FL3H_PETCR
ID FL3H_PETCR Reviewed; 368 AA.
AC Q7XZQ7;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Flavanone 3-dioxygenase;
DE EC=1.14.11.9 {ECO:0000269|PubMed:12782296};
DE AltName: Full=Flavanone 3-beta-hydroxylase;
DE AltName: Full=Flavanone 3-hydroxylase;
DE Short=F3H;
DE AltName: Full=Naringenin,2-oxoglutarate 3-dioxygenase;
DE Short=Naringenin 3-dioxygenase;
GN Name=FHT;
OS Petroselinum crispum (Parsley) (Petroselinum hortense).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Apieae; Petroselinum.
OX NCBI_TaxID=4043;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Italian Giant;
RX PubMed=12782296; DOI=10.1016/s0014-5793(03)00479-4;
RA Martens S., Forkmann G., Britsch L., Wellmann F., Matern U., Lukacin R.;
RT "Divergent evolution of flavonoid 2-oxoglutarate-dependent dioxygenases in
RT parsley.";
RL FEBS Lett. 544:93-98(2003).
CC -!- FUNCTION: Involved in the conversion of (2S)-naringenin to (+)-(2R/3R)-
CC dihydrokaempferol.
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:0000269|PubMed:12782296};
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; Evidence={ECO:0000250};
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; AY230248; AAP57394.1; -; mRNA.
DR AlphaFoldDB; Q7XZQ7; -.
DR SMR; Q7XZQ7; -.
DR PRIDE; Q7XZQ7; -.
DR BRENDA; 1.14.11.9; 4694.
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 1: Evidence at protein level;
KW Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW Vitamin C.
FT CHAIN 1..368
FT /note="Flavanone 3-dioxygenase"
FT /id="PRO_0000386541"
FT DOMAIN 191..295
FT /note="Fe2OG dioxygenase"
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 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 368 AA; 41446 MW; BA8DAF9EFA66FC7E CRC64;
MAPSTLTALA QEKTLNSKFV RDEDERPKIA YNKFSDEIPV ISLAGIDDDS VDKRSQICRK
IVEACEDWGI FQVVDHGIDI DLISEMTRLA RQFFALPAEE KLRFDMTGGK KGGFIVSSHL
QGEAVQDWRE IVTYFSYPIQ ARDYSRWPDK PEGWRSITEM YSDELMALAC KLLEVLSEAM
GLEKEGLTKA CVDMDQKVIV NYYPKCPQPN LTLGLKRHTD PGTITLLLQD QVGGLQATRD
GGKTWITVQP VEGAFVVNLG DHGHYLSNGR FKNADHQAVV NSNSSRMSIA TFQNPAPNAT
VYPLKIREGE KAVMEEPITF AEMYKRKMSR DIEMATLKKL AKEKVLQDQE VEKAKLQMTP
KSADEIFA
