ID IDI1_SCHPO Reviewed; 227 AA. AC Q10132; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 16-JUN-2009, entry version 66. DE RecName: Full=Isopentenyl-diphosphate Delta-isomerase; DE EC=5.3.3.2; DE AltName: Full=Isopentenyl pyrophosphate isomerase; DE Short=IPP isomerase; GN Name=idi1; ORFNames=SPBC106.15; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=95263448; PubMed=7744766; DOI=10.1074/jbc.270.19.11298; RA Hahn F.M., Poulter C.D.; RT "Isolation of Schizosaccharomyces pombe isopentenyl diphosphate RT isomerase cDNA clones by complementation and synthesis of the enzyme RT in Escherichia coli."; RL J. Biol. Chem. 270:11298-11303(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; 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., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- FUNCTION: Catalyzes the 1,3-allylic rearrangement of the CC homoallylic substrate isopentenyl (IPP) to its highly CC electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). CC -!- CATALYTIC ACTIVITY: Isopentenyl diphosphate = dimethylallyl CC diphosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl-PP biosynthesis; CC dimethylallyl-PP from isopentenyl-PP: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the IPP isomerase type 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U21154; AAA80596.1; -; mRNA. DR EMBL; CU329671; CAB53731.1; -; Genomic_DNA. DR PIR; A56442; A56442. DR RefSeq; NP_595164.1; -. DR GeneID; 2540174; -. DR KEGG; spo:SPBC106.15; -. DR NMPDR; fig|4896.1.peg.1030; -. DR GeneDB_Spombe; SPBC106.15; -. DR OMA; Q10132; NYELGIP. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-003261-MON; -. DR BRENDA; 5.3.3.2; 653. DR ArrayExpress; Q10132; -. DR GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe. DR GO; GO:0005634; C:nucleus; IDA:GeneDB_SPombe. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase act...; IEA:EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR011876; IsopentenylPP_isomerase_typ1. DR InterPro; IPR000086; NUDIX_hydrolase_core. DR Gene3D; G3DSA:3.90.79.10; NUDIX_hydrolase; 1. DR PANTHER; PTHR10885; IPP_isom_1; 1. DR Pfam; PF00293; NUDIX; 1. DR PIRSF; PIRSF018427; Isopntndiph_ism; 1. DR ProDom; PD004109; IPP_isomerase; 1. DR TIGRFAMs; TIGR02150; IPP_isom_1; 1. PE 2: Evidence at transcript level; KW Carotenoid biosynthesis; Cholesterol biosynthesis; Complete proteome; KW Cytoplasm; Isomerase; Isoprene biosynthesis; Lipid synthesis; KW Magnesium; Metal-binding; Steroid biosynthesis; Sterol biosynthesis. FT CHAIN 1 227 Isopentenyl-diphosphate Delta-isomerase. FT /FTId=PRO_0000205230. FT ACT_SITE 87 87 By similarity. FT ACT_SITE 152 152 By similarity. FT METAL 41 41 Magnesium (By similarity). FT METAL 52 52 Magnesium (By similarity). FT METAL 150 150 Magnesium (By similarity). FT METAL 152 152 Magnesium (By similarity). FT BINDING 37 37 Substrate (By similarity). FT BINDING 71 71 Substrate (By similarity). FT BINDING 75 75 Substrate (By similarity). FT BINDING 88 88 Substrate (By similarity). SQ SEQUENCE 227 AA; 26864 MW; A811B5CA2C9AA834 CRC64; MSSQQEKKDY DEEQLRLMEE VCIVVDENDV PLRYGTKKEC HLMENINKGL LHRAFSMFIF DEQNRLLLQQ RAEEKITFPS LWTNTCCSHP LDVAGERGNT LPEAVEGVKN AAQRKLFHEL GIQAKYIPKD KFQFLTRIHY LAPSTGAWGE HEIDYILFFK GKVELDINPN EVQAYKYVTM EELKEMFSDP QYGFTPWFKL ICEHFMFKWW QDVDHASKFQ DTLIHRC //