AC PRU01407; DC Domain; TR PROSITE; PS52062; DAHPS_II; 1; level=0 XX Names: DAHPS class-II core TIM-barrel domain Function: Although there is no significant sequence similarity between the class-II DAHPSs and the class-I DAHPSs and KDOPSs, they share a characteristic (beta/alpha)8 TIM-barrel fold in which the eight parallel beta-strands are each followed by alpha-helices, and similar active site architecture. XX CC -!- SIMILARITY: Belongs to the class-II DAHP synthase family. XX case and KW Transferase KW Metal-binding end case FT From: PS52062 FT DOMAIN from..to FT /note="DAHPS class-II TIM-barrel #" FT BINDING 11 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: C FT BINDING 50 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT Group: 2; Condition: R FT BINDING 208 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT Group: 2; Condition: [ED] FT BINDING 209 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT Group: 2; Condition: R FT BINDING 231 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT Group: 2; Condition: K FT BINDING 262 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT Group: 2; Condition: R FT BINDING 294 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: H FT BINDING 336 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: E FT BINDING 366 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: D XX Chop: Nter=0; Cter=0; Size: 18-415; Related: None; Repeats: 1; Topology: Undefined; Example: P21357; Scope: Eukaryota Bacteria Comments: None; XX # Version: 3 # Last updated date: 2025-04-07 # Created date: 2025-04-04 //