IDI2_HUMAN
ID IDI2_HUMAN Reviewed; 227 AA.
AC Q9BXS1;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Isopentenyl-diphosphate delta-isomerase 2;
DE EC=5.3.3.2 {ECO:0000269|PubMed:17202134};
DE AltName: Full=Isopentenyl pyrophosphate isomerase 2;
DE Short=IPP isomerase 2;
DE Short=IPPI2;
GN Name=IDI2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION,
RP AND PATHWAY.
RX PubMed=17202134; DOI=10.1074/jbc.m610922200;
RA Clizbe D.B., Owens M.L., Masuda K.R., Shackelford J.E., Krisans S.K.;
RT "IDI2, a second isopentenyl diphosphate isomerase in mammals.";
RL J. Biol. Chem. 282:6668-6676(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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:0000269|PubMed:17202134}.
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:0000269|PubMed:17202134};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17202134};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22.8 uM for isopentenyl {ECO:0000269|PubMed:17202134};
CC Vmax=0.12 umol/min/mg enzyme with isopentenyl as substrate
CC {ECO:0000269|PubMed:17202134};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:17202134};
CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate:
CC step 1/1. {ECO:0000269|PubMed:17202134}.
CC -!- INTERACTION:
CC Q9BXS1; Q86U70-2: LDB1; NbExp=4; IntAct=EBI-766127, EBI-11979761;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17202134}.
CC -!- TISSUE SPECIFICITY: Muscle-specific expression.
CC {ECO:0000269|PubMed:17202134}.
CC -!- SIMILARITY: Belongs to the IPP isomerase type 1 family. {ECO:0000305}.
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DR EMBL; AF291755; AAK29358.1; -; Genomic_DNA.
DR EMBL; AF271729; AAK49436.1; -; Genomic_DNA.
DR EMBL; AF271726; AAK49436.1; JOINED; Genomic_DNA.
DR EMBL; AF271727; AAK49436.1; JOINED; Genomic_DNA.
DR EMBL; AF271728; AAK49436.1; JOINED; Genomic_DNA.
DR EMBL; AF271725; AAK49437.1; -; mRNA.
DR EMBL; AK056950; BAB71322.1; -; mRNA.
DR EMBL; BC017778; AAH17778.1; -; mRNA.
DR CCDS; CCDS7055.1; -.
DR RefSeq; NP_150286.1; NM_033261.2.
DR PDB; 2PNY; X-ray; 1.81 A; A=1-227.
DR PDBsum; 2PNY; -.
DR AlphaFoldDB; Q9BXS1; -.
DR SMR; Q9BXS1; -.
DR BioGRID; 124870; 13.
DR IntAct; Q9BXS1; 13.
DR STRING; 9606.ENSP00000277517; -.
DR SwissLipids; SLP:000001268; -.
DR iPTMnet; Q9BXS1; -.
DR PhosphoSitePlus; Q9BXS1; -.
DR BioMuta; IDI2; -.
DR DMDM; 20978506; -.
DR EPD; Q9BXS1; -.
DR jPOST; Q9BXS1; -.
DR MassIVE; Q9BXS1; -.
DR MaxQB; Q9BXS1; -.
DR PaxDb; Q9BXS1; -.
DR PeptideAtlas; Q9BXS1; -.
DR PRIDE; Q9BXS1; -.
DR Antibodypedia; 23799; 120 antibodies from 19 providers.
DR DNASU; 91734; -.
DR Ensembl; ENST00000277517.2; ENSP00000277517.1; ENSG00000148377.6.
DR GeneID; 91734; -.
DR KEGG; hsa:91734; -.
DR MANE-Select; ENST00000277517.2; ENSP00000277517.1; NM_033261.3; NP_150286.1.
DR UCSC; uc001ifv.1; human.
DR CTD; 91734; -.
DR DisGeNET; 91734; -.
DR GeneCards; IDI2; -.
DR HGNC; HGNC:23487; IDI2.
DR HPA; ENSG00000148377; Tissue enriched (skeletal).
DR MIM; 615389; gene.
DR neXtProt; NX_Q9BXS1; -.
DR OpenTargets; ENSG00000148377; -.
DR PharmGKB; PA134935136; -.
DR VEuPathDB; HostDB:ENSG00000148377; -.
DR eggNOG; KOG0142; Eukaryota.
DR GeneTree; ENSGT00390000008527; -.
DR HOGENOM; CLU_060552_0_1_1; -.
DR InParanoid; Q9BXS1; -.
DR OMA; VEQEYNH; -.
DR OrthoDB; 1281908at2759; -.
DR PhylomeDB; Q9BXS1; -.
DR TreeFam; TF300129; -.
DR BioCyc; MetaCyc:HS07522-MON; -.
DR PathwayCommons; Q9BXS1; -.
DR Reactome; R-HSA-191273; Cholesterol biosynthesis.
DR SABIO-RK; Q9BXS1; -.
DR SignaLink; Q9BXS1; -.
DR UniPathway; UPA00059; UER00104.
DR BioGRID-ORCS; 91734; 64 hits in 1072 CRISPR screens.
DR EvolutionaryTrace; Q9BXS1; -.
DR GenomeRNAi; 91734; -.
DR Pharos; Q9BXS1; Tbio.
DR PRO; PR:Q9BXS1; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9BXS1; protein.
DR Bgee; ENSG00000148377; Expressed in hindlimb stylopod muscle and 68 other tissues.
DR Genevisible; Q9BXS1; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IDA:UniProtKB.
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 GO; GO:0046490; P:isopentenyl diphosphate metabolic process; IDA:MGI.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; 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 2"
FT /id="PRO_0000205228"
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 /evidence="ECO:0000255"
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 HELIX 1..4
FT /evidence="ECO:0007829|PDB:2PNY"
FT HELIX 11..16
FT /evidence="ECO:0007829|PDB:2PNY"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:2PNY"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:2PNY"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:2PNY"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:2PNY"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:2PNY"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:2PNY"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2PNY"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:2PNY"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:2PNY"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2PNY"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:2PNY"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2PNY"
FT HELIX 102..116
FT /evidence="ECO:0007829|PDB:2PNY"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:2PNY"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:2PNY"
FT STRAND 128..156
FT /evidence="ECO:0007829|PDB:2PNY"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:2PNY"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:2PNY"
FT HELIX 176..188
FT /evidence="ECO:0007829|PDB:2PNY"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:2PNY"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:2PNY"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:2PNY"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:2PNY"
SQ SEQUENCE 227 AA; 26753 MW; 2FD79B076D94A7D0 CRC64;
MSDINLDWVD RRQLQRLEEM LIVVDENDKV IGADTKRNCH LNENIEKGLL HRAFSVVLFN
TKNRILIQQR SDTKVTFPGY FTDSCSSHPL YNPAELEEKD AIGVRRAAQR RLQAELGIPG
EQISPEDIVF MTIYHHKAKS DRIWGEHEIC YLLLVRKNVT LNPDPSETKS ILYLSQEELW
ELLEREARGE VKVTPWLRTI AERFLYRWWP HLDDVTPFVE LHKIHRV
