FL3H3_ORYSJ
ID FL3H3_ORYSJ Reviewed; 326 AA.
AC Q7XR84; Q0J988;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Flavanone 3-dioxygenase 3 {ECO:0000305};
DE EC=1.14.11.9 {ECO:0000269|PubMed:18413994};
DE AltName: Full=Flavanone 3-beta-hydroxylase 3 {ECO:0000305};
DE AltName: Full=Flavanone 3-hydroxylase 3 {ECO:0000303|PubMed:18413994};
DE Short=OsF3H-3 {ECO:0000303|PubMed:18413994};
DE AltName: Full=Flavonoid 3-hydroxylase {ECO:0000303|PubMed:18726614};
DE Short=OsF3H {ECO:0000303|PubMed:18726614};
GN Name=F3H-3 {ECO:0000303|PubMed:18726614};
GN Synonyms=F3H {ECO:0000303|PubMed:18726614};
GN OrderedLocusNames=Os04g0667200 {ECO:0000312|EMBL:BAS91520.1},
GN LOC_Os04g57160 {ECO:0000305};
GN ORFNames=OSJNBa0043A12.1 {ECO:0000312|EMBL:CAE02796.1};
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).
RN [6]
RP FUNCTION, AND INDUCTION BY LIGHT.
RX PubMed=18726614; DOI=10.1007/s00425-008-0806-1;
RA Shih C.H., Chu H., Tang L.K., Sakamoto W., Maekawa M., Chu I.K., Wang M.,
RA Lo C.;
RT "Functional characterization of key structural genes in rice flavonoid
RT biosynthesis.";
RL Planta 228:1043-1054(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 (PubMed:18413994, PubMed:18726614). Converts (2S)-eriodictyol to (+)-
CC taxifolin and (2S)-naringenin to (+)-(2R/3R)-dihydrokaempferol in vitro
CC (PubMed:18413994). {ECO:0000269|PubMed:18413994,
CC ECO:0000269|PubMed:18726614}.
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=6.3 uM for S-eriodictyol {ECO:0000269|PubMed:18413994};
CC Vmax=0.5 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 very low levels in roots, leaves,
CC stems and seeds. {ECO:0000269|PubMed:18413994}.
CC -!- INDUCTION: Induced by light. {ECO:0000269|PubMed:18726614}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF16099.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL606619; CAE02796.1; -; Genomic_DNA.
DR EMBL; AP008210; BAF16099.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014960; BAS91520.1; -; Genomic_DNA.
DR RefSeq; XP_015633792.1; XM_015778306.1.
DR RefSeq; XP_015633793.1; XM_015778307.1.
DR AlphaFoldDB; Q7XR84; -.
DR SMR; Q7XR84; -.
DR STRING; 4530.OS04T0667200-01; -.
DR PaxDb; Q7XR84; -.
DR PRIDE; Q7XR84; -.
DR EnsemblPlants; Os04t0667200-01; Os04t0667200-01; Os04g0667200.
DR GeneID; 4337325; -.
DR Gramene; Os04t0667200-01; Os04t0667200-01; Os04g0667200.
DR KEGG; osa:4337325; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_4_1; -.
DR InParanoid; Q7XR84; -.
DR OMA; HYAHPLC; -.
DR OrthoDB; 830141at2759; -.
DR BRENDA; 1.14.11.9; 4460.
DR UniPathway; UPA00154; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
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 Reference proteome; Vitamin C.
FT CHAIN 1..326
FT /note="Flavanone 3-dioxygenase 3"
FT /id="PRO_0000440774"
FT DOMAIN 175..276
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 200
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 202
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 257
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 267
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 326 AA; 36841 MW; 4E5DEE154CE5A168 CRC64;
MSDTSKGIPQ EQLPSQELHP PPMPVINLGH LSLDDPTVRS RVVNDIAKAC RDLGYFQVIS
HGISQSVMDG AIEAASEFFK LPNEIKKEYA SDDIRQPVRY DTSSKDGISM SRAFLKHYAH
PLCDWLQYWP QQPPIYREYM AKYAVEVRVV ALKLMEAILE GLGIGKEYMQ EKFEEGLQLL
SVNCYPKVSQ SDTSIGLAAH SDYGLLTILL TSCQGLEVVD RSSNSWKVVQ QLPHALHVHV
GDHMEVLSNG RIKTVVHRAV LNPQEARISL ASIHGFALHE KVSSAKELVD EENPQKYKEN
SFNDFLEHLT ANMDNRQRNF LESLRM
