ID   FLS_MATIN               Reviewed;         291 AA.
AC   O04395;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   16-JUN-2009, entry version 50.
DE   RecName: Full=Flavonol synthase/flavanone 3-hydroxylase;
DE            Short=FLS;
DE            EC=1.14.11.23;
DE            EC=1.14.11.9;
DE   Flags: Fragment;
OS   Matthiola incana (Common stock).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Matthiola.
OX   NCBI_TaxID=3724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Flower bud, and Petal;
RA   Henkel J., Forkmann G.;
RT   "Cloning and expression of a flavonol synthase gene from common stock
RT   (Matthiola incana).";
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family.
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DR   EMBL; AF001391; AAB58800.1; -; mRNA.
DR   HSSP; Q96323; 1GP6.
DR   BRENDA; 1.14.11.23; 228993.
DR   BRENDA; 1.14.11.9; 228993.
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    291       Flavonol synthase/flavanone 3-
FT                                hydroxylase.
FT                                /FTId=PRO_0000067295.
FT   METAL       175    175       Iron (By similarity).
FT   METAL       177    177       Iron (By similarity).
FT   METAL       231    231       Iron (By similarity).
FT   NON_TER       1      1
SQ   SEQUENCE   291 AA;  33430 MW;  6B8E4E3D2834720A CRC64;
     QVPVVDLSCP DEELVARTVV KASEDWGVFQ VVNHGIPTEL IQRLQKVGRE FFELPEAEKR
     SCAREAGSVE GYGRRIELDI KKRKGIVDQI YLSTWPPSSV NYRYWPKSPP DYREVNEEYA
     RHVKTLSEKI MEWLSEGLGL GREAIKEVNG CWYVMNINHY PPYPHSDSFN GLEPHTDING
     LTLIITNEIP GLQVFKDDHW IEVEYIPSAI IVNIGDQIMM LSNGKYKNVL HKTTVDKEKT
     RMSWPVLVSP TYDMVVGPLP ELTSEDDPPK FKPIAYKDYV HNKITFLKNK S
//