TPS2_CANSA
ID TPS2_CANSA Reviewed; 615 AA.
AC A7IZZ2;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=(+)-alpha-pinene synthase, chloroplastic;
DE EC=4.2.3.121;
DE Flags: Precursor;
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], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL 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. The major
CC product is (+)-alpha-pinene.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (1R,5R)-alpha-pinene + diphosphate;
CC Xref=Rhea:RHEA:32575, ChEBI:CHEBI:28261, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.121; Evidence={ECO:0000269|Ref.1};
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=10.5 uM for Geranyl pyrophosphate {ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius. {ECO:0000269|Ref.1};
CC -!- PATHWAY: Terpene metabolism; (-)-alpha-pinene biosynthesis; (-)-alpha-
CC pinene 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; DQ839405; ABI21838.1; -; mRNA.
DR AlphaFoldDB; A7IZZ2; -.
DR SMR; A7IZZ2; -.
DR PRIDE; A7IZZ2; -.
DR UniPathway; UPA00985; UER00927.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0046248; P:alpha-pinene biosynthetic process; IEA:UniProtKB-UniPathway.
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..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..615
FT /note="(+)-alpha-pinene synthase, chloroplastic"
FT /id="PRO_0000363061"
FT MOTIF 367..371
FT /note="DDXXD motif"
FT BINDING 367
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 512
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 615 AA; 71842 MW; B2F7200C752522FB CRC64;
MHCMAVRHFA PSSSLSIFSS TNINNHFFGR EIFTPKTSNI TTKKSRSRPN CNPIQCSLAK
SPSSDTSTIV RRSANYDPPI WSFDFIQSLP CKYKGEPYTS RSNKLKEEVK KMLVGMENSL
VQLELIDTLQ RLGISYHFEN EIISILKEYF TNISTNKNPK YDLYATALEF RLLREYGYAI
PQEIFNDFKD ETGKFKASIK NDDIKGVLAL YEASFYVKNG ENILEEARVF TTEYLKRYVM
MIDQNIILND NMAILVRHAL EMPLHWRTIR AEAKWFIEEY EKTQDKNGTL LEFAKLDFNM
LQSIFQEDLK HVSRWWEHSE LGKNKMVYAR DRLVEAFLWQ VGVRFEPQFS HFRRISARIY
ALITIIDDIY DVYGTLEELE LFTKAVERWD AKTIHELPDY MKLPFFTLFN TVNEMAYDVL
EEHNFVTVEY LKNSWAELCR CYLEEAKWFY SGYKPTLKKY IENASLSIGG QIIFVYAFFS
LTKSITNEAL ESLQEGHHAA CRQGSLMLRL ADDLGTLSDE MKRGDVPKSI QCYMHDTGAS
EDEAREHIKF LISEIWKEMN DEDEYNSIFS KEFVQACKNL GRMSLFMYQH GDGHASQDSH
SRKRISDLII NPIPL
