ID   IDI1_MESAU              Reviewed;         227 AA.
AC   O35586;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Isopentenyl-diphosphate Delta-isomerase 1;
DE            EC=5.3.3.2 {ECO:0000250|UniProtKB:Q13907};
DE   AltName: Full=Isopentenyl pyrophosphate isomerase 1;
DE            Short=IPP isomerase 1;
DE            Short=IPPI1;
GN   Name=IDI1;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX   PubMed=9228075; DOI=10.1074/jbc.272.30.18945;
RA   Paton V.G., Shackelford J.E., Krisans S.K.;
RT   "Cloning and subcellular localization of hamster and rat isopentenyl
RT   diphosphate dimethylallyl diphosphate isomerase. A PTS1 motif targets the
RT   enzyme to peroxisomes.";
RL   J. Biol. Chem. 272:18945-18950(1997).
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:0000250|UniProtKB:Q13907}.
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:0000250|UniProtKB:Q13907};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q13907};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q13907};
CC   -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC       biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate:
CC       step 1/1. {ECO:0000250|UniProtKB:Q13907}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q13907}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:9228075}.
CC   -!- SIMILARITY: Belongs to the IPP isomerase type 1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF003836; AAC53283.1; -; mRNA.
DR   AlphaFoldDB; O35586; -.
DR   SMR; O35586; -.
DR   STRING; 10036.XP_005071822.1; -.
DR   eggNOG; KOG0142; Eukaryota.
DR   BRENDA; 5.3.3.2; 3239.
DR   UniPathway; UPA00059; UER00104.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR   GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; 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-KW.
DR   CDD; cd02885; IPP_Isomerase; 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   2: Evidence at transcript level;
KW   Acetylation; Cholesterol biosynthesis; Cholesterol metabolism; Isomerase;
KW   Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW   Metal-binding; Peroxisome; Reference proteome; Steroid biosynthesis;
KW   Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT   CHAIN           1..227
FT                   /note="Isopentenyl-diphosphate Delta-isomerase 1"
FT                   /id="PRO_0000205224"
FT   DOMAIN          49..199
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           225..227
FT                   /note="Microbody targeting signal"
FT   ACT_SITE        86
FT   ACT_SITE        148
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         176
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13907"
SQ   SEQUENCE   227 AA;  26317 MW;  F500A6586385E803 CRC64;
     MPEINTSHLD EQQVQLLAEM CILIDENDNK IGADTKKNCH LNENIDKGLL HRAFSVFLFN
     TENKLLLQQR SDAKITFPGC FTNSCCSHPL SNPGELEEND AIGVKRAAQR RLKAELGIPL
     EEVDPNEMHY LTRIYYKAQS DGIWGEHEID YILFLKKNVT LNPDPNEIKS YCYVSKEELK
     ELVKKAASGE VKLTPWFKII VDTFLFKWWD NLNHLSQFVD HEKIHRM