ID A0A0W0VBJ3_9GAMM Unreviewed; 342 AA.
AC A0A0W0VBJ3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=Ljor_1779 {ECO:0000313|EMBL:KTD17473.1};
OS Legionella jordanis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=456 {ECO:0000313|EMBL:KTD17473.1, ECO:0000313|Proteomes:UP000055035};
RN [1] {ECO:0000313|EMBL:KTD17473.1, ECO:0000313|Proteomes:UP000055035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL-540 {ECO:0000313|EMBL:KTD17473.1,
RC ECO:0000313|Proteomes:UP000055035};
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:KTD17473.1}.
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DR EMBL; LNYJ01000011; KTD17473.1; -; Genomic_DNA.
DR RefSeq; WP_058471222.1; NZ_RDQQ01000012.1.
DR AlphaFoldDB; A0A0W0VBJ3; -.
DR STRING; 456.Ljor_1779; -.
DR PATRIC; fig|456.5.peg.1900; -.
DR OrthoDB; 9795032at2; -.
DR Proteomes; UP000055035; 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:UP000055035}.
FT DOMAIN 176..340
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; 37604 MW; 267E1B7D125F5BF4 CRC64;
MQDNYSQFER RKQDHIELAL RDSNQASELN VLDQFSLCHE ALPDLDFSDI VIASNRFGRA
VEKPFFVSSM TAGHRDAVNI NHNLMEACAA SRWAMGVGSQ RRELTDPQAA HEWSLLRRNF
PKLNLFSNLG IAQLIHSPIE QIQRLTDALE AEALIIHCNP LQEALQPEGT PQFKGCWQAL
SDLTARLAIP VVIKETGCGF STTTLQRLND LGIAAVDVSG LGGTHWGRIE GQRAAEGSVQ
QKAAISFRNW GIDTVQSVKN AVSIAPKFEI WGSGGVRHGL DAAKLFALGV SSVGFAKPML
NAALEQANAV FELMMTIEYE LKVAMFCTGS RVLSELKEKA CR
//
