ID FL3H_CALCH Reviewed; 356 AA. AC Q05963; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 05-MAY-2009, entry version 49. 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; GN Name=FHT; OS Callistephus chinensis (China aster). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Astereae; OC Callistephus. OX NCBI_TaxID=13379; 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; X72593; CAA51191.1; -; mRNA. DR PIR; S38336; S32147. DR HSSP; Q96323; 1GP4. DR BRENDA; 1.14.11.9; 275959. 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 1 356 Naringenin,2-oxoglutarate 3-dioxygenase. FT /FTId=PRO_0000067284. FT METAL 73 73 Iron (Potential). FT METAL 215 215 Iron (Potential). FT METAL 217 217 Iron (Potential). FT METAL 273 273 Iron (Potential). SQ SEQUENCE 356 AA; 40210 MW; BE622A4A8C39BA0B CRC64; MAAPISLKWE EHSLHENKFV RDEDERPKVP YNTFSNEIPV ISLAGIDGCR RAEICDEIVK ACEDWGIFQV VDHGVDTKLL SDMTGLARDF FHLPTQEKLR FDMTGGKKGG FIVSSHLQGE AVQDWREIVT YFSYPIKARD YSRWPDKPNE WRAVTEEYSK VLMGLACKLL EVLSEAMGLE KEALTKACVD MDQKVVVNYY PKCPQPDLTL GLKRHTDPGT ITLLLQDQVG GLQATRDGGE SWITVKPVEG AFVVNLGDHG HYLSNGRFKN ADHQAVVNSS TSRLSIATFQ NPAPEAIVYP LKINEGEKSI MEEPMTFMEM YKKKMSTDLE LARLKKLAKD KQQDLEVVKP IQNIFA //