ID   CHSY_BETPN              Reviewed;         395 AA.
AC   P51075; P93069;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Chalcone synthase;
DE            EC=2.3.1.74;
DE   AltName: Full=Naringenin-chalcone synthase;
GN   Name=CHS;
OS   Betula pendula (European white birch) (Betula verrucosa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Betulaceae; Betula.
OX   NCBI_TaxID=3505;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf;
RA   Pellinen R., Korhonen M., Overmyer K., Lapinjoki S., Kangasjaervi J.;
RT   "Induction of different defence responses in birch (Betula pendula Roth)
RT   upon ozone and UV-B stresses.";
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 119-157.
RC   TISSUE=Leaf;
RA   Talvinen J., Pellinen R., Roy S., Julkunen-Tiitto R., Eloranta T.,
RA   Kangasjaervi J.;
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The primary product of this enzyme is 4,2',4',6'-
CC       tetrahydroxychalcone (also termed naringenin-chalcone or chalcone)
CC       which can under specific conditions spontaneously isomerize into
CC       naringenin.
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   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC   -!- INDUCTION: By ozone.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
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DR   EMBL; Y11022; CAA71904.1; -; mRNA.
DR   EMBL; X77513; CAA54649.1; -; Genomic_DNA.
DR   PIR; S41957; S41957.
DR   AlphaFoldDB; P51075; -.
DR   SMR; P51075; -.
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: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   2: Evidence at transcript level;
KW   Acyltransferase; Flavonoid biosynthesis; Transferase.
FT   CHAIN           1..395
FT                   /note="Chalcone synthase"
FT                   /id="PRO_0000215955"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
SQ   SEQUENCE   395 AA;  43016 MW;  18D25119A8891A17 CRC64;
     MASVEEIRKA QRAHGPATVL AIGTATPSNC ITQADYPDYY FRITKSDHMT ELKEKFKRMC
     DKSMIKKRYM YLNEEILNEN PNMCAYMAPS LDARQTIVVV EVPKLGKEAA TKAIKEWGQP
     KSKITHLVFC TTSGVDMPGA DYQLTKLLGL RPSVKRLMMY QQGCFAGGTV LRLAKDLAEN
     NKGARVLVVC SEITAVTFRG PTDTHLDSLV GQALFGDGAA AVIVGADPDT SVERPLFELI
     SAAQTILPDS DGAIDGHLRE VGLTFHLLKD VPGIISKNIE KSLAEAFAPL GISDWNSLFW
     IAHPGGPAIL DQVESKLGLK EEKLRATRHV LSEYGNMSSA CVLFILDEMR RNSLEGGKVT
     TGEGLEWGVL FGFGPGLTVE TVVLHSVPVP VEASH