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UniProtKB/Swiss-Prot entry P28012


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CFI1_MEDSA
Primary accession number P28012
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 53)
Name and origin of the protein
Protein name Chalcone--flavonone isomerase 1
Synonyms Chalcone isomerase 1
EC 5.5.1.6
Gene name
Name: CHI1
Synonyms: CHI-1
From
Medicago sativa (Alfalfa) [TaxID: 3879] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Trifolieae; Medicago.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Iroquois;
DOI=10.1007/BF00029858; PubMed=8193301 [NCBI, ExPASy, EBI, Israel, Japan]
McKhann H.I., Hirsch A.M.;
"Isolation of chalcone synthase and chalcone isomerase cDNAs from alfalfa (Medicago sativa L.): highest transcript levels occur in young roots and root tips.";
Plant Mol. Biol. 24:767-777(1994).
[2]
ERRATUM.
McKhann H.I., Hirsch A.M.;
Plant Mol. Biol. 25:759-759(1994).
[3]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH (2S)-NARINGENIN, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TYR-106.
DOI=10.1038/79025; PubMed=10966651 [NCBI, ExPASy, EBI, Israel, Japan]
Jez J.M., Bowman M.E., Dixon R.A., Noel J.P.;
"Structure and mechanism of the evolutionarily unique plant enzyme chalcone isomerase.";
Nat. Struct. Biol. 7:786-791(2000).
[4]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF THR-48; TYR-106; ASN-113 AND THR-190.
DOI=10.1021/bi0255266; PubMed=11955065 [NCBI, ExPASy, EBI, Israel, Japan]
Jez J.M., Bowman M.E., Noel J.P.;
"Role of hydrogen bonds in the reaction mechanism of chalcone isomerase.";
Biochemistry 41:5168-5176(2002).
[5]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1074/jbc.M109224200; PubMed=11698411 [NCBI, ExPASy, EBI, Israel, Japan]
Jez J.M., Noel J.P.;
"Reaction mechanism of chalcone isomerase. pH dependence, diffusion control, and product binding differences.";
J. Biol. Chem. 277:1361-1369(2002).
Comments
  • FUNCTION: Catalyzes the intramolecular cyclization of bicyclic chalcones into tricyclic (S)-flavanones. Responsible for the isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone) into naringenin.
  • CATALYTIC ACTIVITY: A chalcone = a flavanone.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=8.4 µM for 4,2',4'-trihydroxychalcone (at pH 7.5 and 25 degrees Celsius);
    KM=15.7 µM for 6'-deoxychalcone (at pH 7.5 and 25 degrees Celsius);
    KM=22.7 µM for 2',4'-dihydroxychalcone (at pH 7.5 and 25 degrees Celsius);
    KM=42.5 µM for 4,2'-dihydroxychalcone (at pH 7.5 and 25 degrees Celsius);
    KM=112 µM for 4,2',4',6'-tetrahydroxychalcone (at pH 7.5 and 25 degrees Celsius);
    pH dependence:   Optimum pH is 7-8.5 with 4,2',4'-trihydroxychalcone as substrate, at 25 degrees Celsius;
  • PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
  • DEVELOPMENTAL STAGE: Highest expression in young root tips.
  • MISCELLANEOUS: Part of the biosynthetic pathway for all classes of flavonoids, a large class of secondary plant metabolites, many of which are brightly colored.
  • SIMILARITY: Belongs to the chalcone isomerase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M91079; AAB41524.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S44371; S44371.
3D structure databases
PDB
1EYP; X-ray; 2.50 A; A/B=1-222.[ExPASy / RCSB / EBI]
1EYQ; X-ray; 1.85 A; A/B=1-222.[ExPASy / RCSB / EBI]
1FM7; X-ray; 2.30 A; A/B=1-222.[ExPASy / RCSB / EBI]
1FM8; X-ray; 2.30 A; A/B=1-222.[ExPASy / RCSB / EBI]
1JEP; X-ray; 2.10 A; A/B=1-222.[ExPASy / RCSB / EBI]
1JX0; X-ray; 2.85 A; A/B=1-222.[ExPASy / RCSB / EBI]
1JX1; X-ray; 2.30 A; A/B/C/D/E/F=1-222.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EYP; -.
1EYQ; -.
1FM7; -.
1FM8; -.
1JEP; -.
1JX0; -.
1JX1; -.
ModBase P28012.
Ontologies
GO
GO:0045430; Molecular function: chalcone isomerase activity (inferred from electronic annotation from InterPro).
GO:0009813; Biological process: flavonoid biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR003466; Chalcone_isomerase.
IPR016088; Chalcone_isomerase_3-sand.
Graphical view of domain structure.
Gene3D G3DSA:3.50.70.10; Chalcone; 1.
Pfam PF02431; Chalcone; 1.
Pfam graphical view of domain structure.
BLOCKS P28012.
ProtoNet P28012.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Flavonoid biosynthesis; Isomerase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   222  222     Chalcone--flavonone isomerase 1. PRO_0000166434
BINDING   48    48        Substrate (By similarity). 
BINDING   113   113        Substrate (By similarity). 
BINDING   190   190        Substrate (By similarity). 
SITE   106   106  1     Important for catalytic activity. 
MUTAGEN   48    48        T->A: Strongly reduced reaction rate. 
MUTAGEN   48    48        T->S: Reduced reaction rate. 
MUTAGEN   106   106        Y->F: Strongly reduced reaction rate. 
MUTAGEN   113   113        N->A: Reduced reaction rate. 
MUTAGEN   190   190        T->A: Reduced reaction rate. 
STRAND   8    10  3      
STRAND   13    15  3      
STRAND   17    20  4      
TURN   22    24  3      
STRAND   27    40  14      
STRAND   43    55  13      
HELIX   58    66  9      
HELIX   71    75  5      
HELIX   78    86  9      
STRAND   91    99  9      
HELIX   103   120  18      
HELIX   126   139  14      
STRAND   149   155  7      
TURN   156   158  3      
STRAND   159   169  11      
STRAND   175   179  5      
HELIX   181   192  12      
HELIX   200   214  15      
Sequence information
Length: 222 AA [This is the length of the unprocessed precursor] Molecular weight: 23826 Da [This is the MW of the unprocessed precursor] CRC64: 7767A72084AB4800 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAASITAITV ENLEYPAVVT SPVTGKSYFL GGAGERGLTI EGNFIKFTAI GVYLEDIAVA 

        70         80         90        100        110        120 
SLAAKWKGKS SEELLETLDF YRDIISGPFE KLIRGSKIRE LSGPEYSRKV MENCVAHLKS 

       130        140        150        160        170        180 
VGTYGDAEAE AMQKFAEAFK PVNFPPGASV FYRQSPDGIL GLSFSPDTSI PEKEAALIEN 

       190        200        210        220 
KAVSSAVLET MIGEHAVSPD LKRCLAARLP ALLNEGAFKI GN 

P28012 in FASTA format

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