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FPPS_MAIZE
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   03-AUG-2022, entry version 118.
DE   RecName: Full=Farnesyl pyrophosphate synthase;
DE            Short=FPP synthase;
DE            Short=FPS;
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   Name=FPS;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Wisconsin 64A; TISSUE=Endosperm;
RX   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 the
CC       ultimate product farnesyl pyrophosphate.
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   -!- 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}.
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DR   EMBL; L39789; AAB39276.1; -; mRNA.
DR   PIR; T03291; T03291.
DR   RefSeq; NP_001105039.1; NM_001111569.1.
DR   AlphaFoldDB; P49353; -.
DR   SMR; P49353; -.
DR   STRING; 4577.GRMZM2G168681_P01; -.
DR   PaxDb; P49353; -.
DR   PRIDE; P49353; -.
DR   EnsemblPlants; Zm00001eb342550_T002; Zm00001eb342550_P002; Zm00001eb342550.
DR   GeneID; 541903; -.
DR   Gramene; Zm00001eb342550_T002; Zm00001eb342550_P002; Zm00001eb342550.
DR   KEGG; zma:541903; -.
DR   MaizeGDB; 86802; -.
DR   eggNOG; KOG0711; Eukaryota.
DR   HOGENOM; CLU_028376_3_0_1; -.
DR   OrthoDB; 1066656at2759; -.
DR   UniPathway; UPA00259; UER00368.
DR   UniPathway; UPA00260; UER00369.
DR   Proteomes; UP000007305; Chromosome 8.
DR   ExpressionAtlas; P49353; baseline and differential.
DR   Genevisible; P49353; ZM.
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   CDD; cd00685; Trans_IPPS_HT; 1.
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.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE   2: Evidence at transcript level;
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..350
FT                   /note="Farnesyl pyrophosphate synthase"
FT                   /id="PRO_0000123958"
FT   BINDING         55
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         58
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         94
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         101
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         101
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         105
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         105
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         110
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         198
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         263
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
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
 
 
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