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AROQ_WOLSU
ID   AROQ_WOLSU              Reviewed;         166 AA.
AC   Q7M8I1;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=WS1645;
OS   Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS   11488 / FDC 602W) (Vibrio succinogenes).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Wolinella.
OX   NCBI_TaxID=273121;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC   11488 / FDC 602W;
RX   PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA   Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA   Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA   Meyer F., Lederer H., Schuster S.C.;
RT   "Complete genome sequence and analysis of Wolinella succinogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
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; BX571661; CAE10676.1; -; Genomic_DNA.
DR   RefSeq; WP_011139460.1; NC_005090.1.
DR   AlphaFoldDB; Q7M8I1; -.
DR   SMR; Q7M8I1; -.
DR   STRING; 273121.WS1645; -.
DR   EnsemblBacteria; CAE10676; CAE10676; WS1645.
DR   KEGG; wsu:WS1645; -.
DR   eggNOG; COG0757; Bacteria.
DR   HOGENOM; CLU_090968_1_0_7; -.
DR   OMA; AYTHYSY; -.
DR   OrthoDB; 1872106at2; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000000422; 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;
KW   Reference proteome.
FT   CHAIN           1..166
FT                   /note="3-dehydroquinate dehydratase"
FT                   /id="PRO_0000159941"
FT   ACT_SITE        22
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   ACT_SITE        99
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         100..101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   SITE            17
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
SQ   SEQUENCE   166 AA;  18169 MW;  2B367C28D8B2A8D6 CRC64;
     MKVVVIQGPN LNMLGIREQR LYGPMKLEQI HQNMKTFADQ NGMEVEFFQS NLEGEIVDKI
     QECLGDADGI IINPAAYSHT SIAIRDAISA VSLPTLEVHI TNIHAREEFR RHSLTAEVAA
     GVIAGFGPFG YHMAMIAMHQ ILSELGALKE AQAKAQAQAQ EGAKES
 
 
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