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Y8742_DICDI
ID   Y8742_DICDI             Reviewed;         393 AA.
AC   Q55EU7;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Probable farnesyl diphosphate synthase DDB_G0268742;
DE            EC=2.5.1.10;
DE   AltName: Full=(2E,6E)-farnesyl diphosphate synthase;
DE   AltName: Full=Dimethylallyltranstransferase;
DE            EC=2.5.1.1;
DE   AltName: Full=Farnesyl diphosphate synthase;
DE   AltName: Full=Geranyltranstransferase;
GN   ORFNames=DDB_G0268742;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
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: Key enzyme in isoprenoid biosynthesis which catalyzes the
CC       formation of farnesyl diphosphate (FPP), a sterol precursor.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-
CC         geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057,
CC         ChEBI:CHEBI:128769; EC=2.5.1.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-
CC         farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC         ChEBI:CHEBI:175763; EC=2.5.1.10;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by aminobisphosphonate drugs (aBP), such
CC       as risedronate and alendronate. {ECO:0000250}.
CC   -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC       farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC       diphosphate: step 1/1.
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC       geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC       diphosphate: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; AAFI02000004; EAL72960.1; -; Genomic_DNA.
DR   RefSeq; XP_646923.1; XM_641831.1.
DR   AlphaFoldDB; Q55EU7; -.
DR   SMR; Q55EU7; -.
DR   STRING; 44689.DDB0190001; -.
DR   PaxDb; Q55EU7; -.
DR   EnsemblProtists; EAL72960; EAL72960; DDB_G0268742.
DR   GeneID; 8616611; -.
DR   KEGG; ddi:DDB_G0268742; -.
DR   dictyBase; DDB_G0268742; -.
DR   eggNOG; KOG0711; Eukaryota.
DR   HOGENOM; CLU_028376_0_1_1; -.
DR   InParanoid; Q55EU7; -.
DR   OMA; DIMDNGL; -.
DR   PhylomeDB; Q55EU7; -.
DR   UniPathway; UPA00259; UER00368.
DR   UniPathway; UPA00260; UER00369.
DR   PRO; PR:Q55EU7; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IBA:GO_Central.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IBA:GO_Central.
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:0045337; P:farnesyl diphosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR039702; FPS1-like.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
DR   PANTHER; PTHR11525; PTHR11525; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
PE   3: Inferred from homology;
KW   Cholesterol biosynthesis; Cholesterol metabolism; Cytoplasm;
KW   Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW   Metal-binding; Reference proteome; Steroid biosynthesis;
KW   Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase.
FT   CHAIN           1..393
FT                   /note="Probable farnesyl diphosphate synthase DDB_G0268742"
FT                   /id="PRO_0000388256"
FT   BINDING         57
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         60
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         114
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         114
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         123
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         219
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         304
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   393 AA;  45935 MW;  89CCEF89AD1FFCEF CRC64;
     MGSHYKIDLE NEREEFIKVY SILKNDVFDE LPKMKLASNA IDYIKELLNS PTITGGKMYR
     GLGFLYSLNT LLIAKNNFDN NNNNNNNKNS ETSQHEARII GWCLEFLSFF LITDDIMDNG
     LTRRGELCWY RHPSPFNPTE HKVGMLAIND SVLIESFLFF ILKKYFKNKS YYVDLFELFH
     ESIFYTATGQ LLDSSSFHLK RGDFTNFTFE NYSQICINKS SHHVFYLQIK IAILLTDIMD
     NNEKQKDDTT CKEEKDKEKE QEEELIKNIC FNLGIYGQAQ DDYFDCFGDP KVIGKTGTDI
     QENKCSWLIC KANTICNNDQ LNQLKKNYGN DNENDVSIVK SIFKEINIPK HYENFENEQY
     NSILKEIQKL SIISLPKSEI LLFLLKKLFK RSK
 
 
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