CHS1_SOYBN
ID CHS1_SOYBN Reviewed; 388 AA.
AC P24826;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Chalcone synthase 1;
DE EC=2.3.1.74;
DE AltName: Full=Naringenin-chalcone synthase 1;
GN Name=CHS1;
OS Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Williams;
RX PubMed=1868209; DOI=10.1007/bf00023443;
RA Akada S., Kung S.D., Dube S.K.;
RT "The nucleotide sequence of gene 1 of the soybean chalcone synthase
RT multigene family.";
RL Plant Mol. Biol. 16:751-752(1991).
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 -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; X54644; CAA38456.1; -; Genomic_DNA.
DR PIR; S15006; SYSYC1.
DR RefSeq; XP_003531225.1; XM_003531177.3.
DR PDB; 7BUR; X-ray; 1.82 A; A/B=1-388.
DR PDB; 7BUS; X-ray; 2.52 A; A/B=1-388.
DR PDBsum; 7BUR; -.
DR PDBsum; 7BUS; -.
DR AlphaFoldDB; P24826; -.
DR SMR; P24826; -.
DR STRING; 3847.GLYMA08G11620.1; -.
DR EnsemblPlants; KRH42759; KRH42759; GLYMA_08G109400.
DR Gramene; KRH42759; KRH42759; GLYMA_08G109400.
DR eggNOG; ENOG502QRSY; Eukaryota.
DR HOGENOM; CLU_034992_2_0_1; -.
DR InParanoid; P24826; -.
DR OMA; THPIRFS; -.
DR OrthoDB; 950070at2759; -.
DR UniPathway; UPA00154; -.
DR Proteomes; UP000008827; Chromosome 8.
DR Genevisible; P24826; GM.
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:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030639; P:polyketide biosynthetic process; IBA:GO_Central.
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; Reference proteome;
KW Transferase.
FT CHAIN 1..388
FT /note="Chalcone synthase 1"
FT /id="PRO_0000216062"
FT ACT_SITE 164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:7BUR"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:7BUR"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:7BUR"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:7BUR"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:7BUR"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:7BUR"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:7BUR"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:7BUR"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:7BUR"
FT HELIX 91..117
FT /evidence="ECO:0007829|PDB:7BUR"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:7BUR"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:7BUR"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:7BUR"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:7BUR"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:7BUR"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:7BUR"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:7BUR"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:7BUR"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:7BUR"
FT STRAND 218..227
FT /evidence="ECO:0007829|PDB:7BUR"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:7BUR"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:7BUR"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:7BUR"
FT HELIX 270..286
FT /evidence="ECO:0007829|PDB:7BUR"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:7BUR"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:7BUR"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:7BUR"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:7BUR"
FT HELIX 324..333
FT /evidence="ECO:0007829|PDB:7BUR"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:7BUR"
FT HELIX 340..354
FT /evidence="ECO:0007829|PDB:7BUR"
FT TURN 360..363
FT /evidence="ECO:0007829|PDB:7BUS"
FT STRAND 364..373
FT /evidence="ECO:0007829|PDB:7BUR"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:7BUR"
FT STRAND 377..385
FT /evidence="ECO:0007829|PDB:7BUR"
SQ SEQUENCE 388 AA; 42516 MW; 73AC3B59A4E91BB1 CRC64;
MVSVEEIRKA QRAEGPATVM AIGTATPPNC VDQSTYPDYY FRITNSEHMT ELKEKFKRMC
DKSMIKKRYM YLNEEILKEN PSVCAYMAPS LDARQDMVVV EVPKLGKEAA TKAIKEWGQP
KSKITHLIFC TTSGVDMPGA DYQLTKLLGL RPSVKRYMMY QQGCFAGGTV LRLAKDLAEN
NKGARVLVVC SEITAVTFRG PTDTHLDSLV GQALFGDGAA AVIVGSDPLP VEKPLFQLVW
TAQTILPDSE GAIDGHLREV GLTFHLLKDV PGLISKNIEK ALVEAFQPLG ISDYNSIFWI
AHPGGPAILD QVEAKLGLKP EKMEATRHVL SEYGNMSSAC VLFILDQMRK KSIENGLGTT
GEGLDWGVLF GFGPGLTVET VVLRSVTL
