ID GGPPS_YEAST Reviewed; 335 AA. AC Q12051; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 68. DE RecName: Full=Geranylgeranyl pyrophosphate synthetase; DE Short=GGPP synthetase; DE Short=GGPPSase; DE AltName: Full=Geranylgeranyl diphosphate synthase; DE AltName: Full=BET2 suppressor protein 1; DE Includes: DE RecName: Full=Dimethylallyltranstransferase; DE EC=2.5.1.1; DE Includes: DE RecName: Full=Geranyltranstransferase; DE EC=2.5.1.10; DE Includes: DE RecName: Full=Farnesyltranstransferase; DE EC=2.5.1.29; GN Name=BTS1; OrderedLocusNames=YPL069C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RX MEDLINE=95394944; PubMed=7665600; DOI=10.1074/jbc.270.37.21958; RA Jiang Y., Proteau P., Poulter D., Ferro-Novick S.; RT "BTS1 encodes a geranylgeranyl diphosphate synthase in Saccharomyces RT cerevisiae."; RL J. Biol. Chem. 270:21793-21799(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=97313271; PubMed=9169875; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., RA Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., RA Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., RA Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., RA Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., RA Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., RA Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., RA Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., RA Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., RA Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., RA Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., RA Zollner A., Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., RA Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., RA Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., RA Kolodner R.D., LaBaer J.; RT "Approaching a complete repository of sequence-verified protein- RT encoding clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [5] RP FUNCTION. RX PubMed=15296494; DOI=10.1111/j.1600-0854.2004.00213.x; RA Shiflett S.L., Vaughn M.B., Huynh D., Kaplan J., McVey Ward D.; RT "Bph1p, the Saccharomyces cerevisiae homologue of CHS1/beige, RT functions in cell wall formation and protein sorting."; RL Traffic 5:700-710(2004). CC -!- FUNCTION: Catalyzes the trans-addition of the 3 molecules of IPP CC onto DMAPP to form geranylgeranyl pyrophosphate. Required for the CC membrane attachment of YPT1 and SEC4. May be involved in vesicle CC trafficking and protein sorting. CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl CC diphosphate = diphosphate + geranyl diphosphate. CC -!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate CC = diphosphate + trans,trans-farnesyl diphosphate. CC -!- CATALYTIC ACTIVITY: Trans,trans-farnesyl diphosphate + isopentenyl CC diphosphate = diphosphate + geranylgeranyl diphosphate. CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl-PP biosynthesis; CC farnesyl-PP from geranyl-PP and isopentenyl-PP: step 1/1. CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl-PP biosynthesis; CC geranyl-PP from dimethylallyl-PP and isopentenyl-PP: step 1/1. CC -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl-PP biosynthesis; CC geranylgeranyl-PP from farnesyl-PP and isopentenyl-PP: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the FPP/GGPP synthetase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U39205; AAB68296.1; -; Genomic_DNA. DR EMBL; U31632; AAA83262.1; -; Genomic_DNA. DR EMBL; AY692852; AAT92871.1; -; Genomic_DNA. DR PIR; S60921; S60921. DR RefSeq; NP_015256.1; -. DR PDB; 2DH4; X-ray; 1.98 A; A/B=1-335. DR PDB; 2E8T; X-ray; 2.13 A; A/B=1-335. DR PDB; 2E8U; X-ray; 2.08 A; A/B=1-335. DR PDB; 2E8V; X-ray; 1.80 A; A/B=1-335. DR PDB; 2E8W; X-ray; 2.35 A; A/B=1-335. DR PDB; 2E8X; X-ray; 2.04 A; A/B=1-335. DR PDB; 2E90; X-ray; 2.55 A; A/B=1-335. DR PDB; 2E91; X-ray; 2.14 A; A/B=1-335. DR PDB; 2E92; X-ray; 2.31 A; A/B=1-335. DR PDB; 2E93; X-ray; 2.12 A; A/B=1-335. DR PDB; 2E94; X-ray; 2.18 A; A/B=1-335. DR PDB; 2E95; X-ray; 2.20 A; A/B=1-335. DR PDB; 2Z4V; X-ray; 1.86 A; A/B=1-335. DR PDB; 2Z4W; X-ray; 2.45 A; A/B=1-335. DR PDB; 2Z4X; X-ray; 1.90 A; A/B=1-335. DR PDB; 2Z4Y; X-ray; 2.10 A; A/B=1-335. DR PDB; 2Z4Z; X-ray; 2.09 A; A/B=1-335. DR PDB; 2Z50; X-ray; 2.01 A; A/B=1-335. DR PDB; 2Z52; X-ray; 2.13 A; A/B=1-335. DR PDB; 2Z78; X-ray; 2.10 A; A/B=1-335. DR PDB; 2Z7H; X-ray; 2.08 A; A/B=1-335. DR PDB; 2Z7I; X-ray; 2.10 A; A/B=1-335. DR PDB; 2ZEU; X-ray; 2.00 A; A/B=1-335. DR PDB; 2ZEV; X-ray; 2.23 A; A/B=1-335. DR PDBsum; 2DH4; -. DR PDBsum; 2E8T; -. DR PDBsum; 2E8U; -. DR PDBsum; 2E8V; -. DR PDBsum; 2E8W; -. DR PDBsum; 2E8X; -. DR PDBsum; 2E90; -. DR PDBsum; 2E91; -. DR PDBsum; 2E92; -. DR PDBsum; 2E93; -. DR PDBsum; 2E94; -. DR PDBsum; 2E95; -. DR PDBsum; 2Z4V; -. DR PDBsum; 2Z4W; -. DR PDBsum; 2Z4X; -. DR PDBsum; 2Z4Y; -. DR PDBsum; 2Z4Z; -. DR PDBsum; 2Z50; -. DR PDBsum; 2Z52; -. DR PDBsum; 2Z78; -. DR PDBsum; 2Z7H; -. DR PDBsum; 2Z7I; -. DR PDBsum; 2ZEU; -. DR PDBsum; 2ZEV; -. DR IntAct; Q12051; 3. DR Ensembl; YPL069C; Saccharomyces cerevisiae. DR GeneID; 856036; -. DR GenomeReviews; U00094_GR; YPL069C. DR KEGG; sce:YPL069C; -. DR NMPDR; fig|4932.3.peg.6389; -. DR CYGD; YPL069c; -. DR SGD; S000005990; BTS1. DR HOGENOM; Q12051; -. DR OMA; Q12051; GMLHTAS. DR BioCyc; MetaCyc:MON-13701; -. DR BRENDA; 2.5.1.1; 250. DR BRENDA; 2.5.1.10; 250. DR BRENDA; 2.5.1.29; 250. DR NextBio; 980968; -. DR GermOnline; YPL069C; Saccharomyces cerevisiae. DR GO; GO:0005739; C:mitochondrion; IDA:SGD. DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:EC. DR GO; GO:0004311; F:farnesyltranstransferase activity; IDA:SGD. DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:EC. DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR000092; Polyprenyl_synt. DR InterPro; IPR017446; Polyprenyl_synth-rel. DR InterPro; IPR008949; Terpenoid_synth. DR Gene3D; G3DSA:1.10.600.10; Terpenoid_synth; 1. DR PANTHER; PTHR12001; Polyprenyl_synt; 1. DR Pfam; PF00348; polyprenyl_synt; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHET_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHET_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Carotenoid biosynthesis; Complete proteome; Cytoplasm; KW Isoprene biosynthesis; Multifunctional enzyme; Protein transport; KW Transferase; Transport. FT CHAIN 1 335 Geranylgeranyl pyrophosphate synthetase. FT /FTId=PRO_0000228139. FT ACT_SITE 169 169 By similarity. FT HELIX 1 9 FT HELIX 17 30 FT HELIX 36 50 FT HELIX 54 78 FT STRAND 82 84 FT HELIX 90 94 FT HELIX 96 114 FT HELIX 121 150 FT HELIX 159 169 FT HELIX 171 184 FT HELIX 195 219 FT TURN 221 223 FT HELIX 227 231 FT HELIX 236 248 FT HELIX 251 263 FT HELIX 268 280 FT HELIX 284 300 FT HELIX 324 330 FT HELIX 332 334 SQ 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 //