Skip Header

Contribute Send feedback
Read comments (?) or add your own

P49351 (FPPS1_LUPAL) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Farnesyl pyrophosphate synthase 1
Short name=FPP synthase 1
Short name=FPS 1
EC=2.5.1.10
Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase 1
Dimethylallyltranstransferase 1
EC=2.5.1.1
Farnesyl diphosphate synthase 1
Geranyltranstransferase 1
Gene names
Name:FPS1
OrganismLupinus albus (White lupin) (Lupinus termis)
Taxonomic identifier3870 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Genisteae › Lupinus

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
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 + (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 By similarity.

Sequence similarities

Belongs to the FPP/GGPP synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342Farnesyl pyrophosphate synthase 1
PRO_0000123956

Sites

Metal binding931Magnesium 1 By similarity
Metal binding931Magnesium 2 By similarity
Metal binding971Magnesium 1 By similarity
Metal binding971Magnesium 2 By similarity
Metal binding2321Magnesium 3 By similarity
Binding site471Isopentenyl diphosphate By similarity
Binding site501Isopentenyl diphosphate By similarity
Binding site861Isopentenyl diphosphate By similarity
Binding site1021Dimethylallyl diphosphate By similarity
Binding site1031Isopentenyl diphosphate By similarity
Binding site1901Dimethylallyl diphosphate By similarity
Binding site1911Dimethylallyl diphosphate By similarity
Binding site2291Dimethylallyl diphosphate By similarity
Binding site2461Dimethylallyl diphosphate By similarity
Binding site2551Dimethylallyl diphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
P49351 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 591DE4CD29CC711C

FASTA34239,269
        10         20         30         40         50         60 
MADLRSTFLN VYSVLKSELL HDPAFEFSPD SRQWLDRMLD YNVPGGKLNR GLSVIDSYRL 

        70         80         90        100        110        120 
LKDGHELNDD EIFLASALGW CIEWLQAYFL VLDDIMDNSH TRRGQPCWFR VPKVGMIAAN 

       130        140        150        160        170        180 
DGVLLRNHIP RILKKHFRGK PYYADLLDLF NEVEFQTASG QMIDLITTLE GEKDLSKYTL 

       190        200        210        220        230        240 
SLHRRIVQYK TAYYSFYLPV ACALLMVGEN LDNHIDVKNI LVDMGTYFQV QDDYLDCFGA 

       250        260        270        280        290        300 
PETIGKIGTD IEDFKCSWLV VKALELSNDE QKKVLYDNYG KPDPANVAKV KALYDELNLQ 

       310        320        330        340 
GVFTEYESKS YEKLVTSIEA HPSKAVQALL KSFLGKIYKR QK

« Hide

References

[1]"Farnesyl pyrophosphate synthase from white lupin: molecular cloning, expression, and purification of the expressed protein."
Attucci S., Aitken S.M., Gulick P.J., Ibrahim R.K.
Arch. Biochem. Biophys. 321:493-500(1995) [PubMed: 7646076] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Root.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U15777 mRNA. Translation: AAA86687.1.
PIRS66470.

3D structure databases

ProteinModelPortalP49351.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.5.1.10. 3089.

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]
SUPFAMSSF48576. Terpenoid_synth. 1 hit.
PROSITEPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFPPS1_LUPAL
AccessionPrimary (citable) accession number: P49351
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 21, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents