IDI2_STRPS
ID IDI2_STRPS Reviewed; 336 AA.
AC B2ILS5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=SPCG_0379;
OS Streptococcus pneumoniae (strain CGSP14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=516950;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGSP14;
RX PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT "Genome evolution driven by host adaptations results in a more virulent and
RT antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL BMC Genomics 10:158-158(2009).
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; CP001033; ACB89631.1; -; Genomic_DNA.
DR RefSeq; WP_000210618.1; NC_010582.1.
DR PDB; 4N02; X-ray; 1.40 A; A=2-336.
DR PDBsum; 4N02; -.
DR AlphaFoldDB; B2ILS5; -.
DR SMR; B2ILS5; -.
DR EnsemblBacteria; ACB89631; ACB89631; SPCG_0379.
DR KEGG; spw:SPCG_0379; -.
DR HOGENOM; CLU_065515_0_0_9; -.
DR OMA; WDWGIPT; -.
DR BRENDA; 5.3.3.2; 1960.
DR Proteomes; UP000001682; 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; 2.
DR PIRSF; PIRSF003314; IPP_isomerase; 1.
DR TIGRFAMs; TIGR02151; IPP_isom_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Flavoprotein; FMN; Isomerase;
KW Isoprene biosynthesis; Magnesium; Metal-binding; NADP.
FT CHAIN 1..336
FT /note="Isopentenyl-diphosphate delta-isomerase"
FT /id="PRO_1000120546"
FT BINDING 5..6
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 60..62
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 90
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 117
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 179
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 204
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 209
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 253..255
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 274..275
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:4N02"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:4N02"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:4N02"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 66..82
FT /evidence="ECO:0007829|PDB:4N02"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:4N02"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:4N02"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:4N02"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 145..150
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:4N02"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:4N02"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:4N02"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:4N02"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 257..265
FT /evidence="ECO:0007829|PDB:4N02"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 286..306
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 313..317
FT /evidence="ECO:0007829|PDB:4N02"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:4N02"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:4N02"
SQ SEQUENCE 336 AA; 37687 MW; 47F79E51BF2A5934 CRC64;
MTTNRKDEHI LYALEQKSSY NSFDEVELIH SSLPLYNLDE IDLSTEFAGR KWDFPFYINA
MTGGSNKGRE INQKLAQVAE SCGILFVTGS YSAALKNPTD DSFSVKSSHP NLLLGTNIGL
DKPVELGLQT VEEMNPVLLQ VHVNVMQELL MPEGERKFRS WQSHLADYSK QIPVPIVLKE
VGFGMDAKTI ERAYEFGVRT VDLSGRGGTS FAYIENRRSG QRDYLNQWGQ STMQALLNAQ
EWKDKVELLV SGGVRNPLDM IKCLVFGAKA VGLSRTVLEL VETYTVEEVI GIVQGWKADL
RLIMCSLNCA TIADLQKVDY LLYGKLKEAK DQMKKA
