IDI1_RAT
ID IDI1_RAT Reviewed; 227 AA.
AC O35760; Q5FVT3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 ---------------------------------------------------------------------------
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; AF003835; AAC53282.1; -; mRNA.
DR EMBL; BC089786; AAH89786.2; -; mRNA.
DR RefSeq; NP_445991.2; NM_053539.2.
DR AlphaFoldDB; O35760; -.
DR SMR; O35760; -.
DR STRING; 10116.ENSRNOP00000022389; -.
DR BindingDB; O35760; -.
DR ChEMBL; CHEMBL4523132; -.
DR iPTMnet; O35760; -.
DR PhosphoSitePlus; O35760; -.
DR jPOST; O35760; -.
DR PaxDb; O35760; -.
DR PRIDE; O35760; -.
DR GeneID; 89784; -.
DR KEGG; rno:89784; -.
DR UCSC; RGD:621835; rat.
DR CTD; 3422; -.
DR RGD; 621835; Idi1.
DR eggNOG; KOG0142; Eukaryota.
DR HOGENOM; CLU_060552_0_2_1; -.
DR InParanoid; O35760; -.
DR OrthoDB; 1281908at2759; -.
DR PhylomeDB; O35760; -.
DR TreeFam; TF300129; -.
DR BRENDA; 5.3.3.2; 5301.
DR Reactome; R-RNO-191273; Cholesterol biosynthesis.
DR UniPathway; UPA00059; UER00104.
DR PRO; PR:O35760; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; O35760; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:RGD.
DR GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006695; P:cholesterol biosynthetic process; TAS:RGD.
DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009240; P:isopentenyl diphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0035634; P:response to stilbenoid; ISO:RGD.
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_0000205227"
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 /evidence="ECO:0000250"
FT ACT_SITE 148
FT /evidence="ECO:0000250"
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"
FT CONFLICT 110
FT /note="R -> K (in Ref. 1; AAC53282)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="L -> F (in Ref. 1; AAC53282)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 26396 MW; 58943AED08D74DB0 CRC64;
MPEINASNLD EKQVQLLAEM CILIDENDNK IGADTKKNCH LNENIDKGLI HRAFSVFLFN
TENKLLLQQR SDAKITFPGC FTNSCCSHPL NNPGELEEND AMGVKRAAQR RLKAELGIPL
EEVDLNEMNY LTRIYYKAQS DGIWGEHEID YILFLRKNVT LNPDPNEIKS YCYVSKEELK
EILKKEARGE IKLTPWFKII ADAFLFKWWD NLNHLSPFVD HEKIHRM
