ID   THS7_VITVI              Reviewed;         392 AA.
AC   A2ICC6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Stilbene synthase 6;
DE            EC=2.3.1.95;
DE   AltName: Full=Resveratrol synthase 6;
DE   AltName: Full=Trihydroxystilbene synthase 6;
DE            Short=StSy 6;
GN   Name=STS; ORFNames=GSVIVT00009216001, LOC100242994;
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].
RC   STRAIN=cv. Spaetburgunder; TISSUE=Leaf;
RA   Pfeiffer J., Fischer T.C., Forkmann G.;
RT   "Cloning and functional expression of flavonoid genes from Vitis
RT   vinifera.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024;
RX   PubMed=17721507; DOI=10.1038/nature06148;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
CC   -!- FUNCTION: Mediates resistance to pathogens which are sensitive to
CC       stilbenes. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-coumaroyl-CoA + 3 H(+) + 3 malonyl-CoA = 4 CO2 + 4 CoA +
CC         trans-resveratrol; Xref=Rhea:RHEA:11936, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:45713, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57355, ChEBI:CHEBI:57384; EC=2.3.1.95;
CC   -!- PATHWAY: Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene
CC       biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step
CC       2/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
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DR   EMBL; EF192465; ABM67587.1; -; mRNA.
DR   RefSeq; NP_001267934.1; NM_001281005.1.
DR   AlphaFoldDB; A2ICC6; -.
DR   SMR; A2ICC6; -.
DR   STRING; 29760.VIT_16s0100g01200.t01; -.
DR   PRIDE; A2ICC6; -.
DR   GeneID; 100242994; -.
DR   KEGG; vvi:100242994; -.
DR   eggNOG; ENOG502QRSY; Eukaryota.
DR   HOGENOM; CLU_034992_2_0_1; -.
DR   UniPathway; UPA00372; UER00548.
DR   ExpressionAtlas; A2ICC6; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050350; F:trihydroxystilbene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR012328; Chalcone/stilbene_synt_C.
DR   InterPro; IPR001099; Chalcone/stilbene_synt_N.
DR   InterPro; IPR018088; Chalcone/stilbene_synthase_AS.
DR   InterPro; IPR011141; Polyketide_synthase_type-III.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR11877; PTHR11877; 1.
DR   Pfam; PF02797; Chal_sti_synt_C; 1.
DR   Pfam; PF00195; Chal_sti_synt_N; 1.
DR   PIRSF; PIRSF000451; PKS_III; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   PROSITE; PS00441; CHALCONE_SYNTH; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Cytoplasm; Plant defense; Stress response; Transferase.
FT   CHAIN           1..392
FT                   /note="Stilbene synthase 6"
FT                   /id="PRO_0000313089"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
FT   BINDING         55..58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         305..307
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   392 AA;  42840 MW;  0C2E8B22231BB431 CRC64;
     MASVEEFRNA QRAKGPATIL AIGTATPDHC VYQSDYADYY FRVTKSEHMT ELKKKFNRIC
     DKSMIKKRYI HLTEEMLEEH PNIGAYMAPS LNIRQEIITA EVPRLGRDAA LKALKEWGQP
     KSKITHLVFC TTSGVEMPGA DYKLANLLGL ETSVRRVMLY HQGCYAGGTV LRTAKDLAEN
     NAGARVLVVC SEITVVTFRG PSEDALDSLV GQALFGDGSS AVIVGSDPDV SIERPLFQLV
     SAAQTFIPNS AGAIAGNLRE VGLTFHLWPN VPTLISENIE KCLTQAFDPL GISDWNSLFW
     IAHPGGPAIL DAVEAKLNLE KKKLEATRHV LSEYGNMSSA CVLFILDEMR KKSLKGENAT
     TGEGLDWGVL FGFGPGLTIE TVVLHSIPTV TN