ID AROD_ECO55 Reviewed; 252 AA.
AC B7L5P5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 32.
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=EC55989_1860;
OS Escherichia coli (strain 55989 / EAEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55989 / EAEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A.,
RA Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928145; CAU97718.1; -; Genomic_DNA.
DR RefSeq; YP_002402921.1; NC_011748.1.
DR ProteinModelPortal; B7L5P5; -.
DR SMR; B7L5P5; 1-252.
DR STRING; 585055.EC55989_1860; -.
DR EnsemblBacteria; CAU97718; CAU97718; EC55989_1860.
DR GeneID; 7148479; -.
DR KEGG; eck:EC55989_1860; -.
DR PATRIC; 38477178; VBIEscCol113220_1892.
DR eggNOG; COG0710; -.
DR HOGENOM; HOG000105514; -.
DR KO; K03785; -.
DR OMA; IIEWRVD; -.
DR ProtClustDB; PRK02412; -.
DR BioCyc; ECOL585055:GJOM-1896-MONOMER; -.
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_1000124782.
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; 27547 MW; 01B275E01E8A294B CRC64;
MKTVTVKDLV IGTGAPKIIV SLMAKDIARV KSEALAYREA DFDILEWRVD HFADLSNVES
VMAAAKILRE TMPEKPLLFT FRSAKEGGEQ AISTEAYIAL NRAAIDSGLV DMIDLELFTG
DDQVKETVAY AHAHDVKVVM SNHDFHKTPE AEEIIARLRK MQSFDADIPK IALMPQSTND
VLTLLAATLE MQEQYADRPI ITMSMAKTGV ISRLAGEVFG SAATFGAVKK ASAPGQISVN
DLRTVLTILH QA
//
