ID   FPPS_NEZVI              Reviewed;         403 AA.
AC   A0A386JVA3;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2018, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Farnesyl pyrophosphate synthase {ECO:0000305};
DE            Short=NvFPPS {ECO:0000303|PubMed:30267360};
DE            Short=NvIDS2 {ECO:0000303|PubMed:30267360};
DE            EC=2.5.1.68 {ECO:0000269|PubMed:30267360};
DE   AltName: Full=Farnesyl diphosphate synthase {ECO:0000303|PubMed:30267360};
GN   Name=FPPS {ECO:0000303|PubMed:30267360};
OS   Nezara viridula (Southern green stink bug) (Cimex viridulus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Pentatomomorpha; Pentatomoidea; Pentatomidae; Pentatominae; Nezara.
OX   NCBI_TaxID=85310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=30267360; DOI=10.1007/s10886-018-1019-0;
RA   Lancaster J., Lehner B., Khrimian A., Muchlinski A., Luck K.,
RA   Koellner T.G., Weber D.C., Gundersen-Rindal D.E., Tholl D.;
RT   "An IDS-type sesquiterpene synthase produces the pheromone precursor (z)-
RT   alpha-bisabolene in Nezara viridula.";
RL   J. Chem. Ecol. 45:187-197(2019).
CC   -!- FUNCTION: Farnesyl pyrophosphate synthase involved in pheromone
CC       biosynthesis by catalyzing the formation of (2Z,6E)-farnesyl
CC       diphosphate. {ECO:0000269|PubMed:30267360}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2Z,6E)-
CC         farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:23300,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC         ChEBI:CHEBI:162247; EC=2.5.1.68;
CC         Evidence={ECO:0000269|PubMed:30267360};
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: Pheromone biosynthesis. {ECO:0000269|PubMed:30267360}.
CC   -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC       the catalytic activity, presumably through binding to Mg(2+).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; MG748544; AYD76070.1; -; mRNA.
DR   SMR; A0A386JVA3; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033850; F:Z-farnesyl diphosphate synthase activity; IDA:UniProtKB.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0042811; P:pheromone biosynthetic process; IDA:UniProtKB.
DR   CDD; cd00685; Trans_IPPS_HT; 1.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR039702; FPS1-like.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
DR   PANTHER; PTHR11525; PTHR11525; 1.
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   Isoprene biosynthesis; Magnesium; Metal-binding; Transferase.
FT   CHAIN           1..403
FT                   /note="Farnesyl pyrophosphate synthase"
FT                   /id="PRO_0000455290"
FT   MOTIF           156..160
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         156
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         156
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         160
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         160
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
SQ   SEQUENCE   403 AA;  46000 MW;  FA76AA424917845D CRC64;
     MPLAKLCAKK LSSPLMKLCY PNLNGKLPFS NLSNILDNSS LKFHSCNPHI TCRGLSTVAL
     RPQTITKDDK RDFMAVFPDI VRDLTQLNPG ISDLSTLISK IMQYNVSGGK KVRGLTVVYS
     YRMLAPDHAL TPENIRLAQI LGWCVEMLQG FFLVIDDLAD QSITRRGRPC WYRNPDVGLR
     AGSDALLIQS GTFQLLQQHC KDREFYIDLV ELFLDAVRRT TYGQTLDHVS SFPNITHLTM
     DRYNFITKYK TSYYTFHLPV ATAMYMAGIY NTELHRQAKS VLLEMGHYFQ VQDDYLDVFG
     DEEVIGKIGT DIQEGKCTWL AIVAFQRASP SQREILESCY GSKDPEKIKK VKDTFIEIGV
     PAVFHAYEEE TYNLITRQIQ QLSQGLPHEL FLTLLHKTYG RKQ