ID M3VZ04_FELCA Unreviewed; 281 AA.
AC M3VZ04;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 3.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=isopentenyl-diphosphate Delta-isomerase {ECO:0000256|ARBA:ARBA00012057};
DE EC=5.3.3.2 {ECO:0000256|ARBA:ARBA00012057};
GN Name=IDI1 {ECO:0000313|Ensembl:ENSFCAP00000002496.4};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000002496.4, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000002496.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000002496.4,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000002496.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000002496.4,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000002496.4}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000002496.4};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00003951}.
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:0000256|ARBA:ARBA00000374};
CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate:
CC step 1/1. {ECO:0000256|ARBA:ARBA00004826}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the IPP isomerase type 1 family.
CC {ECO:0000256|ARBA:ARBA00007579}.
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DR EMBL; AANG04002256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3VZ04; -.
DR STRING; 9685.ENSFCAP00000002496; -.
DR PaxDb; 9685-ENSFCAP00000002496; -.
DR Ensembl; ENSFCAT00000002714.5; ENSFCAP00000002496.4; ENSFCAG00000002714.5.
DR eggNOG; KOG0142; Eukaryota.
DR GeneTree; ENSGT00390000008527; -.
DR HOGENOM; CLU_060552_0_1_1; -.
DR InParanoid; M3VZ04; -.
DR OMA; LRLCPWF; -.
DR OrthoDB; 777305at2759; -.
DR UniPathway; UPA00059; UER00104.
DR Proteomes; UP000011712; Chromosome B4.
DR Bgee; ENSFCAG00000002714; Expressed in zone of skin and 10 other cell types or tissues.
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: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 Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR011876; IsopentenylPP_isomerase_typ1.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR NCBIfam; TIGR02150; IPP_isom_1; 1.
DR PANTHER; PTHR10885; ISOPENTENYL-DIPHOSPHATE DELTA-ISOMERASE; 1.
DR PANTHER; PTHR10885:SF0; ISOPENTENYL-DIPHOSPHATE DELTA-ISOMERASE; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW Cholesterol biosynthesis {ECO:0000256|ARBA:ARBA00022778};
KW Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022778};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022955};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022955};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023011};
KW Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023011}.
FT DOMAIN 103..253
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 281 AA; 32164 MW; 78B5A7580C5420B5 CRC64;
MWRALARALM VGRPAPRGGS QVWGRSLREG SPAERAFPGS RCRRVAGQVR RTATMPEIDT
DGLDEQQVQL LAEMCILIDE NDNKIGADTK KNCHLNENIE KGLLHRAFSV FLFNTENKLL
LQQRSDAKIT FPGYFTNTCC SHPLSNPGEL EENDAIGVRR AAQRRLKAEL GIPTEEVPPE
EINYLTRIHY KAQSDGIWGE HEIDYILFVK KNVTLNPDPN EIKSYCYVTK EELKELLKKA
ASGEIKITPW FQIIAEAFLF KWWDNLNNLS QFVDHDKIHR M
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