ID   PKS1_RUBID              Reviewed;         391 AA.
AC   Q9AU11;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Polyketide synthase 1;
DE            Short=RiPKS1;
DE            EC=2.3.1.74;
DE   AltName: Full=Naringenin-chalcone synthase PKS1;
GN   Name=PKS1;
OS   Rubus idaeus (Raspberry).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC   Rubus.
OX   NCBI_TaxID=32247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   MUTAGENESIS OF ARG-259 AND PHE-344.
RC   STRAIN=cv. Royalty;
RX   PubMed=11437245; DOI=10.1023/a:1010642517738;
RA   Zheng D., Schroder G., Schroder J., Hrazdina G.;
RT   "Molecular and biochemical characterization of three aromatic polyketide
RT   synthase genes from Rubus idaeus.";
RL   Plant Mol. Biol. 46:1-15(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Glen Moy;
RX   PubMed=19156716; DOI=10.1002/mnfr.200800174;
RA   Kassim A., Poette J., Paterson A., Zait D., McCallum S., Woodhead M.,
RA   Smith K., Hackett C., Graham J.;
RT   "Environmental and seasonal influences on red raspberry anthocyanin
RT   antioxidant contents and identification of quantitative traits loci
RT   (QTL).";
RL   Mol. Nutr. Food Res. 53:625-634(2009).
RN   [3]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Royalty; TISSUE=Leaf;
RX   PubMed=18068110; DOI=10.1016/j.abb.2007.11.013;
RA   Zheng D., Hrazdina G.;
RT   "Molecular and biochemical characterization of benzalacetone synthase and
RT   chalcone synthase genes and their proteins from raspberry (Rubus idaeus
RT   L.).";
RL   Arch. Biochem. Biophys. 470:139-145(2008).
CC   -!- FUNCTION: Polyketide synthase producing naringenin chalcone and
CC       slightly p-coumaryltriacetic acid lactone (CTAL). Can use p-coumaryl-
CC       CoA as substrate. {ECO:0000269|PubMed:11437245}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-coumaroyl-CoA + 2 H(+) + 3 malonyl-CoA = 2',4,4',6'-
CC         tetrahydroxychalcone + 3 CO2 + 4 CoA; Xref=Rhea:RHEA:11128,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57355, ChEBI:CHEBI:57384, ChEBI:CHEBI:77645; EC=2.3.1.74;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10023,
CC         ECO:0000269|PubMed:11437245};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in fruits. {ECO:0000269|PubMed:18068110}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates in fruits when berries are small and
CC       hard green until complete ripening. {ECO:0000269|PubMed:18068110}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
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DR   EMBL; AF292367; AAK15174.1; -; Genomic_DNA.
DR   EMBL; EU862821; ACF72868.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AU11; -.
DR   SMR; Q9AU11; -.
DR   BioCyc; MetaCyc:MON-15027; -.
DR   BRENDA; 2.3.1.212; 5472.
DR   BRENDA; 2.3.1.74; 5472.
DR   UniPathway; UPA00154; -.
DR   GO; GO:0102128; F:chalcone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016210; F:naringenin-chalcone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
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; Transferase.
FT   CHAIN           1..391
FT                   /note="Polyketide synthase 1"
FT                   /id="PRO_0000424286"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
FT   MUTAGEN         259
FT                   /note="R->H: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11437245"
FT   MUTAGEN         344
FT                   /note="F->L: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11437245"
SQ   SEQUENCE   391 AA;  42781 MW;  C785C639BE4006B8 CRC64;
     MVTVDEVRKA QRAEGPATIL AIGTATPPNC VDQSTYPDYY FRITKSEHKT ELKEKFQRMC
     DKSMIKKRYM YLTEEILKEN PSMCEYMAPS LDARQDMVVV EIPKLGKEAA TKAIKEWGQP
     KSKITHLVFC TTSGVDMPGA DYQLTKLLGL RPSVKRLMMY QQGCFAGGTV LRLAKDLAEN
     NKGARVLVVC SEITAVTFRG PSDTHLDSLV GQALFGDGAA AIIVGSDPLP DIERPLFELV
     SAAQTILPDS DGAIDGHLRE VGLTFHLLKD VPGLISKNIE KSLNEAFKPL DITDWNSLFW
     IAHPGGPAIL DQVEAKLGLK PEKLEATRNI LSEYGNMSSA CVLFILDEVR RKSVANGHKT
     TGEGLEWGVL FGFGPGLTVE TVVLHSVAAS T