ID   THS3_ARAHY              Reviewed;         389 AA.
AC   P51069;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Stilbene synthase 3;
DE            EC=2.3.1.95;
DE   AltName: Full=Resveratrol synthase 3;
DE            Short=RS3;
DE   AltName: Full=Trihydroxystilbene synthase 3;
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lanz T., Schroeder G., Schroeder J.;
RT   "Differential regulation of genes for resveratrol synthase in cell cultures
RT   of Arachis hypogaea L.";
RL   Planta 181:169-175(1990).
RN   [2]
RP   ACTIVE SITE, AND MUTAGENESIS.
RX   PubMed=2033084; DOI=10.1016/s0021-9258(18)92914-5;
RA   Lanz T., Tropf S., Marner F.-J., Schroeder J., Schroeder G.;
RT   "The role of cysteines in polyketide synthases. Site-directed mutagenesis
RT   of resveratrol and chalcone synthases, two key enzymes in different plant-
RT   specific pathways.";
RL   J. Biol. Chem. 266:9971-9976(1991).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By stress. Experimentally by elicitor of P.megasperma, yeast
CC       extract and dilution of cell cultures.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
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DR   EMBL; L00952; AAA96434.1; -; Genomic_DNA.
DR   AlphaFoldDB; P51069; -.
DR   SMR; P51069; -.
DR   BRENDA; 2.3.1.95; 404.
DR   UniPathway; UPA00372; UER00548.
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   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; Stress response; Transferase.
FT   CHAIN           1..389
FT                   /note="Stilbene synthase 3"
FT                   /id="PRO_0000216081"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10023,
FT                   ECO:0000269|PubMed:2033084"
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   389 AA;  42816 MW;  F955E9F954820035 CRC64;
     MVSVSGIRKV QRAEGPATVL AIGTANPPNC IDQSTYADYY FRVTNSEHMT DLKKKFQRIC
     ERTQIKNRHM YLTEEILKEN PNMCAYKAPS LDAREDMMIR EVPRVGKEAA TKAIKEWGQP
     MSKITHLIFC TTSGVALPGV DYELIVLLGL DPCVKRYMMY HQGCFAGGTV LRLAKDLAEN
     NKDARVLIVC SENTAVTFRG PSETDMDSLV GQALFADGAA AIIIGSDPVP EVEKPIFELV
     STDQKLVPGS HGAIGGLLRE VGLTFYLNKS VPDIISQNIN DALNKAFDPL GISDYNSIFW
     IAHPGGRAIL DQVEQKVNLK PEKMKATRDV LSNYGNMSSA CVFFIMDLMR KRSLEEGLKT
     TGEGLDWGVL FGFGPGLTIE TVVLRSVAI