ID FL3H1_CROXC Reviewed; 372 AA. AC A0A4D6Q9B0; DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot. DT 03-JUL-2019, sequence version 1. DT 25-MAY-2022, entry version 11. DE RecName: Full=Flavanone 3-dioxygenase F3H1 {ECO:0000305}; DE EC=1.14.11.9 {ECO:0000269|PubMed:31004005}; DE AltName: Full=Flavanone 3'-hydroxylase 1 {ECO:0000303|PubMed:31004005}; DE Short=CcF3H-1 {ECO:0000303|PubMed:31004005}; GN Name=F3H-1 {ECO:0000303|PubMed:31004005}; OS Crocosmia x crocosmiiflora (Montbretia) (Crocosmia aurea x Crocosmia OS pottsii). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Iridaceae; OC Crocoideae; Freesieae; Crocosmia. OX NCBI_TaxID=1053288; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND RP TISSUE SPECIFICITY. RX PubMed=31004005; DOI=10.1104/pp.19.00254; RA Irmisch S., Ruebsam H., Jancsik S., Man Saint Yuen M., Madilao L.L., RA Bohlmann J.; RT "Flavonol biosynthesis genes and their use in engineering the plant RT antidiabetic metabolite montbretin A."; RL Plant Physiol. 180:1277-1290(2019). CC -!- FUNCTION: Catalyzes the 3-beta-hydroxylation of (2S)-flavanones to CC 2R,3R-dihydroflavonols, which are intermediates in the biosynthesis of CC flavonols, anthocyanidins, catechins and proanthocyanidins in plants CC (PubMed:31004005). Can act on naringenin to produce dihydrokaempferol, CC and on eriodictyol to produced dihydroquercetin (PubMed:31004005). CC {ECO:0000269|PubMed:31004005}. 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:31004005}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18622; CC Evidence={ECO:0000269|PubMed:31004005}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2S)-naringenin + 2-oxoglutarate + O2 = (2R,3R)- CC dihydrokaempferol + CO2 + succinate; Xref=Rhea:RHEA:61084, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15401, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:17846, ChEBI:CHEBI:30031; CC Evidence={ECO:0000269|PubMed:31004005}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61085; CC Evidence={ECO:0000269|PubMed:31004005}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-eriodictyol + 2-oxoglutarate + O2 = (2R,3R)- CC dihydroquercetin + CO2 + succinate; Xref=Rhea:RHEA:61088, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:17948, ChEBI:CHEBI:28412, ChEBI:CHEBI:30031; CC Evidence={ECO:0000269|PubMed:31004005}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61089; CC Evidence={ECO:0000269|PubMed:31004005}; CC -!- COFACTOR: CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; CC Evidence={ECO:0000305|PubMed:31004005}; CC Note=Binds 1 ascorbate molecule per subunit. CC {ECO:0000305|PubMed:31004005}; 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 -!- PATHWAY: Flavonoid metabolism. {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed in young cromes. CC {ECO:0000269|PubMed:31004005}. 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; MK562522; QCF41217.1; -; mRNA. DR AlphaFoldDB; A0A4D6Q9B0; -. DR SMR; A0A4D6Q9B0; -. 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-KW. 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..372 FT /note="Flavanone 3-dioxygenase F3H1" FT /id="PRO_0000448071" FT DOMAIN 195..299 FT /note="Fe2OG dioxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT METAL 222 FT /note="Iron" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT METAL 224 FT /note="Iron" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT METAL 280 FT /note="Iron" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 290 FT /note="2-oxoglutarate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" SQ SEQUENCE 372 AA; 41370 MW; 98603F9E589A20AF CRC64; MAPGATATPF LPTVSNETTL RESFVRDEDE RPKVAYNVFS SEIPVISLEG IDEIEGRRVE ICKKIVAACE DWGVFQVVDH GVDAGVIADM TRLAREFFSL PPEDKLRFDM SGGKKGGFIV SSHLQGEAVQ DWREIVTYFS YPIRARDYSR WPDKPEDWRS VTEKYSETLM ELACKLLGVL SEAMGLDTEA ITKACIDMDQ KVVVNFYPKC PQPDLTLGLK RHTDPGTITL LLQDQVGGLQ ATKDGGKTWI TVQPVEGAFV VNLGDHGHFL SNGRFKNADH QAVVNSNTSR LSIATFQNPA PDAIVYPLAI REGEKPVLDE PITFAEMYRR KMSRDLELAK IKKLAKVENQ EVLEKTKVEA VAQPKGLGEI LA //