ID   AROD_HYDS0              Reviewed;         217 AA.
AC   B4U701;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=HY04AAS1_0220;
OS   Hydrogenobaculum sp. (strain Y04AAS1).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobaculum;
OC   unclassified Hydrogenobaculum.
OX   NCBI_TaxID=380749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y04AAS1;
RX   PubMed=19136599; DOI=10.1128/jb.01645-08;
RA   Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
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; CP001130; ACG56912.1; -; Genomic_DNA.
DR   RefSeq; WP_012513269.1; NC_011126.1.
DR   AlphaFoldDB; B4U701; -.
DR   SMR; B4U701; -.
DR   STRING; 380749.HY04AAS1_0220; -.
DR   EnsemblBacteria; ACG56912; ACG56912; HY04AAS1_0220.
DR   KEGG; hya:HY04AAS1_0220; -.
DR   eggNOG; COG0710; Bacteria.
DR   HOGENOM; CLU_064444_2_1_0; -.
DR   OMA; ATMAMGE; -.
DR   OrthoDB; 1298468at2; -.
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; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Schiff base.
FT   CHAIN           1..217
FT                   /note="3-dehydroquinate dehydratase"
FT                   /id="PRO_1000099908"
FT   ACT_SITE        114
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   ACT_SITE        140
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         26..28
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         59
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         178
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         201
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
SQ   SEQUENCE   217 AA;  24817 MW;  7E530D6D2FDAB10A CRC64;
     MKIAIPITDE NFDEVLLKAR NADILEFRVD SFTNKDISFV SGLLKKAKEN GFETILTIRS
     EKEGGAYVEN RVEMFEKLMP LSDYTDIELS STDIIAYISR LSKEYNKKLI VSYHNFEMTP
     ANFVIKETIR EALRYGDIPK IALKANSYED VARLMCSAID IKTPKILISM GEFGKISRIA
     GFIFGSFISY AYLEKPNAPG QLSLEEMLKL KEMFYLR