ID FL3H_MATIN Reviewed; 357 AA. AC Q05965; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 05-MAY-2009, entry version 48. DE RecName: Full=Naringenin,2-oxoglutarate 3-dioxygenase; DE EC=1.14.11.9; DE AltName: Full=Flavonone-3-hydroxylase; DE Short=F3H; DE AltName: Full=FHT; DE Flags: Fragment; GN Name=FHT; 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; RX MEDLINE=94039114; PubMed=8223617; RX DOI=10.1111/j.1432-1033.1993.tb18301.x; RA Britsch L., Dedio J., Saedler H., Forkmann G.; RT "Molecular characterization of flavanone 3 beta-hydroxylases. RT Consensus sequence, comparison with related enzymes and the role of RT conserved histidine residues."; RL Eur. J. Biochem. 217:745-754(1993). CC -!- FUNCTION: Catalyzes the 3-beta-hydroxylation of 2S-flavonones to CC 2R,3R-dihydroflavonols which are intermediates in the biosynthesis CC of flavonols, anthocyanidins, catechins and proanthocyanidins in CC plants. CC -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a CC dihydroflavonol + succinate + CO(2). CC -!- COFACTOR: Iron. CC -!- COFACTOR: Ascorbate. CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid CC biosynthesis. 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; X72594; CAA51192.1; -; mRNA. DR PIR; S38338; S38338. DR HSSP; Q96323; 1GP4. DR BRENDA; 1.14.11.9; 228993. 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 Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; KW Oxidoreductase; Vitamin C. FT CHAIN <1 357 Naringenin,2-oxoglutarate 3-dioxygenase. FT /FTId=PRO_0000067288. FT METAL 74 74 Iron (Potential). FT METAL 216 216 Iron (Potential). FT METAL 218 218 Iron (Potential). FT METAL 274 274 Iron (Potential). FT NON_TER 1 1 SQ SEQUENCE 357 AA; 39982 MW; E74825D07C89D74E CRC64; APGTLTELAG ESKLNSKFVR DEDERPKVAY NEFSDEIPVI SLAGIDDVDG KRGEICREIV EACENWGIFQ VVDHGVDTSL VADMTRLARD FFALPPEEKL RFDMSGGKKG GFIVSSHLQG EAVQDWREIV TYFSYPVRNR DYSRWPDKPQ GWAKVTEEYS EKLMGLACKL LEVLSEAMGL EKESLTNACV DMDQKIVVNY YPKCPQPDLT LGLKRHTDPG TITLLLQDQV GGLQATRDDG NTWITVQPVE GAFVVNLGDH GHFLSNGRFK NADHQAVVNS NSSRLSIATF QNPAPEATVY PLKVREGEKA IMEEPITFAE MYKRKMGRDL ELARLKKLAK EEHNHKEAAK PLDQILA //