ID   AROD_LACLM              Reviewed;         229 AA.
AC   A2RJD1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   02-SEP-2026, entry version 95.
DE   RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00214};
DE            Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214};
DE            EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00214};
DE   AltName: Full=Type I DHQase {ECO:0000255|HAMAP-Rule:MF_00214};
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};
GN   OrderedLocusNames=llmg_0782;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
CC   -!- FUNCTION: Involved in the third step of the chorismate pathway, which
CC       leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-
CC       dehydration of 3-dehydroquinate (DHQ) and introduces the first double
CC       bond of the aromatic ring to yield 3-dehydroshikimate.
CC       {ECO:0000255|HAMAP-Rule:MF_00214}.
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};
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   -!- 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; AM406671; CAL97383.1; -; Genomic_DNA.
DR   RefSeq; WP_011834761.1; NC_009004.1.
DR   AlphaFoldDB; A2RJD1; -.
DR   SMR; A2RJD1; -.
DR   STRING; 416870.llmg_0782; -.
DR   PaxDb; 416870-llmg_0782; -.
DR   KEGG; llm:llmg_0782; -.
DR   eggNOG; COG0710; Bacteria.
DR   HOGENOM; CLU_064444_0_0_9; -.
DR   OrthoDB; 9813659at2; -.
DR   PhylomeDB; A2RJD1; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000000364; Chromosome.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00502; DHQase_I; 1.
DR   FunFam; 3.20.20.70:FF:000047; 3-dehydroquinate dehydratase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00214; AroD; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001381; DHquinase_I.
DR   InterPro; IPR050146; Type-I_3-dehydroquinase.
DR   NCBIfam; TIGR01093; aroD; 1.
DR   PANTHER; PTHR43699; 3-DEHYDROQUINATE DEHYDRATASE; 1.
DR   PANTHER; PTHR43699:SF1; 3-DEHYDROQUINATE DEHYDRATASE; 1.
DR   Pfam; PF01487; DHquinase_I; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Reference proteome; Schiff base.
FT   CHAIN           1..229
FT                   /note="3-dehydroquinate dehydratase"
FT                   /id="PRO_1000043167"
FT   ACT_SITE        121
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   ACT_SITE        146
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         33..35
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         65
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         188
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         207
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         211
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
SQ   SEQUENCE   229 AA;  26309 MW;  935B5537DE78C808 CRC64;
     MRRTKIVVPI MLTELTELEK VSVSDYHSAD IVEWRADFLS ADDIFEMAPK FFEKFKESKI
     LFTLRTVREG GNIQVSEKKY LQILQEILKF DPDYIDVEYF SHGPSFAALK NYREKIVLSY
     HNFDEVPTDL TSRLIKMHEE GTAFVKVAVM PERECDVLDL LQITRDMTLE YGNHFISMAM
     GDLGRLSRIS GYLTGSCWTF ASLENSSAPG QISLKETVEI LDLLENELA
//