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CHSH4_HUMLU
ID   CHSH4_HUMLU             Reviewed;         389 AA.
AC   A0AMG9;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Chalcone synthase H3 {ECO:0000305};
DE            Short=CHS_H1-211 {ECO:0000303|PubMed:17002429};
DE            EC=2.3.1.74 {ECO:0000255|PROSITE-ProRule:PRU10023};
DE   AltName: Full=Naringenin-chalcone synthase CHS_H1-211 {ECO:0000303|PubMed:17002429};
GN   Name=chs_H1-211 {ECO:0000303|PubMed:17002429};
OS   Humulus lupulus (European hop).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Humulus.
OX   NCBI_TaxID=3486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND GENE FAMILY.
RC   STRAIN=cv. Osvals's 72; TISSUE=Lupulin gland;
RX   PubMed=17002429; DOI=10.1021/jf061785g;
RA   Matousek J., Vrba L., Skopek J., Orctova L., Pesina K., Heyerick A.,
RA   Baulcombe D., De Keukeleire D.;
RT   "Sequence analysis of a 'true' chalcone synthase (chs_H1) oligofamily from
RT   hop (Humulus lupulus L.) and PAP1 activation of chs_H1 in heterologous
RT   systems.";
RL   J. Agric. Food Chem. 54:7606-7615(2006).
RN   [2]
RP   PATHWAY, AND REVIEW.
RX   PubMed=30468448; DOI=10.1039/c8np00077h;
RA   Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT   "Non-volatile natural products in plant glandular trichomes: chemistry,
RT   biological activities and biosynthesis.";
RL   Nat. Prod. Rep. 36:626-665(2019).
CC   -!- FUNCTION: Involved in the biosynthesis of prenylated phenolics natural
CC       products which contribute to the bitter taste of beer and display broad
CC       biological activities (Probable). Chalcone synthase that can use 4-
CC       coumaroyl-CoA to produce 4,2',4',6'-tetrahydroxychalcone (also termed
CC       naringenin-chalcone or chalcone) which can, under specific conditions,
CC       spontaneously isomerize into naringenin (By similarity).
CC       {ECO:0000250|UniProtKB:Q9FEY5, ECO:0000305|PubMed:30468448}.
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       {ECO:0000305|PubMed:30468448}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9FEY5}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
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DR   EMBL; AM263201; CAK19319.1; -; mRNA.
DR   AlphaFoldDB; A0AMG9; -.
DR   SMR; A0AMG9; -.
DR   BRENDA; 2.3.1.74; 2716.
DR   UniPathway; UPA00154; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; Cytoplasm; Flavonoid biosynthesis; Transferase.
FT   CHAIN           1..389
FT                   /note="Chalcone synthase H3"
FT                   /id="PRO_0000452943"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
SQ   SEQUENCE   389 AA;  42575 MW;  4936A49AF58A0ECD CRC64;
     MVTVEEVRKA QRAEGPATIL AIGTATPANC ILQSEYPDYY FRITNSEHKT ELKEKFKRMC
     DKSMIRKRYM HLTEEILKEN PNLCAYEAPS LDARQDMVVV EVPKLGKEAA TKAIKEWGQP
     KSKITHVVFC TTSGVDMPGA DYQLTKLLGL RPSVKRLMMY QQGCFAGGTV LRVAKDLAEN
     NKGARVLVVC SEITAVTFRG PNDTHLDSLV GQALFGDGSA ALIIGADPIP EIEKPIFELV
     SAAQTILPDS DGAIDGHLRE VGLTFHLLKD VPGLISKNIE KSLVEAFKPL GISDWNSLFW
     IAHPGGPAIL DQVESKLALK PEKLRATRHV LGEYGNMSSA CVLFILDEMR RKCAEDGLKT
     TGEGLEWGVL FGFGPGLTVE TVVLHSVGI
 
 
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