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P30074

- CHS2_MEDSA

UniProt

P30074 - CHS2_MEDSA

Protein

Chalcone synthase 2

Gene

CHS2

Organism
Medicago sativa (Alfalfa)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    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

    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

    1. naringenin-chalcone synthase activity Source: UniProtKB

    GO - Biological processi

    1. chalcone biosynthetic process Source: UniProtKB
    2. flavonoid biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Flavonoid biosynthesis

    Enzyme and pathway databases

    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 – 118
    Beta strandi18 – 258
    Beta strandi30 – 323
    Helixi33 – 353
    Helixi36 – 438
    Helixi50 – 6213
    Beta strandi67 – 693
    Helixi74 – 796
    Helixi81 – 844
    Beta strandi85 – 873
    Helixi91 – 11727
    Helixi121 – 1233
    Beta strandi126 – 1338
    Beta strandi136 – 1383
    Helixi140 – 1489
    Beta strandi155 – 1617
    Helixi166 – 17914
    Beta strandi185 – 1928
    Helixi194 – 1963
    Helixi206 – 2149
    Beta strandi218 – 22710
    Turni230 – 2323
    Beta strandi237 – 24610
    Beta strandi253 – 2597
    Beta strandi262 – 2676
    Helixi271 – 28717
    Helixi288 – 2903
    Beta strandi297 – 3026
    Helixi307 – 31711
    Helixi321 – 3244
    Helixi325 – 33410
    Helixi338 – 3403
    Helixi341 – 35515
    Turni361 – 3644
    Beta strandi366 – 3749
    Turni375 – 3773
    Beta strandi378 – 3869

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MVSVSEIRKA QRAEGPATIL AIGTANPANC VEQSTYPDFY FKITNSEHKT    50
    ELKEKFQRMC DKSMIKRRYM YLTEEILKEN PNVCEYMAPS LDARQDMVVV 100
    EVPRLGKEAA VKAIKEWGQP KSKITHLIVC TTSGVDMPGA DYQLTKLLGL 150
    RPYVKRYMMY QQGCFAGGTV LRLAKDLAEN NKGARVLVVC SEVTAVTFRG 200
    PSDTHLDSLV GQALFGDGAA ALIVGSDPVP EIEKPIFEMV WTAQTIAPDS 250
    EGAIDGHLRE AGLTFHLLKD VPGIVSKNIT KALVEAFEPL GISDYNSIFW 300
    IAHPGGPAIL DQVEQKLALK PEKMNATREV LSEYGNMSSA CVLFILDEMR 350
    KKSTQNGLKT TGEGLEWGVL FGFGPGLTIE TVVLRSVAI 389
    Length:389
    Mass (Da):42,706
    Last modified:April 1, 1993 - v1
    Checksum:iE03422EE332A5408
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02902 mRNA. Translation: AAA02824.1.
    PIRiS35164.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02902 mRNA. Translation: AAA02824.1 .
    PIRi S35164.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BI5 X-ray 1.56 A 1-389 [» ]
    1BQ6 X-ray 1.56 A 2-389 [» ]
    1CGK X-ray 1.84 A 1-389 [» ]
    1CGZ X-ray 1.70 A 1-389 [» ]
    1CHW X-ray 1.90 A/B 1-389 [» ]
    1CML X-ray 1.69 A 1-389 [» ]
    1D6F X-ray 1.69 A 1-389 [» ]
    1D6H X-ray 2.15 A 3-389 [» ]
    1D6I X-ray 2.00 A/B 2-389 [» ]
    1I86 X-ray 1.50 A 1-389 [» ]
    1I88 X-ray 1.45 A/B 1-389 [» ]
    1I89 X-ray 1.86 A/B 1-389 [» ]
    1I8B X-ray 1.95 A/B 1-389 [» ]
    1JWX X-ray 1.63 A 1-389 [» ]
    1U0V X-ray 1.90 A/B 1-389 [» ]
    1U0W X-ray 2.00 A/B/C/D 1-389 [» ]
    ProteinModelPortali P30074.
    SMRi P30074. Positions 3-389.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00154 .

    Miscellaneous databases

    EvolutionaryTracei P30074.

    Family and domain databases

    Gene3Di 3.40.47.10. 2 hits.
    InterProi IPR012328. 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 ]
    Pfami PF02797. Chal_sti_synt_C. 1 hit.
    PF00195. Chal_sti_synt_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000451. PKS_III. 1 hit.
    SUPFAMi SSF53901. SSF53901. 2 hits.
    PROSITEi PS00441. CHALCONE_SYNTH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 83 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