ID   CFI_DIACA               Reviewed;         221 AA.
AC   Q43754;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 43.
DE   RecName: Full=Chalcone--flavonone isomerase;
DE            Short=Chalcone isomerase;
DE            EC=5.5.1.6;
GN   Name=CHI;
OS   Dianthus caryophyllus (Carnation) (Clove pink).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   Caryophyllales; Caryophyllaceae; Dianthus.
OX   NCBI_TaxID=3570;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Tanga; TISSUE=Petal;
RA   Henkel J., Ruhnau-Brich B., Dedio J., Wassenegger M., Sommer H.,
RA   Forkmann G.;
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the intramolecular cyclization of bicyclic
CC       chalcones into tricyclic (S)-flavanones. Responsible for the
CC       isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed
CC       chalcone) into naringenin (By similarity).
CC   -!- CATALYTIC ACTIVITY: A chalcone = a flavanone.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid
CC       biosynthesis.
CC   -!- MISCELLANEOUS: Part of the biosynthetic pathway for all classes of
CC       flavonoids, a large class of secondary plant metabolites, many of
CC       which are brightly colored.
CC   -!- SIMILARITY: Belongs to the chalcone isomerase family.
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DR   EMBL; Z67989; CAA91931.1; -; mRNA.
DR   PIR; T10712; T10712.
DR   HSSP; P28012; 1JX1.
DR   BRENDA; 5.5.1.6; 21500.
DR   GO; GO:0045430; F:chalcone isomerase activity; IEA:EC.
DR   GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016088; Chalcone_isomerase_3-sand.
DR   InterPro; IPR003466; Chalcone_isomerase_subgr.
DR   Gene3D; G3DSA:3.50.70.10; Chalcone; 1.
DR   Pfam; PF02431; Chalcone; 1.
PE   2: Evidence at transcript level;
KW   Flavonoid biosynthesis; Isomerase.
FT   CHAIN         1    221       Chalcone--flavonone isomerase.
FT                                /FTId=PRO_0000166430.
FT   BINDING      47     47       Substrate (By similarity).
FT   BINDING     112    112       Substrate (By similarity).
FT   BINDING     189    189       Substrate (By similarity).
FT   SITE        105    105       Important for catalytic activity (By
FT                                similarity).
SQ   SEQUENCE   221 AA;  24088 MW;  184FDD5496D03888 CRC64;
     MAEITQIQVE SHVFPPEVKP PGSDKTFFLG GAGVRGLEIQ GKFIKFTAIA VYIEDDAVSS
     LAVKWKGKTA DELTDSVDFF KDIVTGPFEK FTQVTMILPL TGQQYSEKVV ENCVAHWKSV
     GTYTDAESEA TQKFLQVFKN VSNPPGASIL FTQSPLGSLT ISFSKDGSLP ENGKEVIVNK
     QLSEAVLQSI IGKHGVSPEA KKSLSARLSD LINQHENPKK E
//