ID   FL3H_HORVU              Reviewed;         377 AA.
AC   P28038;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   04-NOV-2026, entry version 107.
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   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Triumph; TISSUE=Testa;
RX   AGRICOLA=IND92043518;
RA   Meldgaard M.;
RT   "Expression of chalcone synthase, dihydroflavonol reductase and flavanone-
RT   3-hydroxylase in mutants of barley deficient in anthocyanin and
RT   proantocyanidin biosynthesis.";
RL   Theor. Appl. Genet. 83:695-706(1992).
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}.
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DR   EMBL; X58138; CAA41146.1; -; mRNA.
DR   PIR; S14647; S14647.
DR   AlphaFoldDB; P28038; -.
DR   SMR; P28038; -.
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..377
FT                   /note="Naringenin,2-oxoglutarate 3-dioxygenase"
FT                   /id="PRO_0000067286"
FT   DOMAIN          193..297
FT                   /note="Fe2OG dioxygenase"
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         222
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         278
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         288
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   377 AA;  42057 MW;  13813A85BB826EF0 CRC64;
     MAPVSNETFL PTEAWGEATL RPSFVRDEDE RPKVAHDRFS DAVPLISLHG IDGARRAQIR
     DRVAAACEDW GIFQVIDHGV DADLIADMTR LAREFFALPA EDKLRYDMSG GKKGGFIVSS
     HLQGEAVQDW REIVTYFSYP VKARDYGRWP EKPAGWCAVV ERYSERLMGL SCNLMGVLSE
     AMGLETEALA KACVDMDQKV VVNFYPRCPQ PDLTLGLKRH TDPGTITLLL QDLVGGLQAT
     RDGGKNWITV QPISGAFVVN LGDHGHFMSN GRFKNADHQA VVNGESSRLS IATFQNPAPD
     ARVWPLAVRE GEEPILEEPI TFTEMYRRKM ERDLDLAKRK KQAKDQLMQQ QLQLQQQQAV
     AAAPMPTATK PLNEILA
//