CHS2_MEDSA
ID CHS2_MEDSA Reviewed; 389 AA.
AC P30074;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Chalcone synthase 2;
DE EC=2.3.1.74;
DE AltName: Full=Naringenin-chalcone synthase 2;
GN Name=CHS2;
OS Medicago sativa (Alfalfa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8507827; DOI=10.1007/bf00014932;
RA Junghans H., Dalkin K., Dixon R.A.;
RT "Stress responses in alfalfa (Medicago sativa L.). 15. Characterization and
RT expression patterns of members of a subset of the chalcone synthase
RT multigene family.";
RL Plant Mol. Biol. 22:239-253(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
RP COENZYME A.
RX PubMed=10426957; DOI=10.1038/11553;
RA Ferrer J.L., Jez J.M., Bowman M.E., Dixon R.A., Noel J.P.;
RT "Structure of chalcone synthase and the molecular basis of plant polyketide
RT biosynthesis.";
RL Nat. Struct. Biol. 6:775-784(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) IN COMPLEX WITH COENZYME A,
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-164;
RP PHE-215; HIS-303 AND ASN-336.
RX PubMed=10653632; DOI=10.1021/bi991489f;
RA Jez J.M., Ferrer J.L., Bowman M.E., Dixon R.A., Noel J.P.;
RT "Dissection of malonyl-coenzyme A decarboxylation from polyketide formation
RT in the reaction mechanism of a plant polyketide synthase.";
RL Biochemistry 39:890-902(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF GLY-256.
RX PubMed=11732902; DOI=10.1021/bi015621z;
RA Jez J.M., Bowman M.E., Noel J.P.;
RT "Structure-guided programming of polyketide chain-length determination in
RT chalcone synthase.";
RL Biochemistry 40:14829-14838(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF PHE-215 AND PHE-265.
RX PubMed=11959984; DOI=10.1073/pnas.082590499;
RA Jez J.M., Bowman M.E., Noel J.P.;
RT "Expanding the biosynthetic repertoire of plant type III polyketide
RT synthases by altering starter molecule specificity.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5319-5324(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND FUNCTION.
RX PubMed=15380179; DOI=10.1016/j.chembiol.2004.05.024;
RA Austin M.B., Bowman M.E., Ferrer J.-L., Schroeder J., Noel J.P.;
RT "An aldol switch discovered in stilbene synthases mediates cyclization
RT specificity of type III polyketide synthases.";
RL Chem. Biol. 11:1179-1194(2004).
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. {ECO:0000269|PubMed:10653632, ECO:0000269|PubMed:11732902,
CC ECO:0000269|PubMed:11959984, ECO:0000269|PubMed:15380179}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.1 uM for malonyl-CoA {ECO:0000269|PubMed:10653632,
CC ECO:0000269|PubMed:11732902, ECO:0000269|PubMed:11959984};
CC KM=4.5 uM for 4-coumaroyl-CoA {ECO:0000269|PubMed:10653632,
CC ECO:0000269|PubMed:11732902, ECO:0000269|PubMed:11959984};
CC KM=2.2 uM for benzoyl-CoA {ECO:0000269|PubMed:10653632,
CC ECO:0000269|PubMed:11732902, ECO:0000269|PubMed:11959984};
CC KM=4.1 uM for hexanoyl-CoA {ECO:0000269|PubMed:10653632,
CC ECO:0000269|PubMed:11732902, ECO:0000269|PubMed:11959984};
CC KM=5.1 uM for phenylacetyl-CoA {ECO:0000269|PubMed:10653632,
CC ECO:0000269|PubMed:11732902, ECO:0000269|PubMed:11959984};
CC KM=5.2 uM for feruloyl-CoA {ECO:0000269|PubMed:10653632,
CC ECO:0000269|PubMed:11732902, ECO:0000269|PubMed:11959984};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:10426957,
CC ECO:0000305|PubMed:10653632}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; L02902; AAA02824.1; -; mRNA.
DR PIR; S35164; S35164.
DR PDB; 1BI5; X-ray; 1.56 A; A=1-389.
DR PDB; 1BQ6; X-ray; 1.56 A; A=2-389.
DR PDB; 1CGK; X-ray; 1.84 A; A=1-389.
DR PDB; 1CGZ; X-ray; 1.70 A; A=1-389.
DR PDB; 1CHW; X-ray; 1.90 A; A/B=1-389.
DR PDB; 1CML; X-ray; 1.69 A; A=1-389.
DR PDB; 1D6F; X-ray; 1.69 A; A=1-389.
DR PDB; 1D6H; X-ray; 2.15 A; A=3-389.
DR PDB; 1D6I; X-ray; 2.00 A; A/B=2-389.
DR PDB; 1I86; X-ray; 1.50 A; A=1-389.
DR PDB; 1I88; X-ray; 1.45 A; A/B=1-389.
DR PDB; 1I89; X-ray; 1.86 A; A/B=1-389.
DR PDB; 1I8B; X-ray; 1.95 A; A/B=1-389.
DR PDB; 1JWX; X-ray; 1.63 A; A=1-389.
DR PDB; 1U0V; X-ray; 1.90 A; A/B=1-389.
DR PDB; 1U0W; X-ray; 2.00 A; A/B/C/D=1-389.
DR PDBsum; 1BI5; -.
DR PDBsum; 1BQ6; -.
DR PDBsum; 1CGK; -.
DR PDBsum; 1CGZ; -.
DR PDBsum; 1CHW; -.
DR PDBsum; 1CML; -.
DR PDBsum; 1D6F; -.
DR PDBsum; 1D6H; -.
DR PDBsum; 1D6I; -.
DR PDBsum; 1I86; -.
DR PDBsum; 1I88; -.
DR PDBsum; 1I89; -.
DR PDBsum; 1I8B; -.
DR PDBsum; 1JWX; -.
DR PDBsum; 1U0V; -.
DR PDBsum; 1U0W; -.
DR AlphaFoldDB; P30074; -.
DR SMR; P30074; -.
DR BRENDA; 2.3.1.74; 3078.
DR SABIO-RK; P30074; -.
DR UniPathway; UPA00154; -.
DR EvolutionaryTrace; P30074; -.
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:0009715; P:chalcone biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Flavonoid biosynthesis; Transferase.
FT CHAIN 1..389
FT /note="Chalcone synthase 2"
FT /id="PRO_0000216007"
FT ACT_SITE 164
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000305"
FT BINDING 55..62
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10426957"
FT BINDING 216..217
FT /ligand="substrate"
FT BINDING 308
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:10426957,
FT ECO:0000269|PubMed:10653632"
FT MUTAGEN 164
FT /note="C->A,D,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10653632"
FT MUTAGEN 215
FT /note="F->S,W,Y: Drastically reduces catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:10653632,
FT ECO:0000269|PubMed:11959984"
FT MUTAGEN 256
FT /note="G->A: Decreases catalytic efficiency 2-fold."
FT /evidence="ECO:0000269|PubMed:11732902"
FT MUTAGEN 256
FT /note="G->F,L: Drastically reduces catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:11732902"
FT MUTAGEN 256
FT /note="G->V: Decreases catalytic efficiency 7-fold."
FT /evidence="ECO:0000269|PubMed:11732902"
FT MUTAGEN 265
FT /note="F->V: Decreases catalytic efficiency 2-fold."
FT /evidence="ECO:0000269|PubMed:11959984"
FT MUTAGEN 303
FT /note="H->A,D,N,T: Drastically reduces catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:10653632"
FT MUTAGEN 303
FT /note="H->Q: Decreases catalytic efficiency 13-fold."
FT /evidence="ECO:0000269|PubMed:10653632"
FT MUTAGEN 336
FT /note="N->A,D,H,K,Q: Drastically reduces catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:10653632"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:1I88"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:1I88"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:1I88"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1I88"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 91..117
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1I88"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:1I88"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1U0V"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:1I88"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:1I88"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:1I88"
FT STRAND 218..227
FT /evidence="ECO:0007829|PDB:1I88"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:1I88"
FT STRAND 237..246
FT /evidence="ECO:0007829|PDB:1I88"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:1I88"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 271..287
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:1I88"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 307..317
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:1I88"
FT HELIX 341..355
FT /evidence="ECO:0007829|PDB:1I88"
FT TURN 361..364
FT /evidence="ECO:0007829|PDB:1I88"
FT STRAND 366..374
FT /evidence="ECO:0007829|PDB:1I88"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:1I88"
FT STRAND 378..386
FT /evidence="ECO:0007829|PDB:1I88"
SQ SEQUENCE 389 AA; 42706 MW; E03422EE332A5408 CRC64;
MVSVSEIRKA QRAEGPATIL AIGTANPANC VEQSTYPDFY FKITNSEHKT ELKEKFQRMC
DKSMIKRRYM YLTEEILKEN PNVCEYMAPS LDARQDMVVV EVPRLGKEAA VKAIKEWGQP
KSKITHLIVC TTSGVDMPGA DYQLTKLLGL RPYVKRYMMY QQGCFAGGTV LRLAKDLAEN
NKGARVLVVC SEVTAVTFRG PSDTHLDSLV GQALFGDGAA ALIVGSDPVP EIEKPIFEMV
WTAQTIAPDS EGAIDGHLRE AGLTFHLLKD VPGIVSKNIT KALVEAFEPL GISDYNSIFW
IAHPGGPAIL DQVEQKLALK PEKMNATREV LSEYGNMSSA CVLFILDEMR KKSTQNGLKT
TGEGLEWGVL FGFGPGLTIE TVVLRSVAI
