FL3H_CALCH
ID FL3H_CALCH Reviewed; 356 AA.
AC Q05963;
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;
GN Name=FHT;
OS Callistephus chinensis (China aster) (Callistemma chinense).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Astereae;
OC Australasian lineages; Asterinae; Callistephus.
OX NCBI_TaxID=13379;
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=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; X72593; CAA51191.1; -; mRNA.
DR PIR; S38336; S32147.
DR AlphaFoldDB; Q05963; -.
DR SMR; Q05963; -.
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..356
FT /note="Naringenin,2-oxoglutarate 3-dioxygenase"
FT /id="PRO_0000067284"
FT DOMAIN 188..292
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 215
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 217
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 273
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 283
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 356 AA; 40210 MW; BE622A4A8C39BA0B CRC64;
MAAPISLKWE EHSLHENKFV RDEDERPKVP YNTFSNEIPV ISLAGIDGCR RAEICDEIVK
ACEDWGIFQV VDHGVDTKLL SDMTGLARDF FHLPTQEKLR FDMTGGKKGG FIVSSHLQGE
AVQDWREIVT YFSYPIKARD YSRWPDKPNE WRAVTEEYSK VLMGLACKLL EVLSEAMGLE
KEALTKACVD MDQKVVVNYY PKCPQPDLTL GLKRHTDPGT ITLLLQDQVG GLQATRDGGE
SWITVKPVEG AFVVNLGDHG HYLSNGRFKN ADHQAVVNSS TSRLSIATFQ NPAPEAIVYP
LKINEGEKSI MEEPMTFMEM YKKKMSTDLE LARLKKLAKD KQQDLEVVKP IQNIFA
