CFI3_ARATH
ID CFI3_ARATH Reviewed; 209 AA.
AC Q8VZW3; Q9FLC7;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable chalcone--flavanone isomerase 3;
DE Short=Chalcone isomerase 3;
DE EC=5.5.1.6;
DE AltName: Full=Chalcone isomerase-like 1;
GN Name=CHI3; Synonyms=CHI-L1, CHIL; OrderedLocusNames=At5g05270;
GN ORFNames=K18I23.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND INDUCTION BY PAP1.
RX PubMed=15807784; DOI=10.1111/j.1365-313x.2005.02371.x;
RA Tohge T., Nishiyama Y., Hirai M.Y., Yano M., Nakajima J., Awazuhara M.,
RA Inoue E., Takahashi H., Goodenowe D.B., Kitayama M., Noji M., Yamazaki M.,
RA Saito K.;
RT "Functional genomics by integrated analysis of metabolome and transcriptome
RT of Arabidopsis plants over-expressing an MYB transcription factor.";
RL Plant J. 42:218-235(2005).
RN [6]
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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 5-209.
RX PubMed=22622584; DOI=10.1038/nature11009;
RA Ngaki M.N., Louie G.V., Philippe R.N., Manning G., Pojer F., Bowman M.E.,
RA Li L., Larsen E., Wurtele E.S., Noel J.P.;
RT "Evolution of the chalcone-isomerase fold from fatty-acid binding to
RT stereospecific catalysis.";
RL Nature 485:530-533(2012).
CC -!- FUNCTION: Involved in anthocyanin biosynthesis.
CC {ECO:0000305|PubMed:15807784}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a chalcone = a flavanone.; EC=5.5.1.6;
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- INDUCTION: Induced by PAP1. {ECO:0000269|PubMed:15807784}.
CC -!- SIMILARITY: Belongs to the chalcone isomerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09970.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB010692; BAB09970.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED90848.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90849.1; -; Genomic_DNA.
DR EMBL; AY063786; AAL36093.1; -; mRNA.
DR EMBL; AY096448; AAM20088.1; -; mRNA.
DR EMBL; AY088019; AAM65565.1; -; mRNA.
DR RefSeq; NP_568154.1; NM_120609.3.
DR RefSeq; NP_850770.1; NM_180439.2.
DR PDB; 4DOK; X-ray; 1.70 A; A/B=5-209.
DR PDBsum; 4DOK; -.
DR AlphaFoldDB; Q8VZW3; -.
DR SMR; Q8VZW3; -.
DR BioGRID; 15688; 4.
DR STRING; 3702.AT5G05270.1; -.
DR PaxDb; Q8VZW3; -.
DR PRIDE; Q8VZW3; -.
DR ProMEX; Q8VZW3; -.
DR ProteomicsDB; 241229; -.
DR EnsemblPlants; AT5G05270.1; AT5G05270.1; AT5G05270.
DR EnsemblPlants; AT5G05270.2; AT5G05270.2; AT5G05270.
DR GeneID; 830409; -.
DR Gramene; AT5G05270.1; AT5G05270.1; AT5G05270.
DR Gramene; AT5G05270.2; AT5G05270.2; AT5G05270.
DR KEGG; ath:AT5G05270; -.
DR Araport; AT5G05270; -.
DR TAIR; locus:2153539; AT5G05270.
DR eggNOG; ENOG502QV3J; Eukaryota.
DR HOGENOM; CLU_058915_1_0_1; -.
DR InParanoid; Q8VZW3; -.
DR OMA; TYHFPAD; -.
DR OrthoDB; 1381233at2759; -.
DR PhylomeDB; Q8VZW3; -.
DR BioCyc; ARA:AT5G05270-MON; -.
DR UniPathway; UPA00154; -.
DR PRO; PR:Q8VZW3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VZW3; baseline and differential.
DR Genevisible; Q8VZW3; AT.
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; IPR016087; Chalcone_isomerase.
DR InterPro; IPR016088; Chalcone_isomerase_3-sand.
DR InterPro; IPR016089; Chalcone_isomerase_bundle_sf.
DR InterPro; IPR036298; Chalcone_isomerase_sf.
DR InterPro; IPR044191; CHI3-like.
DR PANTHER; PTHR47588; PTHR47588; 1.
DR Pfam; PF02431; Chalcone; 1.
DR SUPFAM; SSF54626; SSF54626; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Flavonoid biosynthesis; Isomerase; Reference proteome.
FT CHAIN 1..209
FT /note="Probable chalcone--flavanone isomerase 3"
FT /id="PRO_0000422076"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:4DOK"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:4DOK"
FT STRAND 15..35
FT /evidence="ECO:0007829|PDB:4DOK"
FT STRAND 38..49
FT /evidence="ECO:0007829|PDB:4DOK"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:4DOK"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:4DOK"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:4DOK"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:4DOK"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:4DOK"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:4DOK"
FT HELIX 98..115
FT /evidence="ECO:0007829|PDB:4DOK"
FT HELIX 121..135
FT /evidence="ECO:0007829|PDB:4DOK"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:4DOK"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:4DOK"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:4DOK"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:4DOK"
FT HELIX 175..185
FT /evidence="ECO:0007829|PDB:4DOK"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:4DOK"
FT HELIX 194..208
FT /evidence="ECO:0007829|PDB:4DOK"
SQ SEQUENCE 209 AA; 23332 MW; 587A37BA5A91A0C7 CRC64;
MGTEMVMVHE VPFPPQIITS KPLSLLGQGI TDIEIHFLQV KFTAIGVYLD PSDVKTHLDN
WKGKTGKELA GDDDFFDALA SAEMEKVIRV VVIKEIKGAQ YGVQLENTVR DRLAEEDKYE
EEEETELEKV VGFFQSKYFK ANSVITYHFS AKDGICEIGF ETEGKEEEKL KVENANVVGM
MQRWYLSGSR GVSPSTIVSI ADSISAVLT
