ID   IDI1_MACFA              Reviewed;         227 AA.
AC   Q4R4W5;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 2.
DT   03-AUG-2022, entry version 72.
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; ORFNames=QtrA-12624;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Temporal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:O35586}.
CC   -!- SIMILARITY: Belongs to the IPP isomerase type 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE01860.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB169779; BAE01860.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q4R4W5; -.
DR   SMR; Q4R4W5; -.
DR   STRING; 9541.XP_005564572.1; -.
DR   eggNOG; KOG0142; Eukaryota.
DR   UniPathway; UPA00059; UER00104.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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_0000205223"
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;  26410 MW;  0E5F3AF0A726CA64 CRC64;
     MPEINTDHLD KQQVQLLAEM CILIDENDNK IGAETKKNCH LNENIEKGLL HRAFSVFLFN
     TENKLLLQQR SDAKITFPGC FTNTCCSHPL SNPGELEEND ALGVRRAAQR RLKAELGIPL
     EEVPPEEINY LTRIHYKAQS DGIWGEHEID YILFVRKNVT LNPDPNEIKS FCYVSKEELK
     ELLKKAANGE IKITPWFQII AETFLFKWWD NLNHLNQFVD HEKIHRM