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DCS_CURLO
ID   DCS_CURLO               Reviewed;         389 AA.
AC   C0SVZ5;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Phenylpropanoylacetyl-CoA synthase;
DE            EC=2.3.1.218;
DE   AltName: Full=Diketide CoA synthase;
GN   Name=DCS;
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, TISSUE SPECIFICITY, AND SUBUNIT.
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).
CC   -!- FUNCTION: Catalyzes the formation of feruloyldiketide-CoA by condensing
CC       feruloyl-CoA and malonyl-CoA in the curcuminoid biosynthesis. Has no
CC       activity with cinnamoyl-CoA. {ECO:0000269|PubMed:19258320}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-feruloyl-CoA + H(+) + malonyl-CoA = (E)-feruloylacetyl-CoA
CC         + CO2 + CoA; Xref=Rhea:RHEA:22500, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:87305, ChEBI:CHEBI:142389; EC=2.3.1.218;
CC         Evidence={ECO:0000269|PubMed:19258320};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-coumaroyl-CoA + H(+) + malonyl-CoA = (4-coumaroyl)acetyl-CoA
CC         + CO2 + CoA; Xref=Rhea:RHEA:35115, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57355,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:71211; EC=2.3.1.218;
CC         Evidence={ECO:0000269|PubMed:19258320};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=8.4 uM for malonyl-CoA {ECO:0000269|PubMed:19258320};
CC         Note=kcat is 0.67 min(-1) with malonyl-CoA.;
CC       pH dependence:
CC         Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:19258320};
CC       Temperature dependence:
CC         Optimum temperature is 25-35 degrees Celsius.
CC         {ECO:0000269|PubMed:19258320};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC       {ECO:0000269|PubMed:19258320}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:19258320}.
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; AB495006; BAH56225.1; -; mRNA.
DR   AlphaFoldDB; C0SVZ5; -.
DR   SMR; C0SVZ5; -.
DR   KEGG; ag:BAH56225; -.
DR   BioCyc; MetaCyc:MON-15408; -.
DR   BRENDA; 2.3.1.218; 9125.
DR   UniPathway; UPA00154; -.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:UniProtKB.
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..389
FT                   /note="Phenylpropanoylacetyl-CoA synthase"
FT                   /id="PRO_0000422570"
FT   ACT_SITE        163
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   389 AA;  42047 MW;  ACB9CCA49DA87E4F CRC64;
     MEANGYRITH SADGPATILA IGTANPTNVV DQNAYPDFYF RVTNSEYLQE LKAKFRRICE
     KAAIRKRHLY LTEEILRENP SLLAPMAPSF DARQAIVVEA VPKLAKEAAE KAIKEWGRPK
     SDITHLVFCS ASGIDMPGSD LQLLKLLGLP PSVNRVMLYN VGCHAGGTAL RVAKDLAENN
     RGARVLAVCS EVTVLSYRGP HPAHIESLFV QALFGDGAAA LVVGSDPVDG VERPIFEIAS
     ASQVMLPESA EAVGGHLREI GLTFHLKSQL PSIIASNIEQ SLTTACSPLG LSDWNQLFWA
     VHPGGRAILD QVEARLGLEK DRLAATRHVL SEYGNMQSAT VLFILDEMRN RSAAEGHATT
     GEGLDWGVLL GFGPGLSIET VVLHSCRLN
 
 
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