ID   AROD_ECOLI     STANDARD;      PRT;   252 AA.
AC   P05194;
DT   13-AUG-1987 (Rel. 05, Created)
DT   01-OCT-1994 (Rel. 30, Last sequence update)
DT   15-JUN-2002 (Rel. 41, Last annotation update)
DE   3-dehydroquinate dehydratase (EC 4.2.1.10) (3-dehydroquinase) (Type I
DE   DHQase).
GN   AROD OR B1693.
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=87099996; PubMed=3541912;
RA   Duncan K., Chaudhuri S., Campbell M.S., Coggins J.R.;
RT   "The overexpression and complete amino acid sequence of Escherichia
RT   coli 3-dehydroquinase.";
RL   Biochem. J. 238:475-483(1986).
RN   [2]
RP   REVISIONS, SEQUENCE OF 162-172, AND ACTIVE SITE LYS-170.
RX   MEDLINE=91207275; PubMed=1826831;
RA   Chaudhuri S., Duncan K., Graham L.D., Coggins J.R.;
RT   "Identification of the active-site lysine residues of two
RT   biosynthetic 3-dehydroquinases.";
RL   Biochem. J. 275:1-6(1991).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE=97426617; PubMed=9278503;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12;
RX   MEDLINE=97251357; PubMed=9097039;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
RA   Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
RA   Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
RA   Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
RA   Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [5]
RP   ACTIVE SITE HIS-143, AND SEQUENCE OF 141-158.
RX   MEDLINE=93054505; PubMed=1429576;
RA   Deka R.K., Kleanthous C., Coggins J.R.;
RT   "Identification of the essential histidine residue at the active site
RT   of Escherichia coli dehydroquinase.";
RL   J. Biol. Chem. 267:22237-22242(1992).
CC   -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
CC   -!- PATHWAY: Aromatic amino acids biosynthesis; shikimate pathway;
CC       third step.
CC   -!- SUBUNIT: HOMODIMER.
CC   -!- SIMILARITY: BELONGS TO THE TYPE-I 3-DEHYDROQUINASE FAMILY.
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DR   EMBL; X59503; CAA42091.1; -.
DR   EMBL; X04306; CAA27849.1; ALT_SEQ.
DR   EMBL; AE000264; AAC74763.1; -.
DR   EMBL; D90811; BAA15448.1; -.
DR   PIR; A24508; DWECDQ.
DR   PIR; S14750; S14750.
DR   SWISS-2DPAGE; P05194; COLI.
DR   EcoGene; EG10076; aroD.
DR   InterPro; IPR001381; DHquinase_I.
DR   Pfam; PF01487; DHquinase_I; 1.
DR   TIGRFAMs; TIGR01093; aroD; 1.
DR   PROSITE; PS01028; DEHYDROQUINASE_I; 1.
KW   Aromatic amino acid biosynthesis; Lyase; Complete proteome.
FT   ACT_SITE    143    143
FT   ACT_SITE    170    170       FORMS A SCHIFF-BASE INTERMEDIATE.
SQ   SEQUENCE   252 AA;  27466 MW;  0D4E7FAEAD5FCD48 CRC64;
     MKTVTVKDLV IGTGAPKIIV SLMAKDIASV KSEALAYREA DFDILEWRVD HYADLSNVES
     VMAAAKILRE TMPEKPLLFT FRSAKEGGEQ AISTEAYIAL NRAAIDSGLV DMIDLELFTG
     DDQVKETVAY AHAHDVKVVM SNHDFHKTPE AEEIIARLRK MQSFDADIPK IALMPQSTSD
     VLTLLAATLE MQEQYADRPI ITMSMAKTGV ISRLAGEVFG SAATFGAVKK ASAPGQISVN
     DLRTVLTILH QA
//