CHSY_PINSY
ID CHSY_PINSY Reviewed; 396 AA.
AC P30079;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Chalcone synthase;
DE EC=2.3.1.74;
DE AltName: Full=Naringenin-chalcone synthase;
GN Name=CHS;
OS Pinus sylvestris (Scotch pine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3349;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1536925; DOI=10.1007/bf00040665;
RA Fliegmann J., Schroeder G., Schanz S., Britsch L., Schroeder J.;
RT "Molecular analysis of chalcone and dihydropinosylvin synthase from Scots
RT pine (Pinus sylvestris), and differential regulation of these and related
RT enzyme activities in stressed plants.";
RL Plant Mol. Biol. 18:489-503(1992).
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; X60754; CAA43166.1; -; Genomic_DNA.
DR PIR; S20515; S20515.
DR PDB; 6DXA; X-ray; 2.01 A; A/B=1-396.
DR PDBsum; 6DXA; -.
DR AlphaFoldDB; P30079; -.
DR SMR; P30079; -.
DR BioCyc; MetaCyc:MON-11832; -.
DR UniPathway; UPA00154; -.
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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Flavonoid biosynthesis; Transferase.
FT CHAIN 1..396
FT /note="Chalcone synthase"
FT /id="PRO_0000216042"
FT ACT_SITE 169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:6DXA"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:6DXA"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 55..66
FT /evidence="ECO:0007829|PDB:6DXA"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6DXA"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 96..122
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:6DXA"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:6DXA"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 171..184
FT /evidence="ECO:0007829|PDB:6DXA"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:6DXA"
FT STRAND 223..232
FT /evidence="ECO:0007829|PDB:6DXA"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:6DXA"
FT STRAND 241..251
FT /evidence="ECO:0007829|PDB:6DXA"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:6DXA"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 276..292
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:6DXA"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 312..322
FT /evidence="ECO:0007829|PDB:6DXA"
FT TURN 326..329
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 330..339
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:6DXA"
FT HELIX 346..360
FT /evidence="ECO:0007829|PDB:6DXA"
FT TURN 366..369
FT /evidence="ECO:0007829|PDB:6DXA"
FT STRAND 371..379
FT /evidence="ECO:0007829|PDB:6DXA"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:6DXA"
FT STRAND 383..391
FT /evidence="ECO:0007829|PDB:6DXA"
SQ SEQUENCE 396 AA; 43294 MW; 5B5CFAEE888173B4 CRC64;
MAAGMMKDLE AFRKAQRADG PATILAIGTA TPPNAVDQSS YPDYYFKITN SEHMTELKEK
FRRMCDKSAI KKRYMYLTEE ILKENPKVCE YMAPSLDARQ DMVVVEVPRL GKEAAAKAIK
EWGQPKSKIT HVIFCTTSGV DMPGADYQLT KLLGLRPSVK RVMMYQQGCF AGGTVLRVAK
DLAENNRGAR VLVVCSEITA VTFRGPSDTH LDSMVGQALF GDGAAALIVG ADPVPEVEKP
CFELMWTAQT ILPDSDGAID GHLREVGLTF HLLKDVPGLI SKNIEKSLVE AFQQFGISDW
NQLFWIAHPG GPAILDQVEA KLNLDPKKLS ATRQVLSDYG NMSSACVHFI LDEMRKSSKE
KGCSTTGEGL DVGVLFGFGP GLTVETVVLK SVPLLD
