ID   CHS1_SINAL              Reviewed;         395 AA.
AC   P13416;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Chalcone synthase 1;
DE            EC=2.3.1.74;
DE   AltName: Full=Naringenin-chalcone synthase 1;
GN   Name=CHS1;
OS   Sinapis alba (White mustard) (Brassica hirta).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Sinapis.
OX   NCBI_TaxID=3728;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Cotyledon;
RX   PubMed=1893096; DOI=10.1007/bf00020550;
RA   Batschauer A., Ehmann B., Schaefer E.;
RT   "Cloning and characterization of a chalcone synthase gene from mustard and
RT   its light-dependent expression.";
RL   Plant Mol. Biol. 16:175-185(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 124-395.
RC   TISSUE=Cotyledon;
RX   AGRICOLA=IND91035202; DOI=10.1007/BF00019526;
RA   Ehmann B., Schaefer E.;
RT   "Nucleotide sequences encoding two different chalcone synthases expressed
RT   in cotyledons of SAN 9789 treated mustard (Sinapis alba L.).";
RL   Plant Mol. Biol. 11:869-870(1988).
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   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
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DR   EMBL; X16437; CAA34460.1; -; Genomic_DNA.
DR   EMBL; X14315; CAA32496.1; -; mRNA.
DR   PIR; S14716; SYISC1.
DR   AlphaFoldDB; P13416; -.
DR   SMR; P13416; -.
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   Acetylation; Acyltransferase; Flavonoid biosynthesis; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P13114"
FT   CHAIN           2..395
FT                   /note="Chalcone synthase 1"
FT                   /id="PRO_0000216050"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
FT   MOD_RES         2
FT                   /note="N-acetylvaline"
FT                   /evidence="ECO:0000250|UniProtKB:P13114"
FT   CONFLICT        291
FT                   /note="E -> R (in Ref. 2; CAA32496)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   395 AA;  42994 MW;  C3E8522A4C20E747 CRC64;
     MVMGTPSSLD EIRKAQRADG PAGILAIGTA NPANHVIQAE YPDYYFRITN SEHMTDLKEK
     FKRMCDKSTI RKRHMHLTEE FLKDNPNMCA YMAPSLDARQ DIVVVEVPKL GKEAAVKAIK
     EWGQPKSKIT HVVFCTTSGV DMPGADYQLT KLLGLRPSVK RLMMYQQGCF AGGTVLRLAK
     DLAENNRGAR VLVVCSEITA VTFRGPSDTH LDSLVGQALF SDGAAALIVG SDADISAGEK
     PIFEMVSAAQ TILPDSDGAI DGHLREVGLT FHLLKDVPGL ISKNIEKSLD EAFKPLGISD
     WNSLFWIAHP GGPAILDDVE KKLGLKAEKM RATRHVLSEY GNMSSACVLF ILDEMRRKSV
     EDGVATTGEG LEWGVLFGFG PGLTVETVVL HSVPV