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Reviewed, UniProtKB/Swiss-Prot P30074 (CHS2_MEDSA)

Last modified February 9, 2010. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Chalcone synthase 2
    EC=2.3.1.74
Alternative name(s):
    Naringenin-chalcone synthase 2
Gene names
Name: CHS2
OrganismMedicago sativa (Alfalfa)
Taxonomic identifier3879 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

Protein attributes

Sequence length389 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 can under specific conditions spontaneously isomerize into naringenin.

Catalytic activity

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

Pathway

Secondary metabolite biosynthesis; flavonoid biosynthesis.

Sequence similarities

Belongs to the chalcone/stilbene synthases family.

Ontologies

Keywords
   Biological processFlavonoid biosynthesis
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processflavonoid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionacyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

naringenin-chalcone synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 389389Chalcone synthase 2
PRO_0000216007

Sites

Active site1641

Secondary structure

................................................................. 389
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30074-1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: E03422EE332A5408

FASTA38942,706
        10         20         30         40         50         60 
MVSVSEIRKA QRAEGPATIL AIGTANPANC VEQSTYPDFY FKITNSEHKT ELKEKFQRMC 

        70         80         90        100        110        120 
DKSMIKRRYM YLTEEILKEN PNVCEYMAPS LDARQDMVVV EVPRLGKEAA VKAIKEWGQP 

       130        140        150        160        170        180 
KSKITHLIVC TTSGVDMPGA DYQLTKLLGL RPYVKRYMMY QQGCFAGGTV LRLAKDLAEN 

       190        200        210        220        230        240 
NKGARVLVVC SEVTAVTFRG PSDTHLDSLV GQALFGDGAA ALIVGSDPVP EIEKPIFEMV 

       250        260        270        280        290        300 
WTAQTIAPDS EGAIDGHLRE AGLTFHLLKD VPGIVSKNIT KALVEAFEPL GISDYNSIFW 

       310        320        330        340        350        360 
IAHPGGPAIL DQVEQKLALK PEKMNATREV LSEYGNMSSA CVLFILDEMR KKSTQNGLKT 

       370        380 
TGEGLEWGVL FGFGPGLTIE TVVLRSVAI 

« Hide

References

[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: 8507827] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: 10653632] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02902 mRNA. Translation: AAA02824.1.
PIRS35164.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.3.1.74. 815.

Family and domain databases

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]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
PfamPF02797. Chal_sti_synt_C. 1 hit.
PF00195. Chal_sti_synt_N. 1 hit.
[Graphical view]
PIRSFPIRSF000451. PKS_III. 1 hit.
PROSITEPS00441. CHALCONE_SYNTH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHS2_MEDSA
AccessionPrimary (citable) accession number: P30074
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: February 9, 2010
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents