CURS1_CURLO
ID CURS1_CURLO Reviewed; 389 AA.
AC C0SVZ6;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Curcumin synthase 1;
DE EC=2.3.1.217;
GN Name=CURS1;
OS Curcuma longa (Turmeric) (Curcuma domestica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Zingiberaceae;
OC Curcuma.
OX NCBI_TaxID=136217;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND TISSUE SPECIFICITY.
RX PubMed=19258320; DOI=10.1074/jbc.m900070200;
RA Katsuyama Y., Kita T., Funa N., Horinouchi S.;
RT "Curcuminoid biosynthesis by two type III polyketide synthases in the herb
RT Curcuma longa.";
RL J. Biol. Chem. 284:11160-11170(2009).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF MUTANT GLY-211, FUNCTION,
RP CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF GLY-211 AND HIS-303.
RX PubMed=21148316; DOI=10.1074/jbc.m110.196279;
RA Katsuyama Y., Miyazono K., Tanokura M., Ohnishi Y., Horinouchi S.;
RT "Structural and biochemical elucidation of mechanism for decarboxylative
RT condensation of beta-keto acid by curcumin synthase.";
RL J. Biol. Chem. 286:6659-6668(2011).
CC -!- FUNCTION: Catalyzes the synthesis of curcumin by condensing feruloyl-
CC CoA with a diketide-CoA in the curcuminoid biosynthesis.
CC {ECO:0000269|PubMed:19258320, ECO:0000269|PubMed:21148316}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-feruloyl-CoA + (E)-feruloylacetyl-CoA + H2O = CO2 + 2 CoA
CC + curcumin; Xref=Rhea:RHEA:34823, ChEBI:CHEBI:3962,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:87305, ChEBI:CHEBI:142389; EC=2.3.1.217;
CC Evidence={ECO:0000269|PubMed:19258320, ECO:0000269|PubMed:21148316};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for feruloyl-CoA {ECO:0000269|PubMed:19258320};
CC KM=189 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:19258320};
CC Note=kcat is 1.1 min(-1) with feruloyl-CoA. kcat is 0.85 min(-1) with
CC p-coumaroyl-CoA.;
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:19258320};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:19258320};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC {ECO:0000269|PubMed:19258320}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21148316}.
CC -!- TISSUE SPECIFICITY: Expressed in both the leaf and rhizome, with higher
CC expression in the rhizome. {ECO:0000269|PubMed:19258320}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; AB495007; BAH56226.1; -; mRNA.
DR PDB; 3OV2; X-ray; 2.32 A; A/B/C/D=1-389.
DR PDB; 3OV3; X-ray; 2.50 A; A/B/C/D=1-389.
DR PDBsum; 3OV2; -.
DR PDBsum; 3OV3; -.
DR AlphaFoldDB; C0SVZ6; -.
DR SMR; C0SVZ6; -.
DR KEGG; ag:BAH56226; -.
DR BioCyc; MetaCyc:MON-15409; -.
DR BRENDA; 2.3.1.217; 9125.
DR BRENDA; 2.3.1.219; 9125.
DR UniPathway; UPA00154; -.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:UniProtKB.
DR GO; GO:0102106; F:curcumin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009813; P:flavonoid biosynthetic 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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Flavonoid biosynthesis; Transferase.
FT CHAIN 1..389
FT /note="Curcumin synthase 1"
FT /id="PRO_0000422571"
FT ACT_SITE 164
FT /evidence="ECO:0000250"
FT MUTAGEN 211
FT /note="G->F,W: Strong reduction in enzyme activity."
FT /evidence="ECO:0000269|PubMed:21148316"
FT MUTAGEN 303
FT /note="H->A,Q: Strong reduction in enzyme activity."
FT /evidence="ECO:0000269|PubMed:21148316"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:3OV2"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:3OV2"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:3OV2"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:3OV2"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 91..117
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3OV2"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:3OV2"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 166..180
FT /evidence="ECO:0007829|PDB:3OV2"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:3OV2"
FT STRAND 218..227
FT /evidence="ECO:0007829|PDB:3OV2"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:3OV2"
FT STRAND 236..246
FT /evidence="ECO:0007829|PDB:3OV2"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:3OV2"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:3OV2"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 307..317
FT /evidence="ECO:0007829|PDB:3OV2"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:3OV2"
FT HELIX 341..355
FT /evidence="ECO:0007829|PDB:3OV2"
FT TURN 361..364
FT /evidence="ECO:0007829|PDB:3OV2"
FT STRAND 366..374
FT /evidence="ECO:0007829|PDB:3OV2"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:3OV2"
FT STRAND 378..386
FT /evidence="ECO:0007829|PDB:3OV2"
SQ SEQUENCE 389 AA; 43034 MW; D6532FE43817B2F3 CRC64;
MANLHALRRE QRAQGPATIM AIGTATPPNL YEQSTFPDFY FRVTNSDDKQ ELKKKFRRMC
EKTMVKKRYL HLTEEILKER PKLCSYKEAS FDDRQDIVVE EIPRLAKEAA EKAIKEWGRP
KSEITHLVFC SISGIDMPGA DYRLATLLGL PLTVNRLMIY SQACHMGAAM LRIAKDLAEN
NRGARVLVVA CEITVLSFRG PNEGDFEALA GQAGFGDGAG AVVVGADPLE GIEKPIYEIA
AAMQETVAES QGAVGGHLRA FGWTFYFLNQ LPAIIADNLG RSLERALAPL GVREWNDVFW
VAHPGNWAII DAIEAKLQLS PDKLSTARHV FTEYGNMQSA TVYFVMDELR KRSAVEGRST
TGDGLQWGVL LGFGPGLSIE TVVLRSMPL
