IDI1_BOVIN
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 03-AUG-2022, entry version 100.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q1LZ95-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1LZ95-2; Sequence=VSP_037888;
CC -!- SIMILARITY: Belongs to the IPP isomerase type 1 family. {ECO:0000305}.
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DR EMBL; AAFC03067960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC116133; AAI16134.1; -; mRNA.
DR RefSeq; NP_001069127.1; NM_001075659.1.
DR AlphaFoldDB; Q1LZ95; -.
DR SMR; Q1LZ95; -.
DR STRING; 9913.ENSBTAP00000005323; -.
DR PaxDb; Q1LZ95; -.
DR PeptideAtlas; Q1LZ95; -.
DR PRIDE; Q1LZ95; -.
DR GeneID; 514293; -.
DR KEGG; bta:514293; -.
DR CTD; 3422; -.
DR eggNOG; KOG0142; Eukaryota.
DR HOGENOM; CLU_060552_0_0_1; -.
DR InParanoid; Q1LZ95; -.
DR OrthoDB; 1281908at2759; -.
DR TreeFam; TF300129; -.
DR UniPathway; UPA00059; UER00104.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
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 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; Alternative splicing; Cholesterol biosynthesis;
KW Cholesterol metabolism; Isomerase; Isoprene biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding; Peroxisome;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism.
FT CHAIN 1..227
FT /note="Isopentenyl-diphosphate Delta-isomerase 1"
FT /id="PRO_0000287279"
FT DOMAIN 49..199
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT ACT_SITE 86
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
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"
FT VAR_SEQ 1
FT /note="M -> MMWRALAPARAIGRAASGGGARIGGGARALGRSLKDTPPAVQPTVDG
FT SCLRFPGRRGGWAA (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_037888"
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
