TPS1_CANOD
ID TPS1_CANOD Reviewed; 590 AA.
AC A0A7G5KLV0;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 1.
DT 03-AUG-2022, entry version 6.
DE RecName: Full=Monoterepene synthase TPS1, chloropastic {ECO:0000305};
DE AltName: Full=Alpha-terpinene synthase TPS1 {ECO:0000305};
DE EC=4.2.3.115 {ECO:0000269|PubMed:25956881};
DE AltName: Full=Beta-pinene synthase TPS1 {ECO:0000305};
DE EC=4.2.3.- {ECO:0000269|PubMed:25956881};
DE AltName: Full=Beta-thujene synthase TPS1 {ECO:0000305};
DE EC=4.2.3.177 {ECO:0000269|PubMed:25956881};
DE AltName: Full=Sabinene synthase TPS1 {ECO:0000305};
DE EC=4.2.3.- {ECO:0000269|PubMed:25956881};
DE AltName: Full=Terpene synthase 1 {ECO:0000303|PubMed:25956881};
DE Short=CoTPS1 {ECO:0000303|PubMed:25956881};
DE Flags: Precursor;
GN Name=TPS1 {ECO:0000303|PubMed:25956881};
OS Cananga odorata (Ylang-ylang tree) (Uvaria odorata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Magnoliales; Annonaceae;
OC Ambavioideae; Cananga.
OX NCBI_TaxID=13393;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND MOTIF.
RX PubMed=25956881; DOI=10.1093/jxb/erv196;
RA Jin J., Kim M.J., Dhandapani S., Tjhang J.G., Yin J.L., Wong L.,
RA Sarojam R., Chua N.H., Jang I.C.;
RT "The floral transcriptome of ylang ylang (Cananga odorata var. fruticosa)
RT uncovers biosynthetic pathways for volatile organic compounds and a
RT multifunctional and novel sesquiterpene synthase.";
RL J. Exp. Bot. 66:3959-3975(2015).
CC -!- FUNCTION: Monoterpene synthase involved in the biosynthesis of volatile
CC organic compounds (PubMed:25956881). Mediates the conversion of (2E)-
CC geranyl diphosphate (GPP) into beta-thujene, sabinene, beta-pinene and
CC alpha-terpinene (PubMed:25956881). Does not use (2E,6E)-farnesyl
CC diphosphate (FPP) as substrate (PubMed:25956881).
CC {ECO:0000269|PubMed:25956881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = beta-thujene + diphosphate;
CC Xref=Rhea:RHEA:54072, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:138047; EC=4.2.3.177;
CC Evidence={ECO:0000269|PubMed:25956881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54073;
CC Evidence={ECO:0000269|PubMed:25956881};
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:25956881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68637;
CC Evidence={ECO:0000269|PubMed:25956881};
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:25956881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25667;
CC Evidence={ECO:0000269|PubMed:25956881};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = alpha-terpinene + diphosphate;
CC Xref=Rhea:RHEA:32563, ChEBI:CHEBI:10334, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.115;
CC Evidence={ECO:0000269|PubMed:25956881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32564;
CC Evidence={ECO:0000269|PubMed:25956881};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q40577}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:25956881}.
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|PubMed:25956881}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; MN230105; QMW48842.1; -; mRNA.
DR UniPathway; UPA00213; -.
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: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..42
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 43..590
FT /note="Monoterepene synthase TPS1, chloropastic"
FT /id="PRO_0000455178"
FT MOTIF 341..345
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:25956881"
FT BINDING 304
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 341
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 341
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 341
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 345
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 483
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 486
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 486
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 490
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 494
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 590 AA; 67802 MW; 2EA504A0753719CE CRC64;
MALNTFLHFP PCSLSSFSCA VPKLPLAIFH KTMARQIRCP RASSQTSEPA LARRSANFQP
TIWTNDFIQS LNSDYSSDVY VQRIEKLKKS VRQSLEEADG PLAQLELIDD LQRLGVGRLF
EREINEMLNG IYMDYKETQA QWNLHFTSMY FRLLRARGFD VSPEIFSRFM DETGNFQTSI
SNDPIGMLSL YEASYLCMPG ETTLDEAQAF TCKHLKYWKE KDVHPTIALQ IEHALELPIH
WRMPRLDSRW YIKLYEEKEG TRPLLLELAK LDFNMVQSAH QTELRKVSRW WSEFGLAEKA
SFARDRLMEG YQWAIGTVFE PEFGQCREVL AKLAQLIAVI DDMYDVYGSP DELELFTDAV
DRWNINTIEG LPDYMKLCFL SIYNTTNQGG YEFLKDHGVD IIPHLRKAWA DYCKALRTEA
RWVNSKYTPT LDEYLNNAYT SASGPLILIH AFFFSGQEPW KEAIDCFVSS NKDIIRLSAT
IFRLTDDLET SAEEIERGDV PKSIQCYMHE AGASEAVSRA HIRGKISEVW RKMNKYLTAP
ATRHKTFNAA AFNLARTSTC VYLYGDGYGV PNGKNKENIT SLTVEPIVLE
