ID   MTPS1_PINCO             Reviewed;         627 AA.
AC   R9QMY7;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Monoterpene synthase like 1, chloroplastic {ECO:0000303|PubMed:23679205};
DE            Short=PcTPS-mono1 {ECO:0000303|PubMed:23679205};
DE            EC=4.2.3.- {ECO:0000250|UniProtKB:R9QMW8};
DE   Flags: Precursor;
GN   Name=TPS-mono1 {ECO:0000303|PubMed:23679205};
OS   Pinus contorta (Shore pine) (Lodgepole pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=23679205; DOI=10.1186/1471-2229-13-80;
RA   Hall D.E., Yuen M.M.S., Jancsik S., Quesada A.L., Dullat H.K., Li M.,
RA   Henderson H., Arango-Velez A., Liao N.Y., Docking R.T., Chan S.K.,
RA   Cooke J.E.K., Breuil C., Jones S.J.M., Keeling C.I., Bohlmann J.;
RT   "Transcriptome resources and functional characterization of monoterpene
RT   synthases for two host species of the mountain pine beetle, lodgepole pine
RT   (Pinus contorta) and jack pine (Pinus banksiana).";
RL   BMC Plant Biol. 13:80-80(2013).
CC   -!- FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of
CC       monoterpene natural products included in conifer oleoresin secretions
CC       and volatile emissions; these compounds contribute to biotic and
CC       abiotic stress defense against herbivores and pathogens.
CC       {ECO:0000250|UniProtKB:R9QMW8}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC       {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC   -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC       {ECO:0000269|PubMed:23679205}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:23679205}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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. Tpsd subfamily.
CC       {ECO:0000305}.
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DR   EMBL; JQ240294; AFU73846.1; -; mRNA.
DR   UniPathway; UPA00213; -.
DR   UniPathway; UPA00924; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IDA:UniProtKB.
DR   CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR   Gene3D; 1.10.600.10; -; 1.
DR   Gene3D; 1.50.10.130; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR   InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR   InterPro; IPR001906; Terpene_synth_N.
DR   InterPro; IPR036965; Terpene_synth_N_sf.
DR   InterPro; IPR005630; Terpene_synthase_metal-bd.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   Pfam; PF01397; Terpene_synth; 1.
DR   Pfam; PF03936; Terpene_synth_C; 1.
DR   SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR   SUPFAM; SSF48239; SSF48239; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT   TRANSIT         1..50
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           51..627
FT                   /note="Monoterpene synthase like 1, chloroplastic"
FT                   /id="PRO_0000455030"
FT   MOTIF           378..382
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         378
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         378
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         382
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         382
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         530
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   627 AA;  71852 MW;  60B08AE9B336A5FC CRC64;
     MDLISVLPST SKSCVCMHKP LSSSTHKLKP FCRTIRILGM PRPRKSVLMA SSMSMSVNTL
     VSDDDIQRRT GGYHSNLWND DVIQFLSTPY GELAYRERGE RLIDEVRDIF SSMSLEDGEF
     SDLIQRLWMV DNVERLGIDR HFKNEIKSAL DYVYSYWSEK GIGCGTKSII TNLNSTALGF
     RTLPLHGYPV SADVLKHFRN QIGQFVSCPS ETEEDIRSMV NLYRASLIAF PGEEVMEEAE
     SFSEKYLKET LQKIPDCSLS REIGDVLEHG WHTNLPRFEA RNYIDVFGQD TKNMESNRKT
     EKLLELAKLE FNIFQSIQKT ELESLLRWWN DSGSPQITFT RHRHVEYYTL ASCIAFEPQH
     SGFRLGFAKA CHIITVLDDM YDLFGTVEEL KLFTAAIKRW DPSATDCLPQ YMKGIYMMVY
     NTVNEMSAEA QKAQGRDTLN YARQAWEVYL DSYMQEAKWI ATGYLPTFEE YLENGKVSSG
     HRVSALQPML TMDIPFPPHI LKEVDFPSNL NDLACAILRL RGDTRCYQED RARGEETSCI
     SCYMIDNPGA TEEDALNHLN VMISGVIKEL NWELLKPDSS VPISSKKINF DITRAFHYGY
     KYRDGYSVSS VETKSLVMRT LLEPVPL