CHSY_ARATH
ID CHSY_ARATH Reviewed; 395 AA.
AC P13114; Q43132; Q940L6; Q941R9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Chalcone synthase;
DE EC=2.3.1.74;
DE AltName: Full=Naringenin-chalcone synthase;
DE AltName: Full=Protein TRANSPARENT TESTA 4;
GN Name=CHS; Synonyms=TT4; OrderedLocusNames=At5g13930;
GN ORFNames=MAC12.11, MAC12.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3386631; DOI=10.1128/mcb.8.5.1985-1992.1988;
RA Feinbaum R.L., Ausubel F.M.;
RT "Transcriptional regulation of the Arabidopsis thaliana chalcone synthase
RT gene.";
RL Mol. Cell. Biol. 8:1985-1992(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8528278; DOI=10.1046/j.1365-313x.1995.08050659.x;
RA Shirley B.W., Kubasek W.L., Storz G., Bruggemann E., Koornneef M.,
RA Ausubel F.M., Goodman H.M.;
RT "Analysis of Arabidopsis mutants deficient in flavonoid biosynthesis.";
RL Plant J. 8:659-671(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT JK196.
RC STRAIN=cv. Est;
RA Bharti A.K., Tyagi A.K., Khurana J.P.;
RT "Physiological and molecular characterization of transparent testa mutants
RT of Arabidopsis impaired in phenylpropanoid pathway.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11018155; DOI=10.1093/oxfordjournals.molbev.a026248;
RA Koch M.A., Haubold B., Mitchell-Olds T.;
RT "Comparative evolutionary analysis of chalcone synthase and alcohol
RT dehydrogenase loci in Arabidopsis, Arabis, and related genera
RT (Brassicaceae).";
RL Mol. Biol. Evol. 17:1483-1498(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 81-205 AND 348-395.
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, ACETYLATION [LARGE SCALE
RP ANALYSIS] AT ALA-2 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]
RP (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
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 -!- INTERACTION:
CC P13114; Q9C5W9: ARF18; NbExp=3; IntAct=EBI-1546775, EBI-3946783;
CC P13114; P41088: CHI1; NbExp=4; IntAct=EBI-1546775, EBI-1546761;
CC P13114; P51102: DFRA; NbExp=4; IntAct=EBI-1546775, EBI-1546795;
CC P13114; Q96330: FLS1; NbExp=3; IntAct=EBI-1546775, EBI-1774454;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=P13114-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P13114-2; Sequence=VSP_057945;
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; M20308; AAA32771.1; -; Genomic_DNA.
DR EMBL; S80554; AAB35812.1; -; Genomic_DNA.
DR EMBL; Y18602; CAC80089.1; -; Genomic_DNA.
DR EMBL; Y18603; CAC80090.1; -; Genomic_DNA.
DR EMBL; AF112086; AAF23561.1; -; Genomic_DNA.
DR EMBL; AB005230; BAB11121.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91961.1; -; Genomic_DNA.
DR EMBL; AY044331; AAK73272.1; -; mRNA.
DR EMBL; AY054278; AAL06937.1; -; mRNA.
DR EMBL; AY058155; AAL25571.1; -; mRNA.
DR EMBL; AY090376; AAL91279.1; -; mRNA.
DR EMBL; AY087778; AAM65314.1; -; mRNA.
DR EMBL; BT000596; AAN18165.1; -; mRNA.
DR EMBL; Z17650; CAA79023.1; -; mRNA.
DR EMBL; Z17649; CAA79022.1; -; mRNA.
DR PIR; A27721; SYMUCN.
DR RefSeq; NP_196897.1; NM_121396.4. [P13114-1]
DR PDB; 6DXB; X-ray; 1.55 A; A/B/C/D=1-395.
DR PDB; 6DXD; X-ray; 1.59 A; A/B/C/D=1-395.
DR PDB; 6DXE; X-ray; 1.61 A; A/C=1-395.
DR PDBsum; 6DXB; -.
DR PDBsum; 6DXD; -.
DR PDBsum; 6DXE; -.
DR AlphaFoldDB; P13114; -.
DR SMR; P13114; -.
DR BioGRID; 16519; 11.
DR IntAct; P13114; 8.
DR MINT; P13114; -.
DR STRING; 3702.AT5G13930.1; -.
DR iPTMnet; P13114; -.
DR PaxDb; P13114; -.
DR PRIDE; P13114; -.
DR ProteomicsDB; 246835; -. [P13114-1]
DR EnsemblPlants; AT5G13930.1; AT5G13930.1; AT5G13930. [P13114-1]
DR GeneID; 831241; -.
DR Gramene; AT5G13930.1; AT5G13930.1; AT5G13930. [P13114-1]
DR KEGG; ath:AT5G13930; -.
DR Araport; AT5G13930; -.
DR TAIR; locus:2159098; AT5G13930.
DR eggNOG; ENOG502S4A6; Eukaryota.
DR HOGENOM; CLU_034992_2_0_1; -.
DR InParanoid; P13114; -.
DR OMA; NFMGCYA; -.
DR PhylomeDB; P13114; -.
DR BioCyc; ARA:AT5G13930-MON; -.
DR BioCyc; MetaCyc:AT5G13930-MON; -.
DR BRENDA; 2.3.1.74; 399.
DR UniPathway; UPA00154; -.
DR PRO; PR:P13114; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P13114; baseline and differential.
DR Genevisible; P13114; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
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:0009926; P:auxin polar transport; IMP:TAIR.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IMP:TAIR.
DR GO; GO:0030639; P:polyketide biosynthetic process; IBA:GO_Central.
DR GO; GO:0031540; P:regulation of anthocyanin biosynthetic process; IEP:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0009629; P:response to gravity; IMP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR GO; GO:0010224; P:response to UV-B; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
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 3D-structure; Acetylation; Acyltransferase; Alternative initiation;
KW Flavonoid biosynthesis; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..395
FT /note="Chalcone synthase"
FT /id="PRO_0000215954"
FT ACT_SITE 169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..2
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_057945"
FT MUTAGEN 309
FT /note="H->Y: In JK196."
FT CONFLICT 42
FT /note="P -> H (in Ref. 7; AAL06937)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="M -> K (in Ref. 7; AAL06937)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="G -> S (in Ref. 2; AAB35812)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="L -> S (in Ref. 7; AAL06937)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="T -> S (in Ref. 7; AAL06937)"
FT /evidence="ECO:0000305"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:6DXB"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:6DXB"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:6DXB"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6DXB"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 96..122
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:6DXB"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:6DXB"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:6DXB"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 171..184
FT /evidence="ECO:0007829|PDB:6DXB"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:6DXB"
FT STRAND 223..232
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:6DXB"
FT STRAND 242..252
FT /evidence="ECO:0007829|PDB:6DXB"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:6DXB"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 277..293
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:6DXB"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 331..340
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:6DXB"
FT HELIX 347..362
FT /evidence="ECO:0007829|PDB:6DXB"
FT TURN 367..370
FT /evidence="ECO:0007829|PDB:6DXB"
FT STRAND 372..380
FT /evidence="ECO:0007829|PDB:6DXB"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:6DXB"
FT STRAND 384..392
FT /evidence="ECO:0007829|PDB:6DXB"
FT INIT_MET P13114-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES P13114-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 395 AA; 43116 MW; 3FCED2BCF2CCAB0E CRC64;
MVMAGASSLD EIRQAQRADG PAGILAIGTA NPENHVLQAE YPDYYFRITN SEHMTDLKEK
FKRMCDKSTI RKRHMHLTEE FLKENPHMCA YMAPSLDTRQ DIVVVEVPKL GKEAAVKAIK
EWGQPKSKIT HVVFCTTSGV DMPGADYQLT KLLGLRPSVK RLMMYQQGCF AGGTVLRIAK
DLAENNRGAR VLVVCSEITA VTFRGPSDTH LDSLVGQALF SDGAAALIVG SDPDTSVGEK
PIFEMVSAAQ TILPDSDGAI DGHLREVGLT FHLLKDVPGL ISKNIVKSLD EAFKPLGISD
WNSLFWIAHP GGPAILDQVE IKLGLKEEKM RATRHVLSEY GNMSSACVLF ILDEMRRKSA
KDGVATTGEG LEWGVLFGFG PGLTVETVVL HSVPL
