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TPS3_COFAR
ID   TPS3_COFAR              Reviewed;         596 AA.
AC   R4YZC3;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2013, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Linalool synthase TPS3, chloroplastic {ECO:0000303|PubMed:23398891};
DE            EC=4.2.3.- {ECO:0000269|PubMed:23398891};
DE   AltName: Full=Cis-ocimene synthase TPS2, chloroplastic {ECO:0000303|PubMed:23398891};
DE            EC=4.2.3.- {ECO:0000269|PubMed:23398891};
DE   AltName: Full=Myrcene synthase TPS3, chloroplastic {ECO:0000303|PubMed:23398891};
DE            EC=4.2.3.15 {ECO:0000269|PubMed:23398891};
DE   AltName: Full=Trans-ocimene synthase TPS2, chloroplastic {ECO:0000303|PubMed:23398891};
DE            EC=4.2.3.106 {ECO:0000269|PubMed:23398891};
DE   Flags: Precursor;
GN   Name=TPS3 {ECO:0000303|PubMed:23398891};
GN   ORFNames=LOC113713511 {ECO:0000312|RefSeq:XP_027093045.1},
GN   LOC113713556 {ECO:0000312|RefSeq:XP_027093111.1};
OS   Coffea arabica (Arabian coffee).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC   Bertiereae - Coffeeae clade; Coffeeae; Coffea.
OX   NCBI_TaxID=13443;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Catuai Red; TISSUE=Flower, Fruit, and Seed;
RX   PubMed=23398891; DOI=10.1016/j.phytochem.2013.01.005;
RA   Del Terra L., Lonzarich V., Asquini E., Navarini L., Graziosi G.,
RA   Suggi Liverani F., Pallavicini A.;
RT   "Functional characterization of three Coffea arabica L. monoterpene
RT   synthases: insights into the enzymatic machinery of coffee aroma.";
RL   Phytochemistry 89:6-14(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Caturra red;
RA   Zimin A.V., Yepes M., Maldonado C.E., Navarro L., Kovaka S., Pertea M.,
RA   Gaitan A., Aldwinckle H.;
RT   "The Coffea arabica cultivar Caturra genome provides a strong foundation
RT   for breeding and functional genomics studies in coffee.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Monoterpene synthase (mono-TPS) involved in the biosynthesis
CC       of monoterpenes natural products, constituent of coffee beverage aroma
CC       (PubMed:23398891). Catalyzes the conversion of (2E)-geranyl diphosphate
CC       (GPP) into linalool and beta-myrcene, and, as minor products, cis-
CC       ocimene and trans-ocimene (PubMed:23398891). Not able to use
CC       geranylgeranyl pyrophosphate (GGPP) and farnesyl pyrophosphate (FPP) as
CC       substrates (PubMed:23398891). {ECO:0000269|PubMed:23398891}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate;
CC         Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58057; EC=4.2.3.15;
CC         Evidence={ECO:0000269|PubMed:23398891};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966;
CC         Evidence={ECO:0000269|PubMed:23398891};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate + H2O = diphosphate + linalool;
CC         Xref=Rhea:RHEA:68708, ChEBI:CHEBI:15377, ChEBI:CHEBI:17580,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58057;
CC         Evidence={ECO:0000269|PubMed:23398891};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68709;
CC         Evidence={ECO:0000269|PubMed:23398891};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = (Z)-beta-ocimene + diphosphate;
CC         Xref=Rhea:RHEA:68824, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC         ChEBI:CHEBI:87574; Evidence={ECO:0000269|PubMed:23398891};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68825;
CC         Evidence={ECO:0000269|PubMed:23398891};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = (E)-beta-ocimene + diphosphate;
CC         Xref=Rhea:RHEA:32691, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC         ChEBI:CHEBI:64280; EC=4.2.3.106;
CC         Evidence={ECO:0000269|PubMed:23398891};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32692;
CC         Evidence={ECO:0000269|PubMed:23398891};
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: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:23398891}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in flowers and fruits.
CC       {ECO:0000269|PubMed:23398891}.
CC   -!- DEVELOPMENTAL STAGE: Observed at early stages of flowers and fruits
CC       development (PubMed:23398891). Expressed in flowers and drupes at 10
CC       weeks after pollination, and, at low levels, in fruits at 15 weeks of
CC       ripening (PubMed:23398891). {ECO:0000269|PubMed:23398891}.
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. Tpsb subfamily.
CC       {ECO:0000305}.
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DR   EMBL; HE985294; CCM43929.1; -; mRNA.
DR   RefSeq; XP_027093045.1; XM_027237244.1.
DR   RefSeq; XP_027093111.1; XM_027237310.1.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000515148; Chromosome 10c.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0050551; F:myrcene synthase activity; IDA:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0016098; P:monoterpenoid metabolic 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; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..39
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..596
FT                   /note="Linalool synthase TPS3, chloroplastic"
FT                   /id="PRO_0000455260"
FT   MOTIF           345..349
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         345
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         345
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         349
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         349
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         489
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         493
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   596 AA;  68839 MW;  C8A170F9DE2AD5A8 CRC64;
     MISSLNPLFT THRSGVIAQQ FFASSAAASI NSVSSLKIAA CSKTKLVDQS PLRQSGNHQL
     LSSDFNHLQS LKNDYAEEKY KSRCEVLKEQ VKMMLDQEMD VVNQLELIDD LQRLGLSYHF
     GDEITSVLSG IYNRKSMNKM RNQWGLYATC LEFRLLRQHG FDVSQEIFDC FKDEKGDFRP
     SLCEDSKGML YLYEASYLES ENEESNLEMA RRFAAKTLKK NLDEKRVDQD LVALVQHALE
     LPLHWRMMRL EARWFIDIYE ERSNRNPILL ELAKLDFNIV QAAHQNDLTY TLRWWRSTCL
     AEKLTFARDM MVENFFWTVG IISDPQRGNG RRILTKVVAL ITAIDDIYDC YGTLDELEVF
     TTAVERWDVN SIDQLPDCMK ICFLALYNFV NEMAYDALKE QGVNIIPYLR KSWADLCKAY
     LQEAKWFFSG EVPTLQQYLN NAWISISAPA FLVHAYFCVD YPINKDHLQY LDNYHKIIRC
     SAMILRLTND LGTSPESEVL NVGDVPKSIR CYMKETGACE EKAREHLRFL ITEAWKQMEE
     AQTLDSPFSS TFNGIAVNLA RMGLCMYQHG DGHGHQNSEP RDRILSLLFE PICCLA
 
 
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