AC MF_00354; DC Protein; auto TR HAMAP; MF_00354; -; 1; level=0 XX Names: Idi_2 XX ID IDI2 DE RecName: Full=Isopentenyl-diphosphate delta-isomerase; DE Short=IPP isomerase; DE EC=5.3.3.2; DE AltName: Full=Type 2 isopentenyl diphosphate isomerase; DE Short=IDI-2; DE AltName: Full=Isopentenyl pyrophosphate isomerase; DE AltName: Full=Isopentenyl diphosphate:dimethylallyl diphosphate isomerase; GN Name=fni; XX CC -!- FUNCTION: Involved in the biosynthesis of isoprenoids. Catalyzes the CC 1,3-allylic rearrangement of the homoallylic substrate isopentenyl CC (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP). CC -!- CATALYTIC ACTIVITY: CC Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; CC Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; CC EC=5.3.3.2; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC -!- COFACTOR: CC Name=NADPH; Xref=ChEBI:CHEBI:57783; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SUBUNIT: Homooctamer. Dimer of tetramers. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the IPP isomerase type 2 family. XX DR Pfam; PF01070; FMN_dh; 1; trigger=no DR NCBIfam; TIGR02151; IPP_isom_2; 1; trigger=no XX KW Cytoplasm KW Flavoprotein KW FMN KW Isomerase KW Isoprene biosynthesis KW Magnesium KW Metal-binding KW NADP XX GO GO:0000287; F:magnesium ion binding GO GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity GO GO:0010181; F:FMN binding GO GO:0070402; F:NADPH binding GO GO:0008299; P:isoprenoid biosynthetic process GO GO:0005737; C:cytoplasm XX FT From: IDI2_SACSH (P61615) FT BINDING 66..68 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Optional; Condition: [GAS]-[MIL]-T case FT BINDING 274..275 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Optional; Condition: G-G else FT BINDING 275..277 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Optional; Condition: G-x-[RK] end case FT BINDING 296..297 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Optional; Condition: [AS]-x FT BINDING 7..8 FT /ligand="substrate" FT Optional; Condition: [RK]-K FT BINDING 96..98 FT /ligand="substrate" FT Optional; Condition: S-x-[RKH] FT BINDING 161 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: E FT BINDING 65 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Optional; Condition: [TS] FT BINDING 96 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: S FT BINDING 125 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: N FT BINDING 160 FT /ligand="substrate" FT Condition: Q FT BINDING 193 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: K FT BINDING 218 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: S FT BINDING 223 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: T XX Size: 329-374; Related: None; Template: P61615; Q746I8; P50740; Q8DUI9; Q58272; Q9KWG2; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: in HALSA Comments: None XX # Revision 1.29 2023/06/01 //