ID AROQ_ACTPL Reviewed; 154 AA. AC P43877; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 119. 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; OS Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=715; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 27088 / DSM 13472 / CCM 5869 / CCUG 41656 / S4074 / RC Serotype 1; RX PubMed=8170389; DOI=10.1111/j.1365-2958.1994.tb00307.x; RA Lalonde G., O'Hanley P.D., Stocker B.A.D., Denich K.T.; RT "Characterization of a 3-dehydroquinase gene from Actinobacillus RT pleuropneumoniae with homology to the eukaryotic genes qa-2 and QUTE."; RL Mol. Microbiol. 11:273-280(1994). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND SUBUNIT. RX PubMed=14993670; DOI=10.1107/s090744490302969x; RA Maes D., Gonzalez-Ramirez L.A., Lopez-Jaramillo J., Yu B., De Bondt H., RA Zegers I., Afonina E., Garcia-Ruiz J.M., Gulnik S.; RT "Structural study of the type II 3-dehydroquinate dehydratase from RT Actinobacillus pleuropneumoniae."; RL Acta Crystallogr. D 60:463-471(2004). 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:0000269|PubMed:14993670}. CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L19895; AAA72027.1; -; Genomic_DNA. DR PIR; S41538; S41538. DR RefSeq; WP_005599518.1; NZ_CBDBSU010000091.1. DR PDB; 1UQR; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-154. DR AlphaFoldDB; P43877; -. DR SMR; P43877; -. DR GeneID; 48600167; -. DR OMA; AYTHYSY; -. DR OrthoDB; 9790793at2; -. DR UniPathway; UPA00053; UER00086. DR EvolutionaryTrace; P43877; -. DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0019631; P:quinate catabolic process; IEA:TreeGrafter. 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 NCBIfam; NF003804; PRK05395.1-1; 1. DR NCBIfam; NF003805; PRK05395.1-2; 1. DR NCBIfam; NF003806; PRK05395.1-3; 1. DR NCBIfam; NF003807; PRK05395.1-4; 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. DR PDBsum; 1UQR; -. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Lyase. FT CHAIN 1..154 FT /note="3-dehydroquinate dehydratase" FT /id="PRO_0000159862" FT ACT_SITE 23 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 100 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 74 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 80 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 87 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 101..102 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 111 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 18 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:1UQR" FT HELIX 12..14 FT /evidence="ECO:0007829|PDB:1UQR" FT HELIX 20..22 FT /evidence="ECO:0007829|PDB:1UQR" FT HELIX 28..41 FT /evidence="ECO:0007829|PDB:1UQR" FT STRAND 45..50 FT /evidence="ECO:0007829|PDB:1UQR" FT HELIX 54..63 FT /evidence="ECO:0007829|PDB:1UQR" FT TURN 64..67 FT /evidence="ECO:0007829|PDB:1UQR" FT STRAND 70..74 FT /evidence="ECO:0007829|PDB:1UQR" FT HELIX 78..81 FT /evidence="ECO:0007829|PDB:1UQR" FT HELIX 83..92 FT /evidence="ECO:0007829|PDB:1UQR" FT STRAND 96..102 FT /evidence="ECO:0007829|PDB:1UQR" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:1UQR" FT HELIX 109..111 FT /evidence="ECO:0007829|PDB:1UQR" FT HELIX 117..119 FT /evidence="ECO:0007829|PDB:1UQR" FT STRAND 120..127 FT /evidence="ECO:0007829|PDB:1UQR" FT HELIX 130..144 FT /evidence="ECO:0007829|PDB:1UQR" FT HELIX 147..151 FT /evidence="ECO:0007829|PDB:1UQR" SQ SEQUENCE 154 AA; 17179 MW; 6DDC809E9B276BC4 CRC64; MKKILLLNGP NLNMLGKREP HIYGSQTLSD IEQHLQQSAQ AQGYELDYFQ ANGEESLINR IHQAFQNTDF IIINPGAFTH TSVAIRDALL AVSIPFIEVH LSNVHAREPF RHHSYLSDVA KGVICGLGAK GYDYALDFAI SELQKIQLGE MMNG //