ID A0A1Y0IU52_9BACL Unreviewed; 351 AA.
AC A0A1Y0IU52;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Isopentenyl-diphosphate delta-isomerase {ECO:0000256|HAMAP-Rule:MF_00354};
DE Short=IPP isomerase {ECO:0000256|HAMAP-Rule:MF_00354};
DE EC=5.3.3.2 {ECO:0000256|HAMAP-Rule:MF_00354};
DE AltName: Full=Isopentenyl diphosphate:dimethylallyl diphosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00354};
DE AltName: Full=Isopentenyl pyrophosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00354};
DE AltName: Full=Type 2 isopentenyl diphosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00354};
DE Short=IDI-2 {ECO:0000256|HAMAP-Rule:MF_00354};
GN Name=fni {ECO:0000256|HAMAP-Rule:MF_00354};
GN ORFNames=CBW65_20140 {ECO:0000313|EMBL:ARU63025.1};
OS Tumebacillus avium.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Tumebacillus.
OX NCBI_TaxID=1903704 {ECO:0000313|EMBL:ARU63025.1, ECO:0000313|Proteomes:UP000195437};
RN [1] {ECO:0000313|Proteomes:UP000195437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR23208 {ECO:0000313|Proteomes:UP000195437};
RA Sung H.;
RL Submitted (MAY-2017) 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:0000256|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:0000256|HAMAP-Rule:MF_00354};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917,
CC ECO:0000256|HAMAP-Rule:MF_00354};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00354};
CC -!- COFACTOR:
CC Name=NADPH; Xref=ChEBI:CHEBI:57783;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00354};
CC -!- SUBUNIT: Homooctamer. Dimer of tetramers.
CC {ECO:0000256|ARBA:ARBA00025810, ECO:0000256|HAMAP-Rule:MF_00354}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00354}.
CC -!- SIMILARITY: Belongs to the IPP isomerase type 2 family.
CC {ECO:0000256|HAMAP-Rule:MF_00354}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00354}.
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DR EMBL; CP021434; ARU63025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0IU52; -.
DR KEGG; tum:CBW65_20140; -.
DR OrthoDB; 9795032at2; -.
DR Proteomes; UP000195437; 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; 1.
DR PIRSF; PIRSF003314; IPP_isomerase; 1.
DR SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00354};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_00354};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_00354};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00354};
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP-
KW Rule:MF_00354};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00354};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00354};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00354}.
FT DOMAIN 167..323
FT /note="FMN-dependent dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01070"
FT BINDING 6..7
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 62..64
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 92..94
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 92
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 121
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 183
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 213
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 280..281
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
SQ SEQUENCE 351 AA; 37355 MW; F18A0AD681CC8BD1 CRC64;
MSIEQRKLDH VRYALELPIS ESTGFSDLSF VHRALPESDL ADVSLATSIG GLDLSSPILL
NAMTGGAGPT EAINGKLAEL AKHCGIAMAV GSQRAALKDP ALVSTYRIVR DVNPDGIIIG
NLGAGATVED AKRAVEMIGA DLLHLHLNVA QELTMPEGDR SFSGLVEKIR QVVEGVGVPV
IVKEVGNGMS IETFRVLAET GVKVVDVAGR GGTNFVAIEN RRRSGLQFQH MESWGQTTAV
SLLEAQEFLH RFDLIGSGGV QNAHDAAKCL ALGAKAVGLA GAVLRPLMEL GVEQAVEMMD
HLHSELRAIV TLQGCRSVLE LAERPVMVRG ETAQWCQLRG VALEPLARRG L
//
