O14230 (FPPS_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Farnesyl pyrophosphate synthase
Short name=FPP synthase
Short name=FPS
EC=2.5.1.10

Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase
Dimethylallyltranstransferase
EC=2.5.1.1
Farnesyl diphosphate synthase
Geranyltranstransferase

Gene names

Name:	fps1
ORF Names:	SPAC6F12.13c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	347 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Ref.4
Catalytic activity	Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate. Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-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.
Subunit structure	Interacts with spo9. Ref.4
Subcellular location	Cytoplasm. Nucleus Ref.3.
Sequence similarities	Belongs to the FPP/GGPP synthase family.

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Isoprene biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW ergosterol biosynthetic process Inferred from genetic interaction. Source: GeneDB_Spombe farnesyl diphosphate biosynthetic process Inferred from genetic interaction. Source: GeneDB_Spombe negative regulation of G0 to G1 transition Inferred from mutant phenotype. Source: GeneDB_Spombe protein prenylation Inferred by curator. Source: GeneDB_Spombe protein targeting to membrane Inferred by curator. Source: GeneDB_Spombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_Spombe nucleus Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	dimethylallyltranstransferase activity Inferred from genetic interaction. Source: GeneDB_Spombe geranyltranstransferase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 347	347	Farnesyl pyrophosphate synthase		PRO_0000123951
Sites
	Metal binding	95	1	Magnesium 1 By similarity
	Metal binding	95	1	Magnesium 2 By similarity
	Metal binding	99	1	Magnesium 1 By similarity
	Metal binding	99	1	Magnesium 2 By similarity
	Metal binding	235	1	Magnesium 3 By similarity
	Binding site	50	1	Isopentenyl diphosphate By similarity
	Binding site	53	1	Isopentenyl diphosphate By similarity
	Binding site	88	1	Isopentenyl diphosphate By similarity
	Binding site	104	1	Dimethylallyl diphosphate By similarity
	Binding site	105	1	Isopentenyl diphosphate By similarity
	Binding site	192	1	Dimethylallyl diphosphate By similarity
	Binding site	193	1	Dimethylallyl diphosphate By similarity
	Binding site	232	1	Dimethylallyl diphosphate By similarity
	Binding site	249	1	Dimethylallyl diphosphate By similarity
	Binding site	258	1	Dimethylallyl diphosphate By similarity
Experimental info
	Mutagenesis	90	1	F → C: Complements lethality of fps1-delete strain. Ref.4
	Mutagenesis	104	1	R → Q: No affect on GGPP synthase activity. Ref.4
	Sequence conflict	203	1	A → E in BAA13767. Ref.2
	Sequence conflict	346 – 347	2	NK → ISKFLVLCF in BAA13767. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O14230 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 483029A5FC15B9F5	FASTA	347	39,516
	10 20 30 40 50 60 MSAVDKRAKF ESALPVFVDE IVNYLKTINI PDDVTEWYKN SLFHNTLGGK YNRGLSVIDS 70 80 90 100 110 120 YEILLGHPLD EAAYMKAAVL GWMVELLQSF FLIADDIMDA SKTRRGQPCW YLMPGVGNIA 130 140 150 160 170 180 INDAFMVESA IYFLLKKHFR QESCYVDLIE LFHDVTFQTE LGQQLDLLTA PEDSVDLSKF 190 200 210 220 230 240 SLQKHSFIVI YKTAFYSFYL PVALAMHLAG VATPENLKCA QDILIILGKY FQVQDDYLDC 250 260 270 280 290 300 YGDPTVTGKI GTDILDNKCS WIINLALAKC TPEQRVILDD NYGRKDSESE KRVKAVFEEL 310 320 330 340 NIRGEFENYE ESEVSEIKKL IDGVDESTGL KKSIFTTFLG KIYKRNK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed: 9501991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-347. Strain: PR745.
[3]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]	"Geranylgeranyl diphosphate synthase in fission yeast is a heteromer of farnesyl diphosphate synthase (FPS), Fps1, and an FPS-like protein, Spo9, essential for sporulation." Ye Y., Fujii M., Hirata A., Kawamukai M., Shimoda C., Nakamura T. Mol. Biol. Cell 18:3568-3581(2007) [PubMed: 17596513] [Abstract] Cited for: FUNCTION, INTERACTION WITH SPO9, MUTAGENESIS OF PHE-90 AND ARG-104.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB11097.1. D89104 mRNA. Translation: BAA13767.1.
PIR	T11664. T42081.
RefSeq	NP_593299.1. NM_001018729.1.
3D structure databases
ProteinModelPortal	O14230.
ModBase	Search...
Protein-protein interaction databases
STRING	O14230.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC6F12.13c.1; SPAC6F12.13c.1:pep; SPAC6F12.13c.
GeneID	2542898.
GenomeReviews	Gene locus fps1 in contig CU329670_GR.
KEGG	spo:SPAC6F12.13c.
NMPDR	fig|4896.1.peg.3269.
Organism-specific databases
GeneDB_Spombe	SPAC6F12.13c.
Phylogenomic databases
eggNOG	fuNOG05213.
GeneTree	EFGT00050000002300.
HOGENOM	HBG328346.
OMA	RDFMAVF.
OrthoDB	EOG4SFDFW.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000998-MONOMER.
Gene expression databases
ArrayExpress	O14230.
Family and domain databases
InterPro	IPR000092. Polyprenyl_synt. IPR008949. Terpenoid_synth. [Graphical view]
Gene3D	G3DSA:1.10.600.10. Terpenoid_synth. 1 hit.
KO	K00787.
Pfam	PF00348. polyprenyl_synt. 1 hit. [Graphical view]
SUPFAM	SSF48576. Terpenoid_synth. 1 hit.
PROSITE	PS00723. POLYPRENYL_SYNTHASE_1. 1 hit. PS00444. POLYPRENYL_SYNTHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FPPS_SCHPO

Accession

Primary (citable) accession number: O14230
Secondary accession number(s): P78756

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	December 14, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program