TPS16_SOLLC
ID TPS16_SOLLC Reviewed; 553 AA.
AC G8H5N3; G5CV53;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Terpene synthase 16 {ECO:0000303|PubMed:21813655, ECO:0000303|PubMed:21818683};
DE Short=SlTPS16 {ECO:0000303|PubMed:21813655, ECO:0000303|PubMed:21818683};
GN Name=TPS16 {ECO:0000303|PubMed:21813655, ECO:0000303|PubMed:21818683};
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 [MRNA], PATHWAY, AND GENE FAMILY.
RC STRAIN=cv. Moneymaker;
RX PubMed=21818683; DOI=10.1007/s11103-011-9813-x;
RA Bleeker P.M., Spyropoulou E.A., Diergaarde P.J., Volpin H., De Both M.T.J.,
RA Zerbe P., Bohlmann J., Falara V., Matsuba Y., Pichersky E., Haring M.A.,
RA Schuurink R.C.;
RT "RNA-seq discovery, functional characterization, and comparison of
RT sesquiterpene synthases from Solanum lycopersicum and Solanum habrochaites
RT trichomes.";
RL Plant Mol. Biol. 77:323-336(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND GENE FAMILY.
RC STRAIN=cv. M82;
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: Sesquiterpene synthase involved in the biosynthesis of
CC volatile compounds (PubMed:21818683). No activity detected with geranyl
CC diphosphate (GPP) and farnesyl diphosphate (FPP) as substrates
CC (PubMed:21818683). {ECO:0000269|PubMed:21818683}.
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:21818683}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, trichomes and flowers.
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|UniProtKB:Q40577}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; JN402394; AEM23831.1; -; mRNA.
DR EMBL; JN412090; AEP82781.1; -; Genomic_DNA.
DR RefSeq; NP_001239042.2; NM_001252113.2.
DR GeneID; 100820703; -.
DR KEGG; sly:100820703; -.
DR OrthoDB; 360509at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; G8H5N3; baseline and differential.
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 2: Evidence at transcript level;
KW Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..553
FT /note="Terpene synthase 16"
FT /id="PRO_0000454693"
FT MOTIF 303..307
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 457
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 104
FT /note="G -> D (in Ref. 2; AEP82781)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="E -> Q (in Ref. 2; AEP82781)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="N -> S (in Ref. 2; AEP82781)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="I -> V (in Ref. 2; AEP82781)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 64521 MW; ABDA5467674589E7 CRC64;
MELCTQTVPA DHEVEITRRV GSHHPTVWGD HFLAYANLSG ASEEEEKQHE DLKEEVRKML
VMAPSNALEK LELINTIQCL GVAYHFEHEI ESYMCTHYEE YWIGDLHAIA LCFRLLRQQG
YRVSCDAYKK FTDDQGNFKI ELINDVHGML SLYEAAQFRV HGEEILDEAL NFTTTQLKLI
LPKLSNSPLA QQVANALKFP IKDGIVRVEA RKYISFYQQN QNHNQLLLNF AKLDFNILQM
LHKKELCDIT RWWKELEIVK TLPYVRDRLA EVYFWSLGVY FEPQYSTARK ILTKNISMIS
LIDDTYDIYG TLDELTLFTE AIERWNIDAS EQLQLPSYMK IIYCGLLDVY DEIKKDLANE
NKSFLINYSI IEMKKMVMAY FQEAKWYYGK TIPKMEEYMK NGISTSAYVQ IATTSWLGMG
NVATKDSFDW IVNEPPILVA SSIIARLLND LLSHEEEQKR GDAPSGVECY MKEYGVTKEE
AHIKIRNTIE NSWKDLYEEY FKVNGTIIPR VLLMCIINLA RVIEFIYKDE DAYTFPKNNL
KDVIYRILID PII
