ID   AROQ1_BRADU             Reviewed;         155 AA.
AC   Q89MA1;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=3-dehydroquinate dehydratase 1;
DE            Short=3-dehydroquinase 1;
DE            EC=4.2.1.10;
DE   AltName: Full=Type II DHQase 1;
GN   Name=aroQ1; OrderedLocusNames=bll4292;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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:0000250}.
CC   -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000040; BAC49557.1; -; Genomic_DNA.
DR   RefSeq; NP_770932.1; NC_004463.1.
DR   RefSeq; WP_011087065.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89MA1; -.
DR   SMR; Q89MA1; -.
DR   STRING; 224911.27352554; -.
DR   EnsemblBacteria; BAC49557; BAC49557; BAC49557.
DR   GeneID; 64024023; -.
DR   KEGG; bja:bll4292; -.
DR   PATRIC; fig|224911.44.peg.4032; -.
DR   eggNOG; COG0757; Bacteria.
DR   HOGENOM; CLU_090968_2_0_5; -.
DR   InParanoid; Q89MA1; -.
DR   OMA; AYTHYSY; -.
DR   PhylomeDB; Q89MA1; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000002526; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Reference proteome.
FT   CHAIN           1..155
FT                   /note="3-dehydroquinate dehydratase 1"
FT                   /id="PRO_0000159877"
FT   ACT_SITE        28
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        106
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         107..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            23
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   155 AA;  16743 MW;  3FADB5C6B56A6D2D CRC64;
     MAEPATDTIL VLNGPNLNML GTREPEKYGH ATLADVEALC RETAASFGLK ADCRQSNREG
     ELIDFIHEAH ARKMKGIIIN AGGYSHTSIA LHDALLAVQI PTVEVHVTNI HARESFRHHS
     YTARAAFASL CGFGIEGYRL AIQGLAAKLG LKPKA