THS1_ARAHY
ID THS1_ARAHY Reviewed; 389 AA.
AC P20178;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Stilbene synthase 1;
DE EC=2.3.1.95;
DE AltName: Full=Resveratrol synthase 1;
DE Short=RS1;
DE AltName: Full=Trihydroxystilbene synthase 1;
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.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Hain R., Schreier P.H., Schroeder G., Schroeder J.;
RT "Stilbene synthase gene.";
RL Patent number EP0309862, 05-APR-1989.
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 yeast extract and elicitor
CC from P.megasperma.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; X62299; CAA44185.1; -; Genomic_DNA.
DR EMBL; X62298; CAA44184.1; -; Genomic_DNA.
DR EMBL; A00769; CAA00091.1; -; Unassigned_DNA.
DR PIR; S00334; S00334.
DR AlphaFoldDB; P20178; -.
DR SMR; P20178; -.
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 1"
FT /id="PRO_0000216079"
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 VARIANT 236
FT /note="I -> L"
SQ SEQUENCE 389 AA; 42733 MW; 0E0D58C4832F0431 CRC64;
MVSVSGIRKV QRAEGPATVL AIGTANPPNC VDQSTYADYY FRVTNGEHMT DLKKKFQRIC
ERTQIKNRHM YLTEEILKEN PNMCAYKAPS LDAREDMMIR EVPRVGKEAA TKAIKEWGQP
MSKITHLIFC TTSGVALPGV DYELIVLLGL DPSVKRYMMY HQGCFAGGTV LRLAKDLAEN
NKDARVLIVC SENTAVTFRG PNETDMDSLV GQALFADGAA AIIIGSDPVP EVENPIFEIV
STDQQLVPNS HGAIGGLLRE VGLTFYLNKS VPDIISQNIN GALSKAFDPL GISDYNSIFW
IAHLGGRAIL DQVEQKVNLK PEKMKATRDV LSNYGNMSSA CVFFIMDLMR KKSLETGLKT
TGEGLDWGVL FGFGPGLTIE TVVLRSMAI
