ID   IDI1_BOVIN              Reviewed;         227 AA.
AC   Q1LZ95;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   16-JUN-2009, entry version 25.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) 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; BC116133; AAI16134.1; ALT_INIT; mRNA.
DR   IPI; IPI00717782; -.
DR   RefSeq; NP_001069127.1; -.
DR   UniGene; Bt.3764; -.
DR   SMR; Q1LZ95; 69-287.
DR   Ensembl; ENSBTAG00000004075; Bos taurus.
DR   GeneID; 514293; -.
DR   KEGG; bta:514293; -.
DR   HOVERGEN; Q1LZ95; -.
DR   BRENDA; 5.3.3.2; 251.
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_0000287279.
FT   ACT_SITE     86     86       Proton acceptor (By similarity).
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;  26467 MW;  DFD065798697F520 CRC64;
     MPEVSTDDLD ERQVQLMAEM CILVDENDRR IGAETKKNCH LNENIERGLL HRAFSVFLFN
     TENKLLLQQR SDAKITFPGC FTNTCCSHPL SNPSELEEND AIGVRRAAQR RLKAELGIPM
     EEVPPEEINY LTRIHYKAQS DSIWGEHEID YILLVKKNVT LNPDPNEIKS YCYVTKEELE
     ELIGKAAHGE IKITPWFQII ADTFLFKWWD NLNRLNLFVD HEKIHRM
//