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   03-AUG-2022, entry version 81.
DE   RecName: Full=Naringenin,2-oxoglutarate 3-dioxygenase;
DE            EC=1.14.11.9 {ECO:0000250|UniProtKB:Q7XZQ7};
DE   AltName: Full=FHT;
DE   AltName: Full=Flavanone-3-hydroxylase;
DE            Short=F3H;
GN   Name=FHT;
OS   Dianthus caryophyllus (Carnation) (Clove pink).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Caryophyllaceae; Caryophylleae; Dianthus.
OX   NCBI_TaxID=3570;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Flower bud;
RX   PubMed=8223617; 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. Consensus
RT   sequence, comparison with related enzymes and the role of conserved
RT   histidine residues.";
RL   Eur. J. Biochem. 217:745-754(1993).
CC   -!- FUNCTION: Catalyzes the 3-beta-hydroxylation of 2S-flavanones to 2R,3R-
CC       dihydroflavonols which are intermediates in the biosynthesis of
CC       flavonols, anthocyanidins, catechins and proanthocyanidins in plants.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + a (2S)-flavan-4-one + O2 = a (2R,3R)-
CC         dihydroflavonol + CO2 + succinate; Xref=Rhea:RHEA:18621,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:138188, ChEBI:CHEBI:140377;
CC         EC=1.14.11.9; Evidence={ECO:0000250|UniProtKB:Q7XZQ7};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00805};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X72592; CAA51190.1; -; mRNA.
DR   EMBL; X70378; CAA49839.1; -; Genomic_DNA.
DR   PIR; S31921; S31921.
DR   AlphaFoldDB; Q05964; -.
DR   SMR; Q05964; -.
DR   UniPathway; UPA00154; -.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.330; -; 1.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   2: Evidence at transcript level;
KW   Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW   Vitamin C.
FT   CHAIN           1..365
FT                   /note="Naringenin,2-oxoglutarate 3-dioxygenase"
FT                   /id="PRO_0000067285"
FT   DOMAIN          191..295
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         218
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         220
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         276
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         286
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
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