ID FL3H_MALDO Reviewed; 364 AA. AC Q06942; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 05-MAY-2009, entry version 47. 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; OS Malus domestica (Apple) (Malus sylvestris). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Rosales; Rosaceae; Maloideae; Malus. OX NCBI_TaxID=3750; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Leaf; RX MEDLINE=94269194; PubMed=8208851; DOI=10.1104/pp.103.1.291; RA Davies K.M.; RT "A cDNA clone for flavanone 3-hydroxylase from Malus."; RL Plant Physiol. 103:291-291(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Fuji; TISSUE=Peelings; RA Lee J.-R., Hong S.-T., Yoo Y.G., Kim S.-R.; RT "Molecular cloning and expression of anthocyanin biosynthesis genes RT from 'Fuji apple'."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. 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; X69664; CAA49353.1; -; mRNA. DR EMBL; AF117270; AAD26206.1; -; mRNA. DR PIR; S31458; S31458. DR BRENDA; 1.14.11.9; 66979. 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 1 364 Naringenin,2-oxoglutarate 3-dioxygenase. FT /FTId=PRO_0000067287. FT METAL 76 76 Iron (Potential). FT METAL 218 218 Iron (Potential). FT METAL 220 220 Iron (Potential). FT METAL 276 276 Iron (Potential). SQ SEQUENCE 364 AA; 40771 MW; B84793FCF831CE44 CRC64; MAPATTLTSI AHEKTLQQKF VRDEDERPKV AYNDFSNEIP IISLAGIDEV EGRRGEICKK IVAACEDWGI FQIVDHGVDA ELISEMTGLA REFFALPSEE KLRFDMSGGK KGGFIVSSHL QGEAVQDWRE IVTYFSYPIR HRDYSRWPDK PEAWREVTKK YSDELMGLAC KLLGVLSEAM GLDTEALTKA CVDMDQKVVV NFYPKCPQPD LTLGLKRHTD PGTITLLLQD QVGGLQATRD DGKTWITVQP VEGAFVVNLG DHGHLLSNGR FKNADHQAVV NSNSSRLSIA TFQNPAQEAI VYPLSVREGE KPILEAPITY TEMYKKKMSK DLELARLKKL AKEQQSQDLE KAKVDTKPVD DIFA //