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   16-JUN-2009, entry version 24.
DE   RecName: Full=Isopentenyl-diphosphate Delta-isomerase 1;
DE            EC=5.3.3.2;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; 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
CC       homoallylic substrate isopentenyl (IPP) to its highly
CC       electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP)
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Isopentenyl diphosphate = dimethylallyl
CC       diphosphate.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl-PP biosynthesis;
CC       dimethylallyl-PP from isopentenyl-PP: step 1/1.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome (By similarity).
CC   -!- SIMILARITY: Belongs to the IPP isomerase type 1 family.
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DR   EMBL; AB169779; BAE01860.1; ALT_INIT; mRNA.
DR   SMR; Q4R4W5; 8-227.
DR   HOVERGEN; Q4R4W5; -.
DR   BRENDA; 5.3.3.2; 3438.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase act...; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011876; IsopentenylPP_isomerase_typ1.
DR   InterPro; IPR000086; NUDIX_hydrolase_core.
DR   Gene3D; G3DSA:3.90.79.10; NUDIX_hydrolase; 1.
DR   PANTHER; PTHR10885; IPP_isom_1; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   PIRSF; PIRSF018427; Isopntndiph_ism; 1.
DR   ProDom; PD004109; IPP_isomerase; 1.
DR   TIGRFAMs; TIGR02150; IPP_isom_1; 1.
PE   2: Evidence at transcript level;
KW   Carotenoid biosynthesis; Cholesterol biosynthesis; Isomerase;
KW   Isoprene biosynthesis; Lipid synthesis; Magnesium; Metal-binding;
KW   Peroxisome; Steroid biosynthesis; Sterol biosynthesis.
FT   CHAIN         1    227       Isopentenyl-diphosphate Delta-isomerase
FT                                1.
FT                                /FTId=PRO_0000205223.
FT   MOTIF       225    227       Microbody targeting signal.
FT   ACT_SITE     86     86
FT   ACT_SITE    148    148
FT   METAL        40     40       Magnesium (By similarity).
FT   METAL        51     51       Magnesium (By similarity).
FT   METAL       146    146       Magnesium (By similarity).
FT   METAL       148    148       Magnesium (By similarity).
FT   BINDING      36     36       Substrate (By similarity).
FT   BINDING      70     70       Substrate (By similarity).
FT   BINDING      74     74       Substrate (By similarity).
FT   BINDING      87     87       Substrate (By similarity).
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
//