Reviewed, UniProtKB/Swiss-Prot Q09152 (FPPS1_ARATH)

Names and origin

Protein names

Recommended name:
    Farnesyl pyrophosphate synthetase 1, mitochondrial
      Short name=FPP synthetase 1
      Short name=FPS 1
Alternative name(s):
    Farnesyl diphosphate synthetase 1
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
Ordered Locus Names:	At5g47770
ORF Names:	MCA23.9

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	384 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
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	Mitochondrion. Cytoplasm.
Tissue specificity	The FPS1L mRNA accumulates preferentially in inflorescences, whereas the FPS1S mRNA is predominantly expressed in roots and inflorescences.
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 Mitochondrion
Coding sequence diversity	Alternative initiation
Domain	Transit peptide
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	mitochondrion 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...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform Mitochondrial (identifier: Q09152-1)

Also known as: FPS1L;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Cytoplasmic (identifier: Q09152-2)

Also known as: FPS1S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 384		Farnesyl pyrophosphate synthetase 1, mitochondrial		PRO_0000016469
Sites
	Metal binding	135	1	Magnesium 1 By similarity
	Metal binding	135	1	Magnesium 2 By similarity
	Metal binding	139	1	Magnesium 1 By similarity
	Metal binding	139	1	Magnesium 2 By similarity
	Metal binding	274	1	Magnesium 3 By similarity
	Binding site	89	1	Isopentenyl diphosphate By similarity
	Binding site	92	1	Isopentenyl diphosphate By similarity
	Binding site	128	1	Isopentenyl diphosphate By similarity
	Binding site	144	1	Dimethylallyl diphosphate By similarity
	Binding site	145	1	Isopentenyl diphosphate By similarity
	Binding site	232	1	Dimethylallyl diphosphate By similarity
	Binding site	233	1	Dimethylallyl diphosphate By similarity
	Binding site	271	1	Dimethylallyl diphosphate By similarity
	Binding site	288	1	Dimethylallyl diphosphate By similarity
	Binding site	297	1	Dimethylallyl diphosphate By similarity
Natural variations
	Alternative sequence	1 – 41	41	Missing in isoform Cytoplasmic.		VSP_018808
Experimental info
	Sequence conflict	218	1	A → S in CAA53433. Ref.4
	Sequence conflict	231	1	Y → H in CAA53433. Ref.4
	Sequence conflict	324	1	P → T in CAA53433. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Mitochondrial (FPS1L) [UniParc]. Last modified June 6, 2002. Version 2. Checksum: E6808489D07D4F29	FASTA	384	44,261
	10 20 30 40 50 60 MSVSCCCRNL GKTIKKAIPS HHLHLRSLGG SLYRRRIQSS SMETDLKSTF LNVYSVLKSD 70 80 90 100 110 120 LLHDPSFEFT NESRLWVDRM LDYNVRGGKL NRGLSVVDSF KLLKQGNDLT EQEVFLSCAL 130 140 150 160 170 180 GWCIEWLQAY FLVLDDIMDN SVTRRGQPCW FRVPQVGMVA INDGILLRNH IHRILKKHFR 190 200 210 220 230 240 DKPYYVDLVD LFNEVELQTA CGQMIDLITT FEGEKDLAKY SLSIHRRIVQ YKTAYYSFYL 250 260 270 280 290 300 PVACALLMAG ENLENHIDVK NVLVDMGIYF QVQDDYLDCF ADPETLGKIG TDIEDFKCSW 310 320 330 340 350 360 LVVKALERCS EEQTKILYEN YGKPDPSNVA KVKDLYKELD LEGVFMEYES KSYEKLTGAI 370 380 EGHQSKAIQA VLKSFLAKIY KRQK
	Isoform Cytoplasmic (FPS1S). Checksum: 048B6CC7519A7476	FASTA	343	39,697
	10 20 30 40 50 60 METDLKSTFL NVYSVLKSDL LHDPSFEFTN ESRLWVDRML DYNVRGGKLN RGLSVVDSFK 70 80 90 100 110 120 LLKQGNDLTE QEVFLSCALG WCIEWLQAYF LVLDDIMDNS VTRRGQPCWF RVPQVGMVAI 130 140 150 160 170 180 NDGILLRNHI HRILKKHFRD KPYYVDLVDL FNEVELQTAC GQMIDLITTF EGEKDLAKYS 190 200 210 220 230 240 LSIHRRIVQY KTAYYSFYLP VACALLMAGE NLENHIDVKN VLVDMGIYFQ VQDDYLDCFA 250 260 270 280 290 300 DPETLGKIGT DIEDFKCSWL VVKALERCSE EQTKILYENY GKPDPSNVAK VKDLYKELDL 310 320 330 340 EGVFMEYESK SYEKLTGAIE GHQSKAIQAV LKSFLAKIYK RQK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Arabidopsis thaliana FPS1 gene generates a novel mRNA that encodes a mitochondrial farnesyl-diphosphate synthase isoform." Cunillera N., Boronat A., Ferrer A. J. Biol. Chem. 272:15381-15388(1997) [PubMed: 9182568] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE INITIATION. Strain: cv. Columbia.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence features of the regions of 1,081,958 bp covered by seventeen physically assigned P1 and TAC clones." Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N., Tabata S. DNA Res. 5:379-391(1998) [PubMed: 10048488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Cloning of an Arabidopsis thaliana cDNA coding for farnesyl diphosphate synthase by functional complementation in yeast." Delourme D., Lacroute F., Karst F. Plant Mol. Biol. 26:1867-1873(1994) [PubMed: 7858223] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-384. Strain: cv. Landsberg erecta.
[5]	"Arabidopsis thaliana contains two differentially expressed farnesyl-diphosphate synthase genes." Cunillera N., Arro M., Delourme D., Karst F., Boronat A., Ferrer A. J. Biol. Chem. 271:7774-7780(1996) [PubMed: 8631820] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 42-384. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U80605 mRNA. Translation: AAB49290.1. L46367 Genomic DNA. Translation: AAF44787.1. L46367 Genomic DNA. Translation: AAB07264.1. AB016886 Genomic DNA. Translation: BAB11324.1. AF370324 mRNA. Translation: AAK44139.1. AY063112 mRNA. Translation: AAL34286.1. X75789 mRNA. Translation: CAA53433.1.
IPI	IPI00548843. IPI00760338.
PIR	S52009.
RefSeq	NP_199588.1.
UniGene	At.21206 Rra.3843
3D structure databases
SMR	Q09152. Positions 47-380.
ModBase	Search...
Protein-protein interaction databases
STRING	Q09152.
Proteomic databases
PRIDE	Q09152.
Genome annotation databases
GeneID	834828.
GenomeReviews	Gene locus AT5G47770 in contig BA000015_GR.
KEGG	ath:AT5G47770.
NMPDR	fig|3702.1.peg.26592.
Organism-specific databases
TAIR	At5g47770.
Phylogenomic databases
eggNOG	KOG0711.
HOGENOM	HBG328346.
InParanoid	Q09152.
OMA	MIKTHIQ.
PhylomeDB	Q09152.
Enzyme and pathway databases
BioCyc	MetaCyc:AT5G47770-MONOMER.
BRENDA	2.5.1.1. 302. 2.5.1.10. 302.
Gene expression databases
ArrayExpress	Q09152.
Genevestigator	Q09152.
GermOnline	AT5G47770. Arabidopsis thaliana.
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

FPPS1_ARATH

Accession

Primary (citable) accession number: Q09152
Secondary accession number(s): Q42573, Q8W504, Q93Y84

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	June 6, 2002
Last modified:	February 9, 2010
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)