ID CRTE_PSEVU Reviewed; 307 AA. AC P22873; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 02-SEP-2026, entry version 101. DE RecName: Full=Geranylgeranyl diphosphate synthase; DE Short=GGPP synthase; DE EC=2.5.1.29; DE AltName: Full=Farnesyltranstransferase; GN Name=crtE; OS Pseudescherichia vulneris (Escherichia vulneris). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Pseudescherichia. OX NCBI_TaxID=566; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 39368 / Eho10; RX PubMed=2263648; DOI=10.1073/pnas.87.24.9975; RA Armstrong G.A., Alberti M., Hearst J.E.; RT "Conserved enzymes mediate the early reactions of carotenoid biosynthesis RT in nonphotosynthetic and photosynthetic prokaryotes."; RL Proc. Natl. Acad. Sci. U.S.A. 87:9975-9979(1990). RN [2] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=1495965; DOI=10.1073/pnas.89.15.6761; RA Math S.K., Hearst J.E., Poulter C.D.; RT "The crtE gene in Erwinia herbicola encodes geranylgeranyl diphosphate RT synthase."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6761-6764(1992). CC -!- FUNCTION: Catalyzes the condensation of farnesyl diphosphate (FPP) and CC isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate CC (GGPP) needed for biosynthesis of carotenoids and diterpenes. CC {ECO:0000269|PubMed:1495965}. 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 Evidence={ECO:0000269|PubMed:1495965}; 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; geranylgeranyl diphosphate CC biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and CC isopentenyl diphosphate: step 1/1. 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; M38424; AAA24819.1; -; Genomic_DNA. DR EMBL; M87280; AAA64977.1; -; Genomic_DNA. DR PIR; C39273; C39273. DR AlphaFoldDB; P22873; -. DR SMR; P22873; -. DR BioCyc; MetaCyc:MONOMER-18246; -. DR UniPathway; UPA00389; UER00564. DR GO; GO:0004311; F:geranylgeranyl diphosphate synthase activity; IDA:UniProtKB. DR GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; IDA:UniProtKB. DR CDD; cd00685; Trans_IPPS_HT; 1. DR FunFam; 1.10.600.10:FF:000001; Geranylgeranyl diphosphate 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; PTHR43281; FARNESYL DIPHOSPHATE SYNTHASE; 1. DR PANTHER; PTHR43281:SF1; FARNESYL DIPHOSPHATE SYNTHASE; 1. DR Pfam; PF00348; polyprenyl_synt; 1. DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1. PE 1: Evidence at protein level; KW Carotenoid biosynthesis; Isoprene biosynthesis; Magnesium; Metal-binding; KW Transferase. FT CHAIN 1..307 FT /note="Geranylgeranyl diphosphate synthase" FT /id="PRO_0000123992" FT BINDING 52 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 55 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 86 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 93 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 93 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 99 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 99 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 104 FT /ligand="(2E,6E)-farnesyl diphosphate" FT /ligand_id="ChEBI:CHEBI:175763" FT /evidence="ECO:0000250" FT BINDING 105 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 188 FT /ligand="(2E,6E)-farnesyl diphosphate" FT /ligand_id="ChEBI:CHEBI:175763" FT /evidence="ECO:0000250" FT BINDING 189 FT /ligand="(2E,6E)-farnesyl diphosphate" FT /ligand_id="ChEBI:CHEBI:175763" FT /evidence="ECO:0000250" FT BINDING 226 FT /ligand="(2E,6E)-farnesyl diphosphate" FT /ligand_id="ChEBI:CHEBI:175763" FT /evidence="ECO:0000250" SQ SEQUENCE 307 AA; 33242 MW; 6A534C6194CE9F59 CRC64; MVSGSKAGVS PHREIEVMRQ SIDDHLAGLL PETDSQDIVS LAMREGVMAP GKRIRPLLML LAARDLRYQG SMPTLLDLAC AVELTHTASL MLDDMPCMDN AELRRGQPTT HKKFGESVAI LASVGLLSKA FGLIAATGDL PGERRAQAVN ELSTAVGVQG LVLGQFRDLN DAALDRTPDA ILSTNHLKTG ILFSAMLQIV AIASASSPST RETLHAFALD FGQAFQLLDD LRDDHPETGK DRNKDAGKST LVNRLGADAA RQKLREHIDS ADKHLTFACP QGGAIRQFMH LWFGHHLADW SPVMKIA //