TPS1_CANSA
ID TPS1_CANSA Reviewed; 622 AA.
AC A7IZZ1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=(-)-limonene synthase, chloroplastic;
DE EC=4.2.3.16;
DE AltName: Full=(-)-(4S)-limonene synthase;
DE AltName: Full=CsTPS1;
DE Flags: Precursor;
GN Name=TPS1;
OS Cannabis sativa (Hemp) (Marijuana).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Cannabis.
OX NCBI_TaxID=3483;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=cv. Skunk; TISSUE=Trichome gland;
RA Guennewich N., Page J.E., Koellner T.G., Degenhardt J., Kutchan T.M.;
RT "Functional expression and characterization of trichome-specific (-)-
RT limonene synthase and a (+)-alpha-pinene synthase from Cannabis sativa.";
RL Nat. Prod. Commun. 2:223-232(2007).
CC -!- FUNCTION: Involved in monoterpene (C10) olefins biosynthesis.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.8 uM for Geranyl pyrophosphate {ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius. {ECO:0000269|Ref.1};
CC -!- PATHWAY: Terpene metabolism; (4S)-limonene biosynthesis; (4S)-limonene
CC from geranyl diphosphate: step 1/1.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Trichome. {ECO:0000269|Ref.1}.
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 -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; DQ839404; ABI21837.1; -; mRNA.
DR AlphaFoldDB; A7IZZ1; -.
DR SMR; A7IZZ1; -.
DR UniPathway; UPA00984; UER00925.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050552; F:(4S)-limonene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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; Transit peptide.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 61..622
FT /note="(-)-limonene synthase, chloroplastic"
FT /id="PRO_0000363060"
FT MOTIF 373..377
FT /note="DDXXD motif"
FT BINDING 373
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 518
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 522
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 526
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 622 AA; 72385 MW; 12156C07DC94D133 CRC64;
MQCIAFHQFA SSSSLPIWSS IDNRFTPKTS ITSISKPKPK LKSKSNLKSR SRSSTCYSIQ
CTVVDNPSST ITNNSDRRSA NYGPPIWSFD FVQSLPIQYK GESYTSRLNK LEKDVKRMLI
GVENSLAQLE LIDTIQRLGI SYRFENEIIS ILKEKFTNNN DNPNPNYDLY ATALQFRLLR
QYGFEVPQEI FNNFKNHKTG EFKANISNDI MGALGLYEAS FHGKKGESIL EEARIFTTKC
LKKYKLMSSS NNNNMTLISL LVNHALEMPL QWRITRSEAK WFIEEIYERK QDMNPTLLEF
AKLDFNMLQS TYQEELKVLS RWWKDSKLGE KLPFVRDRLV ECFLWQVGVR FEPQFSYFRI
MDTKLYVLLT IIDDMHDIYG TLEELQLFTN ALQRWDLKEL DKLPDYMKTA FYFTYNFTNE
LAFDVLQEHG FVHIEYFKKL MVELCKHHLQ EAKWFYSGYK PTLQEYVENG WLSVGGQVIL
MHAYFAFTNP VTKEALECLK DGHPNIVRHA SIILRLADDL GTLSDELKRG DVPKSIQCYM
HDTGASEDEA REHIKYLISE SWKEMNNEDG NINSFFSNEF VQVCQNLGRA SQFIYQYGDG
HASQNNLSKE RVLGLIITPI PM
