ID   FL3H_VITVI              Reviewed;         364 AA.
AC   P41090;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=F3H;
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Lambrusco Foglia Frastagliata;
RX   PubMed=8193299; DOI=10.1007/bf00029856;
RA   Sparvoli F., Martin C., Scienza A., Gavazzi G., Tonelli C.;
RT   "Cloning and molecular analysis of structural genes involved in flavonoid
RT   and stilbene biosynthesis in grape (Vitis vinifera L.).";
RL   Plant Mol. Biol. 24:743-755(1994).
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; X75965; CAA53579.1; -; mRNA.
DR   AlphaFoldDB; P41090; -.
DR   SMR; P41090; -.
DR   STRING; 29760.VIT_04s0023g03370.t01; -.
DR   PRIDE; P41090; -.
DR   eggNOG; KOG0143; Eukaryota.
DR   BRENDA; 1.14.11.9; 6671.
DR   UniPathway; UPA00154; -.
DR   ExpressionAtlas; P41090; baseline and differential.
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..364
FT                   /note="Naringenin,2-oxoglutarate 3-dioxygenase"
FT                   /id="PRO_0000067290"
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   364 AA;  40875 MW;  2C1FBEEF1EADD674 CRC64;
     MAPTTLTALA GEKTLQSSFV RDEDERPKVA YNDFSNEIPV ISLTKESMKL AAVVDEICRK
     IVEACEDWGI FQVVNHGVDS NLISEMTRLA REFFALPPEE NVRFDMSGGK KGGFIVSSHL
     QGEAVQDWRE IVTYFSYPLR TRDYSRWPDK PEGWRSVTQE YSEKLMGLAC KLLEVLSEAM
     DLDKDALTNA CVDMDQKVVV NFYPQCPQPD LTLGLKRHTD PGTITLLLQD QVGGLQATRD
     GGKTWITVQP VEGAFVVNLG DHGHYLSNGR FKNADHQAVV NSNHSRLSIA TFQNPAPEAT
     VYPLKIREGE KAVLEGPITF AEMYRRKMSK DLELARLKKL AKEQQLQDVE KAKLESKPID
     QILA