ID   CHS3_SINAL              Reviewed;         395 AA.
AC   P13417;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Chalcone synthase 3;
DE            EC=2.3.1.74;
DE   AltName: Full=Naringenin-chalcone synthase 3;
GN   Name=CHS3;
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 [MRNA].
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).
RN   [2]
RP   ACTIVE SITE, AND MUTAGENESIS.
RX   PubMed=2033084; DOI=10.1016/s0021-9258(18)92914-5;
RA   Lanz T., Tropf S., Marner F.-J., Schroeder J., Schroeder G.;
RT   "The role of cysteines in polyketide synthases. Site-directed mutagenesis
RT   of resveratrol and chalcone synthases, two key enzymes in different plant-
RT   specific pathways.";
RL   J. Biol. Chem. 266:9971-9976(1991).
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; X14314; CAA32495.1; -; mRNA.
DR   PIR; S06877; SYISC3.
DR   AlphaFoldDB; P13417; -.
DR   SMR; P13417; -.
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 3"
FT                   /id="PRO_0000216051"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10023,
FT                   ECO:0000269|PubMed:2033084"
FT   MOD_RES         2
FT                   /note="N-acetylvaline"
FT                   /evidence="ECO:0000250|UniProtKB:P13114"
SQ   SEQUENCE   395 AA;  43065 MW;  6AAFC21FED90548C CRC64;
     MVMGTPSSLD EIRKAQRADG PAGILAIGTA NPANHVIQAE YPDYYFRITN SEHMTDLKEK
     FKRMCDKSTI RKRHMHLTEE FLKDNPNMCA YMAPSLDARQ DIVVVEVPKL GKEAAVKAIK
     EWGQPKSKIT HVVFCTTSGV DMPGADYQLT KLLGLRPSVK RLMMYQQGCF AGGTVLRLAK
     DLAENNRGAR VLVVCSEITA VTFRGPSDTH LDSLVGQALF SDGAAAIIVG SDPDTSVGEK
     PIFEMVSAAQ TILPDSDGAI DGHLREVGLT FHLLKDVPGL ISKNIEKSLD EAFKPLGISD
     WNSLFWIAHP GGPAILDDVE KKLGLKAEKM RATRHVLSEY GNMSSACVLF ILDEMRRKSK
     EDGVATTGEG LEWGVLFGFG PGLTVETVVL HSVPV