ERG20_SCHPO
ID ERG20_SCHPO Reviewed; 347 AA.
AC O14230; P78756;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Farnesyl pyrophosphate synthase {ECO:0000303|PubMed:17596513};
DE Short=FPP synthase {ECO:0000303|PubMed:17596513};
DE Short=FPS {ECO:0000303|PubMed:17596513};
DE EC=2.5.1.10 {ECO:0000305|PubMed:17596513};
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase {ECO:0000303|PubMed:17596513};
DE AltName: Full=Dimethylallyltranstransferase {ECO:0000303|PubMed:17596513};
DE EC=2.5.1.1 {ECO:0000305|PubMed:17596513};
DE AltName: Full=Farnesyl diphosphate synthase {ECO:0000303|PubMed:17596513};
DE AltName: Full=Geranyltranstransferase {ECO:0000303|PubMed:17596513};
GN Name=fps1 {ECO:0000303|PubMed:17596513}; ORFNames=SPAC6F12.13c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-347.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP FUNCTION, INTERACTION WITH SPO9, MUTAGENESIS OF PHE-90 AND ARG-104, AND
RP PATHWAY.
RX PubMed=17596513; DOI=10.1091/mbc.e07-02-0112;
RA Ye Y., Fujii M., Hirata A., Kawamukai M., Shimoda C., Nakamura T.;
RT "Geranylgeranyl diphosphate synthase in fission yeast is a heteromer of
RT farnesyl diphosphate synthase (FPS), Fps1, and an FPS-like protein, Spo9,
RT essential for sporulation.";
RL Mol. Biol. Cell 18:3568-3581(2007).
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:17596513). Fps1 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:17596513). 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 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 fps1 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 (Probable). {ECO:0000269|PubMed:17596513, ECO:0000305}.
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:0000305|PubMed:17596513};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22409;
CC Evidence={ECO:0000305|PubMed:17596513};
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:0000305|PubMed:17596513};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19362;
CC Evidence={ECO:0000305|PubMed:17596513};
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:0000305|PubMed:17596513}.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC diphosphate: step 1/1. {ECO:0000305|PubMed:17596513}.
CC -!- SUBUNIT: Interacts with spo9. {ECO:0000269|PubMed:17596513}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11097.1; -; Genomic_DNA.
DR EMBL; D89104; BAA13767.1; -; mRNA.
DR PIR; T11664; T11664.
DR PIR; T42081; T42081.
DR RefSeq; NP_593299.1; NM_001018729.2.
DR AlphaFoldDB; O14230; -.
DR SMR; O14230; -.
DR BioGRID; 279342; 5.
DR STRING; 4896.SPAC6F12.13c.1; -.
DR MaxQB; O14230; -.
DR PaxDb; O14230; -.
DR PRIDE; O14230; -.
DR EnsemblFungi; SPAC6F12.13c.1; SPAC6F12.13c.1:pep; SPAC6F12.13c.
DR GeneID; 2542898; -.
DR KEGG; spo:SPAC6F12.13c; -.
DR PomBase; SPAC6F12.13c; fps1.
DR VEuPathDB; FungiDB:SPAC6F12.13c; -.
DR eggNOG; KOG0711; Eukaryota.
DR HOGENOM; CLU_028376_1_0_1; -.
DR InParanoid; O14230; -.
DR OMA; DENYGQK; -.
DR PhylomeDB; O14230; -.
DR Reactome; R-SPO-191273; Cholesterol biosynthesis.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR PRO; PR:O14230; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; ISO:PomBase.
DR GO; GO:0004337; F:geranyltranstransferase activity; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006696; P:ergosterol biosynthetic process; ISO:PomBase.
DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IC:PomBase.
DR GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; IC:PomBase.
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 1: Evidence at protein level;
KW Cytoplasm; Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Metal-binding; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..347
FT /note="Farnesyl pyrophosphate synthase"
FT /id="PRO_0000123951"
FT BINDING 50
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 53
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 88
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 99
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="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 105
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 192
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 193
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 232
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 249
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 258
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT MUTAGEN 90
FT /note="F->C: Complements lethality of fps1-delete strain."
FT /evidence="ECO:0000269|PubMed:17596513"
FT MUTAGEN 104
FT /note="R->Q: No effect on GGPP synthase activity."
FT /evidence="ECO:0000269|PubMed:17596513"
FT CONFLICT 203
FT /note="A -> E (in Ref. 2; BAA13767)"
FT /evidence="ECO:0000305"
FT CONFLICT 346..347
FT /note="NK -> ISKFLVLCF (in Ref. 2; BAA13767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 39516 MW; 483029A5FC15B9F5 CRC64;
MSAVDKRAKF ESALPVFVDE IVNYLKTINI PDDVTEWYKN SLFHNTLGGK YNRGLSVIDS
YEILLGHPLD EAAYMKAAVL GWMVELLQSF FLIADDIMDA SKTRRGQPCW YLMPGVGNIA
INDAFMVESA IYFLLKKHFR QESCYVDLIE LFHDVTFQTE LGQQLDLLTA PEDSVDLSKF
SLQKHSFIVI YKTAFYSFYL PVALAMHLAG VATPENLKCA QDILIILGKY FQVQDDYLDC
YGDPTVTGKI GTDILDNKCS WIINLALAKC TPEQRVILDD NYGRKDSESE KRVKAVFEEL
NIRGEFENYE ESEVSEIKKL IDGVDESTGL KKSIFTTFLG KIYKRNK
