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IDI2_STAAW
ID   IDI2_STAAW              Reviewed;         349 AA.
AC   Q8NV55;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=MW2267;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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; BA000033; BAB96132.1; -; Genomic_DNA.
DR   RefSeq; WP_001279387.1; NC_003923.1.
DR   AlphaFoldDB; Q8NV55; -.
DR   SMR; Q8NV55; -.
DR   EnsemblBacteria; BAB96132; BAB96132; BAB96132.
DR   KEGG; sam:MW2267; -.
DR   HOGENOM; CLU_065515_0_0_9; -.
DR   OMA; WDWGIPT; -.
DR   Proteomes; UP000000418; 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; 1.
DR   PIRSF; PIRSF003314; IPP_isomerase; 1.
DR   TIGRFAMs; TIGR02151; IPP_isom_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Flavoprotein; FMN; Isomerase; Isoprene biosynthesis; Magnesium;
KW   Metal-binding; NADP.
FT   CHAIN           1..349
FT                   /note="Isopentenyl-diphosphate delta-isomerase"
FT                   /id="PRO_0000134426"
FT   BINDING         9..10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         65..67
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         95..97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         95
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         124
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         155
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         186
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         211
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         216
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         262..264
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         283..284
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
SQ   SEQUENCE   349 AA;  38769 MW;  36DE9A22EDCDDEC5 CRC64;
     MSDFQREQRK NEHVEIAMAQ SDAMYSDFDK MRFVHHSIPS INVNDIDLTS QTPDLTMAYP
     VYINAMTGGS EWTKNINEKL AVVARETGLA MAVGSTHAAL RNPRMAETFT IARKMNPEGM
     IFSNVGADVP VEKALEAVEL LEAQALQIHV NSPQELVMPE GNREFVTWLD NIASIVSRVS
     VPVIIKEVGF GMSKELMHDL QQIGVKYVDV SGKGGTNFVD IENERRANKD MDYLSSWGQS
     TVESLLETTA YQSEISVFAS GGLRTPLDAI KSLALGAKAT GMSRPFLNQV ENNGIAHTVA
     YVESFIEHMK SIMTMLDAKN IDDLTQKQIV FSPEILSWIE QRSLNIHRG
 
 
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