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IDI2_STRGC
ID   IDI2_STRGC              Reviewed;         334 AA.
AC   A8AUV1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=SGO_0242;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
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; CP000725; ABV10499.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8AUV1; -.
DR   SMR; A8AUV1; -.
DR   STRING; 467705.SGO_0242; -.
DR   EnsemblBacteria; ABV10499; ABV10499; SGO_0242.
DR   KEGG; sgo:SGO_0242; -.
DR   eggNOG; COG1304; Bacteria.
DR   HOGENOM; CLU_065515_0_0_9; -.
DR   OMA; WDWGIPT; -.
DR   Proteomes; UP000001131; 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; Reference proteome.
FT   CHAIN           1..334
FT                   /note="Isopentenyl-diphosphate delta-isomerase"
FT                   /id="PRO_1000079386"
FT   BINDING         5..6
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         60..62
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         90
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         117
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         148
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         179
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         204
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         209
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         253..255
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         274..275
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
SQ   SEQUENCE   334 AA;  37622 MW;  80D21C33F3AD65A7 CRC64;
     MSQNRKDDHI KYALEQRPGY NSFDEMELVH RSLPKYDLAE IDLSTHFAGR DWEFPFYINA
     MTGGSQKGSQ INEKLAQVAE SCGLLFVTGS YSAALKNPSD TSYQVATGRP NLLLATNIGL
     DKPYQAAQQA VADLQPLFLQ IHVNLMQELL MPEGEREFRS WRQHLTDYSQ RLDLPLILKE
     VGFGMDRSTV EEARSLGIQT FDISGRGGTS FAYIENQRGG NRDYLNDWGQ STLQSLLALQ
     PMRDEVELLA SGGVRHPLDM IKALVLGAKA VGLSRAMLDL VKNYSVEEVI DIVEGWKSDL
     RLIMCALSCR NLQELKNVPY LLYGRLKEAQ EQIK
 
 
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