ID   DPS2_PINST              Reviewed;         396 AA.
AC   P48408;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Pinosylvin synthase 2 {ECO:0000303|PubMed:7698342};
DE            EC=2.3.1.146 {ECO:0000269|PubMed:7698342};
DE   AltName: Full=Dihydropinosylvin synthase 2;
DE   AltName: Full=Stilbene synthase 2 {ECO:0000303|PubMed:7698342};
DE            Short=STS 2;
GN   Name=STS2 {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       Kinetic parameters:
CC         KM=3.6 uM for cinnamoyl-CoA {ECO:0000269|PubMed:7698342};
CC         KM=22 uM for dihydrocinnamoyl-CoA {ECO:0000269|PubMed:7698342};
CC       pH dependence:
CC         Optimum pH is 6-7. {ECO:0000269|PubMed:7698342};
CC   -!- PATHWAY: Phytoalexin biosynthesis; pinosylvin biosynthesis.
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; Z46915; CAA87013.1; -; mRNA.
DR   PIR; S68773; S68773.
DR   AlphaFoldDB; P48408; -.
DR   SMR; P48408; -.
DR   KEGG; ag:CAA87013; -.
DR   BioCyc; MetaCyc:MON-11733; -.
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 2"
FT                   /id="PRO_0000216077"
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;  43112 MW;  BA87BE471B10285A CRC64;
     MSVGMGVDLE AFRKSQRADG FASILAIGTA NPPNVVDQST YPDYYFRNTN NEDNTDLKDK
     FKRICERSAI KKRHMYLTEE ILKKNPELCA FLEVPSLDTR QAMLAVEVPR LGKEAAEKAI
     EEWGQPKSRI THLIFCTTTT PDLPGADFEV AKLLGLHPSV KRVGVFQHGC FAGGTVLRLA
     KDLAENNRGA RVLVVCSENT AVTFRGPSET HLDGLVGLAL FGDGAAALIV GADPIPQVEK
     PCFEIVWTAQ TVVPNSDGAI SGKLREVGLT FQLKGAVPDL ISTNIEKCLV EAFSQFNISD
     WNQLFWIAHP GGRAILDQVE ASLNLDPTKL RATRHVMSEY GNMSSACVHF ILDETRKASR
     QNGCSTSGGG FQMGVLFGFG PGLTVETVVL KSIPFP