ID GGPPS_RAT Reviewed; 300 AA. AC Q6F596; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 04-NOV-2026, entry version 144. DE RecName: Full=Geranylgeranyl pyrophosphate synthase; DE Short=GGPP synthase; DE Short=GGPPSase; DE EC=2.5.1.-; DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase; DE AltName: Full=Dimethylallyltranstransferase; DE EC=2.5.1.1; DE AltName: Full=Farnesyl diphosphate synthase; DE AltName: Full=Farnesyltranstransferase; DE EC=2.5.1.29; DE AltName: Full=Geranylgeranyl diphosphate synthase; DE AltName: Full=Geranyltranstransferase; DE EC=2.5.1.10; GN Name=Ggps1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC TISSUE=Testis; RX PubMed=15598886; DOI=10.1093/jb/mvh130; RA Matsumura Y., Kuzuguchi T., Sagami H.; RT "Relationship between intron 4b splicing of the rat geranylgeranyl RT diphosphate synthase gene and the active enzyme expression level."; RL J. Biochem. 136:301-312(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the trans-addition of the three molecules of IPP CC onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor CC of carotenoids and geranylated proteins. CC {ECO:0000250|UniProtKB:O95749}. CC -!- CATALYTIC ACTIVITY: CC Reaction=isopentenyl diphosphate + dimethylallyl diphosphate = (2E)- CC geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, CC ChEBI:CHEBI:128769; EC=2.5.1.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=isopentenyl diphosphate + (2E)-geranyl diphosphate = (2E,6E)- CC farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, CC ChEBI:CHEBI:175763; EC=2.5.1.10; CC -!- CATALYTIC ACTIVITY: CC Reaction=isopentenyl diphosphate + (2E,6E)-farnesyl diphosphate = CC (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; CC Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250}; CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; CC farnesyl diphosphate from geranyl diphosphate and isopentenyl CC diphosphate: step 1/1. CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl CC diphosphate: step 1/1. CC -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate CC biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and CC isopentenyl diphosphate: step 1/1. CC -!- SUBUNIT: Homohexamer; trimer of homodimers. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, perinuclear CC region {ECO:0000250|UniProtKB:O95749}. Cytoplasm, myofibril, sarcomere, CC Z line {ECO:0000250|UniProtKB:O95749}. CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB118237; BAD30051.1; -; Genomic_DNA. DR EMBL; AB118238; BAD30052.1; -; mRNA. DR EMBL; AB118239; BAD30053.1; -; mRNA. DR EMBL; AB118240; BAD30054.1; -; mRNA. DR EMBL; BC090327; AAH90327.1; -; mRNA. DR RefSeq; NP_001007627.1; NM_001007626.4. DR RefSeq; XP_038951449.1; XM_039095521.2. DR RefSeq; XP_038951450.1; XM_039095522.2. DR SMR; Q6F596; -. DR STRING; 10116.ENSRNOP00000073229; -. DR iPTMnet; Q6F596; -. DR PhosphoSitePlus; Q6F596; -. DR PaxDb; 10116-ENSRNOP00000073229; -. DR Ensembl; ENSRNOT00000095806.2; ENSRNOP00000094969.2; ENSRNOG00000016767.8. DR Ensembl; ENSRNOT00055017085; ENSRNOP00055013737; ENSRNOG00055010127. DR Ensembl; ENSRNOT00060025776; ENSRNOP00060020600; ENSRNOG00060015024. DR Ensembl; ENSRNOT00065035349; ENSRNOP00065028460; ENSRNOG00065020819. DR GeneID; 291211; -. DR KEGG; rno:291211; -. DR UCSC; RGD:1359680; rat. DR CTD; 9453; -. DR AGR; RGD:1359680; -. DR RGD; 1359680; Ggps1. DR eggNOG; KOG0777; Eukaryota. DR GeneTree; ENSGT00940000153498; -. DR InParanoid; Q6F596; -. DR OMA; AAAFNCW; -. DR OrthoDB; 6921389at2759; -. DR PhylomeDB; Q6F596; -. DR BRENDA; 2.5.1.29; 5301. DR Reactome; R-RNO-9969896; Lanosterol biosynthesis. DR UniPathway; UPA00259; UER00368. DR UniPathway; UPA00260; UER00369. DR UniPathway; UPA00389; UER00564. DR PRO; PR:Q6F596; -. DR Bgee; ENSRNOG00000016767; Expressed in thymus and 19 other cell types or tissues. DR ExpressionAtlas; Q6F596; baseline and differential. DR CDD; cd00685; Trans_IPPS_HT; 1. DR FunFam; 1.10.600.10:FF:000009; Geranylgeranyl pyrophosphate synthase; 1. DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf. DR InterPro; IPR000092; Polyprenyl_synt. DR InterPro; IPR033749; Polyprenyl_synt_CS. DR PANTHER; PTHR12001; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1. DR PANTHER; PTHR12001:SF44; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1. DR Pfam; PF00348; polyprenyl_synt; 1. DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1. DR SFLD; SFLDG01017; Polyprenyl_Transferase_Like; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:RGD. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0030018; C:Z disc; ISS:UniProtKB. DR GO; GO:0004337; F:(2E,6E)-farnesyl diphosphate synthase activity; ISO:RGD. DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004311; F:geranylgeranyl diphosphate synthase activity; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; ISO:RGD. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central. DR GO; GO:0006720; P:isoprenoid metabolic process; ISS:UniProtKB. DR GO; GO:0045337; P:trans, trans-farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Proteomes; UP000002494; Chromosome 17. DR AlphaFoldDB; Q6F596; -. DR FunCoup; Q6F596; 3025. PE 2: Evidence at transcript level; KW Acetylation; Cytoplasm; Isoprene biosynthesis; Lipid metabolism; Magnesium; KW Metal-binding; Reference proteome; Transferase. FT CHAIN 1..300 FT /note="Geranylgeranyl pyrophosphate synthase" FT /id="PRO_0000123964" FT BINDING 25 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 28 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 57 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 64 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 64 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 68 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 68 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 73 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT BINDING 74 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 151 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT BINDING 152 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT BINDING 185 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT BINDING 202 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT BINDING 212 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:O95749" SQ SEQUENCE 300 AA; 34778 MW; A3C47E3F9BB81876 CRC64; MEKTKEKAER ILLEPYKYLL QLPGKQVRTK LSQAFNHWLK VPEDKLQIII EVTEMLHNAS LLIDDIEDSS KLRRGFPVAH SIYGVPSVIN SANYVYFLGL EKVLTLDHPD AVKLFTRQLL ELHQGQGLDI YWRDTYTCPT EEEYKAMVLQ KTGGLFGLAV GLMQLFSDYK EDLKPLLDTL GLFFQIRDDY ANLHSKEYSE NKSFCEDLTE GKFSFPTIHA IWSRPESTQV QNILRQRTEN IDIKKYCVQY LEDVGSFEYT RYTLRELEAK AYKQIEACGG NPSLVALVKH LSKMFTEENE //