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Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((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)

 GGPPS_YEAST             Reviewed;         335 AA.
Q12051; D6W3U6;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 148.
RecName: Full=Geranylgeranyl pyrophosphate synthase;
Short=GGPP synthase;
Short=GGPPSase;
EC=2.5.1.-;
AltName: Full=(2E,6E)-farnesyl diphosphate synthase;
AltName: Full=BET2 suppressor protein 1;
AltName: Full=Dimethylallyltranstransferase;
EC=2.5.1.1;
AltName: Full=Farnesyl diphosphate synthase;
AltName: Full=Farnesyltranstransferase;
EC=2.5.1.29;
AltName: Full=Geranylgeranyl diphosphate synthase;
AltName: Full=Geranyltranstransferase;
EC=2.5.1.10;
Name=BTS1; OrderedLocusNames=YPL069C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=7665600; DOI=10.1074/jbc.270.37.21958;
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 204508 / S288c;
PubMed=9169875;
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]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
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).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
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).
[6]
FUNCTION.
PubMed=15296494; DOI=10.1111/j.1600-0854.2004.00213.x;
Shiflett S.L., Vaughn M.B., Huynh D., Kaplan J., McVey Ward D.;
"Bph1p, the Saccharomyces cerevisiae homologue of CHS1/beige,
functions in cell wall formation and protein sorting.";
Traffic 5:700-710(2004).
[7]
SUBUNIT, AND MUTAGENESIS OF GLU-7; LEU-8 AND ILE-9.
PubMed=19245203; DOI=10.1021/ja808699c;
Lo C.-H., Chang Y.-H., Wright J.D., Chen S.-H., Kan D., Lim C.,
Liang P.-H.;
"Combined experimental and theoretical study of long-range
interactions modulating dimerization and activity of yeast
geranylgeranyl diphosphate synthase.";
J. Am. Chem. Soc. 131:4051-4062(2009).
[8]
X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS,
AND SUBUNIT.
PubMed=16554305; DOI=10.1074/jbc.M512886200;
Chang T.-H., Guo R.-T., Ko T.-P., Wang A.H.-J., Liang P.-H.;
"Crystal structure of type-III geranylgeranyl pyrophosphate synthase
from Saccharomyces cerevisiae and the mechanism of product chain
length determination.";
J. Biol. Chem. 281:14991-15000(2006).
[9]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ISOPENTENYL
DIPHOSPHATE; FARNESYL DIPHOSPHATE AND MAGNESIUM, COFACTOR, AND
SUBUNIT.
PubMed=17535895; DOI=10.1073/pnas.0702254104;
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.;
"Bisphosphonates target multiple sites in both cis- and trans-
prenyltransferases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10022-10027(2007).
-!- 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. {ECO:0000269|PubMed:15296494,
ECO:0000269|PubMed:7665600}.
-!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl
diphosphate = diphosphate + geranyl diphosphate.
-!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate
= diphosphate + (2E,6E)-farnesyl diphosphate.
-!- CATALYTIC ACTIVITY: (2E,6E)-farnesyl diphosphate + isopentenyl
diphosphate = diphosphate + geranylgeranyl diphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:17535895};
Note=Binds 3 Mg(2+) ions per subunit.
{ECO:0000269|PubMed:17535895};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.2 uM for farnesyl diphosphate;
KM=0.8 uM for isopentenyl diphosphate;
-!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate
biosynthesis; farnesyl diphosphate from geranyl diphosphate and
isopentenyl diphosphate: step 1/1.
-!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate
biosynthesis; geranyl diphosphate from dimethylallyl diphosphate
and isopentenyl diphosphate: step 1/1.
-!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate
biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate
and isopentenyl diphosphate: step 1/1.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
{ECO:0000305}.
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EMBL; U39205; AAB68296.1; -; Genomic_DNA.
EMBL; U31632; AAA83262.1; -; Genomic_DNA.
EMBL; AY692852; AAT92871.1; -; Genomic_DNA.
EMBL; BK006949; DAA11362.1; -; Genomic_DNA.
PIR; S60921; S60921.
RefSeq; NP_015256.1; NM_001183883.1.
PDB; 2DH4; X-ray; 1.98 A; A/B=1-335.
PDB; 2E8T; X-ray; 2.13 A; A/B=1-335.
PDB; 2E8U; X-ray; 2.08 A; A/B=1-335.
PDB; 2E8V; X-ray; 1.80 A; A/B=1-335.
PDB; 2E8W; X-ray; 2.35 A; A/B=1-335.
PDB; 2E8X; X-ray; 2.04 A; A/B=1-335.
PDB; 2E90; X-ray; 2.55 A; A/B=1-335.
PDB; 2E91; X-ray; 2.14 A; A/B=1-335.
PDB; 2E92; X-ray; 2.31 A; A/B=1-335.
PDB; 2E93; X-ray; 2.12 A; A/B=1-335.
PDB; 2E94; X-ray; 2.18 A; A/B=1-335.
PDB; 2E95; X-ray; 2.20 A; A/B=1-335.
PDB; 2Z4V; X-ray; 1.86 A; A/B=1-335.
PDB; 2Z4W; X-ray; 2.45 A; A/B=1-335.
PDB; 2Z4X; X-ray; 1.90 A; A/B=1-335.
PDB; 2Z4Y; X-ray; 2.10 A; A/B=1-335.
PDB; 2Z4Z; X-ray; 2.09 A; A/B=1-335.
PDB; 2Z50; X-ray; 2.01 A; A/B=1-335.
PDB; 2Z52; X-ray; 2.13 A; A/B=1-335.
PDB; 2Z78; X-ray; 2.10 A; A/B=1-335.
PDB; 2Z7H; X-ray; 2.08 A; A/B=1-335.
PDB; 2Z7I; X-ray; 2.10 A; A/B=1-335.
PDB; 2ZEU; X-ray; 2.00 A; A/B=1-335.
PDB; 2ZEV; X-ray; 2.23 A; A/B=1-335.
PDBsum; 2DH4; -.
PDBsum; 2E8T; -.
PDBsum; 2E8U; -.
PDBsum; 2E8V; -.
PDBsum; 2E8W; -.
PDBsum; 2E8X; -.
PDBsum; 2E90; -.
PDBsum; 2E91; -.
PDBsum; 2E92; -.
PDBsum; 2E93; -.
PDBsum; 2E94; -.
PDBsum; 2E95; -.
PDBsum; 2Z4V; -.
PDBsum; 2Z4W; -.
PDBsum; 2Z4X; -.
PDBsum; 2Z4Y; -.
PDBsum; 2Z4Z; -.
PDBsum; 2Z50; -.
PDBsum; 2Z52; -.
PDBsum; 2Z78; -.
PDBsum; 2Z7H; -.
PDBsum; 2Z7I; -.
PDBsum; 2ZEU; -.
PDBsum; 2ZEV; -.
ProteinModelPortal; Q12051; -.
SMR; Q12051; -.
BioGrid; 36110; 1023.
DIP; DIP-8889N; -.
IntAct; Q12051; 5.
STRING; 4932.YPL069C; -.
BindingDB; Q12051; -.
ChEMBL; CHEMBL1075251; -.
MaxQB; Q12051; -.
PaxDb; Q12051; -.
PRIDE; Q12051; -.
EnsemblFungi; YPL069C; YPL069C; YPL069C.
GeneID; 856036; -.
KEGG; sce:YPL069C; -.
EuPathDB; FungiDB:YPL069C; -.
SGD; S000005990; BTS1.
GeneTree; ENSGT00390000010417; -.
HOGENOM; HOG000169461; -.
InParanoid; Q12051; -.
KO; K00804; -.
OMA; LEMCACK; -.
OrthoDB; EOG092C3Q3X; -.
BioCyc; MetaCyc:YPL069C-MONOMER; -.
BioCyc; YEAST:YPL069C-MONOMER; -.
BRENDA; 2.5.1.29; 984.
Reactome; R-SCE-191273; Cholesterol biosynthesis.
SABIO-RK; Q12051; -.
UniPathway; UPA00259; UER00368.
UniPathway; UPA00260; UER00369.
UniPathway; UPA00389; UER00564.
EvolutionaryTrace; Q12051; -.
PRO; PR:Q12051; -.
Proteomes; UP000002311; Chromosome XVI.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
GO; GO:0004311; F:farnesyltranstransferase activity; IDA:CACAO.
GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; IDA:CACAO.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0016114; P:terpenoid biosynthetic process; IDA:SGD.
Gene3D; 1.10.600.10; -; 1.
InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
InterPro; IPR000092; Polyprenyl_synt.
InterPro; IPR033749; Polyprenyl_synt_CS.
Pfam; PF00348; polyprenyl_synt; 1.
SUPFAM; SSF48576; SSF48576; 1.
PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
1: Evidence at protein level;
3D-structure; Carotenoid biosynthesis; Complete proteome; Cytoplasm;
Isoprene biosynthesis; Magnesium; Metal-binding; Protein transport;
Reference proteome; Transferase; Transport.
CHAIN 1 335 Geranylgeranyl pyrophosphate synthase.
/FTId=PRO_0000228139.
METAL 75 75 Magnesium 1.
{ECO:0000269|PubMed:16554305,
ECO:0000269|PubMed:17535895}.
METAL 75 75 Magnesium 2.
{ECO:0000269|PubMed:16554305,
ECO:0000269|PubMed:17535895}.
METAL 79 79 Magnesium 1.
{ECO:0000269|PubMed:16554305,
ECO:0000269|PubMed:17535895}.
METAL 79 79 Magnesium 2.
{ECO:0000269|PubMed:16554305,
ECO:0000269|PubMed:17535895}.
METAL 209 209 Magnesium 3.
{ECO:0000269|PubMed:16554305,
ECO:0000269|PubMed:17535895}.
BINDING 36 36 Isopentenyl diphosphate.
{ECO:0000269|PubMed:17535895}.
BINDING 39 39 Isopentenyl diphosphate.
{ECO:0000269|PubMed:17535895}.
BINDING 68 68 Isopentenyl diphosphate.
{ECO:0000269|PubMed:17535895}.
BINDING 84 84 Dimethylallyl diphosphate.
{ECO:0000269|PubMed:17535895}.
BINDING 85 85 Isopentenyl diphosphate.
{ECO:0000269|PubMed:17535895}.
BINDING 169 169 Dimethylallyl diphosphate.
{ECO:0000269|PubMed:17535895}.
BINDING 170 170 Dimethylallyl diphosphate.
{ECO:0000269|PubMed:17535895}.
BINDING 206 206 Dimethylallyl diphosphate.
{ECO:0000269|PubMed:17535895}.
BINDING 213 213 Dimethylallyl diphosphate.
{ECO:0000269|PubMed:17535895}.
BINDING 223 223 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 233 233 Dimethylallyl diphosphate.
{ECO:0000269|PubMed:17535895}.
SITE 107 107 Important for determining product chain
length.
MUTAGEN 7 7 E->G: No effect. Monomer; when associated
with G-8. {ECO:0000269|PubMed:19245203}.
MUTAGEN 8 8 L->G: Monomer and homodimer. Monomer;
when associated with G-7.
{ECO:0000269|PubMed:19245203}.
MUTAGEN 9 9 I->G: Mostly monomer. Exclusively
monomer; when associated with G-8.
Reduces enzyme activity 1000-fold.
{ECO:0000269|PubMed:19245203}.
MUTAGEN 107 107 Y->A: Reduced affinity for isopentenyl
diphosphate (IPP).
MUTAGEN 108 108 F->A: Reduced affinity for isopentenyl
diphosphate (IPP).
MUTAGEN 139 139 H->A: Reduced affinity for isopentenyl
diphosphate (IPP).
HELIX 1 9 {ECO:0000244|PDB:2E8V}.
HELIX 17 31 {ECO:0000244|PDB:2E8V}.
STRAND 32 34 {ECO:0000244|PDB:2E8X}.
HELIX 38 50 {ECO:0000244|PDB:2E8V}.
HELIX 54 78 {ECO:0000244|PDB:2E8V}.
STRAND 82 84 {ECO:0000244|PDB:2E8V}.
HELIX 90 93 {ECO:0000244|PDB:2E8V}.
HELIX 96 113 {ECO:0000244|PDB:2E8V}.
HELIX 114 117 {ECO:0000244|PDB:2E8V}.
HELIX 121 150 {ECO:0000244|PDB:2E8V}.
TURN 151 153 {ECO:0000244|PDB:2Z4V}.
HELIX 159 169 {ECO:0000244|PDB:2E8V}.
HELIX 171 184 {ECO:0000244|PDB:2E8V}.
HELIX 195 215 {ECO:0000244|PDB:2E8V}.
TURN 221 223 {ECO:0000244|PDB:2DH4}.
HELIX 227 230 {ECO:0000244|PDB:2E8V}.
HELIX 236 247 {ECO:0000244|PDB:2E8V}.
HELIX 251 263 {ECO:0000244|PDB:2E8V}.
HELIX 268 280 {ECO:0000244|PDB:2E8V}.
HELIX 284 300 {ECO:0000244|PDB:2E8V}.
HELIX 325 330 {ECO:0000244|PDB:2Z4V}.
TURN 331 333 {ECO:0000244|PDB:2Z4V}.
SEQUENCE 335 AA; 38651 MW; 4C7D6527FF29F157 CRC64;
MEAKIDELIN NDPVWSSQNE SLISKPYNHI LLKPGKNFRL NLIVQINRVM NLPKDQLAIV
SQIVELLHNS SLLIDDIEDN APLRRGQTTS HLIFGVPSTI NTANYMYFRA MQLVSQLTTK
EPLYHNLITI FNEELINLHR GQGLDIYWRD FLPEIIPTQE MYLNMVMNKT GGLFRLTLRL
MEALSPSSHH GHSLVPFINL LGIIYQIRDD YLNLKDFQMS SEKGFAEDIT EGKLSFPIVH
ALNFTKTKGQ TEQHNEILRI LLLRTSDKDI KLKLIQILEF DTNSLAYTKN FINQLVNMIK
NDNENKYLPD LASHSDTATN LHDELLYIID HLSEL


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