ID A0A0W0XYK5_9GAMM Unreviewed; 342 AA.
AC A0A0W0XYK5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=Lrub_0261 {ECO:0000313|EMBL:KTD49819.1};
OS Legionella rubrilucens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=458 {ECO:0000313|EMBL:KTD49819.1, ECO:0000313|Proteomes:UP000054608};
RN [1] {ECO:0000313|EMBL:KTD49819.1, ECO:0000313|Proteomes:UP000054608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA-270A-C2 {ECO:0000313|EMBL:KTD49819.1,
RC ECO:0000313|Proteomes:UP000054608};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTD49819.1}.
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DR EMBL; LNYT01000004; KTD49819.1; -; Genomic_DNA.
DR RefSeq; WP_058530403.1; NZ_LNYT01000004.1.
DR AlphaFoldDB; A0A0W0XYK5; -.
DR STRING; 458.Lrub_0261; -.
DR PATRIC; fig|458.5.peg.270; -.
DR OrthoDB; 9795032at2; -.
DR Proteomes; UP000054608; Unassembled WGS sequence.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000054608}.
FT DOMAIN 175..338
FT /note="FMN-dependent dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01070"
FT BINDING 11..12
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 68
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 69..71
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 99..101
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 99
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 128
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 194
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 219
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 224
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 275..277
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
FT BINDING 296..297
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00354"
SQ SEQUENCE 342 AA; 37341 MW; 726E86239DC1FECA CRC64;
MQNRYSQFEK RKQDHIELAL MPCNQTEEMN DLDTIDLVHD ALPDLDFADI SLHGIRFGEP
VRTPFLVSSM TAGHQDAARI NRSLIAACAD KGWAMGVGSQ RRELMDDEAA FEWLPLRRDY
PQVTLMSNIG IAQLIDTPVK RIQQLTEALG ARALIVHCNP LQEVIQPEGT PQFKGCWQAI
ERVVTALTIP VVIKETGCGF SASTLSRLNN LGIAAVDVSG LGGTHWGRIE GHRASDSPER
QQAAKTFANW GITTVASVQQ AAALNPQYEL WGSGGVRHGL DAARLIALGA STVGFAKPML
EVALKGVEQV VERMTTIEYE LKVAMFCTGS LHLSDLKGKA CP
//
