ID   CHS2_HORVU              Reviewed;         399 AA.
AC   Q96562;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Chalcone synthase 2;
DE            EC=2.3.1.74;
DE   AltName: Full=Naringenin-chalcone synthase 2;
GN   Name=CHS2;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Pallas / P-02; TISSUE=Leaf;
RX   PubMed=9678580; DOI=10.1023/a:1006031822141;
RA   Christensen A.B., Gregersen P.L., Schroeder J., Collinge D.B.;
RT   "A chalcone synthase with an unusual substrate preference is expressed in
RT   barley leaves in response to UV light and pathogen attack.";
RL   Plant Mol. Biol. 37:849-857(1998).
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. Substrate preference is feruloyl-CoA = caffeoyl-CoA >>
CC       cinnamoyl-CoA.
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: Strong in response to inoculation with fungi.
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; Y09233; CAA70435.1; -; mRNA.
DR   PIR; T04485; T04485.
DR   AlphaFoldDB; Q96562; -.
DR   SMR; Q96562; -.
DR   EnsemblPlants; HORVU.MOREX.r2.1HG0073890.1; HORVU.MOREX.r2.1HG0073890.1.CDS.1; HORVU.MOREX.r2.1HG0073890.
DR   EnsemblPlants; HORVU.MOREX.r2.1HG0073890.1.mrna1; HORVU.MOREX.r2.1HG0073890.1.mrna1.cds1; HORVU.MOREX.r2.1HG0073890.1.
DR   Gramene; HORVU.MOREX.r2.1HG0073890.1; HORVU.MOREX.r2.1HG0073890.1.CDS.1; HORVU.MOREX.r2.1HG0073890.
DR   Gramene; HORVU.MOREX.r2.1HG0073890.1.mrna1; HORVU.MOREX.r2.1HG0073890.1.mrna1.cds1; HORVU.MOREX.r2.1HG0073890.1.
DR   UniPathway; UPA00154; -.
DR   ExpressionAtlas; Q96562; baseline and differential.
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..399
FT                   /note="Chalcone synthase 2"
FT                   /id="PRO_0000215980"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
SQ   SEQUENCE   399 AA;  43189 MW;  B41F54CD647FF22D CRC64;
     MAAVRLKEVR MAQRAEGLAT VLAIGTAVPA NCVYQATYPD YYFRVTKSEH LADLKEKFQR
     MCDKSMIRKR HMHLTEEILI KNPKICAHME TSLDARHAIA LVEVPKLGQG AAEKAIKEWG
     QPLSKITHLV FCTTSGVDMP GADYQLTKLL GLSPTVKRLM MYQQGCFGGA TVLRLAKDIA
     ENNRGARVLV VCSEITAMAF RGPCKSHLDS LVGHALFGDG AAAAIIGADP DQLDEQPVFQ
     LVSASQTILP ESEGAIDGHL TEAGLTIHLL KDVPGLISEN IEQALEDAFE PLGIHNWNSI
     FWIAHPGGPA ILDRVEDRVG LDKKRMRASR EVLSEYGNMS SASVLFVLDV MRKSSAKDGL
     ATTGEGKDWG VLFGFGPGLT VETLVLHSVP VPVPTAASA