SEQUENCE   152 AA;  17331 MW;  23818774348A75C6 CRC64;
     MVNTFRILLI NGPNLNLLGI REPHIYGYEA LSDVVANLYK TSESLGIHMD HFQSNAEHEL
     IECIHKSYKN SDFIIINPAA FTHTSIALRD AFLSVNIAFI EVHLSNIHIR EKFRYHSYLS
     DIALGVICGF GVYGYHCALH MAHKYLSKKI NK