AROQ_HELPJ
ID AROQ_HELPJ Reviewed; 170 AA.
AC Q9ZM37;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=jhp_0386;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD05961.1; -; Genomic_DNA.
DR PIR; H71937; H71937.
DR RefSeq; WP_000699286.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZM37; -.
DR SMR; Q9ZM37; -.
DR STRING; 85963.jhp_0386; -.
DR EnsemblBacteria; AAD05961; AAD05961; jhp_0386.
DR KEGG; hpj:jhp_0386; -.
DR PATRIC; fig|85963.30.peg.624; -.
DR eggNOG; COG0757; Bacteria.
DR OMA; AYTHYSY; -.
DR UniPathway; UPA00053; UER00086.
DR Proteomes; UP000000804; 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; cd00466; DHQase_II; 1.
DR Gene3D; 3.40.50.9100; -; 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 PANTHER; PTHR21272; PTHR21272; 1.
DR Pfam; PF01220; DHquinase_II; 1.
DR PIRSF; PIRSF001399; DHquinase_II; 1.
DR SUPFAM; SSF52304; SSF52304; 1.
DR TIGRFAMs; TIGR01088; aroQ; 1.
DR PROSITE; PS01029; DEHYDROQUINASE_II; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase.
FT CHAIN 1..170
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000159906"
FT ACT_SITE 22
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 102
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 103..104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 17
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 170 AA; 18809 MW; B6EE402D8AF39920 CRC64;
MKILVIQGPN LNMLGHRDPR LYGMVTLDQI HEIMQTFVKQ GNLDVELEFF QTNFEGEIID
KIQESVGSDY EGIIINPGAF SHTSIAIADA IMLAGKPVIE VHLTNIQARE EFRKNSYTGA
ACGGVIMGFG PLGYNMALMA MVNILAEMKA FQEAQKNNPN NPNNPINNQK