ID CRTE_CERS4 Reviewed; 288 AA. AC P54976; Q3J195; Q9RFC5; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 3. DT 04-NOV-2026, entry version 134. DE RecName: Full=Geranylgeranyl diphosphate synthase; DE Short=GGPP synthase; DE EC=2.5.1.29; DE AltName: Full=Farnesyltranstransferase; GN Name=crtE; OrderedLocusNames=RHOS4_18710; ORFNames=RSP_0265; OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter OS sphaeroides). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rhodobacterales; Paracoccaceae; Cereibacter. OX NCBI_TaxID=272943; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7721699; DOI=10.1128/jb.177.8.2064-2073.1995; RA Lang H.P., Cogdell R.J., Takaichi S., Hunter C.N.; RT "Complete DNA sequence, specific Tn5 insertion map, and gene assignment of RT the carotenoid biosynthesis pathway of Rhodobacter sphaeroides."; RL J. Bacteriol. 177:2064-2073(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10648776; DOI=10.1093/nar/28.4.862; RA Choudhary M., Kaplan S.; RT "DNA sequence analysis of the photosynthesis region of Rhodobacter RT sphaeroides 2.4.1."; RL Nucleic Acids Res. 28:862-867(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC RC 12203 / NCIMB 8253 / ATH 2.4.1.; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.; RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. 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:0000250}. 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; 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 -!- SEQUENCE CAUTION: CC Sequence=ABA79439.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AJ010302; CAB38744.1; -; Genomic_DNA. DR EMBL; AF195122; AAF24294.1; -; Genomic_DNA. DR EMBL; CP000143; ABA79439.2; ALT_INIT; Genomic_DNA. DR PIR; S49625; S49625. DR PIR; T50750; T50750. DR RefSeq; WP_011338112.1; NC_007493.2. DR AlphaFoldDB; P54976; -. DR SMR; P54976; -. DR STRING; 272943.RSP_0265; -. DR EnsemblBacteria; ABA79439; ABA79439; RSP_0265. DR GeneID; 3719275; -. DR GeneID; 48979870; -. DR KEGG; rsp:RSP_0265; -. DR PATRIC; fig|272943.9.peg.2209; -. DR eggNOG; COG0142; Bacteria. DR OMA; ACCEMGA; -. DR OrthoDB; 9805316at2; -. DR PhylomeDB; P54976; -. DR UniPathway; UPA00389; UER00564. DR Proteomes; UP000002703; Chromosome 1. DR GO; GO:0004311; F:geranylgeranyl diphosphate synthase activity; ISS:UniProtKB. DR GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; ISS: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 3: Inferred from homology; KW Carotenoid biosynthesis; Chlorophyll biosynthesis; Isoprene biosynthesis; KW Magnesium; Metal-binding; Photosynthesis; Reference proteome; Transferase. FT CHAIN 1..288 FT /note="Geranylgeranyl diphosphate synthase" FT /id="PRO_0000123995" FT BINDING 43 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 73 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 80 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 80 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 86 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 86 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 91 FT /ligand="(2E,6E)-farnesyl diphosphate" FT /ligand_id="ChEBI:CHEBI:175763" FT /evidence="ECO:0000250" FT BINDING 92 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 170 FT /ligand="(2E,6E)-farnesyl diphosphate" FT /ligand_id="ChEBI:CHEBI:175763" FT /evidence="ECO:0000250" FT BINDING 171 FT /ligand="(2E,6E)-farnesyl diphosphate" FT /ligand_id="ChEBI:CHEBI:175763" FT /evidence="ECO:0000250" FT BINDING 205 FT /ligand="(2E,6E)-farnesyl diphosphate" FT /ligand_id="ChEBI:CHEBI:175763" FT /evidence="ECO:0000250" FT CONFLICT 53 FT /note="A -> R (in Ref. 1; CAB38744)" FT /evidence="ECO:0000305" FT CONFLICT 57 FT /note="D -> S (in Ref. 1; CAB38744)" FT /evidence="ECO:0000305" FT CONFLICT 60 FT /note="A -> V (in Ref. 2; AAF24294)" FT /evidence="ECO:0000305" FT CONFLICT 123 FT /note="R -> G (in Ref. 1; CAB38744)" FT /evidence="ECO:0000305" FT CONFLICT 128 FT /note="Q -> R (in Ref. 1; CAB38744)" FT /evidence="ECO:0000305" FT CONFLICT 234 FT /note="N -> S (in Ref. 1; CAB38744)" FT /evidence="ECO:0000305" FT CONFLICT 247 FT /note="R -> G (in Ref. 1; CAB38744)" FT /evidence="ECO:0000305" FT CONFLICT 264 FT /note="G -> A (in Ref. 1; CAB38744)" FT /evidence="ECO:0000305" FT CONFLICT 277 FT /note="E -> D (in Ref. 1; CAB38744)" FT /evidence="ECO:0000305" SQ SEQUENCE 288 AA; 30229 MW; FAB8D98C8557A8A2 CRC64; MAFEQRIEAA MAAAIARGQG SEAPSKLATA LDYAVTPGGA RIRPTLLLSV ATACGDDRPA LSDAAAVALE LIHCASLVHD DLPCFDDAEI RRGKPTVHRA YSEPLAILTG DSLIVMGFEV LARAAADQPQ RALQLVTALA VRTGMPMGIC AGQGWESESQ INLSAYHRAK TGALFIAATQ MGAIAAGYEA EPWEELGARI GEAFQVADDL RDALCDAETL GKPAGQDEIH ARPNAVREYG VEGAAKRLKD ILGGAIASIP SCPGEAMLAE MVRRYAEKIV PAQVAARV //