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Q12051 (GGPPS_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Geranylgeranyl pyrophosphate synthase

Short name=GGPP synthase
Short name=GGPPSase
Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase
BET2 suppressor protein 1
Dimethylallyltranstransferase
EC=2.5.1.1
Farnesyl diphosphate synthase
Farnesyltranstransferase
EC=2.5.1.29
Geranylgeranyl diphosphate synthase
Geranyltranstransferase
EC=2.5.1.10
Gene names
Name:BTS1
Ordered Locus Names:YPL069C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the trans-addition of the 3 molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. Required for the membrane attachment of YPT1 and SEC4. May be involved in vesicle trafficking and protein sorting. Ref.1 Ref.6

Catalytic activity

Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate.

Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate.

(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate.

Cofactor

Binds 3 magnesium ions per subunit. Ref.9

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.

Isoprenoid biosynthesis; geranylgeranyl diphosphate biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate: step 1/1.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

Present with 2840 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Belongs to the FPP/GGPP synthase family.

Biophysicochemical properties

Kinetic parameters:

KM=3.2 µM for farnesyl diphosphate

KM=0.8 µM for isopentenyl diphosphate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 335335Geranylgeranyl pyrophosphate synthase
PRO_0000228139

Sites

Metal binding751Magnesium 1
Metal binding751Magnesium 2
Metal binding791Magnesium 1
Metal binding791Magnesium 2
Metal binding2091Magnesium 3
Binding site361Isopentenyl diphosphate
Binding site391Isopentenyl diphosphate
Binding site681Isopentenyl diphosphate
Binding site841Dimethylallyl diphosphate
Binding site851Isopentenyl diphosphate
Binding site1691Dimethylallyl diphosphate
Binding site1701Dimethylallyl diphosphate
Binding site2061Dimethylallyl diphosphate
Binding site2131Dimethylallyl diphosphate
Binding site2231Dimethylallyl diphosphate By similarity
Binding site2331Dimethylallyl diphosphate
Site1071Important for determining product chain length

Experimental info

Mutagenesis71E → G: No effect. Monomer; when associated with G-8. Ref.7
Mutagenesis81L → G: Monomer and homodimer. Monomer; when associated with G-7. Ref.7
Mutagenesis91I → G: Mostly monomer. Exclusively monomer; when associated with G-8. Reduces enzyme activity 1000-fold. Ref.7
Mutagenesis1071Y → A: Reduced affinity for isopentenyl diphosphate (IPP).
Mutagenesis1081F → A: Reduced affinity for isopentenyl diphosphate (IPP).
Mutagenesis1391H → A: Reduced affinity for isopentenyl diphosphate (IPP).

Secondary structure

...................................... 335
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12051 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4C7D6527FF29F157

FASTA33538,651
        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 

« Hide

References

« Hide 'large scale' references
[1]"BTS1 encodes a geranylgeranyl diphosphate synthase in Saccharomyces cerevisiae."
Jiang Y., Proteau P., Poulter D., Ferro-Novick S.
J. Biol. Chem. 270:21793-21799(1995) [PubMed: 7665600] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
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. expand/collapse author list , 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.
Nature 387:103-105(1997) [PubMed: 9169875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"Bph1p, the Saccharomyces cerevisiae homologue of CHS1/beige, functions in cell wall formation and protein sorting."
Shiflett S.L., Vaughn M.B., Huynh D., Kaplan J., McVey Ward D.
Traffic 5:700-710(2004) [PubMed: 15296494] [Abstract]
Cited for: FUNCTION.
[7]"Combined experimental and theoretical study of long-range interactions modulating dimerization and activity of yeast geranylgeranyl diphosphate synthase."
Lo C.-H., Chang Y.-H., Wright J.D., Chen S.-H., Kan D., Lim C., Liang P.-H.
J. Am. Chem. Soc. 131:4051-4062(2009) [PubMed: 19245203] [Abstract]
Cited for: SUBUNIT, MUTAGENESIS OF GLU-7; LEU-8 AND ILE-9.
[8]"Crystal structure of type-III geranylgeranyl pyrophosphate synthase from Saccharomyces cerevisiae and the mechanism of product chain length determination."
Chang T.-H., Guo R.-T., Ko T.-P., Wang A.H.-J., Liang P.-H.
J. Biol. Chem. 281:14991-15000(2006) [PubMed: 16554305] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, SUBUNIT.
[9]"Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases."
Guo R.-T., Cao R., Liang P.-H., Ko T.-P., Chang T.-H., Hudock M.P., Jeng W.-Y., Chen C.K.-M., Zhang Y., Song Y., Kuo C.-J., Yin F., Oldfield E., Wang A.H.-J.
Proc. Natl. Acad. Sci. U.S.A. 104:10022-10027(2007) [PubMed: 17535895] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ISOPENTENYL DIPHOSPHATE; FARNESYL DIPHOSPHATE AND MAGNESIUM, COFACTOR, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U39205 Genomic DNA. Translation: AAB68296.1.
U31632 Genomic DNA. Translation: AAA83262.1.
AY692852 Genomic DNA. Translation: AAT92871.1.
BK006949 Genomic DNA. Translation: DAA11362.1.
PIRS60921.
RefSeqNP_015256.1. NM_001183883.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DH4X-ray1.98A/B1-335[»]
2E8TX-ray2.13A/B1-335[»]
2E8UX-ray2.08A/B1-335[»]
2E8VX-ray1.80A/B1-335[»]
2E8WX-ray2.35A/B1-335[»]
2E8XX-ray2.04A/B1-335[»]
2E90X-ray2.55A/B1-335[»]
2E91X-ray2.14A/B1-335[»]
2E92X-ray2.31A/B1-335[»]
2E93X-ray2.12A/B1-335[»]
2E94X-ray2.18A/B1-335[»]
2E95X-ray2.20A/B1-335[»]
2Z4VX-ray1.86A/B1-335[»]
2Z4WX-ray2.45A/B1-335[»]
2Z4XX-ray1.90A/B1-335[»]
2Z4YX-ray2.10A/B1-335[»]
2Z4ZX-ray2.09A/B1-335[»]
2Z50X-ray2.01A/B1-335[»]
2Z52X-ray2.13A/B1-335[»]
2Z78X-ray2.10A/B1-335[»]
2Z7HX-ray2.08A/B1-335[»]
2Z7IX-ray2.10A/B1-335[»]
2ZEUX-ray2.00A/B1-335[»]
2ZEVX-ray2.23A/B1-335[»]
ProteinModelPortalQ12051.
SMRQ12051. Positions 1-335.
ModBaseSearch...

Protein-protein interaction databases

IntActQ12051. 5 interactions.
STRINGQ12051.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL069C; YPL069C; YPL069C.
GeneID856036.
KEGGsce:YPL069C.
NMPDRfig|4932.3.peg.6389.

Organism-specific databases

CYGDYPL069c.
SGDS000005990. BTS1.

Phylogenomic databases

eggNOGfuNOG04319.
GeneTreeEFGT00050000002292.
HOGENOMHBG397395.
OMAIHSIRSN.
OrthoDBEOG4QVGMM.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13701.

Gene expression databases

ArrayExpressQ12051.
GenevestigatorQ12051.
GermOnlineYPL069C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000092. Polyprenyl_synt.
IPR017446. Polyprenyl_synth-rel.
IPR008949. Terpenoid_synth.
[Graphical view]
Gene3DG3DSA:1.10.600.10. Terpenoid_synth. 1 hit.
KOK00804.
PANTHERPTHR12001. Polyprenyl_synt. 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...

Other

NextBio980968.

Entry information

Entry nameGGPPS_YEAST
AccessionPrimary (citable) accession number: Q12051
Secondary accession number(s): D6W3U6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: November 1, 1996
Last modified: December 14, 2011
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families