FL3H2_ORYSJ
ID FL3H2_ORYSJ Reviewed; 342 AA.
AC Q8W2X5; Q109B6; Q336X1;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Flavanone 3-dioxygenase 2 {ECO:0000305};
DE EC=1.14.11.9 {ECO:0000269|PubMed:18413994};
DE AltName: Full=Flavanone 3-beta-hydroxylase 2 {ECO:0000305};
DE AltName: Full=Flavanone 3-hydroxylase 2 {ECO:0000303|PubMed:18413994};
DE Short=OsF3H-2 {ECO:0000303|PubMed:18413994};
GN Name=F3H-2 {ECO:0000303|PubMed:18413994};
GN OrderedLocusNames=Os10g0536400 {ECO:0000312|EMBL:BAF27083.1},
GN LOC_Os10g39140 {ECO:0000312|EMBL:ABB47934.2};
GN ORFNames=OSJNBa0040D23.1 {ECO:0000312|EMBL:AAM76343.1},
GN OSJNBb0060I05.4 {ECO:0000312|EMBL:AAL58118.1};
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=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
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=5.7 uM for S-eriodictyol {ECO:0000269|PubMed:18413994};
CC Vmax=0.4 umol/sec/mg enzyme toward S-eriodictyol
CC {ECO:0000269|PubMed:18413994};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8W2X5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8W2X5-2; Sequence=VSP_058987, VSP_058988;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and stems. Expressed at
CC low levels in seeds. {ECO:0000269|PubMed:18413994}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AC092697; AAL58118.1; -; Genomic_DNA.
DR EMBL; AC074196; AAM76343.1; -; Genomic_DNA.
DR EMBL; DP000086; ABB47934.2; -; Genomic_DNA.
DR EMBL; DP000086; ABG66222.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF27083.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT11823.1; -; Genomic_DNA.
DR EMBL; AK061357; BAG87874.1; -; mRNA.
DR RefSeq; XP_015614471.1; XM_015758985.1. [Q8W2X5-1]
DR AlphaFoldDB; Q8W2X5; -.
DR SMR; Q8W2X5; -.
DR STRING; 4530.OS10T0536400-01; -.
DR PRIDE; Q8W2X5; -.
DR EnsemblPlants; Os10t0536400-01; Os10t0536400-01; Os10g0536400. [Q8W2X5-2]
DR GeneID; 4349238; -.
DR Gramene; Os10t0536400-01; Os10t0536400-01; Os10g0536400. [Q8W2X5-2]
DR KEGG; osa:4349238; -.
DR eggNOG; KOG0143; Eukaryota.
DR InParanoid; Q8W2X5; -.
DR OMA; QQIAGAC; -.
DR OrthoDB; 755305at2759; -.
DR BRENDA; 1.14.11.9; 4460.
DR UniPathway; UPA00154; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
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; 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 Alternative splicing; Dioxygenase; Flavonoid biosynthesis; Iron;
KW Metal-binding; Oxidoreductase; Reference proteome; Vitamin C.
FT CHAIN 1..342
FT /note="Flavanone 3-dioxygenase 2"
FT /id="PRO_0000440773"
FT DOMAIN 193..293
FT /note="Fe2OG dioxygenase"
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 219
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 274
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 284
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT VAR_SEQ 174..178
FT /note="AISES -> STLKP (in isoform 2)"
FT /id="VSP_058987"
FT VAR_SEQ 179..342
FT /note="Missing (in isoform 2)"
FT /id="VSP_058988"
SQ SEQUENCE 342 AA; 38731 MW; 6E1E03B087483067 CRC64;
MAAEAEQQHQ LLSTAVHDTM PGKYVRPESQ RPRLDLVVSD ARIPVVDLAS PDRAAVVSAV
GDACRTHGFF QVVNHGIDAA LIASVMEVGR EFFRLPAEEK AKLYSDDPAK KIRLSTSFNV
RKETVHNWRD YLRLHCYPLH QFVPDWPSNP PSFKEIIGTY CTEVRELGFR LYEAISESLG
LEGGYMRETL GEQEQHMAVN YYPQCPEPEL TYGLPAHTDP NALTILLMDD QVAGLQVLND
GKWIAVNPQP GALVINIGDQ LQALSNGKYR SVWHRAVVNS DRERMSVASF LCPCNSVELG
PAKKLITDDS PAVYRNYTYD EYYKKFWSRN LDQEHCLELF RT
