ID DPS1_PINST STANDARD; PRT; 396 AA. AC P48407; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE PINOSYLVIN SYNTHASE 1 (EC 2.3.1.-) (STILBENE SYNTHASE 1) (STS 1). GN STS1. OS Pinus strobus (Eastern white pine). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC euphyllophytes; Spermatophyta; Coniferopsida; Coniferales; Pinaceae; OC Pinus. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 95212569. 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: STS 1 HAS ONLY 3-5% OF THE ACTIVITY OF STS 2, A LOWER CC OPTIMAL PH, AND SYNTHESIZES A SECOND UNKNOWN PRODUCT WITH CC CINNAMOYL-COA. CC -!- CATALYTIC ACTIVITY: 3 MALONYL-COA + DIHYDROCINNAMOYL-COA = 4 COA + CC PINOSYLVIN + 3 CO2. CC -!- PATHWAY: INVOLVED IN THE SYNTHESIS OF STILBENE-TYPE PHYTOALEXINS. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- INDUCTION: BY STRESS. CC -!- SIMILARITY: BELONGS TO THE CHALCONE/STILBENE SYNTHASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; -. DR PFAM; PF00195; Chal_stil_synt; 1. DR PROSITE; PS00441; CHALCONE_SYNTH; 1. KW Transferase; Acyltransferase; Multigene family. FT ACT_SITE 170 170 BY SIMILARITY. FT SITE 313 313 RESPONSIBLE FOR THE DIFFERENT ENZYMATIC FT PROPERTIES OF STS1 AND STS2. SQ SEQUENCE 396 AA; 43080 MW; EBFBE124 CRC32; 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 //