ID   PKS5_RUBID              Reviewed;         391 AA.
AC   B0LDU6;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   23-FEB-2022, entry version 48.
DE   RecName: Full=Polyketide synthase 5;
DE            Short=RiPKS5;
DE            EC=2.3.1.74;
DE   AltName: Full=Naringenin-chalcone synthase PKS5;
GN   Name=PKS5;
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, TISSUE
RP   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. Can use p-
CC       coumaryl-CoA as substrate. {ECO:0000269|PubMed:18068110}.
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:18068110};
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 red and
CC       full size. {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; EF694718; ABV54603.1; -; Genomic_DNA.
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 5"
FT                   /id="PRO_0000424290"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
SQ   SEQUENCE   391 AA;  42832 MW;  9A5FC40E059B6F41 CRC64;
     MVTVDEVRKA QRAEGPATVL AIGTATPPNC IDQSTYPDYY FRITNSEHKT ELKEKFQRMC
     DKSMIKKRYM YLTEEILKEN PSMCEYMAPS LDARQDMVVV EIPKLGKEAA TKAIKEWGQP
     KSKITHLVFC TTSGVDMPGA DYQLTKLLGL RPSVKRLMMY QQGCFAGGTV LRLAKDLAEN
     NRGARVLVVC SEIXAVTFRG PSDTHLDSLV GQALFGDGAA AIIVGADPLP KIERPLFELV
     SAAQTILPDS DGAIDGHLRE VGLTFHLLKD VPGLISKNIE KSLNEAFKPL DITDWNSLFW
     IAHPGGPAIL DQVETKLGLK PEKLEATRHI LSEYGNMSSA CVLFILDEVR RKSATNGLKT
     TGEGLEWGVL FGFGPGLTVE TVVLHSVGVT A