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AROQ_ERWT9
ID   AROQ_ERWT9              Reviewed;         150 AA.
AC   B2VGX5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=ETA_02790;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
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; CU468135; CAO95325.1; -; Genomic_DNA.
DR   RefSeq; WP_012440044.1; NC_010694.1.
DR   AlphaFoldDB; B2VGX5; -.
DR   SMR; B2VGX5; -.
DR   STRING; 465817.ETA_02790; -.
DR   EnsemblBacteria; CAO95325; CAO95325; ETA_02790.
DR   KEGG; eta:ETA_02790; -.
DR   eggNOG; COG0757; Bacteria.
DR   HOGENOM; CLU_090968_1_0_6; -.
DR   OMA; AYTHYSY; -.
DR   OrthoDB; 1872106at2; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000001726; 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..150
FT                   /note="3-dehydroquinate dehydratase"
FT                   /id="PRO_1000097599"
FT   ACT_SITE        26
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   ACT_SITE        103
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         104..105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   SITE            21
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
SQ   SEQUENCE   150 AA;  16361 MW;  490CFBFF77C2DED8 CRC64;
     MSDKLHVLLL NGPNLNLLGT REPEKYGHTS LDEIVSELTL QASALGVTLS HLQSNAEHAL
     IDRIHQAKGN VDYIVINPAA FTHTSVALRD ALLAVSIPFI EVHLSNVHAR EPFRHHSYLS
     DISTGVICGL GVDGYSWALQ TAVKRLSLSH
 
 
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