Reviewed, UniProtKB/Swiss-Prot Q12051 (GGPPS_YEAST)

Names and origin

Protein names

Recommended name:
    Geranylgeranyl pyrophosphate synthetase
      Short name=GGPP synthetase
      Short name=GGPPSase
Alternative name(s):
    Geranylgeranyl diphosphate synthase
    BET2 suppressor protein 1
Including the following 3 domains:
    1- Recommended name:
            Dimethylallyltranstransferase
              EC=2.5.1.1
    2- Recommended name:
            Geranyltranstransferase
              EC=2.5.1.10
    3- Recommended name:
            Farnesyltranstransferase
              EC=2.5.1.29

Gene names

Name:	BTS1
Ordered Locus Names:	YPL069C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
Protein existence	Evidence 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.5
Catalytic activity	Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate. Geranyl diphosphate + isopentenyl diphosphate = diphosphate + trans,trans-farnesyl diphosphate. Trans,trans-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate.
Cofactor	Binds 3 magnesium ions per subunit. Ref.8
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.4
Sequence similarities	Belongs to the FPP/GGPP synthetase family.
Biophysicochemical properties	Kinetic parameters: KM=3.2 µM for farnesyl diphosphate KM=0.8 µM for isopentenyl diphosphate

Ontologies

Keywords
Biological process	Carotenoid biosynthesis Isoprene biosynthesis Protein transport Transport
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	carotenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: SGD
Molecular function	dimethylallyltranstransferase activity Inferred from electronic annotation. Source: EC farnesyltranstransferase activity Ref.1 Inferred from direct assay. Source: SGD geranyltranstransferase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 335

335

Geranylgeranyl pyrophosphate synthetase

PRO_0000228139

Sites

Metal binding

75

1

Magnesium 1

Metal binding

75

1

Magnesium 2

Metal binding

79

1

Magnesium 1

Metal binding

79

1

Magnesium 2

Metal binding

209

1

Magnesium 3

Binding site

36

1

Isopentenyl diphosphate

Binding site

39

1

Isopentenyl diphosphate

Binding site

68

1

Isopentenyl diphosphate

Binding site

84

1

Dimethylallyl diphosphate

Binding site

85

1

Isopentenyl diphosphate

Binding site

169

1

Dimethylallyl diphosphate

Binding site

170

1

Dimethylallyl diphosphate

Binding site

206

1

Dimethylallyl diphosphate

Binding site

213

1

Dimethylallyl diphosphate

Binding site

223

1

Dimethylallyl diphosphate By similarity

Binding site

233

1

Dimethylallyl diphosphate

Site

107

1

Important for determining product chain length

Experimental info

Mutagenesis

7

1

E → G: No effect. Monomer; when associated with G-8. Ref.6

Mutagenesis

8

1

L → G: Monomer and homodimer. Monomer; when associated with G-7. Ref.6

Mutagenesis

9

1

I → G: Mostly monomer. Exclusively monomer; when associated with G-8. Reduces enzyme activity 1000-fold. Ref.6

Mutagenesis

107

1

Y → A: Reduced affinity for isopentenyl diphosphate (IPP).

Mutagenesis

108

1

F → A: Reduced affinity for isopentenyl diphosphate (IPP).

Mutagenesis

139

1

H → A: Reduced affinity for isopentenyl diphosphate (IPP).

Secondary structure

1

.

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335

Helix Strand Turn

Details...

Helix

1 – 9

9

Helix

17 – 30

14

Helix

36 – 50

15

Helix

54 – 78

25

Beta 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

Sequences

	Sequence		Length	Mass (Da)
	Q12051-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 4C7D6527FF29F157	FASTA	335	38,651
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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. , 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.
[4]	"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].
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.

PIR

S60921.

RefSeq

NP_015256.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DH4	X-ray	1.98	A/B	1-335	[»]
2E8T	X-ray	2.13	A/B	1-335	[»]
2E8U	X-ray	2.08	A/B	1-335	[»]
2E8V	X-ray	1.80	A/B	1-335	[»]
2E8W	X-ray	2.35	A/B	1-335	[»]
2E8X	X-ray	2.04	A/B	1-335	[»]
2E90	X-ray	2.55	A/B	1-335	[»]
2E91	X-ray	2.14	A/B	1-335	[»]
2E92	X-ray	2.31	A/B	1-335	[»]
2E93	X-ray	2.12	A/B	1-335	[»]
2E94	X-ray	2.18	A/B	1-335	[»]
2E95	X-ray	2.20	A/B	1-335	[»]
2Z4V	X-ray	1.86	A/B	1-335	[»]
2Z4W	X-ray	2.45	A/B	1-335	[»]
2Z4X	X-ray	1.90	A/B	1-335	[»]
2Z4Y	X-ray	2.10	A/B	1-335	[»]
2Z4Z	X-ray	2.09	A/B	1-335	[»]
2Z50	X-ray	2.01	A/B	1-335	[»]
2Z52	X-ray	2.13	A/B	1-335	[»]
2Z78	X-ray	2.10	A/B	1-335	[»]
2Z7H	X-ray	2.08	A/B	1-335	[»]
2Z7I	X-ray	2.10	A/B	1-335	[»]
2ZEU	X-ray	2.00	A/B	1-335	[»]
2ZEV	X-ray	2.23	A/B	1-335	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q12051. 5 interactions.

STRING

Q12051.

Genome annotation databases

Ensembl

YPL069C; YPL069C; YPL069C; Saccharomyces cerevisiae. [Genome view]

GeneID

856036.

KEGG

sce:YPL069C.

NMPDR

fig|4932.3.peg.6389.

Organism-specific databases

CYGD

YPL069c.

SGD

S000005990. BTS1.

Phylogenomic databases

eggNOG

fuNOG04319.

HOGENOM

HBG397395.

OMA

DIEDNSI.

OrthoDB

EOG9D285X.

PhylomeDB

Q12051.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13701.

BRENDA

2.5.1.1. 250.
2.5.1.10. 250.
2.5.1.29. 250.

Gene expression databases

ArrayExpress

Q12051.

Genevestigator

Q12051.

GermOnline

YPL069C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000092. Polyprenyl_synt.
IPR017446. Polyprenyl_synth-rel.
IPR008949. Terpenoid_synth.
[Graphical view]

Gene3D

G3DSA:1.10.600.10. Terpenoid_synth. 1 hit.

PANTHER

PTHR12001. Polyprenyl_synt. 1 hit.

Pfam

PF00348. polyprenyl_synt. 1 hit.
[Graphical view]

PROSITE

PS00723. POLYPRENYL_SYNTHET_1. 1 hit.
PS00444. POLYPRENYL_SYNTHET_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

980968.

Entry information

Entry name

GGPPS_YEAST

Accession

Primary (citable) accession number: Q12051

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)