ID   FL3H_MALDO              Reviewed;         364 AA.
AC   Q06942;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 86.
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;
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=8208851; DOI=10.1104/pp.103.1.291;
RA   Davies K.M.;
RT   "A cDNA clone for flavanone 3-hydroxylase from Malus.";
RL   Plant Physiol. 103:291-291(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Fuji; TISSUE=Peelings;
RA   Lee J.-R., Hong S.-T., Yoo Y.G., Kim S.-R.;
RT   "Molecular cloning and expression of anthocyanin biosynthesis genes from
RT   'Fuji apple'.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
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; X69664; CAA49353.1; -; mRNA.
DR   EMBL; AF117270; AAD26206.1; -; mRNA.
DR   PIR; S31458; S31458.
DR   AlphaFoldDB; Q06942; -.
DR   SMR; Q06942; -.
DR   STRING; 3750.XP_008336931.1; -.
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..364
FT                   /note="Naringenin,2-oxoglutarate 3-dioxygenase"
FT                   /id="PRO_0000067287"
FT   DOMAIN          191..295
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   REGION          343..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  40771 MW;  B84793FCF831CE44 CRC64;
     MAPATTLTSI AHEKTLQQKF VRDEDERPKV AYNDFSNEIP IISLAGIDEV EGRRGEICKK
     IVAACEDWGI FQIVDHGVDA ELISEMTGLA REFFALPSEE KLRFDMSGGK KGGFIVSSHL
     QGEAVQDWRE IVTYFSYPIR HRDYSRWPDK PEAWREVTKK YSDELMGLAC KLLGVLSEAM
     GLDTEALTKA CVDMDQKVVV NFYPKCPQPD LTLGLKRHTD PGTITLLLQD QVGGLQATRD
     DGKTWITVQP VEGAFVVNLG DHGHLLSNGR FKNADHQAVV NSNSSRLSIA TFQNPAQEAI
     VYPLSVREGE KPILEAPITY TEMYKKKMSK DLELARLKKL AKEQQSQDLE KAKVDTKPVD
     DIFA