ID   AROQ_SYNY3              Reviewed;         152 AA.
AC   P73367;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=3-dehydroquinate dehydratase;
DE            Short=3-dehydroquinase;
DE            EC=4.2.1.10;
DE   AltName: Full=Type II DHQase;
GN   Name=aroQ; OrderedLocusNames=sll1112;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate.
CC       {ECO:0000250}.
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;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       3/7.
CC   -!- SUBUNIT: Homododecamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000022; BAA17398.1; -; Genomic_DNA.
DR   PIR; S77551; S77551.
DR   AlphaFoldDB; P73367; -.
DR   SMR; P73367; -.
DR   IntAct; P73367; 1.
DR   STRING; 1148.gene:10498261; -.
DR   PaxDb; 1148-1652476; -.
DR   EnsemblBacteria; BAA17398; BAA17398; BAA17398.
DR   KEGG; syn:sll1112; -.
DR   eggNOG; COG0757; Bacteria.
DR   InParanoid; P73367; -.
DR   PhylomeDB; P73367; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019631; P:quinate catabolic process; IBA:GO_Central.
DR   CDD; cd00466; DHQase_II; 1.
DR   Gene3D; 3.40.50.9100; Dehydroquinase, class II; 1.
DR   HAMAP; MF_00169; AroQ; 1.
DR   InterPro; IPR001874; DHquinase_II.
DR   InterPro; IPR018509; DHquinase_II_CS.
DR   InterPro; IPR036441; DHquinase_II_sf.
DR   NCBIfam; TIGR01088; aroQ; 1.
DR   PANTHER; PTHR21272; CATABOLIC 3-DEHYDROQUINASE; 1.
DR   PANTHER; PTHR21272:SF3; CATABOLIC 3-DEHYDROQUINASE; 1.
DR   Pfam; PF01220; DHquinase_II; 1.
DR   PIRSF; PIRSF001399; DHquinase_II; 1.
DR   SUPFAM; SSF52304; Type II 3-dehydroquinate dehydratase; 1.
DR   PROSITE; PS01029; DEHYDROQUINASE_II; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Reference proteome.
FT   CHAIN           1..152
FT                   /note="3-dehydroquinate dehydratase"
FT                   /id="PRO_0000159933"
FT   ACT_SITE        26
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        103
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         104..105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            21
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   152 AA;  16375 MW;  360092AEF938A2C6 CRC64;
     MTTVWKVLVL HGPNLNLLGQ REPGIYGSLT LGEIDACLRE DGVDLEAEVS TFQSNSEGQL
     VTAIHGALGN YHGIVFNAAA YTHTSIALRD ALAAVQLPCV EVHLSNIHKR ESFRHISHIA
     PVAIGQICGF GLNSYRLGLR ALVDYLNGQA DS
//