AROD_ENTFA
ID AROD_ENTFA Reviewed; 253 AA.
AC P36923;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000303|PubMed:25072253};
DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000303|PubMed:25072253};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:25072253};
DE AltName: Full=Type I DHQase {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000303|PubMed:25072253};
DE AltName: Full=Type I dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214};
DE Short=DHQ1 {ECO:0000255|HAMAP-Rule:MF_00214};
GN Name=aroD {ECO:0000255|HAMAP-Rule:MF_00214}; Synonyms=ebsD;
GN OrderedLocusNames=EF_1731;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=OG1SSP;
RX PubMed=8226689; DOI=10.1128/jb.175.22.7421-7429.1993;
RA Bensing B.A., Dunny G.M.;
RT "Cloning and molecular analysis of genes affecting expression of binding
RT substance, the recipient-encoded receptor(s) mediating mating aggregate
RT formation in Enterococcus faecalis.";
RL J. Bacteriol. 175:7421-7429(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 700802 / V583;
RX PubMed=25072253; DOI=10.1371/journal.pone.0103598;
RA Cheung V.W., Xue B., Hernandez-Valladares M., Go M.K., Tung A., Aguda A.H.,
RA Robinson R.C., Yew W.S.;
RT "Identification of polyketide inhibitors targeting 3-dehydroquinate
RT dehydratase in the shikimate pathway of Enterococcus faecalis.";
RL PLoS ONE 9:E103598-E103598(2014).
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 Lys-170
CC at the active site. {ECO:0000269|PubMed:25072253}.
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:25072253};
CC -!- ACTIVITY REGULATION: Inhibited by flavonoids such as datiscetin,
CC naringenin, marein and phloretin. {ECO:0000269|PubMed:25072253}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=65 uM for 3-dehydroquinate (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:25072253};
CC Note=kcat is 110 sec(-1) for dehydratase activity with 3-
CC dehydroquinate (at pH 7.5 and 25 degrees Celsius).
CC {ECO:0000269|PubMed:25072253};
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:25072253}.
CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00214}.
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DR EMBL; L23802; AAC36854.1; -; Unassigned_DNA.
DR EMBL; AE016830; AAO81505.1; -; Genomic_DNA.
DR PIR; D49939; D49939.
DR RefSeq; NP_815435.1; NC_004668.1.
DR RefSeq; WP_002357400.1; NZ_KE136528.1.
DR PDB; 4PH6; X-ray; 2.20 A; A/B=1-253.
DR PDBsum; 4PH6; -.
DR AlphaFoldDB; P36923; -.
DR SMR; P36923; -.
DR STRING; 226185.EF_1731; -.
DR EnsemblBacteria; AAO81505; AAO81505; EF_1731.
DR GeneID; 60894026; -.
DR KEGG; efa:EF1731; -.
DR PATRIC; fig|226185.9.peg.1628; -.
DR eggNOG; COG0710; Bacteria.
DR HOGENOM; CLU_064444_0_0_9; -.
DR OMA; ATMAMGE; -.
DR BRENDA; 4.2.1.10; 2095.
DR UniPathway; UPA00053; UER00086.
DR Proteomes; UP000001415; Chromosome.
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 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Lyase; Reference proteome; Schiff base.
FT CHAIN 1..253
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000138843"
FT ACT_SITE 143
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT ACT_SITE 170
FT /note="Schiff-base intermediate with substrate"
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 STRAND 4..6
FT /evidence="ECO:0007829|PDB:4PH6"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:4PH6"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:4PH6"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:4PH6"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:4PH6"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:4PH6"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:4PH6"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:4PH6"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:4PH6"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:4PH6"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:4PH6"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:4PH6"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:4PH6"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:4PH6"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:4PH6"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:4PH6"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:4PH6"
FT HELIX 178..194
FT /evidence="ECO:0007829|PDB:4PH6"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:4PH6"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:4PH6"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:4PH6"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:4PH6"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:4PH6"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:4PH6"
SQ SEQUENCE 253 AA; 28085 MW; F8F1436A80906B02 CRC64;
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VLTLLSATNE MYTHYASVPI VTMSMGQLGM ISRVTGQLFG SALTFGSAQQ ASAPGQLSVQ
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