ID   CURS2_CURLO             Reviewed;         391 AA.
AC   C6L7V8;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Curcumin synthase 2;
DE            EC=2.3.1.217;
GN   Name=CURS2;
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.
CC       {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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.3 uM for feruloyl-CoA {ECO:0000269|PubMed:19622354};
CC         KM=89 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:19622354};
CC         Note=kcat is 0.41 min(-1) with feruloyl-CoA. kcat is 0.94 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB506762; BAH85780.1; -; mRNA.
DR   AlphaFoldDB; C6L7V8; -.
DR   SMR; C6L7V8; -.
DR   KEGG; ag:BAH85780; -.
DR   BioCyc; MetaCyc:MON-15410; -.
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   Acyltransferase; Flavonoid biosynthesis; Transferase.
FT   CHAIN           1..391
FT                   /note="Curcumin synthase 2"
FT                   /id="PRO_0000422572"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   391 AA;  43146 MW;  9FE8BB12C5BB0456 CRC64;
     MAMISLQAMR KAQRAQGPAT ILAVGTANPP NLYEQDTYPD YYFRVTNSEH KQELKNKFRL
     MCEKTMVKRR YLYLTPEILK ERPKLCSYME PSFDDRQDIV VEEVPKLAAE AAENAIKEWG
     GDKSAITHLV FCSISGIDMP GADYRLAQLL GLPLAVNRLM LYSQACHMGA AMLRIAKDIA
     ENNRSARVLV VACEITVLSF RGPDERDFQA LAGQAGFGDG AGAMIVGADP VLGVERPLYH
     IMSATQTTVP ESEKAVGGHL REVGLTFHFF NQLPAIIADN VGNSLAEAFE PIGIKDWNNI
     FWVAHPGNWA IMDAIETKLG LEQSKLATAR HVFSEFGNMQ SATVYFVMDE LRKRSAAENR
     ATTGDGLRWG VLFGFGPGIS IETVVLQSVP L