FL3H1_ORYSJ
ID FL3H1_ORYSJ Reviewed; 377 AA.
AC Q7XM21; A0A0P0WFY8; C7J0Y2;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Flavanone 3-dioxygenase 1 {ECO:0000305};
DE EC=1.14.11.9 {ECO:0000269|PubMed:18413994};
DE AltName: Full=Flavanone 3-beta-hydroxylase 1 {ECO:0000305};
DE AltName: Full=Flavanone 3-hydroxylase 1 {ECO:0000303|PubMed:18413994};
DE Short=OsF3H-1 {ECO:0000303|PubMed:18413994};
GN Name=F3H-1 {ECO:0000303|PubMed:18413994};
GN OrderedLocusNames=Os04g0662600 {ECO:0000312|EMBL:BAH92861.1},
GN LOC_Os04g56700 {ECO:0000305};
GN ORFNames=OSJNBa0084K01.10 {ECO:0000312|EMBL:CAE04838.2};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=18413994;
RA Kim J.H., Lee Y.J., Kim B.G., Lim Y., Ahn J.H.;
RT "Flavanone 3beta-hydroxylases from rice: key enzymes for favonol and
RT anthocyanin biosynthesis.";
RL Mol. Cells 25:312-316(2008).
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 Converts (2S)-eriodictyol to (+)-taxifolin and (2S)-naringenin to (+)-
CC (2R/3R)-dihydrokaempferol in vitro. {ECO:0000269|PubMed:18413994}.
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:18413994};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=57.8 uM for S-eriodictyol {ECO:0000269|PubMed:18413994};
CC Vmax=3.1 umol/sec/mg enzyme toward S-eriodictyol
CC {ECO:0000269|PubMed:18413994};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, leaves, stems and
CC seeds. {ECO:0000269|PubMed:18413994}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH92861.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS91470.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL606999; CAE04838.2; -; Genomic_DNA.
DR EMBL; AP008210; BAH92861.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014960; BAS91470.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015634635.1; XM_015779149.1.
DR AlphaFoldDB; Q7XM21; -.
DR SMR; Q7XM21; -.
DR STRING; 4530.OS04T0662600-00; -.
DR PRIDE; Q7XM21; -.
DR GeneID; 9270463; -.
DR KEGG; osa:9270463; -.
DR eggNOG; KOG0143; Eukaryota.
DR InParanoid; Q7XM21; -.
DR OrthoDB; 755371at2759; -.
DR PlantReactome; R-OSA-1119322; Leucodelphinidin biosynthesis.
DR PlantReactome; R-OSA-1119415; Leucopelargonidin and leucocyanidin biosynthesis.
DR PlantReactome; R-OSA-1119531; Flavonoid biosynthesis.
DR UniPathway; UPA00154; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 Reference proteome; Vitamin C.
FT CHAIN 1..377
FT /note="Flavanone 3-dioxygenase 1"
FT /id="PRO_0000440772"
FT DOMAIN 191..295
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 339..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 377 AA; 41559 MW; E5704DAB62538B1E CRC64;
MAPVATTFLP TASNEATLRP SFVRDEDERP RVAYNQFSDA VPVISLQGID EAARAEIRAR
VAGACEEWGI FQVVDHGVDA GLVADMARLA RDFFALPPED KLRFDMSGGK KGGFIVSSHL
QGEAVKDWRE IVTYFSYPVK SRDYSRWPDK PAGWRAVVEQ YSERLMGLAC KLLGVLSEAM
GLDTNALADA CVDMDQKVVV NFYPKCPQPD LTLGLKRHTD PGTITLLLQD LVGGLQATRD
AGKTWITVQP IPGSFVVNLG DHAHYLSNGR FKNADHQAVV NSDCCRLSIA TFQNPAPDAM
VYPLAVRDGE EPILEEPITF AEMYRRKMAR DLELAKLKKK AKEQRQLQQA ALPPPPPTQV
AAELAAQKPK SLDEILA
