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.
Sequence processing	The displayed sequence is not processed.
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.
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.
Pathway	Isoprenoid biosynthesis; farnesyl-PP biosynthesis; farnesyl-PP from geranyl-PP and isopentenyl-PP: step 1/1. Isoprenoid biosynthesis; geranyl-PP biosynthesis; geranyl-PP from dimethylallyl-PP and isopentenyl-PP: step 1/1. Isoprenoid biosynthesis; geranylgeranyl-PP biosynthesis; geranylgeranyl-PP from farnesyl-PP and isopentenyl-PP: step 1/1.
Subcellular location	CytoplasmBy similarity.
Miscellaneous	Present with 2840 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the FPP/GGPP synthetase family.

Ontologies

Keywords
Biological process	Carotenoid biosynthesis Isoprene biosynthesis Protein transport Transport
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	3D-structure Complete proteome Multifunctional enzyme
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 electronic annotation. Source: EC geranyltranstransferase activity Inferred from electronic annotation. Source: EC
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

Active site

169

1

By similarity

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., Ward D.M. Traffic 5:700-710(2004) [PubMed: 15296494] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

PDBMSD

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q12051.

Genome annotation databases

Ensembl

YPL069C. Saccharomyces cerevisiae. [Contig view]

GeneID

856036.

GenomeReviews

Gene locus YPL069C in contig U00094_GR.

KEGG

sce:YPL069C.

NMPDR

fig|4932.3.peg.6389.

Organism-specific databases

CYGD

YPL069c.

SGD

S000005990. BTS1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

Q12051.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13701.

Gene expression databases

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

LinkHub

Q12051.

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:	November 25, 2008
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)