ID   THS3_VITVI              Reviewed;         392 AA.
AC   P51071; F6HP27;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Stilbene synthase 3;
DE            EC=2.3.1.95;
DE   AltName: Full=PSV368;
DE   AltName: Full=Resveratrol synthase 3;
DE   AltName: Full=Trihydroxystilbene synthase 3;
DE            Short=StSy 3;
GN   OrderedLocusNames=VIT_16s0100g01030;
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 [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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-392.
RC   STRAIN=cv. Optima;
RX   PubMed=1898048; DOI=10.1016/0003-9861(91)90234-a;
RA   Melchior F., Kindl H.;
RT   "Coordinate- and elicitor-dependent expression of stilbene synthase and
RT   phenylalanine ammonia-lyase genes in Vitis cv. Optima.";
RL   Arch. Biochem. Biophys. 288:552-557(1991).
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.
CC   -!- INDUCTION: By stress.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
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DR   EMBL; FN596000; CCB56433.1; -; Genomic_DNA.
DR   EMBL; FN597040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; S63227; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P51071; -.
DR   SMR; P51071; -.
DR   STRING; 29760.VIT_16s0100g01030.t01; -.
DR   eggNOG; ENOG502QRSY; Eukaryota.
DR   HOGENOM; CLU_034992_2_0_1; -.
DR   InParanoid; P51071; -.
DR   BRENDA; 2.3.1.95; 6671.
DR   UniPathway; UPA00372; UER00548.
DR   Proteomes; UP000009183; Chromosome 16.
DR   ExpressionAtlas; P51071; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR   GO; GO:0050350; F:trihydroxystilbene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0030639; P:polyketide biosynthetic process; IBA:GO_Central.
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; Reference proteome;
KW   Stress response; Transferase.
FT   CHAIN           1..392
FT                   /note="Stilbene synthase 3"
FT                   /id="PRO_0000216084"
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"
FT   CONFLICT        48..50
FT                   /note="HMT -> PMS (in Ref. 1; S63227)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        100
FT                   /note="V -> A (in Ref. 1; S63227)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   392 AA;  42816 MW;  F0455E63E51F69FA CRC64;
     MASVEEIRNA QRAKGPATIL AIGTATPDHC VYQSDYADYY FRVTKSEHMT ELKKKFNRIC
     DKSMIKKRYI HLTEEMLEEH PNIGAYMAPS LNIRQEIITV EVPKLGKEAA LKALKEWGQP
     KSKITHLVFC TTSGVEMPGA DYKLANLLGL ETSVRRVMLY HQGCYAGGTV LRTAKDLAEN
     NAGARVLVVC SEITVVTFRG PSEDALDSLV GQALFGDGSA AVIVGSDPDV SIERPLFQLV
     SAAQTFIPNS AGAIAGNLRE VGLTFHLWPN VPTLISENVE KCLTQAFDPL GISDWNSLFW
     IAHPGGPAIL DAVEAKLNLD KKKLEATRHV LSEYGNMSSA CVLFILDEMR KKSHKGEKAT
     TGEGLDWGVL FGFGPGLTIE TVVLHSIPMV TN