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Curcumin synthase 1 (EC 2.3.1.217)

 CURS1_CURLO             Reviewed;         389 AA.
C0SVZ6;
29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
26-MAY-2009, sequence version 1.
22-NOV-2017, entry version 36.
RecName: Full=Curcumin synthase 1;
EC=2.3.1.217;
Name=CURS1;
Curcuma longa (Turmeric) (Curcuma domestica).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Zingiberales; Zingiberaceae;
Curcuma.
NCBI_TaxID=136217;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND TISSUE SPECIFICITY.
PubMed=19258320; DOI=10.1074/jbc.M900070200;
Katsuyama Y., Kita T., Funa N., Horinouchi S.;
"Curcuminoid biosynthesis by two type III polyketide synthases in the
herb Curcuma longa.";
J. Biol. Chem. 284:11160-11170(2009).
[2]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF MUTANT GLY-211, FUNCTION,
CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF GLY-211 AND HIS-303.
PubMed=21148316; DOI=10.1074/jbc.M110.196279;
Katsuyama Y., Miyazono K., Tanokura M., Ohnishi Y., Horinouchi S.;
"Structural and biochemical elucidation of mechanism for
decarboxylative condensation of beta-keto acid by curcumin synthase.";
J. Biol. Chem. 286:6659-6668(2011).
-!- FUNCTION: Catalyzes the synthesis of curcumin by condensing
feruloyl-CoA with a diketide-CoA in the curcuminoid biosynthesis.
{ECO:0000269|PubMed:19258320, ECO:0000269|PubMed:21148316}.
-!- CATALYTIC ACTIVITY: Feruloyl-CoA + feruloylacetyl-CoA + H(2)O = 2
CoA + curcumin + CO(2). {ECO:0000269|PubMed:19258320,
ECO:0000269|PubMed:21148316}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=18 uM for feruloyl-CoA {ECO:0000269|PubMed:19258320};
KM=189 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:19258320};
Note=Kcat is 1.1 min(-1) with feruloyl-CoA. Kcat is 0.85 min(-1)
with p-coumaroyl-CoA.;
pH dependence:
Optimum pH is 9.0. {ECO:0000269|PubMed:19258320};
Temperature dependence:
Optimum temperature is 50 degrees Celsius.
{ECO:0000269|PubMed:19258320};
-!- PATHWAY: Secondary metabolite biosynthesis; flavonoid
biosynthesis. {ECO:0000269|PubMed:19258320}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21148316}.
-!- TISSUE SPECIFICITY: Expressed in both the leaf and rhizome, with
higher expression in the rhizome. {ECO:0000269|PubMed:19258320}.
-!- SIMILARITY: Belongs to the chalcone/stilbene synthases family.
{ECO:0000305}.
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EMBL; AB495007; BAH56226.1; -; mRNA.
PDB; 3OV2; X-ray; 2.32 A; A/B/C/D=1-389.
PDB; 3OV3; X-ray; 2.50 A; A/B/C/D=1-389.
PDBsum; 3OV2; -.
PDBsum; 3OV3; -.
ProteinModelPortal; C0SVZ6; -.
SMR; C0SVZ6; -.
KEGG; ag:BAH56226; -.
KO; K13234; -.
BioCyc; MetaCyc:MONOMER-15409; -.
BRENDA; 2.3.1.217; 9125.
BRENDA; 2.3.1.219; 9125.
UniPathway; UPA00154; -.
GO; GO:0102106; F:curcumin synthase activity; IEA:UniProtKB-EC.
GO; GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IDA:UniProtKB.
GO; GO:0009813; P:flavonoid biosynthetic process; IDA:UniProtKB.
Gene3D; 3.40.47.10; -; 2.
InterPro; IPR012328; Chalcone/stilbene_synth_C.
InterPro; IPR001099; Chalcone/stilbene_synthase_N.
InterPro; IPR011141; Polyketide_synthase_type-III.
InterPro; IPR016039; Thiolase-like.
PANTHER; PTHR11877; PTHR11877; 1.
Pfam; PF02797; Chal_sti_synt_C; 1.
Pfam; PF00195; Chal_sti_synt_N; 1.
PIRSF; PIRSF000451; PKS_III; 1.
SUPFAM; SSF53901; SSF53901; 2.
1: Evidence at protein level;
3D-structure; Acyltransferase; Flavonoid biosynthesis; Transferase.
CHAIN 1 389 Curcumin synthase 1.
/FTId=PRO_0000422571.
ACT_SITE 164 164 {ECO:0000250}.
MUTAGEN 211 211 G->F,W: Strong reduction in enzyme
activity. {ECO:0000269|PubMed:21148316}.
MUTAGEN 303 303 H->A,Q: Strong reduction in enzyme
activity. {ECO:0000269|PubMed:21148316}.
HELIX 4 11 {ECO:0000244|PDB:3OV2}.
STRAND 18 25 {ECO:0000244|PDB:3OV2}.
STRAND 30 32 {ECO:0000244|PDB:3OV2}.
HELIX 33 35 {ECO:0000244|PDB:3OV2}.
HELIX 36 43 {ECO:0000244|PDB:3OV2}.
HELIX 50 62 {ECO:0000244|PDB:3OV2}.
STRAND 67 69 {ECO:0000244|PDB:3OV2}.
HELIX 74 79 {ECO:0000244|PDB:3OV2}.
HELIX 81 84 {ECO:0000244|PDB:3OV2}.
STRAND 85 88 {ECO:0000244|PDB:3OV2}.
HELIX 91 117 {ECO:0000244|PDB:3OV2}.
HELIX 121 123 {ECO:0000244|PDB:3OV2}.
STRAND 126 133 {ECO:0000244|PDB:3OV2}.
HELIX 140 148 {ECO:0000244|PDB:3OV2}.
STRAND 154 161 {ECO:0000244|PDB:3OV2}.
HELIX 166 180 {ECO:0000244|PDB:3OV2}.
STRAND 185 192 {ECO:0000244|PDB:3OV2}.
HELIX 194 196 {ECO:0000244|PDB:3OV2}.
HELIX 206 214 {ECO:0000244|PDB:3OV2}.
STRAND 218 227 {ECO:0000244|PDB:3OV2}.
TURN 230 232 {ECO:0000244|PDB:3OV2}.
STRAND 236 246 {ECO:0000244|PDB:3OV2}.
STRAND 253 259 {ECO:0000244|PDB:3OV2}.
STRAND 262 267 {ECO:0000244|PDB:3OV2}.
HELIX 271 276 {ECO:0000244|PDB:3OV2}.
HELIX 280 287 {ECO:0000244|PDB:3OV2}.
HELIX 288 290 {ECO:0000244|PDB:3OV2}.
HELIX 295 297 {ECO:0000244|PDB:3OV2}.
STRAND 298 302 {ECO:0000244|PDB:3OV2}.
HELIX 307 317 {ECO:0000244|PDB:3OV2}.
TURN 321 324 {ECO:0000244|PDB:3OV2}.
HELIX 325 334 {ECO:0000244|PDB:3OV2}.
HELIX 338 340 {ECO:0000244|PDB:3OV2}.
HELIX 341 355 {ECO:0000244|PDB:3OV2}.
TURN 361 364 {ECO:0000244|PDB:3OV2}.
STRAND 366 374 {ECO:0000244|PDB:3OV2}.
TURN 375 377 {ECO:0000244|PDB:3OV2}.
STRAND 378 386 {ECO:0000244|PDB:3OV2}.
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


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