ID   AROD_METST              Reviewed;         235 AA.
AC   Q2NGS8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=3-dehydroquinate dehydratase;
DE            Short=3-dehydroquinase;
DE            EC=4.2.1.10;
DE   AltName: Full=Type I DHQase;
GN   Name=aroD; OrderedLocusNames=Msp_0577;
OS   Methanosphaera stadtmanae (strain DSM 3091).
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16385054; DOI=10.1128/JB.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H.,
RA   Hedderich R., Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this
RT   human intestinal archaeon is restricted to methanol and H2 for methane
RT   formation and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
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   -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000102; ABC56975.1; -; Genomic_DNA.
DR   RefSeq; YP_447618.1; -.
DR   GeneID; 3854828; -.
DR   GenomeReviews; CP000102_GR; Msp_0577.
DR   KEGG; mst:Msp_0577; -.
DR   NMPDR; fig|339860.6.peg.557; -.
DR   HOGENOM; Q2NGS8; -.
DR   OMA; Q2NGS8; IAKLAVM.
DR   BioCyc; MSTA339860:MSP_0577-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_00214; -; 1.
DR   InterPro; IPR018508; 3-dehydroquinate_DH_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001381; DHquinase_I.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF01487; DHquinase_I; 1.
DR   ProDom; PD005337; DHquinase_I; 1.
DR   TIGRFAMs; TIGR01093; aroD; 1.
DR   PROSITE; PS01028; DEHYDROQUINASE_I; FALSE_NEG.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Schiff base.
FT   CHAIN         1    235       3-dehydroquinate dehydratase.
FT                                /FTId=PRO_0000325539.
FT   ACT_SITE    133    133       Proton acceptor (By similarity).
FT   ACT_SITE    159    159       Schiff-base intermediate with substrate
FT                                (By similarity).
SQ   SEQUENCE   235 AA;  26697 MW;  21701FC949F51023 CRC64;
     MIFFLLEGER EIITEICGSI IESNEKDIFK TLDKAVDLDV NYIELRLDVI ENITSKKATS
     IIEKIRNVTD IPIILTNRTK YEGGYFPSTE EDRIKILMDN ASLVEYTDIE LSTNENLRQE
     VIDNANRTII SYHNFEKTPS SEYLENVVNS ALNVGDIAKI AVKPLNIEDT YVLLRLLMEY
     DDLIGISMDK LGSYTRILGP ILGSPVTYTA ITDESAPGQF DVKTTRDILK KLKNY
//