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UniProtKB/Swiss-Prot entry O14230


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

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Entry information
Entry name FPPS_SCHPO
Primary accession number O14230
Secondary accession number P78756
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 56)
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: fps1
ORFNames: SPAC6F12.13c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-347.
STRAIN=PR745;
DOI=10.1093/dnares/4.6.363; PubMed=9501991 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
"Identification of open reading frames in Schizosaccharomyces pombe cDNAs.";
DNA Res. 4:363-369(1997).
[3]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nbt1222; PubMed=16823372 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
[4]
FUNCTION, INTERACTION WITH SPO9, AND MUTAGENESIS OF PHE-90 AND ARG-104.
DOI=10.1091/mbc.E07-02-0112; PubMed=17596513 [NCBI, ExPASy, EBI, Israel, Japan]
Ye Y., Fujii M., Hirata A., Kawamukai M., Shimoda C., Nakamura T.;
"Geranylgeranyl diphosphate synthase in fission yeast is a heteromer of farnesyl diphosphate synthase (FPS), Fps1, and an FPS-like protein, Spo9, essential for sporulation.";
Mol. Biol. Cell 18:3568-3581(2007).
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
CU329670; CAB11097.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D89104; BAA13767.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T11664; T11664.
T42081; T42081.
RefSeq NP_593299.1; -.
3D structure databases
HSSP P08836; 1FPS. [HSSP ENTRY / PDB]
ModBase O14230.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-000998-MON; -.
Organism-specific databases
GeneDB_Spombe SPAC6F12.13c; -.
Gene expression databases
ArrayExpress O14230; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0005634; Cellular component: nucleus (inferred from direct assay from GeneDB_SPombe).
GO:0004161; Molecular function: dimethylallyltranstransferase activity (inferred from genetic interaction from GeneDB_SPombe).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from GeneDB_SPombe).
GO:0006696; Biological process: ergosterol biosynthetic process (inferred from genetic interaction from GeneDB_SPombe).
GO:0045337; Biological process: farnesyl diphosphate biosynthetic process (inferred from genetic interaction from GeneDB_SPombe).
GO:0018342; Biological process: protein prenylation (inferred by curator from GeneDB_SPombe).
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 O14230.
Genome annotation databases
GeneID 2542898; -.
KEGG spo:SPAC6F12.13c; -.
NMPDR fig|4896.1.peg.3269; -.
Other
ProtoNet O14230.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cholesterol biosynthesis; Complete proteome; Cytoplasm; Isoprene biosynthesis; Lipid synthesis; Nucleus; Steroid biosynthesis; Sterol biosynthesis; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   347  347     Farnesyl pyrophosphate synthetase. PRO_0000123951
ACT_SITE   184   184        By similarity. 
MUTAGEN   90    90        F->C: Complements lethality of fps1-delete strain. 
MUTAGEN   104   104        R->Q: No affect on GGPP synthetase activity. 
CONFLICT   203   203        A -> E (in Ref. 2; BAA13767). 
CONFLICT   346   347        NK -> ISKFLVLCF (in Ref. 2; BAA13767). 
Sequence information
Length: 347 AA [This is the length of the unprocessed precursor] Molecular weight: 39516 Da [This is the MW of the unprocessed precursor] CRC64: 483029A5FC15B9F5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSAVDKRAKF ESALPVFVDE IVNYLKTINI PDDVTEWYKN SLFHNTLGGK YNRGLSVIDS 

        70         80         90        100        110        120 
YEILLGHPLD EAAYMKAAVL GWMVELLQSF FLIADDIMDA SKTRRGQPCW YLMPGVGNIA 

       130        140        150        160        170        180 
INDAFMVESA IYFLLKKHFR QESCYVDLIE LFHDVTFQTE LGQQLDLLTA PEDSVDLSKF 

       190        200        210        220        230        240 
SLQKHSFIVI YKTAFYSFYL PVALAMHLAG VATPENLKCA QDILIILGKY FQVQDDYLDC 

       250        260        270        280        290        300 
YGDPTVTGKI GTDILDNKCS WIINLALAKC TPEQRVILDD NYGRKDSESE KRVKAVFEEL 

       310        320        330        340 
NIRGEFENYE ESEVSEIKKL IDGVDESTGL KKSIFTTFLG KIYKRNK 

O14230 in FASTA format

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