ID FLS_EUSGR Reviewed; 334 AA. AC Q9M547; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 04-NOV-2008, entry version 39. 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=FLS; OS Eustoma grandiflorum (Bluebells) (Lisianthus russellianus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Gentianales; Gentianaceae; Chironieae; Eustoma. OX NCBI_TaxID=52518; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Nielsen K.M.; RT "cDNA cloning of flavonol synthase and antisense suppression of RT expression in Lisianthus grandiflorum grise."; RL Submitted (MAR-2000) 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 (By similarity). 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 (By similarity). 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; AF240764; AAF64168.1; -; mRNA. DR HSSP; Q96323; 1GP6. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. 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; 2OG-FeII_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 1 334 Flavonol synthase/flavanone 3- FT hydroxylase. FT /FTId=PRO_0000067293. FT METAL 220 220 Iron (By similarity). FT METAL 222 222 Iron (By similarity). FT METAL 276 276 Iron (By similarity). SQ SEQUENCE 334 AA; 38081 MW; 4097830ABE2534E2 CRC64; MEVQRVQEIA SLSKVIDTIP AEYIRSENEQ PVISTVHGVV LEVPVIDLSD SDEKKIVGLV SEASKEWGIF QVVNHGIPNE VIRKLQEVGK HFFELPQEEK ELIAKPEGSQ SIEGYGTRLQ KEVDGKKGWV DHLFHKIWPP SAINYQFWPK NPPAYREANE EYAKRLQLVV DNLFKYLSLG LDLEPNSFKD GAGGDDLVYL MKINYYPPCP RPDLALGVAH TDMSAITVLV PNEVPGLQVY KDGHWYDCKY IPNALIVHIG DQVEIMSNGK YKSVYHRTTV NKEKTRMSWP VFLEPPPDHE VGPIPKLVNE ENPAKFKTKK YKDYAYCKLN KLPQ //