ID   CFI_CAMSI               Reviewed;         230 AA.
AC   Q45QI7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=Chalcone--flavonone isomerase;
DE            Short=Chalcone isomerase;
DE            EC=5.5.1.6;
GN   Name=CHI;
OS   Camellia sinensis (Tea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; Ericales; Theaceae; Camellia.
OX   NCBI_TaxID=4442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. UPASI-10;
RA   Rani A., Kumar S., Ahuja P.S.;
RT   "Camellia sinensis cultivar UPASI-10 chalcone isomerase (CHI) mRNA.";
RL   Submitted (SEP-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; DQ120521; AAZ17563.2; -; mRNA.
DR   BRENDA; 5.5.1.6; 568.
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    230       Chalcone--flavonone isomerase.
FT                                /FTId=PRO_0000300832.
FT   BINDING      52     52       Substrate (By similarity).
FT   BINDING     117    117       Substrate (By similarity).
FT   BINDING     194    194       Substrate (By similarity).
FT   SITE        110    110       Important for catalytic activity (By
FT                                similarity).
SQ   SEQUENCE   230 AA;  24723 MW;  AACCE599B8E0F2A1 CRC64;
     MSPSQSPSVA QVQIESHVFP PTVKPPGTSK PFFLGGAGER GLEIQGKFIK FTAIGVYLED
     SAIPSLAVKW KGKTAEELTD SVDFFRDIVS GPFEKFTQVT MILPLTGQQY SEKVTENCVA
     YWKAVGTYTD AEAKAIEKFI EVFKDETFPP GGSILFTQSP LGSLTIAFSK DGSLPETGTV
     VMENKQLSEA VLESIIGKHG VSPAAKKSLA ARMSELLKEK PEAQTAAAAE
//