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   16-JUN-2009, entry version 55.
DE   RecName: Full=Flavonol synthase/flavanone 3-hydroxylase;
DE            Short=FLS;
DE            EC=1.14.11.23;
DE            EC=1.14.11.9;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae;
OC   Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pistil;
RX   MEDLINE=97177800; PubMed=9025306;
RX   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
RT   development, and during pollen tube growth in Solanum tuberosum.";
RL   Plant J. 11:105-113(1997).
CC   -!- FUNCTION: Catalyzes the formation of flavonols from
CC       dihydroflavonols. It can act on dihydrokaempferol to produce
CC       kaempferol, on dihydroquercetin to produce quercitin and on
CC       dihydromyricetin to produce myricetin.
CC   -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a
CC       flavonol + succinate + CO(2) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a
CC       dihydroflavonol + succinate + CO(2).
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 ascorbate molecule per subunit (By similarity).
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: Temporally expressed during flower
CC       development.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family.
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DR   EMBL; X92178; CAA63092.1; -; mRNA.
DR   PIR; T07373; T07373.
DR   HSSP; Q96323; 1GP6.
DR   BRENDA; 1.14.11.23; 296.
DR   BRENDA; 1.14.11.9; 296.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045431; F:flavonol synthase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR005123; Oxoglutarate/Fe-dep_Oase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding;
KW   Oxidoreductase; Vitamin C.
FT   CHAIN         1    349       Flavonol synthase/flavanone 3-
FT                                hydroxylase.
FT                                /FTId=PRO_0000067297.
FT   METAL       238    238       Iron (By similarity).
FT   METAL       240    240       Iron (By similarity).
FT   METAL       291    291       Iron (By similarity).
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
//