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 13-SEP-2023, entry version 100. 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:MONOMER-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 CDD; cd00831; CHS_like; 1. 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:SF14; CHALCONE SYNTHASE; 1. DR PANTHER; PTHR11877; HYDROXYMETHYLGLUTARYL-COA SYNTHASE; 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; Thiolase-like; 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 //