IDI1_SCHPO
ID IDI1_SCHPO Reviewed; 229 AA.
AC Q10132;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Isopentenyl-diphosphate delta-isomerase {ECO:0000303|PubMed:7744766};
DE EC=5.3.3.2 {ECO:0000250|UniProtKB:P15496};
DE AltName: Full=Isopentenyl pyrophosphate isomerasee {ECO:0000303|PubMed:7744766};
DE Short=IPP isomerase {ECO:0000303|PubMed:7744766};
GN Name=idi1 {ECO:0000303|PubMed:7744766}; ORFNames=SPBC106.15;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-229, FUNCTION, AND PATHWAY.
RX PubMed=7744766; DOI=10.1074/jbc.270.19.11298;
RA Hahn F.M., Poulter C.D.;
RT "Isolation of Schizosaccharomyces pombe isopentenyl diphosphate isomerase
RT cDNA clones by complementation and synthesis of the enzyme in Escherichia
RT coli.";
RL J. Biol. Chem. 270:11298-11303(1995).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 (PubMed:7744766). Idi1 catalyzes the 1,3-allylic
CC rearrangement of isopentenyl (IPP) to its highly electrophilic allylic
CC isomer, dimethylallyl diphosphate (DMAPP) (PubMed:7744766). 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 mvd1 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 fps1 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:0000269|PubMed:7744766, ECO:0000305}.
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:0000305|PubMed:7744766};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23285;
CC Evidence={ECO:0000305|PubMed:7744766};
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:7744766}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the IPP isomerase type 1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB53731.2; -; Genomic_DNA.
DR EMBL; U21154; AAA80596.1; -; mRNA.
DR PIR; A56442; A56442.
DR RefSeq; NP_595164.2; NM_001021073.2.
DR AlphaFoldDB; Q10132; -.
DR SMR; Q10132; -.
DR STRING; 4896.SPBC106.15.1; -.
DR MaxQB; Q10132; -.
DR PaxDb; Q10132; -.
DR PRIDE; Q10132; -.
DR EnsemblFungi; SPBC106.15.1; SPBC106.15.1:pep; SPBC106.15.
DR GeneID; 2540174; -.
DR KEGG; spo:SPBC106.15; -.
DR PomBase; SPBC106.15; idi1.
DR VEuPathDB; FungiDB:SPBC106.15; -.
DR eggNOG; KOG0142; Eukaryota.
DR HOGENOM; CLU_060552_0_2_1; -.
DR InParanoid; Q10132; -.
DR OMA; DNGLTEH; -.
DR Reactome; R-SPO-191273; Cholesterol biosynthesis.
DR UniPathway; UPA00059; UER00104.
DR PRO; PR:Q10132; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IDA:PomBase.
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; ISO:PomBase.
DR GO; GO:0009240; P:isopentenyl diphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0008202; P:steroid metabolic process; NAS:PomBase.
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 Cytoplasm; Isomerase; Isoprene biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Metal-binding; Nucleus; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism.
FT CHAIN 1..229
FT /note="Isopentenyl-diphosphate delta-isomerase"
FT /id="PRO_0000205230"
FT DOMAIN 52..202
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT ACT_SITE 89
FT /evidence="ECO:0000250|UniProtKB:P15496"
FT ACT_SITE 154
FT /evidence="ECO:0000250|UniProtKB:P15496"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13907"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q46822"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q46822"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13907"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13907"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13907"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q46822"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q46822"
SQ SEQUENCE 229 AA; 27108 MW; A3FE0B29B12AD9A0 CRC64;
MIMSSQQEKK DYDEEQLRLM EEVCIVVDEN DVPLRYGTKK ECHLMENINK GLLHRAFSMF
IFDEQNRLLL QQRAEEKITF PSLWTNTCCS HPLDVAGERG NTLPEAVEGV KNAAQRKLFH
ELGIQAKYIP KDKFQFLTRI HYLAPSTGAW GEHEIDYILF FKGKVELDIN PNEVQAYKYV
TMEELKEMFS DPQYGFTPWF KLICEHFMFK WWQDVDHASK FQDTLIHRC
