FLS3_ARATH
ID FLS3_ARATH Reviewed; 308 AA.
AC Q9FFQ5; Q8LDA5;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Flavonol synthase 3 {ECO:0000303|PubMed:18467451};
DE Short=AtFLS3 {ECO:0000303|PubMed:18467451};
DE EC=1.14.20.6 {ECO:0000269|PubMed:19433090};
GN Name=FLS3 {ECO:0000303|PubMed:18467451};
GN OrderedLocusNames=At5g63590 {ECO:0000312|Araport:AT5G63590};
GN ORFNames=MBK5.5 {ECO:0000312|EMBL:BAB10452.1};
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18467451; DOI=10.1104/pp.108.117457;
RA Owens D.K., Alerding A.B., Crosby K.C., Bandara A.B., Westwood J.H.,
RA Winkel B.S.;
RT "Functional analysis of a predicted flavonol synthase gene family in
RT Arabidopsis.";
RL Plant Physiol. 147:1046-1061(2008).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=19433090; DOI=10.1016/j.febslet.2009.05.006;
RA Preuss A., Stracke R., Weisshaar B., Hillebrecht A., Matern U., Martens S.;
RT "Arabidopsis thaliana expresses a second functional flavonol synthase.";
RL FEBS Lett. 583:1981-1986(2009).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. No-0;
RX PubMed=18998159; DOI=10.1007/s00425-008-0841-y;
RA Stracke R., De Vos R.C., Bartelniewoehner L., Ishihara H., Sagasser M.,
RA Martens S., Weisshaar B.;
RT "Metabolomic and genetic analyses of flavonol synthesis in Arabidopsis
RT thaliana support the in vivo involvement of leucoanthocyanidin
RT dioxygenase.";
RL Planta 229:427-445(2009).
RN [9]
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 formation of flavonols from dihydroflavonols.
CC Possesses low activity in vitro towards dihydrokaempferol and
CC dihydroquercetin producing kaempferol and quercitin, respectively.
CC {ECO:0000269|PubMed:18998159, ECO:0000269|PubMed:19433090}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a (2R,3R)-dihydroflavonol + O2 = a flavonol +
CC CO2 + H2O + succinate; Xref=Rhea:RHEA:21088, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:28802, ChEBI:CHEBI:30031, ChEBI:CHEBI:138188;
CC EC=1.14.20.6; Evidence={ECO:0000269|PubMed:19433090};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21089;
CC Evidence={ECO:0000269|PubMed:19433090};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC {ECO:0000269|PubMed:19433090}.
CC -!- TISSUE SPECIFICITY: Widely expressed at low levels.
CC {ECO:0000269|PubMed:18467451}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:18467451, ECO:0000269|PubMed:18998159}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AB005234; BAB10452.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97772.1; -; Genomic_DNA.
DR EMBL; BT003134; AAO24566.1; -; mRNA.
DR EMBL; AK228300; BAF00243.1; -; mRNA.
DR EMBL; AY086112; AAM63319.1; -; mRNA.
DR RefSeq; NP_201164.1; NM_125754.3.
DR AlphaFoldDB; Q9FFQ5; -.
DR SMR; Q9FFQ5; -.
DR BioGRID; 21720; 1.
DR IntAct; Q9FFQ5; 1.
DR STRING; 3702.AT5G63590.1; -.
DR PaxDb; Q9FFQ5; -.
DR PRIDE; Q9FFQ5; -.
DR ProteomicsDB; 230628; -.
DR EnsemblPlants; AT5G63590.1; AT5G63590.1; AT5G63590.
DR GeneID; 836478; -.
DR Gramene; AT5G63590.1; AT5G63590.1; AT5G63590.
DR KEGG; ath:AT5G63590; -.
DR Araport; AT5G63590; -.
DR TAIR; locus:2160589; AT5G63590.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_2_1; -.
DR InParanoid; Q9FFQ5; -.
DR OMA; HWIDVKY; -.
DR OrthoDB; 755371at2759; -.
DR PhylomeDB; Q9FFQ5; -.
DR BRENDA; 1.14.20.6; 399.
DR UniPathway; UPA00154; -.
DR PRO; PR:Q9FFQ5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFQ5; baseline and differential.
DR Genevisible; Q9FFQ5; AT.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0045431; F:flavonol synthase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009813; P:flavonoid biosynthetic process; ISS:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..308
FT /note="Flavonol synthase 3"
FT /id="PRO_0000418025"
FT DOMAIN 167..267
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 175..177
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q96323"
FT BINDING 192
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q96323,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q96323,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 248
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q96323,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 258..260
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q96323"
FT CONFLICT 93
FT /note="D -> Y (in Ref. 4; AAM63319)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 35452 MW; 341D86A016065229 CRC64;
MEMEKNQHIS SLDIPVIDLS NPDEELVASA VVKASQEWGI FQVVNHGIPT ELILRLLQVG
MEFFELPETE KEAVAKPEDS LDIEGYRTKY QKDLEGRNAW VDHLFHRIWP PSRVNHKFWP
KNPPEYIEVN EEYASHIKKL SEKIMEWLSE GLGLRHEALK EGLGGETIEY LMKINYYPPC
PDPELVVGAP DHTDVNGITL LVANEALGLQ AFKDNQWIDA EYTTSGIIVI IGDQFLRMSN
GKYKSVEHRA KMDKEKTRIS WPVFVESSLD QVFGPLPELI TGDENVPKFK PYVYKDYKFR
KLKKLLLD
