ID   FLS_PETHY               Reviewed;         348 AA.
AC   Q07512;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, 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;
GN   Name=FL;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Old Glory Blue; TISSUE=Petal;
RX   MEDLINE=94108485; PubMed=7904213;
RX   DOI=10.1046/j.1365-313X.1993.04061003.x;
RA   Holton T.A., Brugliera F., Tanaka Y.;
RT   "Cloning and expression of flavonol synthase from Petunia hybrida.";
RL   Plant J. 4:1003-1010(1993).
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 ascorbate molecule per subunit.
CC   -!- COFACTOR: Binds 1 iron ion per subunit.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: Expressed at highest level during the first
CC       stage of flower development.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Z22543; CAA80264.1; -; mRNA.
DR   PIR; S33510; S33510.
DR   HSSP; Q96323; 1GP6.
DR   BRENDA; 1.14.11.23; 2263.
DR   BRENDA; 1.14.11.9; 2263.
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; IPR002283; Isopenicillin-N_synthase.
DR   InterPro; IPR005123; Oxoglutarate/Fe-dep_Oase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   PRINTS; PR00682; IPNSYNTHASE.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding;
KW   Oxidoreductase; Vitamin C.
FT   CHAIN         1    348       Flavonol synthase/flavanone 3-
FT                                hydroxylase.
FT                                /FTId=PRO_0000067296.
FT   METAL       234    234       Iron (By similarity).
FT   METAL       236    236       Iron (By similarity).
FT   METAL       290    290       Iron (By similarity).
SQ   SEQUENCE   348 AA;  39427 MW;  B39E1E4381DE6379 CRC64;
     MKTAQGVSAT LTMEVARVQA IASLSKCMDT IPSEYIRSEN EQPAATTLHG VVLQVPVIDL
     RDPDENKMVK LIADASKEWG IFQLINHGIP DEAIADLQKV GKEFFEHVPQ EEKELIAKTP
     GSNDIEGYGT SLQKEVEGKK GWVDHLFHKI WPPSAVNYRY WPKNPPSYRE ANEEYGKRMR
     EVVDRIFKSL SLGLGLEGHE MIEAAGGDEI VYLLKINYYP PCPRPDLALG VVAHTDMSYI
     TILVPNEVQG LQVFKDGHWY DVKYIPNALI VHIGDQVEIL SNGKYKSVYH RTTVNKDKTR
     MSWPVFLEPP SEHEVGPIPK LLSEANPPKF KTKKYKDYVY CKLNKLPQ
//