FL3H_PETHY
ID FL3H_PETHY Reviewed; 369 AA.
AC Q07353;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=AN3;
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Blue Titan; TISSUE=Flower bud;
RX PubMed=1544919; DOI=10.1016/s0021-9258(18)42777-9;
RA Britsch L., Ruhnau-Brich B., Forkmann G.;
RT "Molecular cloning, sequence analysis, and in vitro expression of flavanone
RT 3 beta-hydroxylase from Petunia hybrida.";
RL J. Biol. Chem. 267:5380-5387(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=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; X60512; CAA43027.1; -; mRNA.
DR PIR; A42110; A42110.
DR PIR; S16780; S16780.
DR AlphaFoldDB; Q07353; -.
DR SMR; Q07353; -.
DR BioCyc; MetaCyc:MON-11838; -.
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:0009805; P:coumarin biosynthetic process; IEA:UniProt.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0002238; P:response to molecule of fungal origin; IEA:UniProt.
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 1: Evidence at protein level;
KW Dioxygenase; Direct protein sequencing; Flavonoid biosynthesis; Iron;
KW Metal-binding; Oxidoreductase; Vitamin C.
FT CHAIN <1..369
FT /note="Naringenin,2-oxoglutarate 3-dioxygenase"
FT /id="PRO_0000067289"
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"
FT NON_TER 1
SQ SEQUENCE 369 AA; 41466 MW; C34034E23B4D5A3F CRC64;
IPRVTPSTLT ALAEEKTLQT SFIRDEDERP KVAYNQFSNE IPIISLEGID DETGKRAEIC
DKIVKACEDW GVFQVVDHGV DAEVISQMTT FAKEFFALPP EEKLRFDMSG GKKGGFIVSS
HLQGEVVQDW REIVTYFSYP TRARDYSRWP DKPEGWIAVT QKYSEKLMEL ACKLLDVLSE
AMGLEKEALT KACVDMDQKV VVNFYPKCPE PDLTLGLKRH TDPGTITLLL QDQVGGLQAT
KDNGKTWITV QPVEGAFVVN LGDHGHFLSN GRFKNADHQA VVNSNSSRLS IATFQNPAPE
AIVYPLKIRE GEKSIMDEPI TFAEMYRRKM SKDLELARLK KQAKEQQLQA EVAAEKAKLE
SKPIEEILA
