ID   AROQ2_BRADU             Reviewed;         149 AA.
AC   Q89GF9;
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 2;
DE            Short=3-dehydroquinase 2;
DE            EC=4.2.1.10;
DE   AltName: Full=Type II DHQase 2;
GN   Name=aroQ2; OrderedLocusNames=bll6386;
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; BAC51651.1; -; Genomic_DNA.
DR   RefSeq; NP_773026.1; NC_004463.1.
DR   RefSeq; WP_011089126.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89GF9; -.
DR   SMR; Q89GF9; -.
DR   STRING; 224911.27354665; -.
DR   EnsemblBacteria; BAC51651; BAC51651; BAC51651.
DR   GeneID; 64026144; -.
DR   KEGG; bja:bll6386; -.
DR   PATRIC; fig|224911.44.peg.6369; -.
DR   eggNOG; COG0757; Bacteria.
DR   HOGENOM; CLU_090968_2_0_5; -.
DR   InParanoid; Q89GF9; -.
DR   OMA; VIECHIS; -.
DR   PhylomeDB; Q89GF9; -.
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..149
FT                   /note="3-dehydroquinate dehydratase 2"
FT                   /id="PRO_0000159878"
FT   ACT_SITE        24
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        101
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         102..103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            19
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   149 AA;  16656 MW;  AA560E13EB409F74 CRC64;
     MSGLVYVLNG PNLNLLGKRQ PHIYGHETLA DVERDCRALG KELGLEIRFH QSNREYELID
     WIHEARETAA GIVMNPAAFT HTSVAILDAL NTFEGTVIEV HISNVHKREE FRHHSFVSKR
     ADGVIAGFGT QGYLLGLRRV AKLLDEAKG