ID   CFI_CANGE               Reviewed;         226 AA.
AC   Q3Y4F4; Q3Y4F3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 14.
DE   RecName: Full=Chalcone--flavonone isomerase;
DE            Short=Chalcone isomerase;
DE            EC=5.5.1.6;
GN   Name=CHI;
OS   Canna generalis (Canna lily) (Canna glauca x Canna indica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Zingiberales; Cannaceae;
OC   Canna.
OX   NCBI_TaxID=341692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Li J., Li M.R., Li H.Q.;
RT   "Isolation and characterization of a Canna generalis gene encoding
RT   chalcone flavonone isomerase.";
RL   Submitted (AUG-2005) 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; DQ160231; AAZ80910.1; -; Genomic_DNA.
DR   EMBL; DQ160232; AAZ80911.1; -; mRNA.
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    226       Chalcone--flavonone isomerase.
FT                                /FTId=PRO_0000314570.
FT   BINDING      51     51       Substrate (By similarity).
FT   BINDING     116    116       Substrate (By similarity).
FT   BINDING     194    194       Substrate (By similarity).
FT   SITE        109    109       Important for catalytic activity (By
FT                                similarity).
FT   CONFLICT     66     66       G -> A (in Ref. 1; AAZ80911).
SQ   SEQUENCE   226 AA;  24228 MW;  F954066B1C11D07B CRC64;
     MAQAGVSLPK LVIGEVTFPP AAAPPGSSSS LFLAGAGERG LEIDRQFVVF TAIGVYLEDL
     AVSTLGPKWK GKTADDLAGN SDFFRDIFTG PFEKFTRITM VKPLSGQQYS EKVEENCVAH
     WKAAGTYTEA EAAAVEKFKE ACKNETFPPG TSILFTHQVS PASLTITFWR EGSMPETGNT
     VIESKALSEA ILESIIGKHG VSPGAKRSVA QRLSEILEEV KLEGSK
//