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UniProtKB/Swiss-Prot entry O59703


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

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Entry information
Entry name GGPPS_SCHPO
Primary accession number O59703
Secondary accession numbers None
Integrated into Swiss-Prot on June 10, 2008
Sequence was last modified on August 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 43)
Name and origin of the protein
Protein name Geranylgeranyl pyrophosphate synthetase
Synonyms GGPP synthetase
GGPPSase
Geranylgeranyl diphosphate synthase
Sporulation-specific protein 9
Includes Dimethylallyltranstransferase
     (EC 2.5.1.1)
Geranyltranstransferase
     (EC 2.5.1.10)
Farnesyltranstransferase
     (EC 2.5.1.29)
Gene name
Name: spo9
ORFNames: SPBC36.06c
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]
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).
[3]
FUNCTION, INTERACTION WITH FPS1, AND MUTAGENESIS OF CYS-95 AND ARG-109.
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
CU329671; CAA19054.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T40301; T40301.
RefSeq NP_595334.1; -.
3D structure databases
HSSP P08836; 1FPS. [HSSP ENTRY / PDB]
ModBase O59703.
Organism-specific databases
GeneDB_Spombe SPBC36.06c; -.
Gene expression databases
ArrayExpress O59703; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0004161; Molecular function: dimethylallyltranstransferase activity (inferred from electronic annotation from EC).
GO:0004311; Molecular function: farnesyltranstransferase activity (inferred from electronic annotation from EC).
GO:0004337; Molecular function: geranyltranstransferase activity (inferred from electronic annotation from EC).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from GeneDB_SPombe).
GO:0004660; Molecular function: protein farnesyltransferase activity (inferred from mutant phenotype from GeneDB_SPombe).
GO:0030437; Biological process: ascospore formation (inferred from mutant phenotype from GeneDB_SPombe).
GO:0016117; Biological process: carotenoid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0018342; Biological process: protein prenylation (inferred from mutant phenotype from GeneDB_SPombe).
GO:0015031; Biological process: protein transport (inferred from electronic annotation from UniProtKB-KW).
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.
Genome annotation databases
GeneID 2540933; -.
KEGG spo:SPBC36.06c; -.
NMPDR fig|4896.1.peg.1200; -.
Other
ProtoNet O59703.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Carotenoid biosynthesis; Complete proteome; Cytoplasm; Isoprene biosynthesis; Multifunctional enzyme; Nucleus; Protein transport; Transferase; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   351  351     Geranylgeranyl pyrophosphate synthetase. PRO_0000339411
MUTAGEN   95    95        C->F: No complement of lethality of fps1-delete strain. 
MUTAGEN   109   109        R->Q: No GGPP synthetase activity. 
Sequence information
Length: 351 AA [This is the length of the unprocessed precursor] Molecular weight: 40946 Da [This is the MW of the unprocessed precursor] CRC64: F5DC90A91CC132E7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVNDFNEKNG IKKRLLDFFP VVLEGIREIL ESMQYFPEET EKLLYSIKRN TLGGKNNRGL 

        70         80         90        100        110        120 
AVLQSLTSLI NRELEEAEFR DAALLGWLIE ILQGCFLMAD DIMDQSIKRR GLDCWYLVVG 

       130        140        150        160        170        180 
VRRAINESQL LEACIPLLIR KYFRNMPYYV DLLDTFREVT FLTELGQQED LLSSRDGEAS 

       190        200        210        220        230        240 
LRSFDLMKYD FIITYKTSFY SFYLPIKCAL LLSRNSNQKA YDTTIKLSKL LGYYFQVQDD 

       250        260        270        280        290        300 
YLDCFGDYTV LGKVGMDIQD NKCTWLVCYA EKFASADQLN LLRAHYGKAG SENIAVIKQL 

       310        320        330        340        350 
YHELQIPELY HKFEDDMVDS ISKEIDLIDE STGLKKCIFT KFFQLIYKRS R 

O59703 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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