ID   CHSF_PETHY              Reviewed;         389 AA.
AC   P22926;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Chalcone synthase F;
DE            EC=2.3.1.74;
DE   AltName: Full=Naringenin-chalcone synthase F;
GN   Name=CHSF;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Violet 30; TISSUE=Leaf;
RX   PubMed=2806915; DOI=10.1016/0378-1119(89)90185-6;
RA   Koes R.E., Spelt C.E., van den Elzen P.J.M., Mol J.N.M.;
RT   "Cloning and molecular characterization of the chalcone synthase multigene
RT   family of Petunia hybrida.";
RL   Gene 81:245-257(1989).
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   -!- TISSUE SPECIFICITY: CHSF does not appear to be pseudogene, but
CC       expression of this gene could not be detected in various floral tissues
CC       nor in seedlings after illumination with UV light.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {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; X14594; CAA32734.1; -; Genomic_DNA.
DR   PIR; B72821; SYPJCF.
DR   AlphaFoldDB; P22926; -.
DR   SMR; P22926; -.
DR   PRIDE; P22926; -.
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..389
FT                   /note="Chalcone synthase F"
FT                   /id="PRO_0000216032"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
SQ   SEQUENCE   389 AA;  42934 MW;  35DA471B679FB7A0 CRC64;
     MVSVEEVRRA QRREGPATIL AIGTATPLNC VDQTTYPDYF FRVTNSDHKT ELKEKFKRMF
     ERSMIKKSYL HLTEEILKEN PSICEHKAPS FDARQDIVVV EVPKLGKEAA QNAIKEWGQP
     KSKITHLVFC TTTGVDMHGA DYQLTKLLGL SPSVKRLMMY QLGCYGGGTV LRLAKDLAEN
     NKGARALVVC SEITAITFHA PSDTDLDVLV GQALFGDGAA SVIIGSDPNL EVEKPLFELV
     SAAQTLVPDC GHKIYGKTSD VGLTFHLHKD VPRLVSQNIE KSLVEVFQPL GIFDWNSIFW
     VGHAGGREIL DQVELKLGLK PEKLNVTRHV MSEYGNMASA CVLFVLDEMR KTSTKEGFGT
     NVEGLEWGVL CSFGPGLTIE TIVLHSVSI