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P49349 (FPPS_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
Synonyms:FPS
Ordered Locus Names:KLLA0A06732g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Protein existenceInferred 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 + (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.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the FPP/GGPP synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 349349Farnesyl pyrophosphate synthase
PRO_0000123949

Sites

Metal binding971Magnesium 1 By similarity
Metal binding971Magnesium 2 By similarity
Metal binding1011Magnesium 1 By similarity
Metal binding1011Magnesium 2 By similarity
Metal binding2371Magnesium 3 By similarity
Binding site481Isopentenyl diphosphate By similarity
Binding site511Isopentenyl diphosphate By similarity
Binding site901Isopentenyl diphosphate By similarity
Binding site1061Dimethylallyl diphosphate By similarity
Binding site1071Isopentenyl diphosphate By similarity
Binding site1941Dimethylallyl diphosphate By similarity
Binding site1951Dimethylallyl diphosphate By similarity
Binding site2341Dimethylallyl diphosphate By similarity
Binding site2511Dimethylallyl diphosphate By similarity
Binding site2601Dimethylallyl diphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
P49349 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 290557C17FAACDCE

FASTA34940,157
        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

« Hide

References

« Hide '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 / NBRC 1267 / 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. expand/collapse author list , 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 / NBRC 1267 / NRRL Y-1140 / WM37.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X76026 Genomic DNA. Translation: CAA53614.1.
CR382121 Genomic DNA. Translation: CAH02888.1.
PIRS50214.
RefSeqXP_451300.1. XM_451300.1.

3D structure databases

ProteinModelPortalP49349.
ModBaseSearch...

Protein-protein interaction databases

STRINGP49349.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2896751.
GenomeReviewsGene locus KLLA0A06732g in contig CR382121_GR.
KEGGkla:KLLA0A06732g.

Phylogenomic databases

eggNOGfuNOG05213.
HOGENOMHBG328346.
OMAENKTSHY.
OrthoDBEOG4SFDFW.

Family and domain databases

InterProIPR000092. Polyprenyl_synt.
IPR008949. Terpenoid_synth.
[Graphical view]
Gene3DG3DSA:1.10.600.10. Terpenoid_synth. 1 hit.
KOK00787.
PfamPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMSSF48576. Terpenoid_synth. 1 hit.
PROSITEPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFPPS_KLULA
AccessionPrimary (citable) accession number: P49349
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: December 14, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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