ID   FL3H_MATIN              Reviewed;         357 AA.
AC   Q05965;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 84.
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;
DE   Flags: Fragment;
GN   Name=FHT;
OS   Matthiola incana (Common stock) (Cheiranthus incanus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Anchonieae; Matthiola.
OX   NCBI_TaxID=3724;
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}.
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DR   EMBL; X72594; CAA51192.1; -; mRNA.
DR   PIR; S38338; S38338.
DR   AlphaFoldDB; Q05965; -.
DR   SMR; Q05965; -.
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..357
FT                   /note="Naringenin,2-oxoglutarate 3-dioxygenase"
FT                   /id="PRO_0000067288"
FT   DOMAIN          189..293
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         216
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
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         274
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         284
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   NON_TER         1
SQ   SEQUENCE   357 AA;  39982 MW;  E74825D07C89D74E CRC64;
     APGTLTELAG ESKLNSKFVR DEDERPKVAY NEFSDEIPVI SLAGIDDVDG KRGEICREIV
     EACENWGIFQ VVDHGVDTSL VADMTRLARD FFALPPEEKL RFDMSGGKKG GFIVSSHLQG
     EAVQDWREIV TYFSYPVRNR DYSRWPDKPQ GWAKVTEEYS EKLMGLACKL LEVLSEAMGL
     EKESLTNACV DMDQKIVVNY YPKCPQPDLT LGLKRHTDPG TITLLLQDQV GGLQATRDDG
     NTWITVQPVE GAFVVNLGDH GHFLSNGRFK NADHQAVVNS NSSRLSIATF QNPAPEATVY
     PLKVREGEKA IMEEPITFAE MYKRKMGRDL ELARLKKLAK EEHNHKEAAK PLDQILA