ID   FLS4_ARATH              Reviewed;         279 AA.
AC   F4KAS1;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Probable flavonol synthase 4;
DE            EC=1.14.20.6;
GN   Name=FLS4; OrderedLocusNames=At5g63595; ORFNames=MBK5;
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   GENE FAMILY, AND NOMENCLATURE.
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).
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;
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   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AB005234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED97773.1; -; Genomic_DNA.
DR   RefSeq; NP_680463.1; NM_148158.2.
DR   AlphaFoldDB; F4KAS1; -.
DR   SMR; F4KAS1; -.
DR   STRING; 3702.AT5G63595.1; -.
DR   PaxDb; F4KAS1; -.
DR   PRIDE; F4KAS1; -.
DR   EnsemblPlants; AT5G63595.1; AT5G63595.1; AT5G63595.
DR   GeneID; 836479; -.
DR   Gramene; AT5G63595.1; AT5G63595.1; AT5G63595.
DR   KEGG; ath:AT5G63595; -.
DR   Araport; AT5G63595; -.
DR   TAIR; locus:504954954; AT5G63595.
DR   eggNOG; KOG0143; Eukaryota.
DR   HOGENOM; CLU_010119_16_2_1; -.
DR   InParanoid; F4KAS1; -.
DR   OrthoDB; 830141at2759; -.
DR   PhylomeDB; F4KAS1; -.
DR   UniPathway; UPA00154; -.
DR   PRO; PR:F4KAS1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; F4KAS1; baseline and differential.
DR   GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR   GO; GO:0045431; F:flavonol synthase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..279
FT                   /note="Probable flavonol synthase 4"
FT                   /id="PRO_0000418026"
FT   DOMAIN          156..256
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         164..166
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         183
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         237
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         247..249
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   279 AA;  31901 MW;  7DE984057F03A42B CRC64;
     MEVERDQHKP PLSLQNNKIP SSQNFPVVDL SNTNGELVAR KVAKASEEWG IFQVVNHGIP
     TELIRRLHKV DTQFFELPES KKEAVAKPAN SKEIQGYEMD DVQGRRSHIF HNLYPSSSVN
     YAFWPKNPPE YREVTEEFAK HAKQLAEEIL GLLSEGAGYL MKINYYRPCP EPDWVMGIKA
     HTDFNGLTLL IPNEIFGLQV FKEDRWLDVD YIYPAVIIII GDQIMKMSNG RYNNVLHRAL
     MDKKKTRMSS VVHIKPPYDM VVSHFPNSPA AIILPSSSL