TPSVS_VITVI
ID TPSVS_VITVI Reviewed; 556 AA.
AC Q6Q3H2; C1JXK7;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Valencene synthase;
DE Short=VvVal;
DE EC=4.2.3.73 {ECO:0000269|PubMed:15464152, ECO:0000269|PubMed:19359488};
DE AltName: Full=7-epi-alpha-selinene synthase;
DE EC=4.2.3.86 {ECO:0000269|PubMed:15464152, ECO:0000269|PubMed:19359488};
GN Name=ValCS;
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Gewuerztraminer;
RX PubMed=15464152; DOI=10.1016/j.phytochem.2004.08.017;
RA Lucker J., Bowen P., Bohlmann J.;
RT "Vitis vinifera terpenoid cyclases: functional identification of two
RT sesquiterpene synthase cDNAs encoding (+)-valencene synthase and (-)-
RT germacrene D synthase and expression of mono- and sesquiterpene synthases
RT in grapevine flowers and berries.";
RL Phytochemistry 65:2649-2659(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Gewuerztraminer;
RA Steinmetz A.A., Lommele A., Drescher B., Driesel A.J.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Cabernet Sauvignon; TISSUE=Flower;
RX PubMed=19359488; DOI=10.1073/pnas.0901387106;
RA Martin D.M., Toub O., Chiang A., Lo B.C., Ohse S., Lund S.T., Bohlmann J.;
RT "The bouquet of grapevine (Vitis vinifera L. cv. Cabernet Sauvignon)
RT flowers arises from the biosynthesis of sesquiterpene volatiles in pollen
RT grains.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:7245-7250(2009).
CC -!- FUNCTION: Involved in the biosynthesis of valencene, a major volatile
CC emitted from flowers of grapevine. Can use farnesyl diphosphate as
CC substrate, but not geranyl diphosphate or geranylgeranyl diphosphate.
CC Produces mainly (+)-valencene and (-)-7-epi-alpha-selinene along with
CC five minor products. {ECO:0000269|PubMed:15464152,
CC ECO:0000269|PubMed:19359488}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-valencene + diphosphate;
CC Xref=Rhea:RHEA:29511, ChEBI:CHEBI:33019, ChEBI:CHEBI:61700,
CC ChEBI:CHEBI:175763; EC=4.2.3.73;
CC Evidence={ECO:0000269|PubMed:15464152, ECO:0000269|PubMed:19359488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-7-epi-alpha-selinene +
CC diphosphate; Xref=Rhea:RHEA:30383, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:62224, ChEBI:CHEBI:175763; EC=4.2.3.86;
CC Evidence={ECO:0000269|PubMed:15464152, ECO:0000269|PubMed:19359488};
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 -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19359488}.
CC Note=Localizes close to lipid bodies in maturing microspores.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and anthers. Detected inside
CC the pollen grains, but not in stems, leaves, tendrils, roots, seeds,
CC pistils or caps. {ECO:0000269|PubMed:15464152,
CC ECO:0000269|PubMed:19359488}.
CC -!- DEVELOPMENTAL STAGE: Expressed at prebloom in flower buds but barely
CC detectable after anthesis and in early stages of fruit onset. Detected
CC again two months after flowering, then increases and reaches a maximum
CC when the fruit is at peak maturity. Also expressed in very young seeds.
CC {ECO:0000269|PubMed:15464152, ECO:0000269|PubMed:19359488}.
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}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; AY561843; AAS66358.1; -; mRNA.
DR EMBL; FJ696653; ACO36239.1; -; mRNA.
DR RefSeq; NP_001268215.1; NM_001281286.1.
DR AlphaFoldDB; Q6Q3H2; -.
DR SMR; Q6Q3H2; -.
DR PRIDE; Q6Q3H2; -.
DR GeneID; 100232955; -.
DR KEGG; vvi:100232955; -.
DR OrthoDB; 360509at2759; -.
DR BioCyc; MetaCyc:MON-14952; -.
DR BRENDA; 4.2.3.73; 6671.
DR BRENDA; 4.2.3.86; 6671.
DR UniPathway; UPA00213; -.
DR ExpressionAtlas; Q6Q3H2; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0102906; F:7-epi-alpha-selinene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0102905; F:valencene synthase activity; IEA:UniProtKB-EC.
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 Cytoplasm; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..556
FT /note="Valencene synthase"
FT /id="PRO_0000412253"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 310..314
FT /note="DDXXD motif"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CONFLICT 469
FT /note="T -> A (in Ref. 3; ACO36239)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="F -> L (in Ref. 3; ACO36239)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 64432 MW; A669761AE73F8454 CRC64;
MSTQVSASSL AQIPQPKNRP VANFHPNIWG DQFITYTPED KVTRACKEEQ IEDLKKEVKR
KLTAAAVANP SQLLNFIDAV QRLGVAYHFE QEIEEALQHI CNSFHDCNDM DGDLYNIALG
FRLLRQQGYT ISCDIFNKFT DERGRFKEAL ISDVRGMLGL YEAAHLRVHG EDILAKALAF
TTTHLKAMVE SLGYHLAEQV AHALNRPIRK GLERLEARWY ISVYQDEAFH DKTLLELAKL
DFNLVQSLHK EELSNLARWW KELDFATKLP FARDRLVEGY FWMHGVYFEP QYLRGRRILT
KVIAMTSILD DIHDAYGTPE ELKLFIEAIE RWDINSINQL PEYMKLCYVA LLDVYKEIEE
EMEKEGNQYR VHYAKEVMKN QVRAYFAEAK WLHEEHVPAF EEYMRVALAS SGYCLLATTS
FVGMGEIATK EAFDWVTSDP KIMSSSNFIT RLMDDIKSHK FEQKRGHVTS AVECYMKQYG
VSEEQVYSEF QKQIENAWLD INQECLKPTA VSMPLLARLL NFTRTMDVIY KEQDSYTHVG
KVMRDNIASV FINAVI
