ID AROD_ECOL6 Reviewed; 252 AA.
AC Q8FH42;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 01-MAY-2013, entry version 66.
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=c2088;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence
RT of uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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
CC phosphoenolpyruvate: step 3/7.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
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DR EMBL; AE014075; AAN80548.1; -; Genomic_DNA.
DR RefSeq; NP_753983.1; NC_004431.1.
DR ProteinModelPortal; Q8FH42; -.
DR SMR; Q8FH42; 1-252.
DR STRING; 199310.c2088; -.
DR EnsemblBacteria; AAN80548; AAN80548; c2088.
DR GeneID; 1036367; -.
DR KEGG; ecc:c2088; -.
DR PATRIC; 18282075; VBIEscCol75197_1954.
DR HOGENOM; HOG000105514; -.
DR KO; K03785; -.
DR OMA; IIEWRVD; -.
DR ProtClustDB; PRK02412; -.
DR UniPathway; UPA00053; UER00086.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:HAMAP.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:HAMAP.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00214; AroD; 1; -.
DR InterPro; IPR018508; 3-dehydroquinate_DH_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001381; DHquinase_I.
DR Pfam; PF01487; DHquinase_I; 1.
DR TIGRFAMs; TIGR01093; aroD; 1.
DR PROSITE; PS01028; DEHYDROQUINASE_I; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Complete proteome; Lyase; Schiff base.
FT CHAIN 1 252 3-dehydroquinate dehydratase.
FT /FTId=PRO_0000138795.
FT REGION 46 48 Substrate binding (By similarity).
FT ACT_SITE 143 143 Proton donor/acceptor (By similarity).
FT ACT_SITE 170 170 Schiff-base intermediate with substrate
FT (By similarity).
FT BINDING 82 82 Substrate (By similarity).
FT BINDING 213 213 Substrate (By similarity).
FT BINDING 232 232 Substrate (By similarity).
FT BINDING 236 236 Substrate (By similarity).
SQ SEQUENCE 252 AA; 27449 MW; 0E9F687C6D590F8C CRC64;
MKTVTVKDLV IGTGAPKIIV SLMAKDIASV KSEALAYREA DFDILEWRVD HYADLSNVES
VIAAAKILRE TMPEKPLLFT FRSAKEGGEQ AISTEAYIAL NRAAIDSGLV DMIDLELFTG
DDQVKETVAY AHAHDVKVVM SNHDFHKTPE AEEIIARLRK MQSFDADIPK IALMPQSTSD
VLTLLAATLE MQEQYADRPI ITMSMAKTGV ISRLAGEVFG SAATFGAVKK ASAPGQISVN
DLRTVLTILH QA
//
