ID   AROQ_CORP2              Reviewed;         146 AA.
AC   P96750; D9QAN7;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=3-dehydroquinate dehydratase;
DE            Short=3-dehydroquinase;
DE            EC=4.2.1.10;
DE   AltName: Full=Type II DHQase;
GN   Name=aroQ; OrderedLocusNames=CpC231_1137;
OS   Corynebacterium pseudotuberculosis (strain C231).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=681645;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C231;
RX   PubMed=9234753; DOI=10.1128/iai.65.8.3048-3056.1997;
RA   Simmons C.P., Hodgson A.L.M., Strugnell R.A.;
RT   "Attenuation and vaccine potential of aroQ mutants of Corynebacterium
RT   pseudotuberculosis.";
RL   Infect. Immun. 65:3048-3056(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C231;
RX   PubMed=21533164; DOI=10.1371/journal.pone.0018551;
RA   Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R.,
RA   Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P., Turk M.Z.,
RA   Seyffert N., Moraes P.M., Soares S.C., Almeida S.S., Castro T.L.,
RA   Abreu V.A., Trost E., Baumbach J., Tauch A., Schneider M.P., McCulloch J.,
RA   Cerdeira L.T., Ramos R.T., Zerlotini A., Dominitini A., Resende D.M.,
RA   Coser E.M., Oliveira L.M., Pedrosa A.L., Vieira C.U., Guimaraes C.T.,
RA   Bartholomeu D.C., Oliveira D.M., Santos F.R., Rabelo E.M., Lobo F.P.,
RA   Franco G.R., Costa A.F., Castro I.M., Dias S.R., Ferro J.A., Ortega J.M.,
RA   Paiva L.V., Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P.,
RA   Falcao P.R., Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C.,
RA   Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.;
RT   "Evidence for reductive genome evolution and lateral acquisition of
RT   virulence functions in two Corynebacterium pseudotuberculosis strains.";
RL   PLoS ONE 6:E18551-E18551(2011).
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; U88628; AAB71615.1; -; Genomic_DNA.
DR   EMBL; CP001829; ADL10613.1; -; Genomic_DNA.
DR   RefSeq; WP_013241997.1; NC_017301.2.
DR   AlphaFoldDB; P96750; -.
DR   SMR; P96750; -.
DR   STRING; 1719.CPTC_01704; -.
DR   EnsemblBacteria; ADL10613; ADL10613; CpC231_1137.
DR   GeneID; 12299568; -.
DR   KEGG; cpq:CPC231_05755; -.
DR   PATRIC; fig|681645.3.peg.1190; -.
DR   eggNOG; COG0757; Bacteria.
DR   HOGENOM; CLU_090968_2_0_11; -.
DR   OMA; CAGIVIN; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000000276; 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..146
FT                   /note="3-dehydroquinate dehydratase"
FT                   /id="PRO_0000159897"
FT   ACT_SITE        22
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        101
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
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            17
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        96
FT                   /note="G -> A (in Ref. 1; AAB71615)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   146 AA;  15967 MW;  E6A005177016548D CRC64;
     MNILVLNGPN LDRLGKRQPE IYGRTTLADV EKLLVKRADA LGVTVIVKQS NYEGELIDWV
     HEAADAGWPV IINPGGLTHT SVSLRDALAE IHDGAGFVEV HISNIHAREE FRHHSFLSPI
     ARGVIAGLGV MGYELALEYL VLNSHS