AC MF_00202; DC Protein; auto TR HAMAP; MF_00202; -; 1; level=0 XX Names: Idi XX ID IDI DE RecName: Full=Isopentenyl-diphosphate Delta-isomerase; DE Short=IPP isomerase; DE EC=5.3.3.2; DE AltName: Full=IPP:DMAPP isomerase; DE AltName: Full=Isopentenyl pyrophosphate isomerase; GN Name=idi; XX CC -!- FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic CC substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, CC 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; case CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when CC substrate is bound.; end case case CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Binds 1 Mn(2+) ion per subunit.; end case CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate CC biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: CC step 1/1. case CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll CC biosynthesis. end case case CC -!- SUBUNIT: Homodimer. end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the IPP isomerase type 1 family. XX DR Pfam; PF00293; NUDIX; 1; trigger=no DR NCBIfam; TIGR02150; IPP_isom_1; 1; trigger=no XX KW Cytoplasm KW Isomerase KW Isoprene biosynthesis case KW Chlorophyll biosynthesis KW Photosynthesis end case case KW Magnesium end case case KW Manganese end case case or KW Metal-binding end case XX GO GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity case GO GO:0015995; P:chlorophyll biosynthetic process end case GO GO:0008299; P:isoprenoid biosynthetic process case GO GO:0015979; P:photosynthesis end case GO GO:0005737; C:cytoplasm XX FT From: IDI_ECOLI (Q46822) FT ACT_SITE 67 FT Condition: C FT ACT_SITE 116 FT Condition: E FT BINDING 25 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT Group: 1; Condition: H FT BINDING 32 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT Group: 1; Condition: H FT BINDING 69 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT Group: 1; Condition: H FT BINDING 87 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: E FT BINDING 114 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT Group: 1; Condition: E FT BINDING 116 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT Group: 1; Condition: E XX Size: 175-213; Related: None; Template: Q46822; Scope: Bacteria; Actinomycetota Bacteria; Pseudomonadota Archaea; Halobacteria Fusion: Nter: None Cter: None Duplicate: in AROAE, PHOLL Plasmid: in AGRRH, AROAE Comments: HALSA and HALMA putative conserved active site cysteine residue is replaced by an alanine. HALSA also possess a type-2 IDI. XX # Revision 1.41 2023/06/01 //