ID   THS2_ARAHY              Reviewed;         313 AA.
AC   P20077;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Putative stilbene synthase 2;
DE            EC=2.3.1.95;
DE   AltName: Full=Resveratrol synthase 2;
DE            Short=RS2;
DE   AltName: Full=Trihydroxystilbene synthase 2;
DE   Flags: Fragment;
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 [MRNA].
RX   PubMed=2450022; DOI=10.1111/j.1432-1033.1988.tb13868.x;
RA   Schroeder G., Brown J.W.S., Schroeder J.;
RT   "Molecular analysis of resveratrol synthase. cDNA, genomic clones and
RT   relationship with chalcone synthase.";
RL   Eur. J. Biochem. 172:161-169(1988).
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   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. As no transcript has
CC       been detected so far, this sequence could come from an incomplete and
CC       non functional gene. {ECO:0000305}.
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DR   EMBL; X62300; CAA44186.1; ALT_SEQ; mRNA.
DR   PIR; S09062; SYNPHS.
DR   AlphaFoldDB; P20077; -.
DR   SMR; P20077; -.
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   SUPFAM; SSF53901; SSF53901; 1.
DR   PROSITE; PS00441; CHALCONE_SYNTH; 1.
PE   5: Uncertain;
KW   Acyltransferase; Cytoplasm; Transferase.
FT   CHAIN           <1..313
FT                   /note="Putative stilbene synthase 2"
FT                   /id="PRO_0000216080"
FT   ACT_SITE        88
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         229..231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   313 AA;  33968 MW;  CF15E18292E3D1D4 CRC64;
     LKENPNMCAY KAPSLDARED MMIREVPRVG KEAATKAIKE WGQPMSKITH LIFCTTSGVA
     LPGVDYELIV LLGLDPSVKR YMMYHQGCFA GGTVLRLAKD LAENNKDARV LIVCSENTAV
     TFRGPSETDM DSLVGQALFA DGAAAIIIGS DPVPEVENPL FEIVSTDQKL VPNSHGAIGG
     LLREVGLTFY LNKSVPDIIS QNINDALSKA FDPLGISDYN SIFWIAHPGG PAILDQVEQK
     VNLKPEKMNA TRDVLSNYGN MSSACVFFIM DLMRKKSLEE GLKTTGEGLD WGVLFGFGPG
     LTIETVVLRS VAI