ID   FLS_SOLTU               Reviewed;         349 AA.
AC   Q41452;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 100.
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};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pistil;
RX   PubMed=9025306; DOI=10.1046/j.1365-313x.1997.11010105.x;
RA   van Eldik G.J., Ruiter R.K., Reijnen W.H., van Herpen M.M.A.,
RA   Schrauwen J.A.M., Wullems G.J.;
RT   "Regulation of flavonol biosynthesis during anther and pistil development,
RT   and during pollen tube growth in Solanum tuberosum.";
RL   Plant J. 11:105-113(1997).
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.
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.
CC   -!- DEVELOPMENTAL STAGE: Temporally expressed during flower development.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; X92178; CAA63092.1; -; mRNA.
DR   PIR; T07373; T07373.
DR   AlphaFoldDB; Q41452; -.
DR   SMR; Q41452; -.
DR   STRING; 4113.PGSC0003DMT400036565; -.
DR   eggNOG; KOG0143; Eukaryota.
DR   UniPathway; UPA00154; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q41452; baseline.
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; Reference proteome; Vitamin C.
FT   CHAIN           1..349
FT                   /note="Flavonol synthase/flavanone 3-hydroxylase"
FT                   /id="PRO_0000067297"
FT   DOMAIN          213..310
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         238
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         240
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         291
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   349 AA;  39728 MW;  ADBBC3F6B10A0E05 CRC64;
     MKTIQGQSAT TALTMEVARV QAISSITKCM DTIPSEYIRS ENEQPAATTL QGVVLEVPVI
     DISNVDDDEE KLVKEIVEAS KEWGIFQVIN HGIPDEVIEN LQKVGKEFFE EVPQEEKELI
     AKKPGAQSLE GYGTSLQKEI EGKKGWVDHL FHKIWPPSAI NYRYWPKNPP SYREANEEYA
     KWLRKVADGI FRSLSLGLGL EGHEMMEAAG SEDIVYMLKI NYYPPCPRPD LALGVVAHTD
     MSYITLLVPN EVQVFKDGHW YDVNYIPNAI IVHIGDQVEI LSNGKYKSVY HRTTVNKYKT
     RMSWPVFLEP SSEHEVGPIP NLINEANPPK FKTKKYKDYV YCKLNKLPQ