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 04-NOV-2026, entry version 90. 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=a (2S)-flavan-4-one + 2-oxoglutarate + O2 = a (2R,3R)- CC dihydroflavonol + succinate + CO2; 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; Evidence={ECO:0000255|PROSITE- CC 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; X72594; CAA51192.1; -; mRNA. DR PIR; S38338; S38338. DR AlphaFoldDB; Q05965; -. DR SMR; Q05965; -. DR UniPathway; UPA00154; -. DR GO; GO:0045486; F:flavanone 3-dioxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway. DR FunFam; 2.60.120.330:FF:000016; Naringenin,2-oxoglutarate 3-dioxygenase; 1. DR Gene3D; 2.60.120.330; B-lactam Antibiotic, Isopenicillin N Synthase, Chain; 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_dom. DR PANTHER; PTHR47991; OXOGLUTARATE/IRON-DEPENDENT DIOXYGENASE; 1. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. DR Pfam; PF14226; DIOX_N; 1. DR SUPFAM; SSF51197; Clavaminate synthase-like; 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 //