CHSH1_HUMLU
ID CHSH1_HUMLU Reviewed; 389 AA.
AC Q9FEY5;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Chalcone synthase H1 {ECO:0000303|Ref.1};
DE Short=CHS_H1 {ECO:0000303|Ref.1};
DE EC=2.3.1.74 {ECO:0000255|PROSITE-ProRule:PRU10023, ECO:0000269|PubMed:29760092, ECO:0000269|Ref.1};
DE AltName: Full=Naringenin-chalcone synthase CHS_H1 {ECO:0000305};
DE AltName: Full=Phloroisovalerophenone synthase {ECO:0000305|PubMed:15170123};
DE Short=3-methyl-1-(trihydroxyphenyl)butan-1-one synthase {ECO:0000305|PubMed:15170123};
DE Short=Valerophenone synthase {ECO:0000303|PubMed:15170123};
DE EC=2.3.1.156 {ECO:0000269|PubMed:15170123};
GN Name=chs_H1 {ECO:0000303|Ref.1};
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Osvals's 72; TISSUE=Leaf;
RX DOI=10.1016/S0168-9452(02)00050-X;
RA Matousek J., Novak P., Briza J., Patzak J., Niedermeierova H.;
RT "Cloning and characterisation of chs-specific DNA and cDNA sequences from
RT hop (Humulus lupulus L.).";
RL Plant Sci. 162:1007-1018(2002).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15170123; DOI=10.1271/bbb.68.1142;
RA Okada Y., Sano Y., Kaneko T., Abe I., Noguchi H., Ito K.;
RT "Enzymatic reactions by five chalcone synthase homologs from hop (Humulus
RT lupulus L.).";
RL Biosci. Biotechnol. Biochem. 68:1142-1145(2004).
RN [3]
RP INDUCTION BY UV-A, 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 [4]
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP INTERACTION WITH CHIL2, AND ACTIVITY REGULATION.
RX PubMed=29760092; DOI=10.1073/pnas.1802223115;
RA Ban Z., Qin H., Mitchell A.J., Liu B., Zhang F., Weng J.-K., Dixon R.A.,
RA Wang G.;
RT "Noncatalytic chalcone isomerase-fold proteins in Humulus lupulus are
RT auxiliary components in prenylated flavonoid biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E5223-E5232(2018).
RN [5]
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 (Ref.1, PubMed:15170123). Also
CC able to produce phlorisovalerophenone (PIVP) from 3-methylbutanoyl-CoA
CC (isovaleryl-CoA) (PubMed:15170123). {ECO:0000269|PubMed:15170123,
CC ECO:0000269|Ref.1, 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 ECO:0000269|PubMed:29760092, ECO:0000269|Ref.1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11129;
CC Evidence={ECO:0000269|PubMed:29760092, ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methylbutanoyl-CoA + 3 H(+) + 3 malonyl-CoA = 3 CO2 + 4 CoA
CC + phlorisovalerophenone; Xref=Rhea:RHEA:23572, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15951, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57345, ChEBI:CHEBI:57384; EC=2.3.1.156;
CC Evidence={ECO:0000269|PubMed:15170123};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23573;
CC Evidence={ECO:0000269|PubMed:15170123};
CC -!- ACTIVITY REGULATION: Stimulated by CHIL2 but inhibited by CHIL1.
CC {ECO:0000269|PubMed:29760092}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.82 uM for 4-coumaroyl-CoA {ECO:0000269|PubMed:29760092};
CC KM=10.06 uM for malonyl-CoA {ECO:0000269|PubMed:29760092};
CC KM=26.57 uM for 4-coumaroyl-CoA (in the presence of CHIL2)
CC {ECO:0000269|PubMed:29760092};
CC KM=59.74 uM for malonyl-CoA (in the presence of CHIL2)
CC {ECO:0000269|PubMed:29760092};
CC Note=kcat is 0.21x10(-3) sec(-1) with 4-coumaroyl-CoA as substrate
CC (PubMed:29760092). kcat is 0.24x10(-3) sec(-1) with malonyl-CoA as
CC substrate (PubMed:29760092). kcat is 1.2x10(-3) sec(-1) with 4-
CC coumaroyl-CoA as substrate (in the presence of CHIL2)
CC (PubMed:29760092). kcat is 4.2x10(-3) sec(-1) with malonyl-CoA as
CC substrate (in the presence of CHIL2) (PubMed:29760092).
CC {ECO:0000269|PubMed:29760092};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC {ECO:0000305|PubMed:30468448}.
CC -!- SUBUNIT: Component an active demethylxanthohumol (DMX) biosynthetic
CC metabolon in glandular trichomes (lupulin glands) that encompasses a
CC chalcone synthase (CHS) and a membrane-bound prenyltransferase
CC (PubMed:29760092). Interacts with CHIL2; this interaction promotes
CC catalytic activity (PubMed:29760092). {ECO:0000269|PubMed:29760092}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29760092}.
CC -!- TISSUE SPECIFICITY: Highly expressed in glandular trichomes (lupulin
CC glands) of maturating cones, to a lower extent, in petioles, flowers
CC and stem apexes of flowering plants, and, at low levels, in roots and
CC leaf blades. {ECO:0000269|Ref.1}.
CC -!- INDUCTION: Accumulates in leaves in response to UV-A.
CC {ECO:0000269|PubMed:17002429}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; AJ304877; CAC19808.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9FEY5; -.
DR SMR; Q9FEY5; -.
DR BioCyc; MetaCyc:MON-12009; -.
DR BRENDA; 2.3.1.74; 2716.
DR UniPathway; UPA00154; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:UniProtKB.
DR GO; GO:0102128; F:chalcone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016210; F:naringenin-chalcone synthase activity; IDA:UniProtKB.
DR GO; GO:0050634; F:phloroisovalerophenone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0070141; P:response to UV-A; IEP:UniProtKB.
DR GO; GO:0019748; P:secondary metabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Flavonoid biosynthesis; Transferase.
FT CHAIN 1..389
FT /note="Chalcone synthase H1"
FT /id="PRO_0000452940"
FT ACT_SITE 164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
SQ SEQUENCE 389 AA; 42534 MW; 68F07CB5B659F586 CRC64;
MVTVEEVRKA QRAEGPATIL AIGTATPANC ILQSEYPDYY FRITNSEHKT ELKEKFKRMC
GKSMIRKRYM HLTEEILKEN PNLCAYEAPS LDARQDMVVV EVPKLGKEAA TKAIKEWGQP
KSEITHVVFC TTSGVDMPGA DYQLTKLLGL RPSVKRLMMY QQGCFAGGTV LRVAKDLAEN
NKGARVLVVC SEITAVTFRG PNDTHLDSLV AQALFGDGSA ALIIGADPIP EIEKPIFELV
SAAQTILPDS DGAIDGHLRE VGLTFHLLKD VPGLISKNIE KSLVEAFKPL GISDWNSLFW
ITHPGGPAIL DQVESKLGLK PEKLRATRHV LGEYGNMSSA CVLFILDEMR RKCAEDGVKT
TGEGLEWGVL FGFGPGLTVE TVVLHSVGI
