AROD_ECOLI
ID AROD_ECOLI Reviewed; 252 AA.
AC P05194;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000303|PubMed:13198937};
DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000303|PubMed:3541912};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:2950851, ECO:0000269|PubMed:7592767};
DE AltName: Full=Type I DHQase {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000303|PubMed:13198937};
DE AltName: Full=Type I dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000303|PubMed:13198937};
DE Short=DHQ1 {ECO:0000255|HAMAP-Rule:MF_00214};
GN Name=aroD {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000303|PubMed:3541912};
GN OrderedLocusNames=b1693, JW1683;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, AND FUNCTION.
RX PubMed=3541912; DOI=10.1042/bj2380475;
RA Duncan K., Chaudhuri S., Campbell M.S., Coggins J.R.;
RT "The overexpression and complete amino acid sequence of Escherichia coli 3-
RT dehydroquinase.";
RL Biochem. J. 238:475-483(1986).
RN [2]
RP PROTEIN SEQUENCE OF 162-172, SEQUENCE REVISION, ACTIVE SITE LYS-170, AND
RP REACTION MECHANISM.
RX PubMed=1826831; DOI=10.1042/bj2750001;
RA Chaudhuri S., Duncan K., Graham L.D., Coggins J.R.;
RT "Identification of the active-site lysine residues of two biosynthetic 3-
RT dehydroquinases.";
RL Biochem. J. 275:1-6(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
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., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION.
RX PubMed=13198937; DOI=10.1016/0006-3002(54)90093-1;
RA Mitsuhashi S., Davis B.D.;
RT "Aromatic biosynthesis. XII. Conversion of 5-dehydroquinic acid to 5-
RT dehydroshikimic acid dy 5-dehydroquinase.";
RL Biochim. Biophys. Acta 15:54-61(1954).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=2950851; DOI=10.1042/bj2390699;
RA Chaudhuri S., Lambert J.M., McColl L.A., Coggins J.R.;
RT "Purification and characterization of 3-dehydroquinase from Escherichia
RT coli.";
RL Biochem. J. 239:699-704(1986).
RN [8]
RP ACTIVE SITE HIS-143, AND PROTEIN SEQUENCE OF 141-158.
RX PubMed=1429576; DOI=10.1016/s0021-9258(18)41660-2;
RA Deka R.K., Kleanthous C., Coggins J.R.;
RT "Identification of the essential histidine residue at the active site of
RT Escherichia coli dehydroquinase.";
RL J. Biol. Chem. 267:22237-22242(1992).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP HIS-143; HIS-146; LYS-170 AND MET-205, MASS SPECTROMETRY, AND REACTION
RP MECHANISM.
RX PubMed=7592767; DOI=10.1074/jbc.270.43.25827;
RA Leech A.P., James R., Coggins J.R., Kleanthous C.;
RT "Mutagenesis of active site residues in type I dehydroquinase from
RT Escherichia coli. Stalled catalysis in a histidine to alanine mutant.";
RL J. Biol. Chem. 270:25827-25836(1995).
CC -!- FUNCTION: Involved in the third step of the chorismate pathway, which
CC leads to the biosynthesis of aromatic amino acids (AroAA). Catalyzes
CC the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first
CC double bond of the aromatic ring to yield 3-dehydroshikimate. The
CC reaction involves the formation of an imine intermediate between the
CC keto group of 3-dehydroquinate and the epsilon-amino group of a Lys-170
CC at the active site. {ECO:0000255|HAMAP-Rule:MF_00214,
CC ECO:0000269|PubMed:13198937, ECO:0000269|PubMed:2950851,
CC ECO:0000269|PubMed:3541912, ECO:0000269|PubMed:7592767}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00214, ECO:0000269|PubMed:2950851,
CC ECO:0000269|PubMed:7592767};
CC -!- ACTIVITY REGULATION: Inhibited by sodium borohydride.
CC {ECO:0000269|PubMed:2950851}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for 3-dehydroquinate (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:7592767};
CC KM=18 uM for 3-dehydroquinate (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:2950851};
CC Note=kcat is 142 sec(-1) for dehydratase activity with 3-
CC dehydroquinate (at pH 7 and 25 degrees Celsius).
CC {ECO:0000269|PubMed:7592767};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7. {ECO:0000255|HAMAP-Rule:MF_00214}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00214,
CC ECO:0000269|PubMed:2950851}.
CC -!- MASS SPECTROMETRY: Mass=27467; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7592767};
CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00214}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X59503; CAA42091.1; -; Genomic_DNA.
DR EMBL; X04306; CAA27849.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U00096; AAC74763.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15448.1; -; Genomic_DNA.
DR PIR; S14750; DWECDQ.
DR RefSeq; NP_416208.1; NC_000913.3.
DR RefSeq; WP_000860201.1; NZ_LN832404.1.
DR AlphaFoldDB; P05194; -.
DR SMR; P05194; -.
DR IntAct; P05194; 6.
DR STRING; 511145.b1693; -.
DR BindingDB; P05194; -.
DR ChEMBL; CHEMBL4709; -.
DR SWISS-2DPAGE; P05194; -.
DR jPOST; P05194; -.
DR PaxDb; P05194; -.
DR PRIDE; P05194; -.
DR EnsemblBacteria; AAC74763; AAC74763; b1693.
DR EnsemblBacteria; BAA15448; BAA15448; BAA15448.
DR GeneID; 946210; -.
DR KEGG; ecj:JW1683; -.
DR KEGG; eco:b1693; -.
DR PATRIC; fig|1411691.4.peg.565; -.
DR EchoBASE; EB0074; -.
DR eggNOG; COG0710; Bacteria.
DR HOGENOM; CLU_064444_0_0_6; -.
DR InParanoid; P05194; -.
DR OMA; ATMAMGE; -.
DR PhylomeDB; P05194; -.
DR BioCyc; EcoCyc:AROD-MON; -.
DR BioCyc; MetaCyc:AROD-MON; -.
DR BRENDA; 4.2.1.10; 2026.
DR SABIO-RK; P05194; -.
DR UniPathway; UPA00053; UER00086.
DR PRO; PR:P05194; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00502; DHQase_I; 1.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Direct protein sequencing; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..252
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000138794"
FT ACT_SITE 143
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:1429576"
FT ACT_SITE 170
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:1826831"
FT BINDING 21
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 46..48
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 82
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 213
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 232
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 236
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT MUTAGEN 143
FT /note="H->A: Loss of dehydratase activity."
FT /evidence="ECO:0000269|PubMed:7592767"
FT MUTAGEN 146
FT /note="H->A: It retains full catalytic activity."
FT /evidence="ECO:0000269|PubMed:7592767"
FT MUTAGEN 170
FT /note="K->A: Loss of dehydratase activity, but it is still
FT able to bind substrate."
FT /evidence="ECO:0000269|PubMed:7592767"
FT MUTAGEN 205
FT /note="M->L: It has little effect on the catalytic
FT efficiency and affinity for 3-dehydroquinate."
FT /evidence="ECO:0000269|PubMed:7592767"
SQ SEQUENCE 252 AA; 27467 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
