ID   ERG20_YEAST             Reviewed;         352 AA.
AC   P08524; D6VW20; P15495;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=Farnesyl pyrophosphate synthase {ECO:0000303|PubMed:8096487};
DE            Short=FPP synthase {ECO:0000303|PubMed:8096487};
DE            Short=FPS {ECO:0000303|PubMed:8096487};
DE            EC=2.5.1.10 {ECO:0000269|PubMed:8096487};
DE   AltName: Full=(2E,6E)-farnesyl diphosphate synthase {ECO:0000303|PubMed:2681213};
DE   AltName: Full=Dimethylallyltranstransferase {ECO:0000303|PubMed:8096487};
DE            EC=2.5.1.1 {ECO:0000269|PubMed:8096487};
DE   AltName: Full=Farnesyl diphosphate synthase {ECO:0000303|PubMed:8096487};
DE   AltName: Full=Geranyltranstransferase {ECO:0000303|PubMed:8096487};
GN   Name=ERG20; Synonyms=BOT3, FDS1, FPP1; OrderedLocusNames=YJL167W;
GN   ORFNames=J0525;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2681213; DOI=10.1016/s0021-9258(19)47284-0;
RA   Anderson M.S., Yarger J.G., Burck C.L., Poulter C.D.;
RT   "Farnesyl diphosphate synthetase. Molecular cloning, sequence, and
RT   expression of an essential gene from Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 264:19176-19184(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 131-352.
RX   PubMed=3036507; DOI=10.1111/j.1432-1033.1987.tb11455.x;
RA   Maarse A.C., Grivell L.A.;
RT   "Nucleotide sequence of the gene encoding the 11-kDa subunit of the
RT   ubiquinol-cytochrome-c oxidoreductase in Saccharomyces cerevisiae.";
RL   Eur. J. Biochem. 165:419-425(1987).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-197.
RC   STRAIN=LB25;
RX   PubMed=8096487; DOI=10.1016/0378-1119(93)90326-x;
RA   Blanchard L., Karst F.;
RT   "Characterization of a lysine-to-glutamic acid mutation in a conservative
RT   sequence of farnesyl diphosphate synthase from Saccharomyces cerevisiae.";
RL   Gene 125:185-189(1993).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [7]
RP   REVIEW ON ERGOSTEROL BIOSYNTHESIS.
RX   PubMed=32679672; DOI=10.3390/genes11070795;
RA   Jorda T., Puig S.;
RT   "Regulation of ergosterol biosynthesis in Saccharomyces cerevisiae.";
RL   Genes (Basel) 11:0-0(2020).
CC   -!- FUNCTION: Farnesyl pyrophosphate synthase; part of the second module of
CC       ergosterol biosynthesis pathway that includes the middle steps of the
CC       pathway (PubMed:8096487). ERG20 catalyzes the sequential condensation
CC       of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then
CC       with the resultant geranylpyrophosphate to the ultimate product
CC       farnesyl pyrophosphate (PubMed:8096487). The second module is carried
CC       out in the vacuole and involves the formation of farnesyl diphosphate,
CC       which is also an important intermediate in the biosynthesis of
CC       ubiquinone, dolichol, heme and prenylated proteins. Activity by the
CC       mevalonate kinase ERG12 first converts mevalonate into 5-
CC       phosphomevalonate. 5-phosphomevalonate is then further converted to 5-
CC       diphosphomevalonate by the phosphomevalonate kinase ERG8. The
CC       diphosphomevalonate decarboxylase MVD1/ERG19 then produces isopentenyl
CC       diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then
CC       catalyzes the 1,3-allylic rearrangement of the homoallylic substrate
CC       isopentenyl (IPP) to its highly electrophilic allylic isomer,
CC       dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate
CC       synthase ERG20 catalyzes the sequential condensation of isopentenyl
CC       pyrophosphate with dimethylallyl pyrophosphate, and then with the
CC       resultant geranylpyrophosphate to the ultimate product farnesyl
CC       pyrophosphate (PubMed:32679672). {ECO:0000269|PubMed:8096487,
CC       ECO:0000303|PubMed:32679672}.
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         Evidence={ECO:0000269|PubMed:8096487};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22409;
CC         Evidence={ECO:0000269|PubMed:8096487};
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         Evidence={ECO:0000269|PubMed:8096487};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19362;
CC         Evidence={ECO:0000269|PubMed:8096487};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q12051};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};
CC   -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC       farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC       diphosphate: step 1/1. {ECO:0000269|PubMed:8096487}.
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC       geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC       diphosphate: step 1/1. {ECO:0000269|PubMed:8096487}.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; J05091; AAA34606.1; -; Genomic_DNA.
DR   EMBL; Z49442; CAA89462.1; -; Genomic_DNA.
DR   EMBL; X05550; CAA29064.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08636.1; -; Genomic_DNA.
DR   PIR; A34441; A34441.
DR   RefSeq; NP_012368.1; NM_001181600.1.
DR   AlphaFoldDB; P08524; -.
DR   SMR; P08524; -.
DR   BioGRID; 33592; 66.
DR   DIP; DIP-1163N; -.
DR   IntAct; P08524; 9.
DR   STRING; 4932.YJL167W; -.
DR   iPTMnet; P08524; -.
DR   MaxQB; P08524; -.
DR   PaxDb; 4932-YJL167W; -.
DR   PeptideAtlas; P08524; -.
DR   EnsemblFungi; YJL167W_mRNA; YJL167W; YJL167W.
DR   GeneID; 853272; -.
DR   KEGG; sce:YJL167W; -.
DR   AGR; SGD:S000003703; -.
DR   SGD; S000003703; ERG20.
DR   VEuPathDB; FungiDB:YJL167W; -.
DR   eggNOG; KOG0711; Eukaryota.
DR   GeneTree; ENSGT00900000141074; -.
DR   HOGENOM; CLU_028376_1_0_1; -.
DR   InParanoid; P08524; -.
DR   OMA; LEMGNFF; -.
DR   OrthoDB; 509027at2759; -.
DR   BioCyc; MetaCyc:MONOMER-655; -.
DR   BioCyc; YEAST:MONOMER-655; -.
DR   BRENDA; 2.5.1.10; 984.
DR   Reactome; R-SCE-191273; Cholesterol biosynthesis.
DR   UniPathway; UPA00259; UER00368.
DR   UniPathway; UPA00260; UER00369.
DR   BioGRID-ORCS; 853272; 9 hits in 10 CRISPR screens.
DR   PRO; PR:P08524; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P08524; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0005773; C:vacuole; NAS:UniProt.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IDA:SGD.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IDA:SGD.
DR   GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IDA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006696; P:ergosterol biosynthetic process; IDA:UniProt.
DR   GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IDA:SGD.
DR   GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IDA:SGD.
DR   CDD; cd00685; Trans_IPPS_HT; 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.
PE   1: Evidence at protein level;
KW   Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW   Metal-binding; Reference proteome; Transferase.
FT   CHAIN           1..352
FT                   /note="Farnesyl pyrophosphate synthase"
FT                   /id="PRO_0000123952"
FT   BINDING         52
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         55
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         93
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         100
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         100
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         104
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         104
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         109
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         110
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         197
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         198
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         237
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         254
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         263
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   MUTAGEN         197
FT                   /note="K->E: In ERG20-2; 14-fold decrease in FPPS
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:8096487"
SQ   SEQUENCE   352 AA;  40483 MW;  79A357BB7BFCEDDA CRC64;
     MASEKEIRRE RFLNVFPKLV EELNASLLAY GMPKEACDWY AHSLNYNTPG GKLNRGLSVV
     DTYAILSNKT VEQLGQEEYE KVAILGWCIE LLQAYFLVAD DMMDKSITRR GQPCWYKVPE
     VGEIAINDAF MLEAAIYKLL KSHFRNEKYY IDITELFHEV TFQTELGQLM DLITAPEDKV
     DLSKFSLKKH SFIVTFKTAY YSFYLPVALA MYVAGITDEK DLKQARDVLI PLGEYFQIQD
     DYLDCFGTPE QIGKIGTDIQ DNKCSWVINK ALELASAEQR KTLDENYGKK DSVAEAKCKK
     IFNDLKIEQL YHEYEESIAK DLKAKISQVD ESRGFKADVL TAFLNKVYKR SK
//