IDI_DICDI
ID IDI_DICDI Reviewed; 239 AA.
AC Q9NH02; Q54GN3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Isopentenyl-diphosphate Delta-isomerase;
DE EC=5.3.3.2;
DE AltName: Full=Isopentenyl pyrophosphate isomerase;
DE Short=IPP isomerase;
DE Short=IPPI;
GN Name=ipi; Synonyms=Dipi, idi; ORFNames=DDB_G0290011;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10804029; DOI=10.1359/jbmr.2000.15.5.971;
RA Grove J.E., Brown R.J., Watts D.J.;
RT "The intracellular target for the antiresorptive aminobisphosphonate drugs
RT in Dictyostelium discoideum is the enzyme farnesyl diphosphate synthase.";
RL J. Bone Miner. Res. 15:971-981(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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}.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate:
CC step 1/1.
CC -!- SIMILARITY: Belongs to the IPP isomerase type 1 family. {ECO:0000305}.
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DR EMBL; AF234169; AAF37873.1; -; mRNA.
DR EMBL; AAFI02000151; EAL62411.1; -; Genomic_DNA.
DR RefSeq; XP_635929.1; XM_630837.1.
DR AlphaFoldDB; Q9NH02; -.
DR SMR; Q9NH02; -.
DR STRING; 44689.DDB0191342; -.
DR PaxDb; Q9NH02; -.
DR EnsemblProtists; EAL62411; EAL62411; DDB_G0290011.
DR GeneID; 8627450; -.
DR KEGG; ddi:DDB_G0290011; -.
DR dictyBase; DDB_G0290011; ipi.
DR eggNOG; KOG0142; Eukaryota.
DR HOGENOM; CLU_060552_0_2_1; -.
DR InParanoid; Q9NH02; -.
DR OMA; DNGLTEH; -.
DR PhylomeDB; Q9NH02; -.
DR Reactome; R-DDI-191273; Cholesterol biosynthesis.
DR UniPathway; UPA00059; UER00104.
DR PRO; PR:Q9NH02; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009240; P:isopentenyl diphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
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 Isomerase; Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Metal-binding; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT CHAIN 1..239
FT /note="Isopentenyl-diphosphate Delta-isomerase"
FT /id="PRO_0000327827"
FT DOMAIN 56..210
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT ACT_SITE 93
FT /evidence="ECO:0000250"
FT ACT_SITE 158
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 239 AA; 27771 MW; EBE88D97861C8A32 CRC64;
MATKSNEENI AEFKGHNEIQ IELMKEECIV VDNDDKPIRP GSKKETHLMV NINNGLLHRA
FSIFLFNGEG KLLLQQRALE KITFPGYWTN TVCSHPLWIV GSELVEENAQ GVKIAAKRKL
NHELGVPLDQ VNIDDFTFMT KIHYKSESKE DPQWGEHEID HILIMQKDGI TINAEPNEVM
DYKYVSQEEL DQLFKDEDEG KVKVTPWFRL IALNHLKPWW NNLNNLKPLV EPTNTIHRY
