ID   CFI_ELAUM               Reviewed;         256 AA.
AC   O65333;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Chalcone--flavanone isomerase;
DE            Short=Chalcone isomerase;
DE            EC=5.5.1.6;
GN   Name=CHI;
OS   Elaeagnus umbellata (Autumn olive) (Elaeagnus crispa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Elaeagnaceae; Elaeagnus.
OX   NCBI_TaxID=43233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Root nodule;
RA   Kim H.-B., Oh C.J., Lee H., An C.-S.;
RT   "A type-I chalcone isomerase mRNA is highly expressed in the root nodules
RT   of Elaeagnus umbellata.";
RL   J. Plant Biol. 46:263-270(2003).
RN   [2]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=17646716;
RA   Kim H.-B., Bae J.H., Lim J.D., Yu C.Y., An C.-S.;
RT   "Expression of a functional type-I chalcone isomerase gene is localized to
RT   the infected cells of root nodules of Elaeagnus umbellata.";
RL   Mol. Cells 23:405-409(2007).
RN   [3]
RP   REVIEW, AND NOMENCLATURE.
RX   PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA   Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA   Tohge T., Fernie A.R.;
RT   "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT   diversity.";
RL   Plant Physiol. Biochem. 72:21-34(2013).
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:17646716}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a chalcone = a flavanone.; EC=5.5.1.6;
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC   -!- TISSUE SPECIFICITY: Nodules. {ECO:0000269|PubMed:17646716,
CC       ECO:0000269|Ref.1}.
CC   -!- DEVELOPMENTAL STAGE: Primarily expressed in the infected cells of the
CC       fixation zones in root nodules. {ECO:0000269|PubMed:17646716}.
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; AF061808; AAC16013.1; -; mRNA.
DR   AlphaFoldDB; O65333; -.
DR   SMR; O65333; -.
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   Flavonoid biosynthesis; Isomerase.
FT   CHAIN           1..256
FT                   /note="Chalcone--flavanone isomerase"
FT                   /id="PRO_0000166431"
FT   REGION          219..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            109
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   256 AA;  27933 MW;  BE23C6712B711E7A CRC64;
     MAPFTKSVTE VQVESVIFPP EVKPPGSSKT LFLGGAGVRG IEIQGKFIKF TAIGVYLEDN
     AVPSLAVKWK GKSAQELTES VEFFRDIVTG PMEKFTRVTT ILPLTGQQYS EKVSENCVAA
     WKSLGIYSDA EAKAIEKFIE IFKDQTFPPA ASNLFTQSPL GSLTMSFSKD GSIPEVGNAV
     LENKLLSEAV LESIIGKHGV SPEAKQNLAT RLVQLLNENS TTDLNESENE KLNSNEVSKE
     EKPLQVEKSA FKEVEV