AC MF_03136; DC Protein; auto c? TR HAMAP; MF_00169; -; 1; level=0 XX Names: qutE XX ID 3DHQ DE RecName: Full=Catabolic 3-dehydroquinase; DE Short=cDHQase; DE EC=4.2.1.10; DE AltName: Full=3-dehydroquinate dehydratase; case and not GN Name=qutE; else case GN Name=qa-2; else case GN Name=DQD1; end case XX CC -!- FUNCTION: Is involved in the catabolism of quinate. Allows the CC utilization of quinate as carbon source via the beta-ketoadipate CC pathway. 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: Aromatic compound metabolism; 3,4-dihydroxybenzoate CC biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 1/2. CC -!- SUBUNIT: Homododecamer. Adopts a ring-like structure, composed of an CC arrangement of two hexameric rings stacked on top of one another. CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family. XX DR Pfam; PF01220; DHquinase_II; 1; trigger=no DR NCBIfam; TIGR01088; AroQ; 1; trigger=no DR PIRSF; PIRSF001399; DHquinase_II; 1; trigger=no DR PROSITE; PS01029; DEHYDROQUINASE_II; 1; trigger=no XX KW Lyase KW Quinate metabolism XX GO GO:0003855; F:3-dehydroquinate dehydratase activity GO GO:0019630; P:quinate metabolic process XX FT From: 3DHQ_EMENI (P05147) FT BINDING 102..103 FT /ligand="substrate" FT Condition: [IV]-[ST] FT ACT_SITE 24 FT /note="Proton acceptor" FT Condition: Y FT ACT_SITE 101 FT /note="Proton donor" FT Condition: H FT BINDING 75 FT /ligand="substrate" FT Condition: N FT BINDING 81 FT /ligand="substrate" FT Condition: H FT BINDING 88 FT /ligand="substrate" FT Condition: D FT BINDING 112 FT /ligand="substrate" FT Condition: R FT SITE 19 FT /note="Transition state stabilizer" FT Condition: R XX Size: 144-175; Related: None; Template: P05147; Scope: Eukaryota; Fungi Fusion: Nter: None Cter: None Duplicate: in ASPFC, ASPFN, ASPFU, ASPTN, FUSV7, NEOFI Plasmid: None Comments: None XX # Revision 1.9 2023/12/07 //