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IDI2_RICBR
ID   IDI2_RICBR              Reviewed;         342 AA.
AC   Q1RIK2;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=RBE_0731;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00354};
CC   -!- COFACTOR:
CC       Name=NADPH; Xref=ChEBI:CHEBI:57783;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00354};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; CP000087; ABE04812.1; -; Genomic_DNA.
DR   RefSeq; WP_011477399.1; NC_007940.1.
DR   AlphaFoldDB; Q1RIK2; -.
DR   SMR; Q1RIK2; -.
DR   STRING; 336407.RBE_0731; -.
DR   EnsemblBacteria; ABE04812; ABE04812; RBE_0731.
DR   KEGG; rbe:RBE_0731; -.
DR   eggNOG; COG1304; Bacteria.
DR   HOGENOM; CLU_065515_1_0_5; -.
DR   OMA; WDWGIPT; -.
DR   OrthoDB; 1186741at2; -.
DR   Proteomes; UP000001951; 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; -; 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   PANTHER; PTHR43665; PTHR43665; 1.
DR   Pfam; PF01070; FMN_dh; 2.
DR   PIRSF; PIRSF003314; IPP_isomerase; 1.
DR   TIGRFAMs; TIGR02151; IPP_isom_2; 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_0000277969"
FT   BINDING         6..7
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         63
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         64..66
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         94..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         94
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         122
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         158
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         189
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         219
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         269..271
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         290..291
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
SQ   SEQUENCE   342 AA;  37076 MW;  5816EBA5A2D09E7A CRC64;
     MLDIKRKQDH IEINLTKNVE SGLSSGFESV QFVHNALPEI NYSSIDTTTT FLNKILQAPI
     LISSMTGGTP RARDINCRLA AAAQKAGIAM GLGSMRTLLT EPSTLDTFTV RNNAPDIVLL
     ANIGAVQLNY GVTPKQCQYL VDSVKADALI LHLNVLQELT QPEGDKNWEN LLPKIKEVVN
     YLSVPVIIKE VGFGLSKKTA KQFIDIGVKI LDVAGSGGTS WSQVEAYRAT NSLQNRIASS
     FINWGIPTLD SLKMVREASK DISVIASGGL KSGIDGAKAI RMGADIFGLA GPFLKAADVS
     ENLVSEEIQL IIEQLKITMM CTGSRTINNL KKAELRMNHI PL
 
 
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