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Q9FUB7 (CHSY_HYPAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chalcone synthase

EC=2.3.1.74
Alternative name(s):
Naringenin-chalcone synthase
OrganismHypericum androsaemum (Tutsan)
Taxonomic identifier140968 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesHypericaceaeHypericeaeHypericum

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which undergoes enzyme-catalyzed or spontaneous isomerization into naringenin.

Catalytic activity

3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO2. Ref.1

Pathway

Secondary metabolite biosynthesis; flavonoid biosynthesis.

Sequence similarities

Belongs to the chalcone/stilbene synthases family. Ref.1

Biophysicochemical properties

Kinetic parameters:

KM=10.8 µM for malonyl-CoA Ref.1

KM=4.9 µM for 4-coumaroyl-CoA Ref.1

KM=6.8 µM for benzoyl-CoA Ref.1

pH dependence:

Optimum pH is 7.0. Ref.1

Temperature dependence:

Optimum temperature is 35 degrees Celsius. Ref.1

Ontologies

Keywords
   Biological processFlavonoid biosynthesis
   Molecular functionAcyltransferase
Transferase
Gene Ontology (GO)
   Biological_processflavonoid biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionnaringenin-chalcone synthase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 390390Chalcone synthase
PRO_0000215982

Sites

Active site1641 By similarity UniProtKB P30074

Experimental info

Mutagenesis2561G → A: 63% active. Ref.1
Mutagenesis2631L → M: No effect. Ref.1
Mutagenesis2651F → Y: 67% active. Ref.1
Mutagenesis3381S → G: No effect. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9FUB7 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 023326D7DFC44327

FASTA39042,713
        10         20         30         40         50         60 
MVTVEEVRKA QRAEGPATVM AIGTAVPPNC VDQATYPDYY FRITNSEHKA ELKEKFQRMC 

        70         80         90        100        110        120 
DKSQIKKRYM YLNEEVLKEN PNMCAYMAPS LDARQDIVVV EVPKLGKEAA VKAIKEWGQP 

       130        140        150        160        170        180 
KSKITHLVFC TTSGVDMPGA DYQLTKLLGL RPSVKRLMMY QQGCFAGGTV LRLAKDLAEN 

       190        200        210        220        230        240 
NKGARVLVVC SEITAVTFRG PTDTHLDSLV GQALFGDGAA AIIIGSDPIP EVEKPLFELV 

       250        260        270        280        290        300 
SAAQTILPDS EGAIDGHLRE VGLTFHLLKD VPGLISKNVE KSLTEAFKPL GISDWNSLFW 

       310        320        330        340        350        360 
IAHPGGPAIL DQVEAKLSLK PEKLRATRHV LSEYGNMSSA CVLFILDEMR RKSKEDGLKT 

       370        380        390 
TGEGIEWGVL FGFGPGLTVE TVVLHSVAIN 

« Hide

References

[1]"Benzophenone synthase and chalcone synthase from Hypericum androsaemum cell cultures: cDNA cloning, functional expression, and site-directed mutagenesis of two polyketide synthases."
Liu B., Falkenstein-Paul H., Schmidt W., Beerhues L.
Plant J. 34:847-855(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-256; LEU-263; PHE-265 AND SER-338.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF315345 mRNA. Translation: AAG30295.1.

3D structure databases

ProteinModelPortalQ9FUB7.
SMRQ9FUB7. Positions 3-389.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.3.1.74. 2742.
UniPathwayUPA00154.

Family and domain databases

Gene3D3.40.47.10. 2 hits.
InterProIPR012328. 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]
PfamPF02797. Chal_sti_synt_C. 1 hit.
PF00195. Chal_sti_synt_N. 1 hit.
[Graphical view]
PIRSFPIRSF000451. PKS_III. 1 hit.
SUPFAMSSF53901. SSF53901. 2 hits.
PROSITEPS00441. CHALCONE_SYNTH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHSY_HYPAN
AccessionPrimary (citable) accession number: Q9FUB7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2001
Last modified: February 19, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways