Reviewed, UniProtKB/Swiss-Prot P49349 (FPPS_KLULA)

Names and origin

Protein names

Recommended name:
    Farnesyl pyrophosphate synthetase
      Short name=FPP synthetase
      Short name=FPS
Alternative name(s):
    Farnesyl diphosphate synthetase
Including the following 2 domains:
    1- Recommended name:
            Dimethylallyltranstransferase
              EC=2.5.1.1
    2- Recommended name:
            Geranyltranstransferase
              EC=2.5.1.10

Gene names

Name:	FPS1
Synonyms:	FPS
Ordered Locus Names:	KLLA0A06732g

Organism

Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

28985 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length	349 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

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. Geranyl diphosphate + isopentenyl diphosphate = diphosphate + trans,trans-farnesyl diphosphate.
Cofactor	Binds 3 magnesium ions per subunit By similarity.
Pathway	Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1. Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the FPP/GGPP synthetase family.

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Isoprene biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dimethylallyltranstransferase activity Inferred from electronic annotation. Source: EC geranyltranstransferase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 349	349	Farnesyl pyrophosphate synthetase		PRO_0000123949
Sites
	Metal binding	97	1	Magnesium 1 By similarity
	Metal binding	97	1	Magnesium 2 By similarity
	Metal binding	101	1	Magnesium 1 By similarity
	Metal binding	101	1	Magnesium 2 By similarity
	Metal binding	237	1	Magnesium 3 By similarity
	Binding site	48	1	Isopentenyl diphosphate By similarity
	Binding site	51	1	Isopentenyl diphosphate By similarity
	Binding site	90	1	Isopentenyl diphosphate By similarity
	Binding site	106	1	Dimethylallyl diphosphate By similarity
	Binding site	107	1	Isopentenyl diphosphate By similarity
	Binding site	194	1	Dimethylallyl diphosphate By similarity
	Binding site	195	1	Dimethylallyl diphosphate By similarity
	Binding site	234	1	Dimethylallyl diphosphate By similarity
	Binding site	251	1	Dimethylallyl diphosphate By similarity
	Binding site	260	1	Dimethylallyl diphosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P49349-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 290557C17FAACDCE	FASTA	349	40,157
	10 20 30 40 50 60 MSDNRAQFLE VFPSLVQELR DILAGYGMPE EAIEWYEKSL NYNTPGGKLN RGLSVVDTYA 70 80 90 100 110 120 LLKGYKSVSE LSAEEYKKVA ILGWCIELLQ AYFLVADDMM DQSITRRGQP CWYKVENVGD 130 140 150 160 170 180 IAINDAFMLE GAIYCLLKKH FRTEPYYVDL LELFHDVTFQ TELGQLLDLI TAPEDKVDLS 190 200 210 220 230 240 KFSLEKHSFI VIFKTAYYSF YLAVALAMFA AGITDSKDLK QASDVLIPLG EYFQIQDDFL 250 260 270 280 290 300 DCFGKPEDIG KIGTDIQDNK CSWVINVALK NATKEQRDIL DENYGRKDSE KEQKCRAVFN 310 320 330 340 ELNIQDIYHK YEEETASNLR EKIANIDESR GFKAEVLTLF LNKIYHRKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Mulder W., Scholten I.H.J.M., Nagelkerken B., Grivell L.A. Biochim. Biophys. Acta 1219:713-718(1994) [PubMed: 7948032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.
[2]	"Genome evolution in yeasts." 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. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X76026 Genomic DNA. Translation: CAA53614.1. CR382121 Genomic DNA. Translation: CAH02888.1.
PIR	S50214.
RefSeq	XP_451300.1.
3D structure databases
SMR	P49349. Positions 2-349.
ModBase	Search...
Protein-protein interaction databases
STRING	P49349.
Genome annotation databases
GeneID	2896751.
GenomeReviews	Gene locus KLLA0A06732g in contig CR382121_GR.
KEGG	kla:KLLA0A06732g.
Phylogenomic databases
eggNOG	fuNOG05213.
HOGENOM	HBG328346.
OMA	MIKTHIQ.
OrthoDB	EOG9D286Q.
PhylomeDB	P49349.
Enzyme and pathway databases
BRENDA	2.5.1.1. 74088. 2.5.1.10. 74088.
Family and domain databases
InterPro	IPR000092. Polyprenyl_synt. IPR008949. Terpenoid_synth. [Graphical view]
Gene3D	G3DSA:1.10.600.10. Terpenoid_synth. 1 hit.
Pfam	PF00348. polyprenyl_synt. 1 hit. [Graphical view]
PROSITE	PS00723. POLYPRENYL_SYNTHET_1. 1 hit. PS00444. POLYPRENYL_SYNTHET_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FPPS_KLULA

Accession

Primary (citable) accession number: P49349

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	January 19, 2010
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)