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Reviewed, UniProtKB/Swiss-Prot Q09152 (FPPS1_ARATH)

Last modified November 25, 2008. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Pathway

Isoprenoid biosynthesis; farnesyl-PP biosynthesis; farnesyl-PP from geranyl-PP and isopentenyl-PP: step 1/1.

Isoprenoid biosynthesis; geranyl-PP biosynthesis; geranyl-PP from dimethylallyl-PP and isopentenyl-PP: 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 384Farnesyl pyrophosphate synthetase 1, mitochondrialPRO_0000016469

Natural variations

Alternative sequence1 – 4141Missing in isoform Cytoplasmic.
VSP_018808

Experimental info

Sequence conflict2181A → S in CAA53433. Ref.4
Sequence conflict2311Y → H in CAA53433. Ref.4
Sequence conflict3241P → T in CAA53433. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform Mitochondrial (FPS1L) [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: E6808489D07D4F29

FASTA38444,261
        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 

« Hide

Isoform Cytoplasmic (FPS1S) [UniParc].

Checksum: 048B6CC7519A7476
Show »

34339,697

References

« Hide '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. expand/collapse author list , 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.

Cross-references

Sequence databases

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.
PIRS52009.
RefSeqNP_199588.1.
UniGeneAt.21206

3D structure databases

HSSPHSSP built from PDB template 1UBY based on UniProtKB P08836.
ModBaseSearch...

Genome annotation databases

GeneID834828.
GenomeReviewsGene locus AT5G47770 in contig BA000015_GR.
KEGGath:AT5G47770.
NMPDRfig|3702.1.peg.26592.

Organism-specific databases

TAIRAt5g47770.

Enzyme and pathway databases

BioCycMetaCyc:AT5G47770-MON.

Gene expression databases

ArrayExpressQ09152.
GermOnlineAT5G47770. Arabidopsis thaliana.

Family and domain databases

InterProIPR000092. Polyprenyl_synt.
IPR008949. Terpenoid_synth.
[Graphical view]
Gene3DG3DSA:1.10.600.10. Terpenoid_synth. 1 hit.
PfamPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
PROSITEPS00723. POLYPRENYL_SYNTHET_1. 1 hit.
PS00444. POLYPRENYL_SYNTHET_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFPPS1_ARATH
AccessionPrimary (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: November 25, 2008
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents