ID FPPS_MAIZE Reviewed; 350 AA. AC P49353; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 16-JUN-2009, entry version 54. DE RecName: Full=Farnesyl pyrophosphate synthetase; DE Short=FPP synthetase; DE Short=FPS; DE AltName: Full=Farnesyl diphosphate synthetase; DE Includes: DE RecName: Full=Dimethylallyltranstransferase; DE EC=2.5.1.1; DE Includes: DE RecName: Full=Geranyltranstransferase; DE EC=2.5.1.10; GN Name=FPS; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Wisconsin 64A; TISSUE=Endosperm; RX MEDLINE=96257218; PubMed=8666271; DOI=10.1016/0378-1119(95)00880-2; RA Li C.P., Larkins B.A.; RT "Identification of a maize endosperm-specific cDNA encoding farnesyl RT pyrophosphate synthetase."; RL Gene 171:193-196(1996). CC -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl CC pyrophosphate with the allylic pyrophosphates, dimethylallyl CC pyrophosphate, and then with the resultant geranylpyrophosphate to CC the ultimate product farnesyl pyrophosphate. CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl CC diphosphate = diphosphate + geranyl diphosphate. CC -!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate CC = diphosphate + trans,trans-farnesyl diphosphate. CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl-PP biosynthesis; CC farnesyl-PP from geranyl-PP and isopentenyl-PP: step 1/1. CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl-PP biosynthesis; CC geranyl-PP from dimethylallyl-PP and isopentenyl-PP: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the FPP/GGPP synthetase 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; L39789; AAB39276.1; -; mRNA. DR PIR; T03291; T03291. DR RefSeq; NP_001105039.1; -. DR UniGene; Zm.95609; -. DR HSSP; P08836; 1UBX. DR GeneID; 541903; -. DR Gramene; P49353; -. DR MaizeGDB; 86802; -. DR BRENDA; 2.5.1.1; 289. DR BRENDA; 2.5.1.10; 289. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:EC. DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:EC. DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR000092; Polyprenyl_synt. DR InterPro; IPR008949; Terpenoid_synth. DR Gene3D; G3DSA:1.10.600.10; Terpenoid_synth; 1. DR Pfam; PF00348; polyprenyl_synt; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHET_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHET_2; 1. PE 2: Evidence at transcript level; KW Cholesterol biosynthesis; Cytoplasm; Isoprene biosynthesis; KW Lipid synthesis; Steroid biosynthesis; Sterol biosynthesis; KW Transferase. FT CHAIN 1 350 Farnesyl pyrophosphate synthetase. FT /FTId=PRO_0000123958. SQ SEQUENCE 350 AA; 40014 MW; A606790FE79FC6C5 CRC64; MAAGGNGAGG DTRAAFARIY KTLKEELLTD PAFEFTEESR QWIDRMVDYN VLGGKCNRGL SVVDSYKLLK GADALGEEET FLACTLGWCI EWLQAFFLVL DDIMDDSHTR RGQPCWFRVP QVGLIAANDG IILRNHISRI LRRHFKGKPY YADLLDLFNE VEFKTASGQL LDLITTHEGE KDLTKYNITV HGRIVQYKTA YYSFYLPVAC ALLLSGENLD NYGDVENILV EMGTYFQVQD DYLDCYGDPE FIGKIGTDIE DYKCSWLVVQ ALERADESQK RILFENYGKK DPACVAKVKN LYKELDLEAV FQEYENESYK KLIADIEAQP SIAVQKVLKS FLHKIYKRQK //