ID FL3H_DIACA Reviewed; 365 AA. AC Q05964; 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; GN Name=FHT; OS Dianthus caryophyllus (Carnation) (Clove pink). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC Caryophyllales; Caryophyllaceae; Dianthus. OX NCBI_TaxID=3570; 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; X72592; CAA51190.1; -; mRNA. DR EMBL; X70378; CAA49839.1; -; Genomic_DNA. DR PIR; S31921; S31921. DR HSSP; Q96323; 1GP6. DR BRENDA; 1.14.11.9; 21500. 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 1 365 Naringenin,2-oxoglutarate 3-dioxygenase. FT /FTId=PRO_0000067285. 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 365 AA; 40964 MW; 55F39E674A9293C9 CRC64; MVAEKPKTLT SLEGDDKLNS NFVRDEDERP KVAYNEFSND IPVISLAGID GEKRGEICRK IVEACEDWGI FQVVDHGVGD DLIADMTRLA REFFALPAEE KLRFDMSGGK KGGFIVSSHL QGEVVQDWRE IVTYFSYPTN SRDYTRWPDK PEGWIKVTEE YSNKLMTLAC TLLGVLSEAM GLELEALTKA CVDMDQKIVV NYYPKCPQPD LTLGLKRHTD PGTITLLLQD QVGGLQATRD GGKTWITVQP VPGAFVVNLG DHGHFLSNGR FKNADHQAVV NSECSRLSIA TFQNPSPDAT VYPLAIREGE NSIMEEPITF ADLYRRKMAK DLEIARHKRL AKEEMPFKEL DEAKFESKSI DQILA //