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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)DescriptionActionsGraphical viewLength
    Active sitei164By similarity1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi211G → F or W: Strong reduction in enzyme activity. 1 Publication1
    Mutagenesisi303H → A or Q: Strong reduction in enzyme activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004225711 – 389Curcumin synthase 1Add BLAST389

    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

    1389
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi4 – 11Combined sources8
    Beta strandi18 – 25Combined sources8
    Beta strandi30 – 32Combined sources3
    Helixi33 – 35Combined sources3
    Helixi36 – 43Combined sources8
    Helixi50 – 62Combined sources13
    Beta strandi67 – 69Combined sources3
    Helixi74 – 79Combined sources6
    Helixi81 – 84Combined sources4
    Beta strandi85 – 88Combined sources4
    Helixi91 – 117Combined sources27
    Helixi121 – 123Combined sources3
    Beta strandi126 – 133Combined sources8
    Helixi140 – 148Combined sources9
    Beta strandi154 – 161Combined sources8
    Helixi166 – 180Combined sources15
    Beta strandi185 – 192Combined sources8
    Helixi194 – 196Combined sources3
    Helixi206 – 214Combined sources9
    Beta strandi218 – 227Combined sources10
    Turni230 – 232Combined sources3
    Beta strandi236 – 246Combined sources11
    Beta strandi253 – 259Combined sources7
    Beta strandi262 – 267Combined sources6
    Helixi271 – 276Combined sources6
    Helixi280 – 287Combined sources8
    Helixi288 – 290Combined sources3
    Helixi295 – 297Combined sources3
    Beta strandi298 – 302Combined sources5
    Helixi307 – 317Combined sources11
    Turni321 – 324Combined sources4
    Helixi325 – 334Combined sources10
    Helixi338 – 340Combined sources3
    Helixi341 – 355Combined sources15
    Turni361 – 364Combined sources4
    Beta strandi366 – 374Combined sources9
    Turni375 – 377Combined sources3
    Beta strandi378 – 386Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3OV2X-ray2.32A/B/C/D1-389[»]
    3OV3X-ray2.50A/B/C/D1-389[»]
    ProteinModelPortaliC0SVZ6.
    SMRiC0SVZ6.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3OV2X-ray2.32A/B/C/D1-389[»]
    3OV3X-ray2.50A/B/C/D1-389[»]
    ProteinModelPortaliC0SVZ6.
    SMRiC0SVZ6.
    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 2, 2016
    This is version 34 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.