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Protein

Curcumin synthase 1

Gene

CURS1

Organism
Curcuma longa (Turmeric) (Curcuma domestica)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of curcumin by condensing feruloyl-CoA with a diketide-CoA in the curcuminoid biosynthesis.2 Publications

Catalytic activityi

Feruloyl-CoA + feruloylacetyl-CoA + H2O = 2 CoA + curcumin + CO2.2 Publications

Kineticsi

Kcat is 1.1 min(-1) with feruloyl-CoA. Kcat is 0.85 min(-1) with p-coumaroyl-CoA.

  1. KM=18 µM for feruloyl-CoA1 Publication
  2. KM=189 µM for p-coumaroyl-CoA1 Publication

    pH dependencei

    Optimum pH is 9.0.1 Publication

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius.1 Publication

    Pathwayi: flavonoid biosynthesis

    This protein is involved in the pathway flavonoid biosynthesis, which is part of Secondary metabolite biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway flavonoid biosynthesis and in Secondary metabolite biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei164 – 1641By similarity

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB
    • transferase activity, transferring acyl groups other than amino-acyl groups Source: UniProtKB

    GO - Biological processi

    • flavonoid biosynthetic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Flavonoid biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15409.
    BRENDAi2.3.1.217. 9125.
    2.3.1.219. 9125.
    UniPathwayiUPA00154.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Curcumin synthase 1 (EC:2.3.1.217)
    Gene namesi
    Name:CURS1
    OrganismiCurcuma longa (Turmeric) (Curcuma domestica)
    Taxonomic identifieri136217 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaZingiberalesZingiberaceaeCurcuma

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi211 – 2111G → F or W: Strong reduction in enzyme activity. 1 Publication
    Mutagenesisi303 – 3031H → A or Q: Strong reduction in enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 389389Curcumin synthase 1PRO_0000422571Add
    BLAST

    Expressioni

    Tissue specificityi

    Expressed in both the leaf and rhizome, with higher expression in the rhizome.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Structurei

    Secondary structure

    1
    389
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 118Combined sources
    Beta strandi18 – 258Combined sources
    Beta strandi30 – 323Combined sources
    Helixi33 – 353Combined sources
    Helixi36 – 438Combined sources
    Helixi50 – 6213Combined sources
    Beta strandi67 – 693Combined sources
    Helixi74 – 796Combined sources
    Helixi81 – 844Combined sources
    Beta strandi85 – 884Combined sources
    Helixi91 – 11727Combined sources
    Helixi121 – 1233Combined sources
    Beta strandi126 – 1338Combined sources
    Helixi140 – 1489Combined sources
    Beta strandi154 – 1618Combined sources
    Helixi166 – 18015Combined sources
    Beta strandi185 – 1928Combined sources
    Helixi194 – 1963Combined sources
    Helixi206 – 2149Combined sources
    Beta strandi218 – 22710Combined sources
    Turni230 – 2323Combined sources
    Beta strandi236 – 24611Combined sources
    Beta strandi253 – 2597Combined sources
    Beta strandi262 – 2676Combined sources
    Helixi271 – 2766Combined sources
    Helixi280 – 2878Combined sources
    Helixi288 – 2903Combined sources
    Helixi295 – 2973Combined sources
    Beta strandi298 – 3025Combined sources
    Helixi307 – 31711Combined sources
    Turni321 – 3244Combined sources
    Helixi325 – 33410Combined sources
    Helixi338 – 3403Combined sources
    Helixi341 – 35515Combined sources
    Turni361 – 3644Combined sources
    Beta strandi366 – 3749Combined sources
    Turni375 – 3773Combined sources
    Beta strandi378 – 3869Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OV2X-ray2.32A/B/C/D1-389[»]
    3OV3X-ray2.50A/B/C/D1-389[»]
    ProteinModelPortaliC0SVZ6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the chalcone/stilbene synthases family.Curated

    Phylogenomic databases

    KOiK13234.

    Family and domain databases

    Gene3Di3.40.47.10. 2 hits.
    InterProiIPR012328. Chalcone/stilbene_synth_C.
    IPR001099. Chalcone/stilbene_synthase_N.
    IPR011141. Polyketide_synthase_type-III.
    IPR016039. Thiolase-like.
    [Graphical view]
    PfamiPF02797. Chal_sti_synt_C. 1 hit.
    PF00195. Chal_sti_synt_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000451. PKS_III. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    C0SVZ6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MANLHALRRE QRAQGPATIM AIGTATPPNL YEQSTFPDFY FRVTNSDDKQ
    60 70 80 90 100
    ELKKKFRRMC EKTMVKKRYL HLTEEILKER PKLCSYKEAS FDDRQDIVVE
    110 120 130 140 150
    EIPRLAKEAA EKAIKEWGRP KSEITHLVFC SISGIDMPGA DYRLATLLGL
    160 170 180 190 200
    PLTVNRLMIY SQACHMGAAM LRIAKDLAEN NRGARVLVVA CEITVLSFRG
    210 220 230 240 250
    PNEGDFEALA GQAGFGDGAG AVVVGADPLE GIEKPIYEIA AAMQETVAES
    260 270 280 290 300
    QGAVGGHLRA FGWTFYFLNQ LPAIIADNLG RSLERALAPL GVREWNDVFW
    310 320 330 340 350
    VAHPGNWAII DAIEAKLQLS PDKLSTARHV FTEYGNMQSA TVYFVMDELR
    360 370 380
    KRSAVEGRST TGDGLQWGVL LGFGPGLSIE TVVLRSMPL
    Length:389
    Mass (Da):43,034
    Last modified:May 26, 2009 - v1
    Checksum:iD6532FE43817B2F3
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB495007 mRNA. Translation: BAH56226.1.

    Genome annotation databases

    KEGGiag:BAH56226.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB495007 mRNA. Translation: BAH56226.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OV2X-ray2.32A/B/C/D1-389[»]
    3OV3X-ray2.50A/B/C/D1-389[»]
    ProteinModelPortaliC0SVZ6.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:BAH56226.

    Phylogenomic databases

    KOiK13234.

    Enzyme and pathway databases

    UniPathwayiUPA00154.
    BioCyciMetaCyc:MONOMER-15409.
    BRENDAi2.3.1.217. 9125.
    2.3.1.219. 9125.

    Family and domain databases

    Gene3Di3.40.47.10. 2 hits.
    InterProiIPR012328. Chalcone/stilbene_synth_C.
    IPR001099. Chalcone/stilbene_synthase_N.
    IPR011141. Polyketide_synthase_type-III.
    IPR016039. Thiolase-like.
    [Graphical view]
    PfamiPF02797. Chal_sti_synt_C. 1 hit.
    PF00195. Chal_sti_synt_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000451. PKS_III. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCURS1_CURLO
    AccessioniPrimary (citable) accession number: C0SVZ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2013
    Last sequence update: May 26, 2009
    Last modified: November 11, 2015
    This is version 33 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.