ID   FLS_EUSER               Reviewed;         334 AA.
AC   Q9M547;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Flavonol synthase/flavanone 3-hydroxylase;
DE            Short=FLS;
DE            EC=1.14.11.9 {ECO:0000250|UniProtKB:Q7XZQ6};
DE            EC=1.14.20.6 {ECO:0000250|UniProtKB:Q7XZQ6};
GN   Name=FLS;
OS   Eustoma exaltatum subsp. russellianum (Bluebells) (Eustoma grandiflorum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Gentianaceae; Chironieae; Chironiinae;
OC   Eustoma.
OX   NCBI_TaxID=52518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Nielsen K.M.;
RT   "cDNA cloning of flavonol synthase and antisense suppression of expression
RT   in Lisianthus grandiflorum grise.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of flavonols from dihydroflavonols.
CC       It can act on dihydrokaempferol to produce kaempferol, on
CC       dihydroquercetin to produce quercitin and on dihydromyricetin to
CC       produce myricetin (By similarity). {ECO:0000250}.
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:0000250|UniProtKB:Q7XZQ6};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + a (2S)-flavan-4-one + O2 = a (2R,3R)-
CC         dihydroflavonol + CO2 + succinate; Xref=Rhea:RHEA:18621,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:138188, ChEBI:CHEBI:140377;
CC         EC=1.14.11.9; Evidence={ECO:0000250|UniProtKB:Q7XZQ6};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC       Note=Binds 1 ascorbate molecule per subunit. {ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF240764; AAF64168.1; -; mRNA.
DR   AlphaFoldDB; Q9M547; -.
DR   SMR; Q9M547; -.
DR   UniPathway; UPA00154; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045431; F:flavonol synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009805; P:coumarin biosynthetic process; IEA:UniProt.
DR   GO; GO:0002238; P:response to molecule of fungal origin; IEA:UniProt.
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   Cytoplasm; Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding;
KW   Oxidoreductase; Vitamin C.
FT   CHAIN           1..334
FT                   /note="Flavonol synthase/flavanone 3-hydroxylase"
FT                   /id="PRO_0000067293"
FT   DOMAIN          196..295
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         220
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         222
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         276
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   334 AA;  38081 MW;  4097830ABE2534E2 CRC64;
     MEVQRVQEIA SLSKVIDTIP AEYIRSENEQ PVISTVHGVV LEVPVIDLSD SDEKKIVGLV
     SEASKEWGIF QVVNHGIPNE VIRKLQEVGK HFFELPQEEK ELIAKPEGSQ SIEGYGTRLQ
     KEVDGKKGWV DHLFHKIWPP SAINYQFWPK NPPAYREANE EYAKRLQLVV DNLFKYLSLG
     LDLEPNSFKD GAGGDDLVYL MKINYYPPCP RPDLALGVAH TDMSAITVLV PNEVPGLQVY
     KDGHWYDCKY IPNALIVHIG DQVEIMSNGK YKSVYHRTTV NKEKTRMSWP VFLEPPPDHE
     VGPIPKLVNE ENPAKFKTKK YKDYAYCKLN KLPQ