TPS32_SOLLC
ID TPS32_SOLLC Reviewed; 548 AA.
AC G5CV45;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Viridiflorene synthase {ECO:0000303|PubMed:21813655};
DE EC=4.2.3.88 {ECO:0000269|PubMed:21813655};
DE AltName: Full=Terpene synthase 32 {ECO:0000303|PubMed:21813655};
DE Short=SlTPS32 {ECO:0000303|PubMed:21813655};
DE EC=4.2.3.- {ECO:0000305};
GN Name=TPS32 {ECO:0000303|PubMed:21813655};
GN OrderedLocusNames=Solyc01g101180 {ECO:0000305};
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 {ECO:0000312|Proteomes:UP000004994};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
CC -!- FUNCTION: Sesquiterpene synthase involved in the production of
CC viridiflorene from (E,E)-farnesyl diphosphate. Can also use (Z,Z)-FPP
CC to make several unidentified sesquiterpenes.
CC {ECO:0000269|PubMed:21813655}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + viridiflorene;
CC Xref=Rhea:RHEA:31811, ChEBI:CHEBI:33019, ChEBI:CHEBI:63444,
CC ChEBI:CHEBI:175763; EC=4.2.3.88;
CC Evidence={ECO:0000269|PubMed:21813655};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in stem and leaf trichomes. Detected in
CC roots, fruits and flowers. {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; JN412081; AEP82773.1; -; Genomic_DNA.
DR RefSeq; NP_001308023.1; NM_001321094.1.
DR AlphaFoldDB; G5CV45; -.
DR SMR; G5CV45; -.
DR STRING; 4081.Solyc01g101180.2.1; -.
DR PaxDb; G5CV45; -.
DR PRIDE; G5CV45; -.
DR GeneID; 101264071; -.
DR KEGG; sly:101264071; -.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR HOGENOM; CLU_003125_7_2_1; -.
DR InParanoid; G5CV45; -.
DR OrthoDB; 360509at2759; -.
DR PhylomeDB; G5CV45; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000004994; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016838; F:carbon-oxygen lyase activity, acting on phosphates; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0045339; P:farnesyl diphosphate catabolic process; IDA:UniProtKB.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
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 Cytoplasm; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..548
FT /note="Viridiflorene synthase"
FT /id="PRO_0000434412"
FT MOTIF 301..305
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 444
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 448
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 452
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 548 AA; 63367 MW; 04F3C0C88EF7356C CRC64;
MALLNNQDEI VRPVANFSPS LWGDRFHSFS LDNQVADKYA QQIETLKEQT RSLLSDAACG
TTLAEKLNLI DIVERLGLAY HFEKQIEDML DQIYKADPNF EAHDLNTLSL QFRILRQHGY
NISQKIFSRF QDANGKFKES LSNDIKGLLN LYEASHVRTH GEDILEEALA FSTAHLESAA
PHLKSPLSKQ VTHALEQSLH KSIPRVETRY FISIYEEEEF KNDVLLRFAK LDYNLLQMLH
KQELSEVSRW WKDLDFVTTL PYARDRAVEC YFWTMGVYAE PQYSQARVML AKTIAMISIV
DDTFDAYGIV KELEVYTDAI QRWDISQMDR LPEYMKVSFK ALLDLYEDYE KELSKDGRSD
VVQYAKERMK EIVRNYFVEA KWFIEGYMPP VSEYLSNALA TSTYYLLTTT SYLGVKSATK
EDFEWLAKNP KILEANVTLC RVVDDIATYE VEKGRGQIAT GIECYMRDYG VSTQVAMDKF
QEMAEIAWKD VNEGILRPTP VSTEILTRIL NLARIIDVTY KHNQDGYTHP EKVLKPHIIA
LLVDSIEI
