ID   AROD_SULAC              Reviewed;         219 AA.
AC   Q4JC71;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Saci_0189;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY79608.1; -; Genomic_DNA.
DR   RefSeq; WP_011277109.1; NC_007181.1.
DR   AlphaFoldDB; Q4JC71; -.
DR   SMR; Q4JC71; -.
DR   STRING; 330779.Saci_0189; -.
DR   EnsemblBacteria; AAY79608; AAY79608; Saci_0189.
DR   GeneID; 3473927; -.
DR   KEGG; sai:Saci_0189; -.
DR   PATRIC; fig|330779.12.peg.181; -.
DR   eggNOG; arCOG02097; Archaea.
DR   HOGENOM; CLU_064444_2_0_2; -.
DR   OMA; MNRPLIV; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Reference proteome; Schiff base.
FT   CHAIN           1..219
FT                   /note="3-dehydroquinate dehydratase"
FT                   /id="PRO_0000138837"
FT   ACT_SITE        114
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   ACT_SITE        139
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         34..36
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         63
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         174
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         193
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         197
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
SQ   SEQUENCE   219 AA;  25568 MW;  D293DCEB16A06E37 CRC64;
     MIYISPKLVV ALPVKELKDL NRIELLINDV DLVELRLDYL SKFDVDILDL FSKYKEKLII
     TLRDKDEGGV NYIDPAFKAN FVRRMEREKF MYDIEARFAL RYQVNVKDKI VSIHYFDNLP
     EFTEVKEIFD KFDEAYLRKI AVIAKRGYRE LLMRVLDNYD NAVVMPMGVN GVERIAFSLL
     GSKLIYAHAG EETAKGQLHY KDVRRILNQL STIMSSPST