ID   TPS_MURHI               Reviewed;         385 AA.
AC   A0A343W969;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2018, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Sesquiterpene alcohol synthase {ECO:0000303|PubMed:30139915};
DE            Short=MhTPS {ECO:0000303|PubMed:30139915};
DE            EC=2.5.1.- {ECO:0000269|PubMed:30139915};
GN   Name=TPS {ECO:0000303|PubMed:30139915};
OS   Murgantia histrionica (Harlequin bug).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Pentatomomorpha; Pentatomoidea; Pentatomidae; Pentatominae; Murgantia.
OX   NCBI_TaxID=460024;
RN   [1] {ECO:0000312|EMBL:AVZ23977.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP   SPECIFICITY, AND MUTAGENESIS OF 77-SER--TRP-80 AND 118-MET-SER-119.
RX   PubMed=30139915; DOI=10.1073/pnas.1800008115;
RA   Lancaster J., Khrimian A., Young S., Lehner B., Luck K., Wallingford A.,
RA   Ghosh S.K.B., Zerbe P., Muchlinski A., Marek P.E., Sparks M.E.,
RA   Tokuhisa J.G., Tittiger C., Koellner T.G., Weber D.C.,
RA   Gundersen-Rindal D.E., Kuhar T.P., Tholl D.;
RT   "De novo formation of an aggregation pheromone precursor by an isoprenyl
RT   diphosphate synthase-related terpene synthase in the harlequin bug.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:E8634-E8641(2018).
CC   -!- FUNCTION: Sesquiterpene alcohol synthase that catalyzes the formation
CC       of (1S,6S,7R)-sesquipiperitol, a terpene intermediate in murgantiol
CC       biosynthesis, a male-released aggregation pheromone.
CC       {ECO:0000269|PubMed:30139915}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + H2O = (1S,6S,7R)-
CC         sesquipiperitol + diphosphate; Xref=Rhea:RHEA:68852,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:173121,
CC         ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:30139915};
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:30139915}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in tissues lining the
CC       cuticle of the abdominal sternites of mature males.
CC       {ECO:0000269|PubMed:30139915}.
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; MG662378; AVZ23977.1; -; mRNA.
DR   SMR; A0A343W969; -.
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; IDA:UniProtKB.
DR   GO; GO:0042811; P:pheromone biosynthetic 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..385
FT                   /note="Sesquiterpene alcohol synthase"
FT                   /id="PRO_0000455286"
FT   MOTIF           123..127
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         123
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         123
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         127
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         127
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   MUTAGEN         77..80
FT                   /note="SDAW->KKVR: Abolished sesquiterpene alcohol synthase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:30139915"
FT   MUTAGEN         118..119
FT                   /note="MS->FF: Abolished sesquiterpene alcohol synthase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:30139915"
SQ   SEQUENCE   385 AA;  44303 MW;  A7C394E2DAD3C40D CRC64;
     MVSIAAKSLP KLSGAVFGQF SRRKQLIQRH WLDTRTDQYY DVLRRIVVPE CKNIASDVPE
     YPERIEKLLY YTNPAFSDAW NFTTELIYRT VADESHQTEE NITKMYLIRA TMDLLFTMSA
     VLDDISDRSE FRKGKKGWHM ICQGGESTAL YDGTQMGLFP LYLLKQYFKN DPGYSRLLET
     VVMTYIKLTI GQTIDVLGQF KKSPSMAEYK RINYYKAGQF VAAGSELAVI HAGITSQDLI
     DKTVEIFTIA GQIIQTWDDF NDYYSSSEQN GKLSCDFMNA GTTWVSAKAM EVFTPSQAVK
     FMECYGSDDQ SKMKTVQELY DEIDMPKLYT EYVLENYNRC ETLIKELPHD RLREACSSYM
     EWLVVRETPD EDSEHKVALC LNISG