AROQ_NAUPA
ID AROQ_NAUPA Reviewed; 163 AA.
AC B9L5V9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00169};
DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00169};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00169};
DE AltName: Full=Type II DHQase {ECO:0000255|HAMAP-Rule:MF_00169};
GN Name=aroQ {ECO:0000255|HAMAP-Rule:MF_00169}; OrderedLocusNames=NAMH_1354;
OS Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales; Nautiliaceae;
OC Nautilia.
OX NCBI_TaxID=598659;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1463 / DSM 18972 / AmH;
RX PubMed=19197347; DOI=10.1371/journal.pgen.1000362;
RA Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K.,
RA Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.;
RT "Adaptations to submarine hydrothermal environments exemplified by the
RT genome of Nautilia profundicola.";
RL PLoS Genet. 5:E1000362-E1000362(2009).
CC -!- FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate.
CC {ECO:0000255|HAMAP-Rule:MF_00169}.
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_00169};
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_00169}.
CC -!- SUBUNIT: Homododecamer. {ECO:0000255|HAMAP-Rule:MF_00169}.
CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00169}.
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DR EMBL; CP001279; ACM92140.1; -; Genomic_DNA.
DR RefSeq; WP_012663512.1; NC_012115.1.
DR AlphaFoldDB; B9L5V9; -.
DR SMR; B9L5V9; -.
DR STRING; 598659.NAMH_1354; -.
DR EnsemblBacteria; ACM92140; ACM92140; NAMH_1354.
DR KEGG; nam:NAMH_1354; -.
DR eggNOG; COG0757; Bacteria.
DR HOGENOM; CLU_090968_3_0_7; -.
DR OMA; VIECHIS; -.
DR OrthoDB; 1872106at2; -.
DR UniPathway; UPA00053; UER00086.
DR Proteomes; UP000000448; 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;
KW Reference proteome.
FT CHAIN 1..163
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_1000123696"
FT ACT_SITE 22
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT ACT_SITE 100
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 101..102
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT SITE 17
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
SQ SEQUENCE 163 AA; 18101 MW; AB628FF68E2A0D4C CRC64;
MKIKVIHGPN LNMLGIREVN LYGPMKLEDI NKNMEAFAKQ NGFEIEFYQS NHEGDIVDAI
QESLNENVDG IIINPAALTH YSVAIRDAIK AVNLPTIEIH MTNTAAREEF RHKSLISDIV
AGTITGFGPF SYHLGLIAMI QILNEIKMAK EAQAKAQAQA NKQ
