ID   AROQ_ENDTX              Reviewed;         143 AA.
AC   B1GZJ3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=TGRD_192;
OS   Endomicrobium trichonymphae.
OC   Bacteria; Elusimicrobia; Endomicrobia; Endomicrobiales; Endomicrobiaceae;
OC   Endomicrobium.
OX   NCBI_TaxID=1408204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18391199; DOI=10.1073/pnas.0801389105;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Complete genome of the uncultured termite group 1 bacteria in a single
RT   host protist cell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(2008).
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; AP009510; BAG13675.1; -; Genomic_DNA.
DR   RefSeq; WP_015423203.1; NC_020419.1.
DR   RefSeq; YP_001956136.1; NC_020419.1.
DR   AlphaFoldDB; B1GZJ3; -.
DR   SMR; B1GZJ3; -.
DR   STRING; 471821.TGRD_192; -.
DR   EnsemblBacteria; BAG13675; BAG13675; TGRD_192.
DR   KEGG; rsd:TGRD_192; -.
DR   PATRIC; fig|471821.5.peg.292; -.
DR   HOGENOM; CLU_090968_2_0_0; -.
DR   OMA; AYTHYSY; -.
DR   OrthoDB; 1872106at2; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000001691; 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..143
FT                   /note="3-dehydroquinate dehydratase"
FT                   /id="PRO_1000097631"
FT   ACT_SITE        23
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   ACT_SITE        100
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         101..102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         111
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   143 AA;  15779 MW;  B63B16F467424FF3 CRC64;
     MKKILVLNGP NINMLGIREP AVYGNITLAE IEKSLSSLAK ELKVEVEFFQ SNHEGKIVDK
     IQDSINKIFG IIINPAALTH TSITIRDALS SISVPTIEVH ISNIYAREEF RHKSYIAAEA
     IGQIAGLGID GYLFALRKMV SLM