ID   AROQ1_PSEPK             Reviewed;         151 AA.
AC   Q88QD4;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
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; Synonyms=aroQ-1; OrderedLocusNames=PP_0560;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(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; AE015451; AAN66187.1; -; Genomic_DNA.
DR   RefSeq; NP_742723.1; NC_002947.4.
DR   RefSeq; WP_010951834.1; NC_002947.4.
DR   AlphaFoldDB; Q88QD4; -.
DR   SMR; Q88QD4; -.
DR   STRING; 160488.PP_0560; -.
DR   EnsemblBacteria; AAN66187; AAN66187; PP_0560.
DR   KEGG; ppu:PP_0560; -.
DR   PATRIC; fig|160488.4.peg.598; -.
DR   eggNOG; COG0757; Bacteria.
DR   HOGENOM; CLU_090968_1_0_6; -.
DR   OMA; AYTHYSY; -.
DR   PhylomeDB; Q88QD4; -.
DR   BioCyc; PPUT160488:G1G01-610-MON; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000000556; 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..151
FT                   /note="3-dehydroquinate dehydratase 1"
FT                   /id="PRO_0000159920"
FT   ACT_SITE        23
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            18
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   151 AA;  16491 MW;  E37D55FE09F680E0 CRC64;
     MATLLVLHGP NLNLLGTREP GHYGAVTLAQ INQDLEQRAR AAGHHLLYLQ SNAEYELIDR
     IHAARNEGVD FILINPAAFT HTSVALRDAL LAVSIPFIEV HLSNVHKREP FRHHSYFSDV
     AVGVICGLGA SGYRLALESA LEQLAANAQP K