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UniProtKB/Swiss-Prot entry P08524


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FPPS_YEAST
Primary accession number P08524
Secondary accession number P15495
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on November 1, 1991 (Sequence version 2)
Annotations were last modified on    June 10, 2008 (Entry version 78)
Name and origin of the protein
Protein name Farnesyl pyrophosphate synthetase
Synonyms FPP synthetase
FPS
Farnesyl diphosphate synthetase
Includes Dimethylallyltranstransferase
     (EC 2.5.1.1)
Geranyltranstransferase
     (EC 2.5.1.10)
Gene name
Name: FPP1
Synonyms: BOT3, ERG20, FDS1
OrderedLocusNames: YJL167W
ORFNames: J0525
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2681213 [NCBI, ExPASy, EBI, Israel, Japan]
Anderson M.S., Yarger J.G., Burck C.L., Poulter C.D.;
"Farnesyl diphosphate synthetase. Molecular cloning, sequence, and expression of an essential gene from Saccharomyces cerevisiae.";
J. Biol. Chem. 264:19176-19184(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8641269 [NCBI, ExPASy, EBI, Israel, Japan]
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
EMBO J. 15:2031-2049(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 131-352.
PubMed=3036507 [NCBI, ExPASy, EBI, Israel, Japan]
Maarse A.C., Grivell L.A.;
"Nucleotide sequence of the gene encoding the 11-kDa subunit of the ubiquinol-cytochrome-c oxidoreductase in Saccharomyces cerevisiae.";
Eur. J. Biochem. 165:419-425(1987).
[4]
MUTANT GLU-197.
STRAIN=LB25;
DOI=10.1016/0378-1119(93)90326-X; PubMed=8096487 [NCBI, ExPASy, EBI, Israel, Japan]
Blanchard L., Karst F.;
"Characterization of a lysine-to-glutamic acid mutation in a conservative sequence of farnesyl diphosphate synthase from Saccharomyces cerevisiae.";
Gene 125:185-189(1993).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J05091; AAA34606.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49442; CAA89462.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X05550; CAA29064.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A34441; A34441.
RefSeq NP_012368.1; -.
3D structure databases
HSSP P08836; 1FPS. [HSSP ENTRY / PDB]
ModBase P08524.
Protein-protein interaction databases
DIP DIP:1163N; -.
IntAct P08524; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-655; -.
Organism-specific databases
CYGD YJL167w; -.
SGD S000003703; ERG20.
Yeast-GFP YJL167W.
Gene expression databases
ArrayExpress P08524; -.
GermOnline YJL167W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0004161; Molecular function: dimethylallyltranstransferase activity (inferred from direct assay from SGD).
GO:0004337; Molecular function: geranyltranstransferase activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0045337; Biological process: farnesyl diphosphate biosynthetic process (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000092; Polyprenyl_synt.
IPR008949; Terpenoid_synth.
Graphical view of domain structure.
Gene3D G3DSA:1.10.600.10; Terpenoid_synth; 1.
Pfam PF00348; polyprenyl_synt; 1.
Pfam graphical view of domain structure.
PROSITE PS00723; POLYPRENYL_SYNTHET_1; 1.
PS00444; POLYPRENYL_SYNTHET_2; 1.
BLOCKS P08524.
Proteomic databases
PeptideAtlas P08524; -.
Genome annotation databases
Ensembl YJL167W; Saccharomyces cerevisiae. [Contig view]
GeneID 853272; -.
GenomeReviews Y13136_GR; YJL167W.
KEGG sce:YJL167W; -.
NMPDR fig|4932.3.peg.3332; -.
Phylogenomic databases
HOGENOM P08524; -.
Other
LinkHub P08524; -.
ProtoNet P08524.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cholesterol biosynthesis; Complete proteome; Cytoplasm; Isoprene biosynthesis; Lipid synthesis; Steroid biosynthesis; Sterol biosynthesis; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   352  352     Farnesyl pyrophosphate synthetase. PRO_0000123952
ACT_SITE   189   189        By similarity. 
MUTAGEN   197   197        K->E: In ERG20-2; 14-fold decrease in FPPS activity. 
Sequence information
Length: 352 AA [This is the length of the unprocessed precursor] Molecular weight: 40483 Da [This is the MW of the unprocessed precursor] CRC64: 79A357BB7BFCEDDA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASEKEIRRE RFLNVFPKLV EELNASLLAY GMPKEACDWY AHSLNYNTPG GKLNRGLSVV 

        70         80         90        100        110        120 
DTYAILSNKT VEQLGQEEYE KVAILGWCIE LLQAYFLVAD DMMDKSITRR GQPCWYKVPE 

       130        140        150        160        170        180 
VGEIAINDAF MLEAAIYKLL KSHFRNEKYY IDITELFHEV TFQTELGQLM DLITAPEDKV 

       190        200        210        220        230        240 
DLSKFSLKKH SFIVTFKTAY YSFYLPVALA MYVAGITDEK DLKQARDVLI PLGEYFQIQD 

       250        260        270        280        290        300 
DYLDCFGTPE QIGKIGTDIQ DNKCSWVINK ALELASAEQR KTLDENYGKK DSVAEAKCKK 

       310        320        330        340        350 
IFNDLKIEQL YHEYEESIAK DLKAKISQVD ESRGFKADVL TAFLNKVYKR SK 

P08524 in FASTA format

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