ID   AROQ2_PSEPK             Reviewed;         149 AA.
AC   Q88K84;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   14-OCT-2008, entry version 36.
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; Synonyms=aroQ-2; OrderedLocusNames=PP_2407;
OS   Pseudomonas putida (strain KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22423060; PubMed=12534463;
RX   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.,
RA   Hance I., Chris Lee P., Holtzapple E.K., Scanlan D., Tran K.,
RA   Moazzez A., Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D.,
RA   Wedler H., Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S.,
RA   Kiewitz C., Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B.,
RA   Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the
RT   metabolically versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
CC   -!- FUNCTION: Catalyzes a trans-dehydration via an enolate
CC       intermediate (By similarity).
CC   -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and PEP:
CC       step 3/7.
CC   -!- SUBUNIT: Homododecamer (By similarity).
CC   -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
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DR   EMBL; AE015451; AAN68019.1; -; Genomic_DNA.
DR   RefSeq; NP_744555.1; -.
DR   HSSP; P15474; 1GU1.
DR   GeneID; 1045534; -.
DR   GenomeReviews; AE015451_GR; PP_2407.
DR   KEGG; ppu:PP_2407; -.
DR   NMPDR; fig|160488.1.peg.2385; -.
DR   TIGR; PP_2407; -.
DR   HOGENOM; Q88K84; -.
DR   BioCyc; PPUT160488:PP_2407-MON; -.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:HAMAP.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic pro...; IEA:HAMAP.
DR   HAMAP; MF_00169; -; 1.
DR   InterPro; IPR001874; DHquinase_II.
DR   Gene3D; G3DSA:3.40.50.9100; DHquinase_II; 1.
DR   PANTHER; PTHR21272; DHquinase_II; 1.
DR   Pfam; PF01220; DHquinase_II; 1.
DR   PIRSF; PIRSF001399; DHquinase_II; 1.
DR   ProDom; PD004527; DHquinase_II; 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;
KW   Complete proteome; Lyase.
FT   CHAIN         1    149       3-dehydroquinate dehydratase 2.
FT                                /FTId=PRO_0000159921.
FT   REGION      102    103       Substrate binding (By similarity).
FT   ACT_SITE     24     24       Proton acceptor (By similarity).
FT   ACT_SITE    101    101       Proton donor (By similarity).
FT   BINDING      75     75       Substrate (By similarity).
FT   BINDING      81     81       Substrate (By similarity).
FT   BINDING      88     88       Substrate (By similarity).
FT   BINDING     112    112       Substrate (By similarity).
FT   SITE         19     19       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   149 AA;  16211 MW;  D10A4D670DA9D124 CRC64;
     MKPLILVLNG PNLNMLGTRE PAQYGHETLA DLAQGCADTA HAHGLEIEFR QTNHEGELID
     WIHAARGRCA GIVINPGAWT HTSVAIRDAL VASELPVIEV HLSNVHKREP FRHLSFVSSI
     AVGVICGLGS HGYRMALSHF AELLQERAA
//