ID   CHS2_MAIZE              Reviewed;         400 AA.
AC   P24825;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Chalcone synthase C2;
DE            EC=2.3.1.74;
DE   AltName: Full=Naringenin-chalcone synthase C2;
GN   Name=C2;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Line C1-P; TISSUE=Leaf;
RX   PubMed=1714383; DOI=10.1002/j.1460-2075.1991.tb07802.x;
RA   Franken P., Niesbach-Kloesgen U., Weydemann U., Marechal-Drouard L.,
RA   Saedler H., Wienand U.;
RT   "The duplicated chalcone synthase genes C2 and Whp (white pollen) of Zea
RT   mays are independently regulated; evidence for translational control of Whp
RT   expression by the anthocyanin intensifying gene in.";
RL   EMBO J. 10:2605-2612(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; X60205; CAA42764.1; -; Genomic_DNA.
DR   PIR; S16598; SYZMCC.
DR   RefSeq; NP_001142246.1; NM_001148774.1.
DR   AlphaFoldDB; P24825; -.
DR   SMR; P24825; -.
DR   STRING; 4577.GRMZM2G151227_P01; -.
DR   PaxDb; P24825; -.
DR   PRIDE; P24825; -.
DR   GeneID; 100274415; -.
DR   KEGG; zma:100274415; -.
DR   MaizeGDB; 13853; -.
DR   eggNOG; ENOG502QRSY; Eukaryota.
DR   HOGENOM; CLU_034992_2_0_1; -.
DR   OrthoDB; 950070at2759; -.
DR   UniPathway; UPA00154; -.
DR   Proteomes; UP000007305; Chromosome 4.
DR   Genevisible; P24825; ZM.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
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   GO; GO:0030639; P:polyketide biosynthetic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   Acyltransferase; Flavonoid biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..400
FT                   /note="Chalcone synthase C2"
FT                   /id="PRO_0000216004"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
SQ   SEQUENCE   400 AA;  43196 MW;  17D1095EE077DEC3 CRC64;
     MAGATVTVEE VRKAQRATGP ATVLAIGTAT PANCVYQADY PDYYFRITKS EHLTDLKEKF
     KRMCDKSMIR KRYMHLTEEF LAENPSMCAY MAPSLDARQD VVVVEVPKLG KAAAQKAIKE
     WGQPKSRITH LVFCTTSGVD MPGADYQLTK ALGLRPSVNR LMMYQQGCFA GGTVLRVAKD
     LAENNRGARV LVVCSEITAV TFRGPSESHL DSLVGQALFG DGAAAVVVGA DPDDRVERPL
     FQLVSAAQTI LPDSEGAIDG HLREVGLTFH LLKDVPGLIS KNIGRALDDA FKPLGISDWN
     SIFWVAHPGG PAILDQVEAK VGLDKARMRA TRHVLSEYGN MSSACVLFIL DEMRKRSAED
     GQATTGEGLD WGVLFGFGPG LTVETVVLHS VPITTGAATA