IDI2_LACCB
ID IDI2_LACCB Reviewed; 344 AA.
AC B3WEJ5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=LCABL_17150;
OS Lacticaseibacillus casei (strain BL23) (Lactobacillus casei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=543734;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL23;
RA Maze A., Boel G., Bourand A., Loux V., Gibrat J.F., Zuniga M., Hartke A.,
RA Deutscher J.;
RT "Lactobacillus casei BL23 complete genome sequence.";
RL Submitted (JUN-2008) 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; FM177140; CAQ66796.1; -; Genomic_DNA.
DR RefSeq; WP_012491618.1; NC_010999.1.
DR AlphaFoldDB; B3WEJ5; -.
DR SMR; B3WEJ5; -.
DR KEGG; lcb:LCABL_17150; -.
DR HOGENOM; CLU_065515_0_0_9; -.
DR OMA; WDWGIPT; -.
DR OrthoDB; 1186741at2; -.
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..344
FT /note="Isopentenyl-diphosphate delta-isomerase"
FT /id="PRO_1000120543"
FT BINDING 9..10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 65..67
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 95
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 124
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 185
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 215
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 259..261
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 280..281
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
SQ SEQUENCE 344 AA; 37403 MW; 238D4D9187ED1607 CRC64;
MTQSQQSHRK DEHVFLAEKY FQSVAHAGFD QVRLLHRALP ETTMAAVDLK PDLPFNWQWP
IYINAMTGGS PQTGKLNAQL GQLAQALGVA IASGSQSVAL RDPQLVPTFA TLRDHDPNGF
ILANVGAGHH ATAAEAAVAM LKANALEIHL NAAQEVIMPE GDRDFMWQAN IKSIIATSQV
PIVVKEVGNG FIREDLQSLQ QLGVQFVDVG GRGGTNFATI ENARRSGHDF AYLQDWGQTT
VESLLEARGL GLAMLATGGV RSPLDVVKAL RLGAHAVGMS GLVLHHLIQT GYEATLAYFQ
NFLHQLRQLY ALLGVTNWQE LQEAPIVLSA DLEHYRQARG LPGI
