ID   FLS_MALDO               Reviewed;         337 AA.
AC   Q9XHG2;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 92.
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   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Fuji; TISSUE=Peelings;
RA   Lee J.-R., Hong S.-T., Kim S.-R.;
RT   "Molecular cloning and expression of a flavonol synthase cDNA from 'Fuji'
RT   apple.";
RL   Submitted (JAN-1999) 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}.
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DR   EMBL; AF119095; AAD26261.1; -; mRNA.
DR   RefSeq; NP_001306179.1; NM_001319250.1.
DR   AlphaFoldDB; Q9XHG2; -.
DR   SMR; Q9XHG2; -.
DR   STRING; 3750.XP_008349814.1; -.
DR   GeneID; 103413102; -.
DR   KEGG; mdm:103413102; -.
DR   OrthoDB; 830141at2759; -.
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   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..337
FT                   /note="Flavonol synthase/flavanone 3-hydroxylase"
FT                   /id="PRO_0000067294"
FT   DOMAIN          198..298
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         223
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         225
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         279
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   337 AA;  38123 MW;  49AE7236145A6072 CRC64;
     MGVESVERER ESNEGTIPAE FIRSENEQPG ITTVHGKVLE VPIIDFSDPD EEKLIVQITE
     ASSNWGMYQI VNHDIPSEVI SKLQAVGKEF FELPQEEKEA YAKPPDSASI EGYGTKLFKE
     ISEGDTTKKG WVDNLFNKIW PPSVVNYQFW PKNPPSYREA NEEYAKHLHN VVEKLFRLLS
     LGLGLEGQEL KKAAGGDNLE YLLKINYYPP CPRPDLALGV VAHTDMSTVT ILVPNDVQGL
     QACKDGRWYD VKYIPNALVI HIGDQMEIMS NGKYTSVLHR TTVNKDKTRI SWPVFLEPPA
     DHVVGPHPQL VNAVNQPKYK TKKYGDYVYC KINKLPQ