CUS_ORYSJ
ID CUS_ORYSJ Reviewed; 402 AA.
AC Q8LIL0; A0A0P0X4L6;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Bisdemethoxycurcumin synthase;
DE EC=2.3.1.211;
DE AltName: Full=Curcuminoid synthase;
GN OrderedLocusNames=Os07g0271500, LOC_Os07g17010;
GN ORFNames=OJ1001_C01.122, OSJNBb0002J01.6;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION, SUBUNIT, AND MUTAGENESIS
RP OF TYR-207; MET-265 AND GLY-274.
RX PubMed=21041675; DOI=10.1073/pnas.1011499107;
RA Morita H., Wanibuchi K., Nii H., Kato R., Sugio S., Abe I.;
RT "Structural basis for the one-pot formation of the diarylheptanoid scaffold
RT by curcuminoid synthase from Oryza sativa.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:19778-19783(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 17-400, AND SUBUNIT.
RX PubMed=21117241; DOI=10.1002/prot.22888;
RA Miyazono K., Um J., Imai F.L., Katsuyama Y., Ohnishi Y., Horinouchi S.,
RA Tanokura M.;
RT "Crystal structure of curcuminoid synthase CUS from Oryza sativa.";
RL Proteins 79:669-673(2011).
CC -!- FUNCTION: Plant-specific type III polyketide synthase (PKS) that
CC catalyzes the one-pot formation of the C6-C7-C6 diarylheptanoid
CC scaffold of bisdemethoxycurcumin by the condensation of two molecules
CC of 4-coumaroyl-CoA and one molecule of malonyl-CoA.
CC {ECO:0000269|PubMed:21041675}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 4-coumaroyl-CoA + H(+) + H2O + malonyl-CoA =
CC bisdemethoxycurcumin + 2 CO2 + 3 CoA; Xref=Rhea:RHEA:34803,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57355, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:71045; EC=2.3.1.211;
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21041675,
CC ECO:0000269|PubMed:21117241}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; AP003797; BAC79571.1; -; Genomic_DNA.
DR EMBL; AP005172; BAD31021.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF21259.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT00940.1; -; Genomic_DNA.
DR EMBL; AK109558; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015646196.1; XM_015790710.1.
DR PDB; 3ALE; X-ray; 2.50 A; A/B/C/D=1-402.
DR PDB; 3OIT; X-ray; 2.00 A; A/B=17-400.
DR PDBsum; 3ALE; -.
DR PDBsum; 3OIT; -.
DR AlphaFoldDB; Q8LIL0; -.
DR SMR; Q8LIL0; -.
DR DIP; DIP-59476N; -.
DR STRING; 4530.OS07T0271500-01; -.
DR PaxDb; Q8LIL0; -.
DR PRIDE; Q8LIL0; -.
DR EnsemblPlants; Os07t0271500-01; Os07t0271500-01; Os07g0271500.
DR GeneID; 4342896; -.
DR Gramene; Os07t0271500-01; Os07t0271500-01; Os07g0271500.
DR KEGG; osa:4342896; -.
DR eggNOG; ENOG502QRSY; Eukaryota.
DR HOGENOM; CLU_034992_2_0_1; -.
DR InParanoid; Q8LIL0; -.
DR OMA; IIPESDH; -.
DR OrthoDB; 950070at2759; -.
DR BioCyc; MetaCyc:MON-16869; -.
DR BRENDA; 2.3.1.211; 4460.
DR BRENDA; 2.3.1.217; 8948.
DR UniPathway; UPA00154; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q8LIL0; OS.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0102452; F:bisdemethoxycurcumin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030639; P:polyketide biosynthetic process; IBA:GO_Central.
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; Reference proteome;
KW Transferase.
FT CHAIN 1..402
FT /note="Bisdemethoxycurcumin synthase"
FT /id="PRO_0000407328"
FT ACT_SITE 174
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000305"
FT MUTAGEN 207
FT /note="Y->F: Loss the bisdemethoxycurcumin-forming activity
FT and formation of bisnoryangonin."
FT /evidence="ECO:0000269|PubMed:21041675"
FT MUTAGEN 265
FT /note="M->L: Loss of the bisdemethoxycurcumin-forming
FT activity and formation of bisnoryangonin."
FT /evidence="ECO:0000269|PubMed:21041675"
FT MUTAGEN 274
FT /note="G->F: Loss of the bisdemethoxycurcumin-forming
FT activity and formation of bisnoryangonin."
FT /evidence="ECO:0000269|PubMed:21041675"
FT CONFLICT 46
FT /note="F -> I (in Ref. 4; AK109558)"
FT /evidence="ECO:0000305"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:3OIT"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:3OIT"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:3OIT"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 101..127
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:3OIT"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:3OIT"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:3OIT"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 176..189
FT /evidence="ECO:0007829|PDB:3OIT"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3OIT"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 217..224
FT /evidence="ECO:0007829|PDB:3OIT"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:3OIT"
FT STRAND 246..255
FT /evidence="ECO:0007829|PDB:3OIT"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:3OIT"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 280..295
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:3OIT"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:3OIT"
FT TURN 334..337
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:3OIT"
FT HELIX 354..364
FT /evidence="ECO:0007829|PDB:3OIT"
FT STRAND 378..385
FT /evidence="ECO:0007829|PDB:3OIT"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:3OIT"
FT STRAND 389..397
FT /evidence="ECO:0007829|PDB:3OIT"
SQ SEQUENCE 402 AA; 43212 MW; 6600EBB8D8E32BC3 CRC64;
MAPTTTMGSA LYPLGEMRRS QRADGLAAVL AIGTANPPNC VTQEEFPDFY FRVTNSDHLT
ALKDKFKRIC QEMGVQRRYL HHTEEMLSAH PEFVDRDAPS LDARLDIAAD AVPELAAEAA
KKAIAEWGRP AADITHLVVT TNSGAHVPGV DFRLVPLLGL RPSVRRTMLH LNGCFAGCAA
LRLAKDLAEN SRGARVLVVA AELTLMYFTG PDEGCFRTLL VQGLFGDGAA AVIVGADADD
VERPLFEIVS AAQTIIPESD HALNMRFTER RLDGVLGRQV PGLIGDNVER CLLDMFGPLL
GGDGGGGWND LFWAVHPGSS TIMDQVDAAL GLEPGKLAAS RRVLSDYGNM SGATVIFALD
ELRRQRKEAA AAGEWPELGV MMAFGPGMTV DAMLLHATSH VN
