CRTE_SYNP2
ID CRTE_SYNP2 Reviewed; 302 AA.
AC B1XJV9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase {ECO:0000303|PubMed:32523588};
DE Short=GGPP synthase;
DE Short=GGPPS {ECO:0000303|PubMed:32523588};
DE EC=2.5.1.29 {ECO:0000269|PubMed:32523588};
DE AltName: Full=Dimethylallyltranstransferase;
DE EC=2.5.1.1 {ECO:0000269|PubMed:32523588};
DE AltName: Full=Geranylgeranyl diphosphate synthase;
DE AltName: Full=Geranyltranstransferase;
DE EC=2.5.1.10 {ECO:0000269|PubMed:32523588};
GN Name=crtE {ECO:0000303|PubMed:32523588, ECO:0000312|EMBL:ACA99087.1};
GN OrderedLocusNames=SYNPCC7002_A1085 {ECO:0000312|EMBL:ACA99087.1};
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:6SXL, ECO:0007744|PDB:6SXN}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 9-300, FUNCTION, CATALYTIC
RP ACTIVITY, PATHWAY, SUBUNIT, AND MUTAGENESIS OF MET-87; SER-88 AND VAL-161.
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RX PubMed=32523588; DOI=10.3389/fpls.2020.00589;
RA Feng Y., Morgan R.M.L., Fraser P.D., Hellgardt K., Nixon P.J.;
RT "Crystal Structure of Geranylgeranyl Pyrophosphate Synthase (CrtE) Involved
RT in Cyanobacterial Terpenoid Biosynthesis.";
RL Front. Plant Sci. 11:589-589(2020).
CC -!- FUNCTION: Catalyzes the sequential condensation of three molecules of
CC isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to
CC yield geranylgeranyl diphosphate (GGPP). Thereby, is a key enzyme for
CC the biosynthesis of terpenenoids. {ECO:0000269|PubMed:32523588}.
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 Evidence={ECO:0000269|PubMed:32523588};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22409;
CC Evidence={ECO:0000305|PubMed:32523588};
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 Evidence={ECO:0000269|PubMed:32523588};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19362;
CC Evidence={ECO:0000305|PubMed:32523588};
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 Evidence={ECO:0000269|PubMed:32523588};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC Evidence={ECO:0000305|PubMed:32523588};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P14324};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324};
CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC diphosphate: step 1/1. {ECO:0000269|PubMed:32523588}.
CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC diphosphate: step 1/1. {ECO:0000269|PubMed:32523588}.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate
CC biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and
CC isopentenyl diphosphate: step 1/1. {ECO:0000269|PubMed:32523588}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:32523588}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; CP000951; ACA99087.1; -; Genomic_DNA.
DR RefSeq; WP_012306710.1; NC_010475.1.
DR PDB; 6SXL; X-ray; 2.50 A; A=9-300, B=11-300.
DR PDB; 6SXN; X-ray; 2.66 A; A=9-299, B/C/D=9-297, E=3-300, F=9-300.
DR PDBsum; 6SXL; -.
DR PDBsum; 6SXN; -.
DR SMR; B1XJV9; -.
DR STRING; 32049.SYNPCC7002_A1085; -.
DR EnsemblBacteria; ACA99087; ACA99087; SYNPCC7002_A1085.
DR KEGG; syp:SYNPCC7002_A1085; -.
DR eggNOG; COG0142; Bacteria.
DR HOGENOM; CLU_014015_0_0_3; -.
DR OMA; CEGQALD; -.
DR BRENDA; 2.5.1.29; 6187.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR UniPathway; UPA00389; UER00564.
DR Proteomes; UP000001688; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 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 1: Evidence at protein level;
KW 3D-structure; Isoprene biosynthesis; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..302
FT /note="Geranylgeranyl pyrophosphate synthase"
FT /id="PRO_0000454933"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT SITE 87
FT /note="Plays an important role in controlling prenyl chain
FT elongation"
FT /evidence="ECO:0000269|PubMed:32523588"
FT SITE 88
FT /note="Plays an important role in controlling prenyl chain
FT elongation"
FT /evidence="ECO:0000269|PubMed:32523588"
FT MUTAGEN 87
FT /note="M->A: Forms the longer C25-geranylfarnesyl
FT pyrophosphate (GFPP) as the major product."
FT /evidence="ECO:0000269|PubMed:32523588"
FT MUTAGEN 87
FT /note="M->Y: Can only generate C15-farnesyl pyrophosphate
FT (FPP) as the final product."
FT /evidence="ECO:0000269|PubMed:32523588"
FT MUTAGEN 88
FT /note="S->F: Can only generate C15-farnesyl pyrophosphate
FT (FPP) as the final product. Also produces some C10-geranyl
FT pyrophosphate (GPP)."
FT /evidence="ECO:0000269|PubMed:32523588"
FT MUTAGEN 161
FT /note="V->M: Produces similar amounts of FPP and GGPP."
FT /evidence="ECO:0000269|PubMed:32523588"
FT HELIX 13..31
FT /evidence="ECO:0007829|PDB:6SXL"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:6SXL"
FT HELIX 55..66
FT /evidence="ECO:0007829|PDB:6SXL"
FT HELIX 71..93
FT /evidence="ECO:0007829|PDB:6SXL"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:6SXL"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6SXL"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:6SXL"
FT HELIX 115..134
FT /evidence="ECO:0007829|PDB:6SXL"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6SXL"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:6SXL"
FT HELIX 160..168
FT /evidence="ECO:0007829|PDB:6SXL"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:6SXN"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:6SXL"
FT HELIX 191..204
FT /evidence="ECO:0007829|PDB:6SXL"
FT HELIX 208..235
FT /evidence="ECO:0007829|PDB:6SXL"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:6SXL"
FT HELIX 262..279
FT /evidence="ECO:0007829|PDB:6SXL"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:6SXL"
FT HELIX 288..298
FT /evidence="ECO:0007829|PDB:6SXL"
SQ SEQUENCE 302 AA; 32477 MW; 97E8E839A1131E84 CRC64;
MVVADAHTQG FSLAQYLQEQ KTIVETALDQ SLVITEPVTI YEAMRYSLLA GGKRLRPILC
LAACEMLGGT AAMAMNTACA LEMIHTMSLI HDDLPAMDND DLRRGKPTNH KVYGEDIAIL
AGDALLSYAF EYVARTPDVP AERLLQVIVR LGQAVGAEGL VGGQVVDLES EGKTDVAVET
LNFIHTHKTG ALLEVCVTAG AILAGAKPEE VQLLSRYAQN IGLAFQIVDD ILDITATAEE
LGKTAGKDLE AQKVTYPSLW GIEKSQAEAQ KLVAEAIASL EPYGEKANPL KALAEYIVNR
KN
