TPS2_COFAR
ID TPS2_COFAR Reviewed; 572 AA.
AC R4YXW8;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Linalool synthase TPS2, 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 TPS2, 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=TPS2 {ECO:0000303|PubMed:23398891};
GN ORFNames=LOC113711778 {ECO:0000312|RefSeq:XP_027090779.1};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCM43928.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; HE985293; CCM43928.1; ALT_INIT; mRNA.
DR RefSeq; XP_027090779.1; XM_027234978.1.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000515148; Chromosome 10e.
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..27
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 28..572
FT /note="Linalool synthase TPS2, chloroplastic"
FT /id="PRO_0000455259"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 321..325
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 10..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 572 AA; 66141 MW; ED0FFEE81F259A66 CRC64;
EVEEPKTKIS ASTAEASSSR ISSAKMTADG TIKLGDQSPL KQSEKDHPVS WDFKLVQSLR
NEYADERYIS RSAMLDQEMN VVNLLELIDN LQRLGLSYHF EDKIRSILSG IYNTIKMRNP
EGLYATALEF RLRRQHGFYV PQEIFESFKD ENGDFNHSLC EDLKGLLYLY EASYLEKENE
SNLEMAREFT AKHLKKILKE KRIDQELEAL VQHALELPLH WRMMRLEARW FIDIYEARSD
RNPILLELAK LDFNIVQAIH QNDLECTLRW WSSTGLAEKL SFARDIMVEN FFWTVGTISD
PQHGNARRLL TKVAALVTAI DDVYDQYGTE DELELFTSVV ERWDVNSIDQ LPDYMKICFL
ALFNFVNEMA YDALKEEGVN IIPYLRKAWA DLCKAYLQEA KWFFSGHIPT LQQYLNNAWT
SISAPLVVVH AYFCVDYPIN KDHVEYLEKC HKIIRCSSMI IRLANDLGTS PESEVLKSAD
VPKSIQCYVK ETGACEEKAR EYLRFLIIEA WKQMNEAQTV DSPFSSTFKG FAVNVARMGQ
CMYQHGDGHA HQNSEPRDRI LSLLFEPISS FA
