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Farnesyl pyrophosphate synthase (FPP synthase) (FPS) (EC 2.5.1.10) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Geranyltranstransferase)

 FPPS_KLULA              Reviewed;         349 AA.
P49349;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
28-MAR-2018, entry version 114.
RecName: Full=Farnesyl pyrophosphate synthase;
Short=FPP synthase;
Short=FPS;
EC=2.5.1.10;
AltName: Full=(2E,6E)-farnesyl diphosphate synthase;
AltName: Full=Dimethylallyltranstransferase;
EC=2.5.1.1;
AltName: Full=Farnesyl diphosphate synthase;
AltName: Full=Geranyltranstransferase;
Name=FPS1; Synonyms=FPS; OrderedLocusNames=KLLA0A06732g;
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC
1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
NCBI_TaxID=284590;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
WM37;
PubMed=7948032; DOI=10.1016/0167-4781(94)90234-8;
Mulder W., Scholten I.H.J.M., Nagelkerken B., Grivell L.A.;
"Isolation and characterisation of the linked genes, FPS1 and QCR8,
coding for farnesyl-diphosphate synthase and the 11 kDa subunit VIII
of the mitochondrial bc1-complex in the yeast Kluyveromyces lactis.";
Biochim. Biophys. Acta 1219:713-718(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
WM37;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
-!- FUNCTION: Catalyzes the sequential condensation of isopentenyl
pyrophosphate with the allylic pyrophosphates, dimethylallyl
pyrophosphate, and then with the resultant geranylpyrophosphate to
the ultimate product farnesyl pyrophosphate.
-!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl
diphosphate = diphosphate + geranyl diphosphate.
-!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate
= diphosphate + (2E,6E)-farnesyl diphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
-!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate
biosynthesis; farnesyl diphosphate from geranyl diphosphate and
isopentenyl diphosphate: step 1/1.
-!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate
biosynthesis; geranyl diphosphate from dimethylallyl diphosphate
and isopentenyl diphosphate: step 1/1.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
{ECO:0000305}.
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EMBL; X76026; CAA53614.1; -; Genomic_DNA.
EMBL; CR382121; CAH02888.1; -; Genomic_DNA.
PIR; S50214; S50214.
RefSeq; XP_451300.1; XM_451300.1.
ProteinModelPortal; P49349; -.
SMR; P49349; -.
STRING; 284590.XP_451300.1; -.
PRIDE; P49349; -.
EnsemblFungi; CAH02888; CAH02888; KLLA0_A06732g.
GeneID; 2896751; -.
KEGG; kla:KLLA0A06732g; -.
eggNOG; KOG0711; Eukaryota.
eggNOG; COG0142; LUCA.
HOGENOM; HOG000160912; -.
InParanoid; P49349; -.
KO; K00787; -.
OMA; ITAPEDH; -.
OrthoDB; EOG092C35ZD; -.
UniPathway; UPA00259; UER00368.
UniPathway; UPA00260; UER00369.
Proteomes; UP000000598; Chromosome A.
GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblFungi.
GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006696; P:ergosterol biosynthetic process; IEA:EnsemblFungi.
GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 1.10.600.10; -; 1.
InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
InterPro; IPR000092; Polyprenyl_synt.
InterPro; IPR033749; Polyprenyl_synt_CS.
Pfam; PF00348; polyprenyl_synt; 1.
SUPFAM; SSF48576; SSF48576; 1.
PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
3: Inferred from homology;
Complete proteome; Cytoplasm; Isoprene biosynthesis;
Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
Reference proteome; Transferase.
CHAIN 1 349 Farnesyl pyrophosphate synthase.
/FTId=PRO_0000123949.
METAL 97 97 Magnesium 1. {ECO:0000250}.
METAL 97 97 Magnesium 2. {ECO:0000250}.
METAL 101 101 Magnesium 1. {ECO:0000250}.
METAL 101 101 Magnesium 2. {ECO:0000250}.
METAL 237 237 Magnesium 3. {ECO:0000250}.
BINDING 48 48 Isopentenyl diphosphate. {ECO:0000250}.
BINDING 51 51 Isopentenyl diphosphate. {ECO:0000250}.
BINDING 90 90 Isopentenyl diphosphate. {ECO:0000250}.
BINDING 106 106 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 107 107 Isopentenyl diphosphate. {ECO:0000250}.
BINDING 194 194 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 195 195 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 234 234 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 251 251 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 260 260 Dimethylallyl diphosphate. {ECO:0000250}.
SEQUENCE 349 AA; 40157 MW; 290557C17FAACDCE CRC64;
MSDNRAQFLE VFPSLVQELR DILAGYGMPE EAIEWYEKSL NYNTPGGKLN RGLSVVDTYA
LLKGYKSVSE LSAEEYKKVA ILGWCIELLQ AYFLVADDMM DQSITRRGQP CWYKVENVGD
IAINDAFMLE GAIYCLLKKH FRTEPYYVDL LELFHDVTFQ TELGQLLDLI TAPEDKVDLS
KFSLEKHSFI VIFKTAYYSF YLAVALAMFA AGITDSKDLK QASDVLIPLG EYFQIQDDFL
DCFGKPEDIG KIGTDIQDNK CSWVINVALK NATKEQRDIL DENYGRKDSE KEQKCRAVFN
ELNIQDIYHK YEEETASNLR EKIANIDESR GFKAEVLTLF LNKIYHRKK


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