ID FPPS1_LUPAL Reviewed; 342 AA. AC P49351; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 04-NOV-2026, entry version 98. DE RecName: Full=Farnesyl pyrophosphate synthase 1; DE Short=FPP synthase 1; DE Short=FPS 1; DE EC=2.5.1.10; DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase 1; DE AltName: Full=Dimethylallyltranstransferase 1; DE EC=2.5.1.1; DE AltName: Full=Farnesyl diphosphate synthase 1; DE AltName: Full=Geranyltranstransferase 1; GN Name=FPS1; OS Lupinus albus (White lupine) (Lupinus termis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC genistoids sensu lato; core genistoids; Genisteae; Lupinus. OX NCBI_TaxID=3870; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Root; RX PubMed=7646076; DOI=10.1006/abbi.1995.1422; RA Attucci S., Aitken S.M., Gulick P.J., Ibrahim R.K.; RT "Farnesyl pyrophosphate synthase from white lupin: molecular cloning, RT expression, and purification of the expressed protein."; RL Arch. Biochem. Biophys. 321:493-500(1995). CC -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl CC pyrophosphate with the allylic pyrophosphates, dimethylallyl CC pyrophosphate, and then with the resultant geranylpyrophosphate to the CC ultimate product farnesyl pyrophosphate. CC -!- CATALYTIC ACTIVITY: CC Reaction=isopentenyl diphosphate + dimethylallyl 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=isopentenyl diphosphate + (2E)-geranyl 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 -!- 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:0000250}. CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U15777; AAA86687.1; -; mRNA. DR PIR; S66470; S66470. DR SMR; P49351; -. DR OrthoDB; 10257492at2759; -. DR UniPathway; UPA00259; UER00368. DR UniPathway; UPA00260; UER00369. DR CDD; cd00685; Trans_IPPS_HT; 1. DR FunFam; 1.10.600.10:FF:000008; Farnesyl pyrophosphate synthase; 1. DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 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:SF0; FARNESYL PYROPHOSPHATE SYNTHASE; 1. DR PANTHER; PTHR11525; FARNESYL-PYROPHOSPHATE SYNTHETASE; 1. DR Pfam; PF00348; polyprenyl_synt; 1. DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1. DR SFLD; SFLDG01017; Polyprenyl_Transferase_Like; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004337; F:(2E,6E)-farnesyl diphosphate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC. DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0045337; P:trans, trans-farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR AlphaFoldDB; P49351; -. PE 2: Evidence at transcript level; KW Cholesterol biosynthesis; Cholesterol metabolism; Cytoplasm; KW Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism; Magnesium; KW Metal-binding; Steroid biosynthesis; Steroid metabolism; KW Sterol biosynthesis; Sterol metabolism; Transferase. FT CHAIN 1..342 FT /note="Farnesyl pyrophosphate synthase 1" FT /id="PRO_0000123956" FT BINDING 47 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 50 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 86 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 93 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 93 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 97 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 97 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 102 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT BINDING 103 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 190 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT BINDING 191 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT BINDING 229 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT BINDING 246 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT BINDING 255 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" SQ SEQUENCE 342 AA; 39269 MW; 591DE4CD29CC711C CRC64; MADLRSTFLN VYSVLKSELL HDPAFEFSPD SRQWLDRMLD YNVPGGKLNR GLSVIDSYRL LKDGHELNDD EIFLASALGW CIEWLQAYFL VLDDIMDNSH TRRGQPCWFR VPKVGMIAAN DGVLLRNHIP RILKKHFRGK PYYADLLDLF NEVEFQTASG QMIDLITTLE GEKDLSKYTL SLHRRIVQYK TAYYSFYLPV ACALLMVGEN LDNHIDVKNI LVDMGTYFQV QDDYLDCFGA PETIGKIGTD IEDFKCSWLV VKALELSNDE QKKVLYDNYG KPDPANVAKV KALYDELNLQ GVFTEYESKS YEKLVTSIEA HPSKAVQALL KSFLGKIYKR QK //