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UniProtKB/Swiss-Prot entry Q12051


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

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Entry information
Entry name GGPPS_YEAST
Primary accession number Q12051
Secondary accession numbers None
Integrated into Swiss-Prot on March 21, 2006
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 59)
Name and origin of the protein
Protein name Geranylgeranyl pyrophosphate synthetase
Synonyms GGPP synthetase
GGPPSase
Geranylgeranyl diphosphate synthase
BET2 suppressor protein 1
Includes Dimethylallyltranstransferase
     (EC 2.5.1.1)
Geranyltranstransferase
     (EC 2.5.1.10)
Farnesyltranstransferase
     (EC 2.5.1.29)
Gene name
Name: BTS1
OrderedLocusNames: YPL069C
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], AND FUNCTION.
DOI=10.1074/jbc.270.37.21958; PubMed=7665600 [NCBI, ExPASy, EBI, Israel, Japan]
Jiang Y., Proteau P., Poulter D., Ferro-Novick S.;
"BTS1 encodes a geranylgeranyl diphosphate synthase in Saccharomyces cerevisiae.";
J. Biol. Chem. 270:21793-21799(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169875 [NCBI, ExPASy, EBI, Israel, Japan]
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[5]
FUNCTION.
DOI=10.1111/j.1600-0854.2004.00213.x; PubMed=15296494 [NCBI, ExPASy, EBI, Israel, Japan]
Shiflett S.L., Vaughn M.B., Huynh D., Kaplan J., Ward D.M.;
"Bph1p, the Saccharomyces cerevisiae homologue of CHS1/beige, functions in cell wall formation and protein sorting.";
Traffic 5:700-710(2004).
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
U39205; AAB68296.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U31632; AAA83262.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY692852; AAT92871.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S60921; S60921.
RefSeq NP_015256.1; -.
3D structure databases
PDB
2DH4; X-ray; 1.98 A; A/B=1-335.[ExPASy / RCSB / EBI]
2E8T; X-ray; 2.13 A; A/B=1-335.[ExPASy / RCSB / EBI]
2E8U; X-ray; 2.08 A; A/B=1-335.[ExPASy / RCSB / EBI]
2E8V; X-ray; 1.80 A; A/B=1-335.[ExPASy / RCSB / EBI]
2E8W; X-ray; 2.35 A; A/B=1-335.[ExPASy / RCSB / EBI]
2E8X; X-ray; 2.04 A; A/B=1-335.[ExPASy / RCSB / EBI]
2E90; X-ray; 2.55 A; A/B=1-335.[ExPASy / RCSB / EBI]
2E91; X-ray; 2.14 A; A/B=1-335.[ExPASy / RCSB / EBI]
2E92; X-ray; 2.31 A; A/B=1-335.[ExPASy / RCSB / EBI]
2E93; X-ray; 2.12 A; A/B=1-335.[ExPASy / RCSB / EBI]
2E94; X-ray; 2.18 A; A/B=1-335.[ExPASy / RCSB / EBI]
2E95; X-ray; 2.20 A; A/B=1-335.[ExPASy / RCSB / EBI]
2Z7H; X-ray; 2.08 A; A/B=1-335.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2DH4; -.
2E8T; -.
2E8U; -.
2E8V; -.
2E8W; -.
2E8X; -.
2E90; -.
2E91; -.
2E92; -.
2E93; -.
2E94; -.
2E95; -.
2Z7H; -.
ModBase Q12051.
Protein-protein interaction databases
IntAct Q12051; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-13701; -.
Organism-specific databases
CYGD YPL069c; -.
SGD S000005990; BTS1.
Yeast-GFP YPL069C.
Gene expression databases
GermOnline YPL069C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0004311; Molecular function: farnesyltranstransferase activity (inferred from direct assay from SGD).
GO:0016114; Biological process: terpenoid biosynthetic process (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000092; Polyprenyl_synt.
IPR017446; Polyprenyl_synth-rel.
IPR008949; Terpenoid_synth.
Graphical view of domain structure.
Gene3D G3DSA:1.10.600.10; Terpenoid_synth; 1.
PANTHER PTHR12001; Polyprenyl_synt; 1.
Pfam PF00348; polyprenyl_synt; 1.
Pfam graphical view of domain structure.
PROSITE PS00723; POLYPRENYL_SYNTHET_1; 1.
PS00444; POLYPRENYL_SYNTHET_2; 1.
BLOCKS Q12051.
Genome annotation databases
Ensembl YPL069C; Saccharomyces cerevisiae. [Contig view]
GeneID 856036; -.
GenomeReviews U00094_GR; YPL069C.
KEGG sce:YPL069C; -.
NMPDR fig|4932.3.peg.6389; -.
Phylogenomic databases
HOGENOM Q12051; -.
Other
LinkHub Q12051; -.
ProtoNet Q12051.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Carotenoid biosynthesis; Complete proteome; Cytoplasm; Isoprene biosynthesis; Multifunctional enzyme; Protein transport; Transferase; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   335  335     Geranylgeranyl pyrophosphate synthetase. PRO_0000228139
ACT_SITE   169   169        By similarity. 
HELIX   1     9  9      
HELIX   17    30  14      
HELIX   36    50  15      
HELIX   54    78  25      
STRAND   82    84  3      
HELIX   90    94  5      
HELIX   96   114  19      
HELIX   121   150  30      
HELIX   159   169  11      
HELIX   171   184  14      
HELIX   195   219  25      
TURN   221   223  3      
HELIX   227   231  5      
HELIX   236   248  13      
HELIX   251   263  13      
HELIX   268   280  13      
HELIX   284   300  17      
HELIX   324   330  7      
HELIX   332   334  3      
Sequence information
Length: 335 AA [This is the length of the unprocessed precursor] Molecular weight: 38651 Da [This is the MW of the unprocessed precursor] CRC64: 4C7D6527FF29F157 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEAKIDELIN NDPVWSSQNE SLISKPYNHI LLKPGKNFRL NLIVQINRVM NLPKDQLAIV 

        70         80         90        100        110        120 
SQIVELLHNS SLLIDDIEDN APLRRGQTTS HLIFGVPSTI NTANYMYFRA MQLVSQLTTK 

       130        140        150        160        170        180 
EPLYHNLITI FNEELINLHR GQGLDIYWRD FLPEIIPTQE MYLNMVMNKT GGLFRLTLRL 

       190        200        210        220        230        240 
MEALSPSSHH GHSLVPFINL LGIIYQIRDD YLNLKDFQMS SEKGFAEDIT EGKLSFPIVH 

       250        260        270        280        290        300 
ALNFTKTKGQ TEQHNEILRI LLLRTSDKDI KLKLIQILEF DTNSLAYTKN FINQLVNMIK 

       310        320        330 
NDNENKYLPD LASHSDTATN LHDELLYIID HLSEL 

Q12051 in FASTA format

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