ID IDI2_RICTY Reviewed; 342 AA. AC Q68WS6; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 99. DE RecName: Full=Isopentenyl-diphosphate delta-isomerase {ECO:0000255|HAMAP-Rule:MF_00354}; DE Short=IPP isomerase {ECO:0000255|HAMAP-Rule:MF_00354}; DE EC=5.3.3.2 {ECO:0000255|HAMAP-Rule:MF_00354}; DE AltName: Full=Isopentenyl diphosphate:dimethylallyl diphosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00354}; DE AltName: Full=Isopentenyl pyrophosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00354}; DE AltName: Full=Type 2 isopentenyl diphosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00354}; DE Short=IDI-2 {ECO:0000255|HAMAP-Rule:MF_00354}; GN Name=fni {ECO:0000255|HAMAP-Rule:MF_00354}; OrderedLocusNames=RT0439; OS Rickettsia typhi (strain ATCC VR-144 / Wilmington). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=257363; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-144 / Wilmington; RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004; RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C., RA Yu X.-J., Walker D.H., Weinstock G.M.; RT "Complete genome sequence of Rickettsia typhi and comparison with sequences RT of other Rickettsiae."; RL J. Bacteriol. 186:5842-5855(2004). 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 {ECO:0000255|HAMAP-Rule:MF_00354}. 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; Evidence={ECO:0000255|HAMAP-Rule:MF_00354}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00354}; CC -!- COFACTOR: CC Name=NADPH; Xref=ChEBI:CHEBI:57783; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00354}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00354}; CC -!- SUBUNIT: Homooctamer. Dimer of tetramers. {ECO:0000255|HAMAP- CC Rule:MF_00354}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00354}. CC -!- SIMILARITY: Belongs to the IPP isomerase type 2 family. CC {ECO:0000255|HAMAP-Rule:MF_00354}. 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; AE017197; AAU03916.1; -; Genomic_DNA. DR RefSeq; WP_011190900.1; NC_006142.1. DR AlphaFoldDB; Q68WS6; -. DR SMR; Q68WS6; -. DR KEGG; rty:RT0439; -. DR eggNOG; COG1304; Bacteria. DR HOGENOM; CLU_065515_1_0_5; -. DR OrthoDB; 9795032at2; -. DR Proteomes; UP000000604; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule. DR GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0070402; F:NADPH binding; IEA:UniProtKB-UniRule. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd02811; IDI-2_FMN; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_00354; Idi_2; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000262; FMN-dep_DH. DR InterPro; IPR011179; IPdP_isomerase. DR NCBIfam; TIGR02151; IPP_isom_2; 1. DR PANTHER; PTHR43665; ISOPENTENYL-DIPHOSPHATE DELTA-ISOMERASE; 1. DR PANTHER; PTHR43665:SF1; ISOPENTENYL-DIPHOSPHATE DELTA-ISOMERASE; 1. DR Pfam; PF01070; FMN_dh; 2. DR PIRSF; PIRSF003314; IPP_isomerase; 1. DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1. PE 3: Inferred from homology; KW Cytoplasm; Flavoprotein; FMN; Isomerase; Isoprene biosynthesis; Magnesium; KW Metal-binding; NADP. FT CHAIN 1..342 FT /note="Isopentenyl-diphosphate delta-isomerase" FT /id="PRO_0000229509" FT BINDING 11..12 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354" FT BINDING 68 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354" FT BINDING 69..71 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354" FT BINDING 99..101 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354" FT BINDING 99 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354" FT BINDING 127 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354" FT BINDING 163 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354" FT BINDING 194 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354" FT BINDING 224 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354" FT BINDING 295..296 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354" SQ SEQUENCE 342 AA; 37359 MW; E973A10B89332FB4 CRC64; MLEEQNSDIE RKQDHIEINL KQNVNSTLKS GLASIKFIHN ALPEINYDNI DTTTTFLGKY MKAPILISSM TGGTTRAKDI NYRLAQAAQK SGIAMGLGSM RILLTKPDTI KTFTVRHVAP DIPLLANIGA VQLNYGVTPK ECQYLIDTIK ADALILHLNV LHELTQPEGN RNWENLLPKI KEVINYLSVP VIIKEVGYGL SKQVAKKLIK VGVKVLDIAG SGGTSWSQVE AYRAKNSMQN RIASSFINWG ITTLDSLKML REVSKDITLI ASGGLQSGID GAKAIRMGAN IFGLAGQLLK AADIAESLVS EEIQLIIEQL KITMLCTGSC TLKDLAKAEI ML //