Reviewed, UniProtKB/Swiss-Prot P49350 (FPPS_ARTAN)

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

Organism

Artemisia annua (Sweet wormwood)

Taxonomic identifier

35608 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Asterales › Asteraceae › Asteroideae › Anthemideae › Artemisia

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
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	Cytoplasm By similarity.
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
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 – 343	343	Farnesyl pyrophosphate synthetase		PRO_0000123954
Sites
	Metal binding	94	1	Magnesium 1 By similarity
	Metal binding	94	1	Magnesium 2 By similarity
	Metal binding	98	1	Magnesium 1 By similarity
	Metal binding	98	1	Magnesium 2 By similarity
	Metal binding	233	1	Magnesium 3 By similarity
	Binding site	49	1	Isopentenyl diphosphate By similarity
	Binding site	52	1	Isopentenyl diphosphate By similarity
	Binding site	87	1	Isopentenyl diphosphate By similarity
	Binding site	103	1	Dimethylallyl diphosphate By similarity
	Binding site	104	1	Isopentenyl diphosphate By similarity
	Binding site	191	1	Dimethylallyl diphosphate By similarity
	Binding site	192	1	Dimethylallyl diphosphate By similarity
	Binding site	230	1	Dimethylallyl diphosphate By similarity
	Binding site	247	1	Dimethylallyl diphosphate By similarity
	Binding site	256	1	Dimethylallyl diphosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P49350-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 431372214500AF68	FASTA	343	39,420
	10 20 30 40 50 60 MSSTDLKSKF LKVYDTLKSE LINDPAFEFD DDSRQWIEKM LDYNVPGGKL NRGLSVVDSY 70 80 90 100 110 120 QLLKGGELSD DEIFLSSALG WCIEWLQAYF LVLDDIMDES HTRRGQPCWF RLPKVGMIAA 130 140 150 160 170 180 NDGILLRNHV PRILKKHFRG KPYYVDLVDL FNEVEFQTAS GQMIDLITTL VGEKDLSKYS 190 200 210 220 230 240 LSIHRRIVQY KTAYYSFYLP VACALLMFGE DLDKHVEVKN VLVEMGTYFQ VQDDYLDCFG 250 260 270 280 290 300 APEVIGKIGT DIEDFKCSWL VVKALELPNE EQKKTLHENY GKKDPASVAK VKEVYHTLNL 310 320 330 340 QAVFEDYEAT SYKKLITSIE NHPSKAVQAV LKSFLGKIYK RQK

References

[1]	"Cloning and analysis of a cDNA encoding farnesyl diphosphate synthase from Artemisia annua." Matsushita Y., Kang W., Charlwood B.V. Gene 172:207-209(1996) [PubMed: 8682304] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	U36376 mRNA. Translation: AAC49452.1.
PIR	JC4846.
3D structure databases
SMR	P49350. Positions 5-343.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.5.1.1. 275466. 2.5.1.10. 275466.
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_ARTAN

Accession

Primary (citable) accession number: P49350

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	January 19, 2010
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)