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P30074

- CHS2_MEDSA

UniProt

P30074 - CHS2_MEDSA

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Protein

Chalcone synthase 2

Gene

CHS2

Organism
Medicago sativa (Alfalfa)
Status
Reviewed - 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

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
Complete GO annotation...

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 – 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 .
PIRi S35164.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 84 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