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Protein

Chalcone synthase 2

Gene

CHS2

Organism
Medicago sativa (Alfalfa)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.4 Publications

Catalytic activityi

3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO2.PROSITE-ProRule annotation

Kineticsi

  1. KM=4.1 µM for malonyl-CoA3 Publications
  2. KM=4.5 µM for 4-coumaroyl-CoA3 Publications
  3. KM=2.2 µM for benzoyl-CoA3 Publications
  4. KM=4.1 µM for hexanoyl-CoA3 Publications
  5. KM=5.1 µM for phenylacetyl-CoA3 Publications
  6. KM=5.2 µM for feruloyl-CoA3 Publications

    Pathway: flavonoid biosynthesis

    This protein is involved in the pathway flavonoid biosynthesis, which is part of Secondary metabolite biosynthesis.
    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 – 1641Acyl-thioester intermediateCurated
    Binding sitei197 – 1971Substrate1 Publication
    Binding sitei308 – 3081Coenzyme A; via amide nitrogen2 Publications

    GO - Molecular functioni

    • naringenin-chalcone synthase activity Source: UniProtKB

    GO - Biological processi

    • chalcone biosynthetic process Source: UniProtKB
    • flavonoid biosynthetic process Source: UniProtKB-UniPathway
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Flavonoid biosynthesis

    Enzyme and pathway databases

    BRENDAi2.3.1.74. 3078.
    UniPathwayiUPA00154.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chalcone synthase 2 (EC:2.3.1.74)
    Alternative name(s):
    Naringenin-chalcone synthase 2
    Gene namesi
    Name:CHS2
    OrganismiMedicago sativa (Alfalfa)
    Taxonomic identifieri3879 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi164 – 1641C → A, D or S: Loss of activity. 1 Publication
    Mutagenesisi215 – 2151F → S, W or Y: Drastically reduces catalytic efficiency. 2 Publications
    Mutagenesisi256 – 2561G → A: Decreases catalytic efficiency 2-fold. 1 Publication
    Mutagenesisi256 – 2561G → F or L: Drastically reduces catalytic efficiency. 1 Publication
    Mutagenesisi256 – 2561G → V: Decreases catalytic efficiency 7-fold. 1 Publication
    Mutagenesisi265 – 2651F → V: Decreases catalytic efficiency 2-fold. 1 Publication
    Mutagenesisi303 – 3031H → A, D, N or T: Drastically reduces catalytic efficiency. 1 Publication
    Mutagenesisi303 – 3031H → Q: Decreases catalytic efficiency 13-fold. 1 Publication
    Mutagenesisi336 – 3361N → A, D, H, K or Q: Drastically reduces catalytic efficiency. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 389389Chalcone synthase 2PRO_0000216007Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    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 – 873Combined sources
    Helixi91 – 11727Combined sources
    Helixi121 – 1233Combined sources
    Beta strandi126 – 1338Combined sources
    Beta strandi136 – 1383Combined sources
    Helixi140 – 1489Combined sources
    Beta strandi155 – 1617Combined sources
    Helixi166 – 17914Combined sources
    Beta strandi185 – 1928Combined sources
    Helixi194 – 1963Combined sources
    Helixi206 – 2149Combined sources
    Beta strandi218 – 22710Combined sources
    Turni230 – 2323Combined sources
    Beta strandi237 – 24610Combined sources
    Beta strandi253 – 2597Combined sources
    Beta strandi262 – 2676Combined sources
    Helixi271 – 28717Combined sources
    Helixi288 – 2903Combined sources
    Beta strandi297 – 3026Combined sources
    Helixi307 – 31711Combined sources
    Helixi321 – 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
    1BI5X-ray1.56A1-389[»]
    1BQ6X-ray1.56A2-389[»]
    1CGKX-ray1.84A1-389[»]
    1CGZX-ray1.70A1-389[»]
    1CHWX-ray1.90A/B1-389[»]
    1CMLX-ray1.69A1-389[»]
    1D6FX-ray1.69A1-389[»]
    1D6HX-ray2.15A3-389[»]
    1D6IX-ray2.00A/B2-389[»]
    1I86X-ray1.50A1-389[»]
    1I88X-ray1.45A/B1-389[»]
    1I89X-ray1.86A/B1-389[»]
    1I8BX-ray1.95A/B1-389[»]
    1JWXX-ray1.63A1-389[»]
    1U0VX-ray1.90A/B1-389[»]
    1U0WX-ray2.00A/B/C/D1-389[»]
    ProteinModelPortaliP30074.
    SMRiP30074. Positions 3-389.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30074.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni55 – 628Coenzyme A binding
    Regioni216 – 2172Substrate binding

    Sequence similaritiesi

    Belongs to the chalcone/stilbene synthases family.Curated

    Family and domain databases

    Gene3Di3.40.47.10. 2 hits.
    InterProiIPR012328. Chalcone/stilbene_synth_C.
    IPR018088. Chalcone/stilbene_synthase_AS.
    IPR001099. Chalcone/stilbene_synthase_N.
    IPR011141. Polyketide_synthase_type-III.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [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.
    PROSITEiPS00441. CHALCONE_SYNTH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P30074-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVSVSEIRKA QRAEGPATIL AIGTANPANC VEQSTYPDFY FKITNSEHKT
    60 70 80 90 100
    ELKEKFQRMC DKSMIKRRYM YLTEEILKEN PNVCEYMAPS LDARQDMVVV
    110 120 130 140 150
    EVPRLGKEAA VKAIKEWGQP KSKITHLIVC TTSGVDMPGA DYQLTKLLGL
    160 170 180 190 200
    RPYVKRYMMY QQGCFAGGTV LRLAKDLAEN NKGARVLVVC SEVTAVTFRG
    210 220 230 240 250
    PSDTHLDSLV GQALFGDGAA ALIVGSDPVP EIEKPIFEMV WTAQTIAPDS
    260 270 280 290 300
    EGAIDGHLRE AGLTFHLLKD VPGIVSKNIT KALVEAFEPL GISDYNSIFW
    310 320 330 340 350
    IAHPGGPAIL DQVEQKLALK PEKMNATREV LSEYGNMSSA CVLFILDEMR
    360 370 380
    KKSTQNGLKT TGEGLEWGVL FGFGPGLTIE TVVLRSVAI
    Length:389
    Mass (Da):42,706
    Last modified:April 1, 1993 - v1
    Checksum:iE03422EE332A5408
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L02902 mRNA. Translation: AAA02824.1.
    PIRiS35164.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L02902 mRNA. Translation: AAA02824.1.
    PIRiS35164.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BI5X-ray1.56A1-389[»]
    1BQ6X-ray1.56A2-389[»]
    1CGKX-ray1.84A1-389[»]
    1CGZX-ray1.70A1-389[»]
    1CHWX-ray1.90A/B1-389[»]
    1CMLX-ray1.69A1-389[»]
    1D6FX-ray1.69A1-389[»]
    1D6HX-ray2.15A3-389[»]
    1D6IX-ray2.00A/B2-389[»]
    1I86X-ray1.50A1-389[»]
    1I88X-ray1.45A/B1-389[»]
    1I89X-ray1.86A/B1-389[»]
    1I8BX-ray1.95A/B1-389[»]
    1JWXX-ray1.63A1-389[»]
    1U0VX-ray1.90A/B1-389[»]
    1U0WX-ray2.00A/B/C/D1-389[»]
    ProteinModelPortaliP30074.
    SMRiP30074. Positions 3-389.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00154.
    BRENDAi2.3.1.74. 3078.

    Miscellaneous databases

    EvolutionaryTraceiP30074.

    Family and domain databases

    Gene3Di3.40.47.10. 2 hits.
    InterProiIPR012328. Chalcone/stilbene_synth_C.
    IPR018088. Chalcone/stilbene_synthase_AS.
    IPR001099. Chalcone/stilbene_synthase_N.
    IPR011141. Polyketide_synthase_type-III.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [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.
    PROSITEiPS00441. CHALCONE_SYNTH. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Stress responses in alfalfa (Medicago sativa L.). 15. Characterization and expression patterns of members of a subset of the chalcone synthase multigene family."
      Junghans H., Dalkin K., Dixon R.A.
      Plant Mol. Biol. 22:239-253(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis."
      Ferrer J.L., Jez J.M., Bowman M.E., Dixon R.A., Noel J.P.
      Nat. Struct. Biol. 6:775-784(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND COENZYME A.
    3. "Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase."
      Jez J.M., Ferrer J.L., Bowman M.E., Dixon R.A., Noel J.P.
      Biochemistry 39:890-902(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) IN COMPLEX WITH COENZYME A, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-164; PHE-215; HIS-303 AND ASN-336.
    4. "Structure-guided programming of polyketide chain-length determination in chalcone synthase."
      Jez J.M., Bowman M.E., Noel J.P.
      Biochemistry 40:14829-14838(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-256.
    5. "Expanding the biosynthetic repertoire of plant type III polyketide synthases by altering starter molecule specificity."
      Jez J.M., Bowman M.E., Noel J.P.
      Proc. Natl. Acad. Sci. U.S.A. 99:5319-5324(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-215 AND PHE-265.
    6. "An aldol switch discovered in stilbene synthases mediates cyclization specificity of type III polyketide synthases."
      Austin M.B., Bowman M.E., Ferrer J.-L., Schroeder J., Noel J.P.
      Chem. Biol. 11:1179-1194(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), FUNCTION.

    Entry informationi

    Entry nameiCHS2_MEDSA
    AccessioniPrimary (citable) accession number: P30074
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: April 1, 2015
    This is version 85 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

    External Data

    Dasty 3

    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 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.