ID   CURS3_CURLO             Reviewed;         390 AA.
AC   C6L7V9;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Curcumin synthase 3;
DE            EC=2.3.1.217;
DE   AltName: Full=Demethoxycurcumin synthase;
DE            EC=2.3.1.219;
GN   Name=CURS3;
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, PATHWAY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19622354; DOI=10.1016/j.febslet.2009.07.029;
RA   Katsuyama Y., Kita T., Horinouchi S.;
RT   "Identification and characterization of multiple curcumin synthases from
RT   the herb Curcuma longa.";
RL   FEBS Lett. 583:2799-2803(2009).
CC   -!- FUNCTION: Catalyzes the synthesis of curcumin by condensing feruloyl-
CC       CoA with a diketide-CoA in the curcuminoid biosynthesis. Also acts as a
CC       demethoxycurcumin synthase by accepting 4-coumaroyl-CoA as a starter
CC       substrate instead of feruloyl-CoA. {ECO:0000269|PubMed:19622354}.
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:19622354};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-4-coumaroyl-CoA + (E)-feruloylacetyl-CoA + H2O = CO2 + 2
CC         CoA + demethoxycurcumin; Xref=Rhea:RHEA:35139, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:65737,
CC         ChEBI:CHEBI:85008, ChEBI:CHEBI:142389; EC=2.3.1.219;
CC         Evidence={ECO:0000269|PubMed:19622354};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4-coumaroyl)acetyl-CoA + 4-coumaroyl-CoA + H2O =
CC         bisdemethoxycurcumin + CO2 + 2 CoA; Xref=Rhea:RHEA:35119,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57355, ChEBI:CHEBI:71045, ChEBI:CHEBI:71211;
CC         EC=2.3.1.219; Evidence={ECO:0000269|PubMed:19622354};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.2 uM for feruloyl-CoA {ECO:0000269|PubMed:19622354};
CC         KM=3.4 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:19622354};
CC         Note=kcat is 0.19 min(-1) with feruloyl-CoA. kcat is 0.36 min(-1)
CC         with p-coumaroyl-CoA.;
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:19622354};
CC       Temperature dependence:
CC         Optimum temperature is 45-55 degrees Celsius.
CC         {ECO:0000269|PubMed:19622354};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC       {ECO:0000269|PubMed:19622354}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
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DR   EMBL; AB506763; BAH85781.1; -; mRNA.
DR   AlphaFoldDB; C6L7V9; -.
DR   SMR; C6L7V9; -.
DR   KEGG; ag:BAH85781; -.
DR   BioCyc; MetaCyc:MON-15411; -.
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:0102103; F:demethoxycurcumin synthase; IEA:UniProtKB-EC.
DR   GO; GO:0102105; F:demethoxycurcumin synthase activity from feruloylacetyl-CoA; 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   Acyltransferase; Flavonoid biosynthesis; Transferase.
FT   CHAIN           1..390
FT                   /note="Curcumin synthase 3"
FT                   /id="PRO_0000422573"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   390 AA;  43099 MW;  8944A923632AC0D7 CRC64;
     MGSLQAMRRA QRAQGPATIM AVGTSNPPNL YEQTSYPDFY FRVTNSDHKH ALKNKFRVIC
     EKTKVKRRYL HLTEEILKQR PKLCSYMEPS FDDRQDIVVE EIPKLAKEAA EKAIKEWGRP
     KSEITHLVFC SISGIDMPGA DYRLATLLGL PLSVNRLMLY SQACHMGAQM LRIAKDLAEN
     NRGARVLAVS CEITVLSFRG PDAGDFEALA CQAGFGDGAA AVVVGADPLP GVERPIYEIA
     AAMQETVPES ERAVGGHLRE IGWTFHFFNQ LPKLIAENIE GSLARAFKPL GISEWNDVFW
     VAHPGNWGIM DAIETKLGLE QGKLATARHV FSEYGNMQSA TVYFVMDEVR KRSAAEGRAT
     TGEGLEWGVL FGFGPGLTIE TVVLRSVPLP