ID   IDI_SALPC               Reviewed;         181 AA.
AC   C0PY11;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Isopentenyl-diphosphate Delta-isomerase {ECO:0000255|HAMAP-Rule:MF_00202};
DE            Short=IPP isomerase {ECO:0000255|HAMAP-Rule:MF_00202};
DE            EC=5.3.3.2 {ECO:0000255|HAMAP-Rule:MF_00202};
DE   AltName: Full=IPP:DMAPP isomerase {ECO:0000255|HAMAP-Rule:MF_00202};
DE   AltName: Full=Isopentenyl pyrophosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00202};
GN   Name=idi {ECO:0000255|HAMAP-Rule:MF_00202}; OrderedLocusNames=SPC_3098;
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594;
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA   Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT   and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(2009).
CC   -!- FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic
CC       substrate isopentenyl (IPP) to its highly electrophilic allylic isomer,
CC       dimethylallyl diphosphate (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00202}.
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_00202};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00202};
CC       Note=Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when
CC       substrate is bound. {ECO:0000255|HAMAP-Rule:MF_00202};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00202};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00202};
CC   -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC       biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate:
CC       step 1/1. {ECO:0000255|HAMAP-Rule:MF_00202}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00202}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00202}.
CC   -!- SIMILARITY: Belongs to the IPP isomerase type 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00202}.
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DR   EMBL; CP000857; ACN47185.1; -; Genomic_DNA.
DR   RefSeq; WP_000133994.1; NC_012125.1.
DR   AlphaFoldDB; C0PY11; -.
DR   SMR; C0PY11; -.
DR   EnsemblBacteria; ACN47185; ACN47185; SPC_3098.
DR   KEGG; sei:SPC_3098; -.
DR   HOGENOM; CLU_060552_2_0_6; -.
DR   OMA; FPLRWAN; -.
DR   UniPathway; UPA00059; UER00104.
DR   Proteomes; UP000001599; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02885; IPP_Isomerase; 1.
DR   HAMAP; MF_00202; Idi; 1.
DR   InterPro; IPR011876; IsopentenylPP_isomerase_typ1.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   Pfam; PF00293; NUDIX; 1.
DR   PIRSF; PIRSF018427; Isopntndiph_ism; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   TIGRFAMs; TIGR02150; IPP_isom_1; 1.
DR   PROSITE; PS51462; NUDIX; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Isoprene biosynthesis; Magnesium; Manganese;
KW   Metal-binding.
FT   CHAIN           1..181
FT                   /note="Isopentenyl-diphosphate Delta-isomerase"
FT                   /id="PRO_1000124559"
FT   DOMAIN          30..164
FT                   /note="Nudix hydrolase"
FT   ACT_SITE        67
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   BINDING         25
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   BINDING         32
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   BINDING         69
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   BINDING         87
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   BINDING         114
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   BINDING         116
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
SQ   SEQUENCE   181 AA;  20781 MW;  1B0EBEA813936526 CRC64;
     MTEEHVVLLD EQDKPSGTLE KYAAHTLNTP LHLAFSCWLF NEDGQLLVTR RSLSKKAWPG
     VWTNSVCGHP QQGETTEEAI IRRCRFELGV EITDLTPVYP HFSYRATDPN GIVENEVCPV
     FAARATSVLQ VNSEEVMDYQ WSEFKSVWKS LLATPWAFSP WMVMQASDEQ ARERLLNYCQ
     R