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 01-OCT-2014, entry version 76. DE RecName: Full=Pinosylvin synthase 1; DE EC=2.3.1.-; DE AltName: Full=Stilbene synthase 1; DE Short=STS 1; GN Name=STS1; OS Pinus strobus (Eastern white pine). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Pinidae; Pinales; Pinaceae; Pinus; Strobus. OX NCBI_TaxID=3348; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. 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 RT from Eastern white pine (Pinus strobus). A single Arg/His difference RT determines the activity and the pH dependence of the enzymes."; RL FEBS Lett. 361:299-302(1995). CC -!- FUNCTION: STS1 has only 3-5% of the activity of STS2 and CC synthesizes a second unknown product with cinnamoyl-CoA. CC -!- CATALYTIC ACTIVITY: 3 malonyl-CoA + cinnamoyl-CoA = 4 CoA + CC pinosylvin + 3 CO(2). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 6.; CC -!- PATHWAY: Phytoalexin biosynthesis; pinosylvin biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- INDUCTION: By stress. CC -!- SIMILARITY: Belongs to the chalcone/stilbene synthases family. CC {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 ProteinModelPortal; P48407; -. DR SMR; P48407; 8-394. DR BioCyc; MetaCyc:MONOMER-11732; -. DR UniPathway; UPA00373; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW. DR Gene3D; 3.40.47.10; -; 2. DR InterPro; IPR012328; Chalcone/stilbene_synth_C. DR InterPro; IPR018088; Chalcone/stilbene_synthase_AS. DR InterPro; IPR001099; Chalcone/stilbene_synthase_N. DR InterPro; IPR011141; Polyketide_synthase_type-III. DR InterPro; IPR016039; Thiolase-like. DR InterPro; IPR016038; Thiolase-like_subgr. 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 Pinosylvin synthase 1. FT /FTId=PRO_0000216076. FT REGION 60 63 Substrate binding. {ECO:0000250}. FT REGION 311 313 Substrate binding. {ECO:0000250}. FT ACT_SITE 170 170 {ECO:0000255|PROSITE-ProRule:PRU10023}. FT BINDING 273 273 Substrate; via carbonyl oxygen. FT {ECO:0000250}. FT SITE 313 313 Responsible for the different enzymatic FT properties 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 //