ID   DPS1_PINST              Reviewed;         396 AA.
AC   P48407;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Pinosylvin synthase 1 {ECO:0000303|PubMed:7698342};
DE            EC=2.3.1.146 {ECO:0000269|PubMed:7698342};
DE   AltName: Full=Dihydropinosylvin synthase 1;
DE   AltName: Full=Stilbene synthase 1 {ECO:0000303|PubMed:7698342};
DE            Short=STS 1;
GN   Name=STS1 {ECO:0000303|PubMed:7698342};
OS   Pinus strobus (Eastern white pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Strobus.
OX   NCBI_TaxID=3348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=7698342; DOI=10.1016/0014-5793(95)00199-j;
RA   Raiber S., Schroeder G., Schroeder J.;
RT   "Molecular and enzymatic characterization of two stilbene synthases from
RT   Eastern white pine (Pinus strobus). A single Arg/His difference determines
RT   the activity and the pH dependence of the enzymes.";
RL   FEBS Lett. 361:299-302(1995).
CC   -!- FUNCTION: Catalyzes the production of pinosylvin from cinnamoyl-CoA and
CC       malonyl-CoA, and dihydropinosylvin from dihydrocinnamoyl-CoA.
CC       {ECO:0000269|PubMed:7698342}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-cinnamoyl-CoA + 3 H(+) + 3 malonyl-CoA = (E)-pinosylvin +
CC         4 CO2 + 4 CoA; Xref=Rhea:RHEA:12552, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:17323, ChEBI:CHEBI:57252,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384; EC=2.3.1.146;
CC         Evidence={ECO:0000269|PubMed:7698342};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phenylpropanoyl-CoA + 3 H(+) + 3 malonyl-CoA = 4 CO2 + 4 CoA
CC         + dihydropinosylvin; Xref=Rhea:RHEA:46096, ChEBI:CHEBI:4579,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:85676;
CC         Evidence={ECO:0000269|PubMed:7698342};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6. {ECO:0000269|PubMed:7698342};
CC   -!- PATHWAY: Phytoalexin biosynthesis; pinosylvin biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By stress.
CC   -!- MISCELLANEOUS: STS1 has only 3-5% of the activity of STS2 and
CC       synthesizes a second unknown product with cinnamoyl-CoA.
CC       {ECO:0000269|PubMed:7698342}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z46914; CAA87012.1; -; mRNA.
DR   PIR; S68772; S68772.
DR   AlphaFoldDB; P48407; -.
DR   SMR; P48407; -.
DR   KEGG; ag:CAA87012; -.
DR   BioCyc; MetaCyc:MON-11732; -.
DR   UniPathway; UPA00373; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050198; F:pinosylvin 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   1: Evidence at protein level;
KW   Acyltransferase; Cytoplasm; Stress response; Transferase.
FT   CHAIN           1..396
FT                   /note="Pinosylvin synthase 1"
FT                   /id="PRO_0000216076"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
FT   BINDING         60..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         311..313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            313
FT                   /note="Responsible for the different enzymatic properties
FT                   of STS1 and STS2"
SQ   SEQUENCE   396 AA;  43080 MW;  A6ACF4F7B9FF11FA CRC64;
     MSVGMGIDLE AFRKSQRADG FASILAIGTA NPPNVVDQST YPDYYFRVTN NEDNTDLKDK
     FKRICERSAI KKRHMYLTEE ILKKNPELCA FLEVPSLDTR QAMLAAEVPR LGKEAAEKAI
     EEWGQPKSRI THLIFCTTTT PDLPGADFEV AKLLGLHPSV KRVGVFQHGC FAGGTVLRLA
     KDLAENNRGA RVLVVCSENT AVTFRGPSET HLDGLVGLAL FGDGASALIV GADPIPQVEK
     PCFEIVWTAQ TVVPNSDGAI SGKLREVGLT FQLKGAVPDL ISTNIEKCLV EAFSQFNISD
     WNQLFWIAHP GGHAILDQVE ASLNLDPTKL RATRHVMSEY GNMSSACVHF ILDETRKASR
     QNGCSTSGGG FQMGVLFGFG PGLTVETVVL KSIPFP