IDI2_STRMU
ID IDI2_STRMU Reviewed; 331 AA.
AC Q8DUI9;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=SMU_939;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS), AND SUBUNIT.
RA Liu Y.H., Fu T.M., Liu X., Su X.D.;
RT "Crystal structure of S. Mutans isopentenyl pyrophosph isomerase.";
RL Submitted (JUL-2011) to the PDB data bank.
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 (Probable).
CC {ECO:0000305|Ref.2}.
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; AE014133; AAN58644.1; -; Genomic_DNA.
DR RefSeq; NP_721338.1; NC_004350.2.
DR RefSeq; WP_002263658.1; NC_004350.2.
DR PDB; 3SR7; X-ray; 2.04 A; A/B/C/D=1-331.
DR PDBsum; 3SR7; -.
DR AlphaFoldDB; Q8DUI9; -.
DR SMR; Q8DUI9; -.
DR STRING; 210007.SMU_939; -.
DR EnsemblBacteria; AAN58644; AAN58644; SMU_939.
DR GeneID; 66817638; -.
DR KEGG; smu:SMU_939; -.
DR PATRIC; fig|210007.7.peg.837; -.
DR eggNOG; COG1304; Bacteria.
DR HOGENOM; CLU_065515_0_0_9; -.
DR OMA; WDWGIPT; -.
DR PhylomeDB; Q8DUI9; -.
DR Proteomes; UP000002512; 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; Reference proteome.
FT CHAIN 1..331
FT /note="Isopentenyl-diphosphate delta-isomerase"
FT /id="PRO_0000134430"
FT BINDING 4..5
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 59..61
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 89
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 116
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 147
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 178
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 203
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 208
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 252..254
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 273..274
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:3SR7"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:3SR7"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:3SR7"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3SR7"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:3SR7"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:3SR7"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3SR7"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:3SR7"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:3SR7"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:3SR7"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:3SR7"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:3SR7"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:3SR7"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:3SR7"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3SR7"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:3SR7"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:3SR7"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:3SR7"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:3SR7"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:3SR7"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:3SR7"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:3SR7"
FT HELIX 274..282
FT /evidence="ECO:0007829|PDB:3SR7"
FT HELIX 285..305
FT /evidence="ECO:0007829|PDB:3SR7"
FT HELIX 312..316
FT /evidence="ECO:0007829|PDB:3SR7"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:3SR7"
FT HELIX 323..328
FT /evidence="ECO:0007829|PDB:3SR7"
SQ SEQUENCE 331 AA; 37309 MW; 2C04210D57CD7B8B CRC64;
MTNRKDDHIK YALDYRSPYN SFDDIELIHH SLPDYDLAEI DLSTHFAGQD FDFPFYINAM
TGGSQKGKEV NEKLAQVADT CGLLFVTGSY STALKNPDDT SYQVKKSRPH LLLATNIGLD
KPYQAGLQAV RDLQPLFLQV HINLMQELLM PEGEREFRSW KKHLSDYAKK LQLPFILKEV
GFGMDVKTIQ TAIDLGVKTV DISGRGGTSF AYIENRRGGN RSYLNQWGQT TAQVLLNAQP
LMDKVEILAS GGIRHPLDII KALVLGAKAV GLSRTMLELV EQHSVHEVIA IVNGWKEDLR
LIMCALNCQT IAELRNVDYL LYGRLREGQR Q
