TPS1_COFAR
ID TPS1_COFAR Reviewed; 606 AA.
AC A0A6P6W6H5; R4YVJ5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 1.
DT 03-AUG-2022, entry version 7.
DE RecName: Full=Limonene synthase, chloroplastic {ECO:0000303|PubMed:23398891};
DE EC=4.2.3.- {ECO:0000269|PubMed:23398891};
DE AltName: Full=Alpha-pinene synthase, chloroplastic {ECO:0000303|PubMed:23398891};
DE EC=4.2.3.- {ECO:0000269|PubMed:23398891};
DE AltName: Full=Beta-farnesene synthase, chloroplastic {ECO:0000305|PubMed:23398891};
DE EC=4.2.3.47 {ECO:0000269|PubMed:23398891};
DE AltName: Full=Beta-myrcene synthase, chloroplastic {ECO:0000303|PubMed:23398891};
DE EC=4.2.3.15 {ECO:0000269|PubMed:23398891};
DE AltName: Full=Beta-pinene synthase, chloroplastic {ECO:0000303|PubMed:23398891};
DE EC=4.2.3.- {ECO:0000269|PubMed:23398891};
DE AltName: Full=Sabinene synthase, chloroplastic {ECO:0000303|PubMed:23398891};
DE EC=4.2.3.- {ECO:0000269|PubMed:23398891};
DE AltName: Full=Terpinolene synthase, chloroplastic {ECO:0000303|PubMed:23398891};
DE EC=4.2.3.113 {ECO:0000269|PubMed:23398891};
DE Flags: Precursor;
GN Name=TPS1 {ECO:0000303|PubMed:23398891};
GN ORFNames=LOC113729710 {ECO:0000312|RefSeq:XP_027109762.1};
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] OF 13-606, FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, TISSUE 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 limonene, beta-pinene, sabinene and beta-myrcene, and, as
CC minor products, alpha-pinene and alpha-terpinolene (PubMed:23398891).
CC Can also, with a low efficiency, use farnesyl pyrophosphate (FPP) as
CC substrate to produce beta-farnesene (PubMed:23398891). Not able to use
CC geranylgeranyl pyrophosphate (GGPP) as substrate (PubMed:23398891).
CC {ECO:0000269|PubMed:23398891}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (E)-beta-farnesene +
CC diphosphate; Xref=Rhea:RHEA:27425, ChEBI:CHEBI:10418,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.47;
CC Evidence={ECO:0000269|PubMed:23398891};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27426;
CC Evidence={ECO:0000269|PubMed:23398891};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + limonene;
CC Xref=Rhea:RHEA:68640, ChEBI:CHEBI:15384, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:23398891};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68641;
CC Evidence={ECO:0000269|PubMed:23398891};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = beta-pinene + diphosphate;
CC Xref=Rhea:RHEA:25666, ChEBI:CHEBI:33019, ChEBI:CHEBI:50025,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:23398891};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25667;
CC Evidence={ECO:0000269|PubMed:23398891};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + sabinene;
CC Xref=Rhea:RHEA:68636, ChEBI:CHEBI:33019, ChEBI:CHEBI:50027,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:23398891};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68637;
CC Evidence={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 = alpha-pinene + diphosphate;
CC Xref=Rhea:RHEA:25662, ChEBI:CHEBI:33019, ChEBI:CHEBI:36740,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:23398891};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25663;
CC Evidence={ECO:0000269|PubMed:23398891};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene;
CC Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.113;
CC Evidence={ECO:0000269|PubMed:23398891};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501;
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: Confined to fruits. {ECO:0000269|PubMed:23398891}.
CC -!- DEVELOPMENTAL STAGE: Observed during fruits development 25 weeks after
CC pollination. {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=CCM43927.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; HE985292; CCM43927.1; ALT_INIT; mRNA.
DR RefSeq; XP_027109762.1; XM_027253961.1.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000515148; Chromosome 2e.
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:0050550; F:pinene synthase activity; IDA:UniProtKB.
DR GO; GO:0080015; F:sabinene synthase activity; IDA:UniProtKB.
DR GO; GO:0046248; P:alpha-pinene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0046250; P:limonene biosynthetic process; IDA:UniProtKB.
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; 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 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..38
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 39..606
FT /note="Limonene synthase, chloroplastic"
FT /id="PRO_0000455258"
FT MOTIF 357..361
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 500
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 504
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 508
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 422
FT /note="R -> K (in Ref. 1; CCM43927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 606 AA; 69977 MW; 38ADE0E627341634 CRC64;
MAIINLPVPT NSSSEVNKHN HLRSCLPSGR ATFTTLSAAA MRSATMAAAN VREQSGQKQQ
LINRRSGNYE APLWEFDYIQ SLKNEYAGDI YVSRANELKE QVKMMLDEED MKLLDCMELV
DGLERLGLAY HFEGRINRLL SSDYKAIHEG NHQRNKEDLY AAALEFRIFR QNGFNVPQDI
FNDFITEDGE FDESLSEDTM GLLSLYEASF LSLEGEATLD LAREFTTKHL NNYLGKENTD
QNLRILVYHA LELPLRWRAP RIEARWYIDA YERSPNVNPT LLELAKIDFN IVQAIHQQDL
KHVSWWWKNI RIAEKLTFIR DRIVENFFWA IGAVFEPQYG SCRRMLTKVF ALITMIDDIY
DVYGTLEELE LFTDAVDRWD VKAIDQLPDY MRVGYLGFFN SINEMAYDAL KEQGVHIVEY
LRKVWADLCK AYLQEAKWYY AGYTPTVEEY LENAWVSMSV PVMLMHAYAG VTNPMNKEAM
DVLDTHDIVR CSSYLLRFAD DLGTSPGEMK RGDVPKLVQC YMKEAGCSEE ESREHVWFLL
RETWKKMNKD SEWAESPFSK TFVTAAKNFG RVALVMYQYG DGHGLHSNPE AKDRILASLF
SPVPPA
