ID   TPS_NEZVI               Reviewed;         378 AA.
AC   A0A386JV86;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2018, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=IDS-type sesquiterpene synthase {ECO:0000303|PubMed:30267360};
DE            Short=NvIDS1 {ECO:0000303|PubMed:30267360};
DE            Short=NvTPS {ECO:0000303|PubMed:30267360};
DE            EC=2.5.1.- {ECO:0000269|PubMed:30267360};
GN   Name=TPS {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, PATHWAY, AND
RP   TISSUE SPECIFICITY.
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: Sesquiterpene alcohol synthase that catalyzes the formation
CC       of the pheromone precursor (Z)-alpha-bisabolene from (2Z,6E)-farnesyl
CC       diphosphate. {ECO:0000269|PubMed:30267360}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2Z,6E)-farnesyl diphosphate = (Z)-alpha-bisabolene +
CC         diphosphate; Xref=Rhea:RHEA:68844, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:49241, ChEBI:CHEBI:162247;
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   -!- TISSUE SPECIFICITY: Highly expressed in male epidermal tissue
CC       associated with the cuticle of ventral sternites.
CC       {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 terpene synthase family. {ECO:0000305}.
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DR   EMBL; MG748543; AYD76069.1; -; mRNA.
DR   SMR; A0A386JV86; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0042811; P:pheromone biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0006714; P:sesquiterpenoid metabolic process; IDA:UniProtKB.
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   PANTHER; PTHR11525; PTHR11525; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Isoprene biosynthesis; Magnesium; Metal-binding; Transferase.
FT   CHAIN           1..378
FT                   /note="IDS-type sesquiterpene synthase"
FT                   /id="PRO_0000455287"
FT   MOTIF           120..124
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         124
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         124
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
SQ   SEQUENCE   378 AA;  43223 MW;  7CCF22A5AA0B032A CRC64;
     MAARAPVHLR GFIARVALNK KNLHARHKLD TDIDKYYYTL HNVIIPDFMD MVKEIPGYPE
     RIKKCVAHTT PSYFEGWAFS TELIYKTVAD KQHQTERNLE KCRIIRALMD MSYAMAGILD
     DYVDKGEFRR GKKVWASVCE GGQEAAIYDS IAVTYLMSLM VKRHFGTDPG YSKLIELFNM
     VPGTAAIGNT LDILDRHDTN YYDDTMWKHS VQNKAANTVF PAATAGLIHA GVLCDDLLDR
     TSEVFGYTGH LFQVWDDFME HYAVKEQSGK GAPDTKYNAK TWATLTAMAH FNEAQAKEFK
     ACYGSTDPAK RSRVRELYDE VNLRGLYIDY LRNTYMVVEE KISKIPDPRI QSACRSYMDW
     LLVEPPQDEE EAESVLNN