ID   CFI1_LOTJA              Reviewed;         226 AA.
AC   Q8H0G2; Q84RQ2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Chalcone--flavanone isomerase 1;
DE            Short=Chalcone isomerase 1;
DE            EC=5.5.1.6;
GN   Name=CHI1;
OS   Lotus japonicus (Lotus corniculatus var. japonicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX   NCBI_TaxID=34305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC   STRAIN=cv. Gifu / B-129; TISSUE=Root;
RX   PubMed=12644647; DOI=10.1104/pp.004820;
RA   Shimada N., Aoki T., Sato S., Nakamura Y., Tabata S., Ayabe S.;
RT   "A cluster of genes encodes the two types of chalcone isomerase involved in
RT   the biosynthesis of general flavonoids and legume-specific 5-
RT   deoxy(iso)flavonoids in Lotus japonicus.";
RL   Plant Physiol. 131:941-951(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Root nodule;
RA   Flemetakis E., Katinakis P.;
RT   "Lotus japonicus nodule chalcone isomerase.";
RL   Submitted (MAR-2003) 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 chalcone)
CC       into naringenin. {ECO:0000269|PubMed:12644647}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a chalcone = a flavanone.; EC=5.5.1.6;
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8H0G2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8H0G2-2; Sequence=VSP_027872;
CC   -!- MISCELLANEOUS: Part of the biosynthetic pathway for all classes of
CC       flavonoids, a large class of secondary plant metabolites, many of which
CC       are brightly colored.
CC   -!- SIMILARITY: Belongs to the chalcone isomerase family. {ECO:0000305}.
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DR   EMBL; AB054801; BAC53983.1; -; mRNA.
DR   EMBL; AJ548840; CAD69022.1; -; mRNA.
DR   AlphaFoldDB; Q8H0G2; -.
DR   SMR; Q8H0G2; -.
DR   ProMEX; Q8H0G2; -.
DR   UniPathway; UPA00154; -.
DR   GO; GO:0045430; F:chalcone isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.890.20; -; 1.
DR   Gene3D; 3.50.70.10; -; 1.
DR   InterPro; IPR044164; CFI.
DR   InterPro; IPR016087; Chalcone_isomerase.
DR   InterPro; IPR016088; Chalcone_isomerase_3-sand.
DR   InterPro; IPR016089; Chalcone_isomerase_bundle_sf.
DR   InterPro; IPR036298; Chalcone_isomerase_sf.
DR   PANTHER; PTHR28039; PTHR28039; 1.
DR   Pfam; PF02431; Chalcone; 1.
DR   SUPFAM; SSF54626; SSF54626; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Flavonoid biosynthesis; Isomerase.
FT   CHAIN           1..226
FT                   /note="Chalcone--flavanone isomerase 1"
FT                   /id="PRO_0000300842"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            110
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         209..226
FT                   /note="LAERLPIVMNQGLLLTGN -> SFG (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_027872"
SQ   SEQUENCE   226 AA;  24431 MW;  7E363F405A87FC0F CRC64;
     MAPAKGSSLT PIQVENLQFP ASVTSPATAK SYFLGGAGER GLTIEGKFIK FTGIGVYLED
     TAVDSLATKW KGKSSQELQD SLDFFRDIIS SPSEKLIRGS KLRPLSGVEY SRKVMENCVA
     HMKSAGTYGE AEATAIEKFA EAFRKVDFPP GSSVFYRQST DGKLGLSFSL DDTIPEEEAV
     VIENKALSEA VLETMIGEHA VSPDLKRCLA ERLPIVMNQG LLLTGN