ID   AROD_STRPG              Reviewed;         228 AA.
AC   A2RF79;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
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}; OrderedLocusNames=SpyM51183;
OS   Streptococcus pyogenes serotype M5 (strain Manfredo).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=160491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Manfredo;
RX   PubMed=17012393; DOI=10.1128/jb.01227-06;
RA   Holden M.T.G., Scott A., Cherevach I., Chillingworth T., Churcher C.,
RA   Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Moule S., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S.,
RA   Skelton J., Whitehead S., Barrell B.G., Kehoe M., Parkhill J.;
RT   "Complete genome of acute rheumatic fever-associated serotype M5
RT   Streptococcus pyogenes strain Manfredo.";
RL   J. Bacteriol. 189:1473-1477(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}.
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DR   EMBL; AM295007; CAM30508.1; -; Genomic_DNA.
DR   RefSeq; WP_002985140.1; NC_009332.1.
DR   AlphaFoldDB; A2RF79; -.
DR   SMR; A2RF79; -.
DR   GeneID; 57852428; -.
DR   KEGG; spf:SpyM51183; -.
DR   HOGENOM; CLU_064444_0_0_9; -.
DR   OMA; FATMSMG; -.
DR   UniPathway; UPA00053; UER00086.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IEA:UniProt.
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; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001381; DHquinase_I.
DR   Pfam; PF01487; DHquinase_I; 1.
DR   TIGRFAMs; TIGR01093; aroD; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Schiff base.
FT   CHAIN           1..228
FT                   /note="3-dehydroquinate dehydratase"
FT                   /id="PRO_1000043200"
FT   ACT_SITE        118
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   ACT_SITE        143
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         30..32
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         62
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         186
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         205
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         209
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
SQ   SEQUENCE   228 AA;  26101 MW;  C1E41938E1A2E424 CRC64;
     MRIVAPVMPR HFDEAQAIDI SKYEDVNLIE WRADFLPKDE IVAVAPAIFE KFAGKEIIFT
     LRTVQEGGNI TLSSQEYVDI IKEINAIYNP DYIDFEYFTH KSVFQEMLDF PNLILSYHNF
     EETPENLMEA FSEMTKLAPR VVKIAVMPQS EQDVLDLMNY TRGFKTLNPE QEFATISMGK
     LGRLSRFAGD VIGSSWTYVS LDHVSGPGQV TLNDMKRIIE VLEMDISN