TPS_MATON
ID TPS_MATON Reviewed; 303 AA.
AC A0A7D0AGU9;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 1.
DT 03-AUG-2022, entry version 5.
DE RecName: Full=Terpene synthase {ECO:0000303|PubMed:31801241};
DE Short=EoTPS {ECO:0000303|PubMed:31801241};
DE EC=3.1.7.11 {ECO:0000269|PubMed:31801241};
GN Name=TPS {ECO:0000303|PubMed:31801241};
OS Matsumurasca onukii (Tea green leafhopper) (Empoasca onukii).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Membracoidea;
OC Cicadellidae; Typhlocybinae; Empoascini; Matsumurasca.
OX NCBI_TaxID=2912585;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=31801241; DOI=10.3390/biom9120808;
RA Zhou Y., Liu X., Yang Z.;
RT "Characterization of terpene synthase from tea green leafhopper being
RT involved in formation of geraniol in tea (camellia sinensis) leaves and
RT potential effect of geraniol on insect-derived endobacteria.";
RL Biomolecules 9:0-0(2019).
CC -!- FUNCTION: Terpene synthase that is able to convert geraniol diphosphate
CC to geraniol in tea leaves. {ECO:0000269|PubMed:31801241}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (2E)-geraniol + diphosphate;
CC Xref=Rhea:RHEA:32679, ChEBI:CHEBI:15377, ChEBI:CHEBI:17447,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=3.1.7.11;
CC Evidence={ECO:0000269|PubMed:31801241};
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 -!- 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; MH383159; QAX24808.1; -; mRNA.
DR SMR; A0A7D0AGU9; -.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Hydrolase; Isoprene biosynthesis; Magnesium; Metal-binding.
FT CHAIN 1..303
FT /note="Terpene synthase"
FT /id="PRO_0000455291"
FT MOTIF 69..73
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
SQ SEQUENCE 303 AA; 34983 MW; 732727CBDA324A33 CRC64;
MEGLVNNSGD KDLDEKLLQP FTYILQVPGK QIRAKLAHAF NYWLKIPNDK LNIVGEIIQM
LHNSSLLIDD IQDNSILRRG IPVAHSIYGV ASTINAANYV IFLAVEKVLR LEHPEATRVC
IDQLLELHRG QGIEIYWRDN FQCPSEDEYK LMTIRKTGGL FMLAIRLMQL FSESDADFTK
LAGILGLYFQ IRDDYCNLCL QEYSENKSFC EDLTEGKFSF PIIHAIRSRP DDRQVIQILR
QRTRDVEVKK YCVTLLEKFG SFSHTRETLA QLDREAREEV ARLGGNPFLE AILNDLLNWD
RTK
