IDI1_CANAL
ID IDI1_CANAL Reviewed; 284 AA.
AC A0A1D8PLI2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Isopentenyl-diphosphate delta-isomerase {ECO:0000250|UniProtKB:P15496};
DE EC=5.3.3.2 {ECO:0000250|UniProtKB:P15496};
DE AltName: Full=Isopentenyl pyrophosphate isomerase {ECO:0000250|UniProtKB:P15496};
DE Short=IPP isomerase {ECO:0000250|UniProtKB:P15496};
GN Name=IDI1 {ECO:0000250|UniProtKB:P15496}; OrderedLocusNames=orf19.2775;
GN ORFNames=CAALFM_C402280WA;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION.
RX PubMed=14653518; DOI=10.1080/1369378031000137233;
RA Song J.L., Lyons C.N., Holleman S., Oliver B.G., White T.C.;
RT "Antifungal activity of fluconazole in combination with lovastatin and
RT their effects on gene expression in the ergosterol and prenylation pathways
RT in Candida albicans.";
RL Med. Mycol. 41:417-425(2003).
CC -!- FUNCTION: Isopentenyl-diphosphate delta-isomerase; part of the second
CC module of ergosterol biosynthesis pathway that includes the middle
CC steps of the pathway (By similarity). IDI1 catalyzes the 1,3-allylic
CC rearrangement of isopentenyl (IPP) to its highly electrophilic allylic
CC isomer, dimethylallyl diphosphate (DMAPP) (By similarity). The second
CC module is carried out in the vacuole and involves the formation of
CC farnesyl diphosphate, which is also an important intermediate in the
CC biosynthesis of ubiquinone, dolichol, heme and prenylated proteins.
CC Activity by the mevalonate kinase ERG12 first converts mevalonate into
CC 5-phosphomevalonate. 5-phosphomevalonate is then further converted to
CC 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The
CC diphosphomevalonate decarboxylase MVD then produces isopentenyl
CC diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then
CC catalyzes the 1,3-allylic rearrangement of the homoallylic substrate
CC isopentenyl (IPP) to its highly electrophilic allylic isomer,
CC dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate
CC synthase ERG20 catalyzes the sequential condensation of isopentenyl
CC pyrophosphate with dimethylallyl pyrophosphate, and then with the
CC resultant geranylpyrophosphate to the ultimate product farnesyl
CC pyrophosphate (Probable). {ECO:0000250|UniProtKB:P15496,
CC ECO:0000305|PubMed:14653518}.
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:P15496};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23285;
CC Evidence={ECO:0000250|UniProtKB:P15496};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q46822};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q46822};
CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate:
CC step 1/1. {ECO:0000305|PubMed:14653518}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the IPP isomerase type 1 family. {ECO:0000305}.
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DR EMBL; CP017626; AOW28999.1; -; Genomic_DNA.
DR RefSeq; XP_720525.2; XM_715432.2.
DR AlphaFoldDB; A0A1D8PLI2; -.
DR SMR; A0A1D8PLI2; -.
DR STRING; 237561.A0A1D8PLI2; -.
DR GeneID; 3637894; -.
DR KEGG; cal:CAALFM_C402280WA; -.
DR CGD; CAL0000180278; IDI1.
DR VEuPathDB; FungiDB:C4_02280W_A; -.
DR eggNOG; KOG0142; Eukaryota.
DR OrthoDB; 1281908at2759; -.
DR UniPathway; UPA00059; UER00104.
DR Proteomes; UP000000559; Chromosome 4.
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:0045337; P:farnesyl diphosphate biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0009240; P:isopentenyl diphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006694; P:steroid 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 3: Inferred from homology;
KW Cytoplasm; Isomerase; Isoprene biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Metal-binding; Reference proteome;
KW Steroid biosynthesis.
FT CHAIN 1..284
FT /note="Isopentenyl-diphosphate delta-isomerase"
FT /id="PRO_0000454169"
FT DOMAIN 90..256
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 128..172
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT ACT_SITE 127
FT /evidence="ECO:0000250|UniProtKB:P15496"
FT ACT_SITE 206
FT /evidence="ECO:0000250|UniProtKB:P15496"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13907"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q46822"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q46822"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13907"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13907"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13907"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q46822"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q46822"
SQ SEQUENCE 284 AA; 32362 MW; 66BFDCF953C97F4B CRC64;
MSSEYAKLVA SLSNQDILTK WPEVTPLKKI SGIPRSAGSD SSDSDLFDGH DEEQIRLMEE
LCIVLDYDDK PVGAGTKKLC HIMDNINAGL LHRAFSVFLF NEDGKLLLQQ RADEKITFAN
MWTNTCCSHP LCVPSELGVD SSLEGSKDVN NLTNAVKGAK VAAQRKLEHE LGIPFEDAPI
ENFTYLTRIH YKSPSGDESS KWGEHEIDYI LILKTKNDIT VNANYNEVRD FKYVSADELK
VMFEDDSLVF TPWFKLICQS FLFKWWDNLD NLDQFKDEEI HRLL
