TPS3_SOLLC
ID TPS3_SOLLC Reviewed; 607 AA.
AC G1JUH1;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=(-)-camphene/tricyclene synthase, chloroplastic;
DE Short=SlTPS3;
DE EC=4.2.3.105;
DE EC=4.2.3.117;
DE AltName: Full=(4S)-limonene synthase;
DE EC=4.2.3.16;
DE AltName: Full=Myrcene synthase;
DE EC=4.2.3.15;
DE Flags: Precursor;
GN Name=TPS3;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND INDUCTION BY JASMONATE.
RX PubMed=21813655; DOI=10.1104/pp.111.179648;
RA Falara V., Akhtar T.A., Nguyen T.T.H., Spyropoulou E.A., Bleeker P.M.,
RA Schauvinhold I., Matsuba Y., Bonini M.E., Schilmiller A.L., Last R.L.,
RA Schuurink R.C., Pichersky E.;
RT "The tomato terpene synthase gene family.";
RL Plant Physiol. 157:770-789(2011).
CC -!- FUNCTION: Monoterpene synthase that catalyzes the formation of camphene
CC and tricyclene from geranyl diphosphate. Produces also lower amounts of
CC limonene and beta-myrcene, and traces of several other monoterpenoids.
CC {ECO:0000269|PubMed:21813655}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + tricyclene;
CC Xref=Rhea:RHEA:32687, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:64266; EC=4.2.3.105;
CC Evidence={ECO:0000269|PubMed:21813655};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (1S,4R)-camphene + diphosphate;
CC Xref=Rhea:RHEA:25484, ChEBI:CHEBI:89, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.117;
CC Evidence={ECO:0000269|PubMed:21813655};
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:21813655};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (4S)-limonene + diphosphate;
CC Xref=Rhea:RHEA:12869, ChEBI:CHEBI:15383, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.16;
CC Evidence={ECO:0000269|PubMed:21813655};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in stem trichomes, green fruits and
CC roots. {ECO:0000269|PubMed:21813655}.
CC -!- INDUCTION: Up-regulated by jasmonic acid treatment.
CC {ECO:0000269|PubMed:21813655}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; JN408284; AEM05853.1; -; Genomic_DNA.
DR RefSeq; NP_001295307.1; NM_001308378.1.
DR AlphaFoldDB; G1JUH1; -.
DR SMR; G1JUH1; -.
DR STRING; 4081.Solyc01g105870.2.1; -.
DR PaxDb; G1JUH1; -.
DR PRIDE; G1JUH1; -.
DR GeneID; 101245212; -.
DR KEGG; sly:101245212; -.
DR eggNOG; ENOG502QUH3; Eukaryota.
DR HOGENOM; CLU_003125_7_2_1; -.
DR InParanoid; G1JUH1; -.
DR OrthoDB; 401091at2759; -.
DR PhylomeDB; G1JUH1; -.
DR BRENDA; 4.2.3.105; 3101.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; G1JUH1; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050552; F:(4S)-limonene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102703; F:camphene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050551; F:myrcene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102701; F:tricyclene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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..28
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 29..607
FT /note="(-)-camphene/tricyclene synthase, chloroplastic"
FT /id="PRO_0000418828"
FT MOTIF 355..359
FT /note="DDXXD motif"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 505
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 509
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 607 AA; 70652 MW; 7E33C0B084A0C019 CRC64;
MSIFSTRYLV TPFSSFSPPK AFVSKACSLS TGQPLNYSPN ISTNIISSSN GIINPIRRSG
NYEPTMWNYE YIQSTHNHHV GEKYMKRFNE LKAEMKKHLM MMLHEESQEL EKLELIDNLQ
RLGVSYHFKD EIIQILRSIH DQSSSEATSA NSLYYTALKF RILRQHGFYI SQDILNDFKD
EQGHFKQSLC KDTKGLLQLY EASFLSTKSE TSTLLESANT FAMSHLKNYL NGGDEENNWM
VKLVRHALEV PLHCMMLRVE TRWYIDIYEN IPNANPLLIE LAKLDFNFVQ AMHQQELRNL
SRWWKKSMLA EKLPFARDRI VEAFQWITGM IFESQENEFC RIMLTKVTAM ATVIDDIYDV
YGTLDELEIF THAIQRMEIK AMDELPHYMK LCYLALFNTS SEIAYQVLKE QGINIMPYLT
KSWADLSKSY LQEARWYYSG YTPSLDEYME NAWISVGSLV MVVNAFFLVT NPITKEVLEY
LFSNKYPDII RWPATIIRLT DDLATSSNEM KRGDVPKSIQ CYMKENGASE EEARKHINLM
IKETWKMINT AQHDNSLFCE KFMGCAVNIA RTGQTIYQHG DGHGIQNYKI QNRISKLFFE
PITISMP
