AROQ_CHESB
ID AROQ_CHESB Reviewed; 145 AA.
AC Q11HL6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, 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=Meso_1714;
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans; unclassified Chelativorans.
OX NCBI_TaxID=266779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BNC1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000390; ABG63109.1; -; Genomic_DNA.
DR RefSeq; WP_011581052.1; NC_008254.1.
DR AlphaFoldDB; Q11HL6; -.
DR SMR; Q11HL6; -.
DR STRING; 266779.Meso_1714; -.
DR EnsemblBacteria; ABG63109; ABG63109; Meso_1714.
DR KEGG; mes:Meso_1714; -.
DR eggNOG; COG0757; Bacteria.
DR HOGENOM; CLU_090968_2_0_5; -.
DR OMA; CAGIVIN; -.
DR OrthoDB; 1872106at2; -.
DR UniPathway; UPA00053; UER00086.
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..145
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_1000023483"
FT ACT_SITE 24
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT ACT_SITE 102
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 103..104
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT SITE 19
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
SQ SEQUENCE 145 AA; 15368 MW; 63CBE5B23D781364 CRC64;
MAKTVYVLNG PNLNTLGKRE PGIYGGKTLA DIEADCRAAA AGLGLEVEFR QSNHEGMLID
WIHEAGERGA GIVLNPGAYG HTSIALHDAI RAVSPLPVIE VHLSNIHARE PFRHRTMTAP
VVAGMICGLG PIGYTLALQA LAARL
