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IDI2_CHLL3
ID   IDI2_CHLL3              Reviewed;         361 AA.
AC   Q3B213;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Plut_1764;
OS   Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon
OS   luteolum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Pelodictyon.
OX   NCBI_TaxID=319225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 273 / BCRC 81028 / 2530;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelodictyon luteolum DSM 273.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000096; ABB24618.1; -; Genomic_DNA.
DR   RefSeq; WP_011358490.1; NC_007512.1.
DR   AlphaFoldDB; Q3B213; -.
DR   SMR; Q3B213; -.
DR   STRING; 319225.Plut_1764; -.
DR   EnsemblBacteria; ABB24618; ABB24618; Plut_1764.
DR   KEGG; plt:Plut_1764; -.
DR   eggNOG; COG1304; Bacteria.
DR   HOGENOM; CLU_065515_1_0_10; -.
DR   OMA; WDWGIPT; -.
DR   OrthoDB; 1186741at2; -.
DR   Proteomes; UP000002709; 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; 1.
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..361
FT                   /note="Isopentenyl-diphosphate delta-isomerase"
FT                   /id="PRO_0000229507"
FT   BINDING         12..13
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         70
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         71..73
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         101..103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         101
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         130
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         166
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         197
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         310..311
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
SQ   SEQUENCE   361 AA;  38707 MW;  660F423196305D2D CRC64;
     MSTTITNSTA ERKHSHVDIC LNGDVAFSTP TTGFERYRLR HNALPEVSFA DITTESRFLG
     RRIGAPLMIS SMTGGYSEAA ELNRQLAETA ERFQLPLGVG SMRQALEDDA YRDSFSVVRR
     HAPTIQIFAN IGAPEVAKGL SDKDLHIMLE MIRADGLIIH LNAAQELFQP EGGTDFRRVL
     DNIADIAAKL PVPVIAKEVG CGISGAVARK LLEAGVQVID VAGAGGISWQ KVEEARYTRR
     FGSDTRFSQE GIEELLNWGI PTAACVVEVD ALRPRTAGGR PFSIIASGGI HSGLDIAKSI
     ALGADLAASA GALLRALHHG TLEATITAWL QDLRASMFLT GSANVAELQN NRPIGDTAKQ
     P
 
 
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