Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

    Pathwayi: 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)DescriptionActionsGraphical viewLength
    Active sitei164Acyl-thioester intermediateCurated1
    Binding sitei197Substrate1 Publication1
    Binding sitei308Coenzyme A; via amide nitrogen2 Publications1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi164C → A, D or S: Loss of activity. 1 Publication1
    Mutagenesisi215F → S, W or Y: Drastically reduces catalytic efficiency. 2 Publications1
    Mutagenesisi256G → A: Decreases catalytic efficiency 2-fold. 1 Publication1
    Mutagenesisi256G → F or L: Drastically reduces catalytic efficiency. 1 Publication1
    Mutagenesisi256G → V: Decreases catalytic efficiency 7-fold. 1 Publication1
    Mutagenesisi265F → V: Decreases catalytic efficiency 2-fold. 1 Publication1
    Mutagenesisi303H → A, D, N or T: Drastically reduces catalytic efficiency. 1 Publication1
    Mutagenesisi303H → Q: Decreases catalytic efficiency 13-fold. 1 Publication1
    Mutagenesisi336N → A, D, H, K or Q: Drastically reduces catalytic efficiency. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002160071 – 389Chalcone synthase 2Add BLAST389

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    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 – 87Combined sources3
    Helixi91 – 117Combined sources27
    Helixi121 – 123Combined sources3
    Beta strandi126 – 133Combined sources8
    Beta strandi136 – 138Combined sources3
    Helixi140 – 148Combined sources9
    Beta strandi155 – 161Combined sources7
    Helixi166 – 179Combined sources14
    Beta strandi185 – 192Combined sources8
    Helixi194 – 196Combined sources3
    Helixi206 – 214Combined sources9
    Beta strandi218 – 227Combined sources10
    Turni230 – 232Combined sources3
    Beta strandi237 – 246Combined sources10
    Beta strandi253 – 259Combined sources7
    Beta strandi262 – 267Combined sources6
    Helixi271 – 287Combined sources17
    Helixi288 – 290Combined sources3
    Beta strandi297 – 302Combined sources6
    Helixi307 – 317Combined sources11
    Helixi321 – 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
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30074.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni55 – 62Coenzyme A binding8
    Regioni216 – 217Substrate binding2

    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.
    [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
    PDB 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.
    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.
    [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...

    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: November 2, 2016
    This is version 90 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.