ID   FL3H_PETHY              Reviewed;         369 AA.
AC   Q07353;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   05-MAY-2009, entry version 54.
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=AN3;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Blue Titan; TISSUE=Flower bud;
RX   MEDLINE=92184791; PubMed=1544919;
RA   Britsch L., Ruhnau-Brich B., Forkmann G.;
RT   "Molecular cloning, sequence analysis, and in vitro expression of
RT   flavanone 3 beta-hydroxylase from Petunia hybrida.";
RL   J. Biol. Chem. 267:5380-5387(1992).
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; X60512; CAA43027.1; -; mRNA.
DR   PIR; A42110; A42110.
DR   PIR; S16780; S16780.
DR   HSSP; Q96323; 1GP6.
DR   BioCyc; MetaCyc:MON-11838; -.
DR   BRENDA; 1.14.11.9; 2263.
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   1: Evidence at protein level;
KW   Dioxygenase; Direct protein sequencing; Flavonoid biosynthesis; Iron;
KW   Metal-binding; Oxidoreductase; Vitamin C.
FT   CHAIN        <1    369       Naringenin,2-oxoglutarate 3-dioxygenase.
FT                                /FTId=PRO_0000067289.
FT   METAL        78     78       Iron (Potential).
FT   METAL       220    220       Iron (Potential).
FT   METAL       222    222       Iron (Potential).
FT   METAL       278    278       Iron (Potential).
FT   NON_TER       1      1
SQ   SEQUENCE   369 AA;  41466 MW;  C34034E23B4D5A3F CRC64;
     IPRVTPSTLT ALAEEKTLQT SFIRDEDERP KVAYNQFSNE IPIISLEGID DETGKRAEIC
     DKIVKACEDW GVFQVVDHGV DAEVISQMTT FAKEFFALPP EEKLRFDMSG GKKGGFIVSS
     HLQGEVVQDW REIVTYFSYP TRARDYSRWP DKPEGWIAVT QKYSEKLMEL ACKLLDVLSE
     AMGLEKEALT KACVDMDQKV VVNFYPKCPE PDLTLGLKRH TDPGTITLLL QDQVGGLQAT
     KDNGKTWITV QPVEGAFVVN LGDHGHFLSN GRFKNADHQA VVNSNSSRLS IATFQNPAPE
     AIVYPLKIRE GEKSIMDEPI TFAEMYRRKM SKDLELARLK KQAKEQQLQA EVAAEKAKLE
     SKPIEEILA
//