GGPPS_RAT
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 03-AUG-2022, entry version 128.
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=dimethylallyl diphosphate + isopentenyl 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=(2E)-geranyl diphosphate + isopentenyl 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=(2E,6E)-farnesyl diphosphate + isopentenyl 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}.
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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_001007626.2.
DR AlphaFoldDB; Q6F596; -.
DR SMR; Q6F596; -.
DR STRING; 10116.ENSRNOP00000022483; -.
DR iPTMnet; Q6F596; -.
DR PhosphoSitePlus; Q6F596; -.
DR PaxDb; Q6F596; -.
DR Ensembl; ENSRNOT00000022483; ENSRNOP00000022483; ENSRNOG00000016767.
DR GeneID; 291211; -.
DR KEGG; rno:291211; -.
DR UCSC; RGD:1359680; rat.
DR CTD; 9453; -.
DR RGD; 1359680; Ggps1.
DR eggNOG; KOG0777; Eukaryota.
DR GeneTree; ENSGT00940000153498; -.
DR InParanoid; Q6F596; -.
DR OMA; FYSKAFF; -.
DR OrthoDB; 981769at2759; -.
DR PhylomeDB; Q6F596; -.
DR TreeFam; TF300101; -.
DR BRENDA; 2.5.1.29; 5301.
DR Reactome; R-RNO-191273; Cholesterol biosynthesis.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR UniPathway; UPA00389; UER00564.
DR PRO; PR:Q6F596; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000016767; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; Q6F596; baseline and differential.
DR Genevisible; Q6F596; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004311; F:farnesyltranstransferase activity; ISS:UniProtKB.
DR GO; GO:0004337; F:geranyltranstransferase activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006720; P:isoprenoid metabolic process; ISS:UniProtKB.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
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
