FL3H_ARATH
ID FL3H_ARATH Reviewed; 358 AA.
AC Q9S818; Q38877; Q9C526; Q9C528; Q9C530; Q9C563; Q9C5V7;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Naringenin,2-oxoglutarate 3-dioxygenase;
DE Short=Naringenin 3-dioxygenase;
DE EC=1.14.11.9 {ECO:0000250|UniProtKB:Q7XZQ7};
DE AltName: Full=F3H;
DE AltName: Full=Flavanone 3-hydroxylase;
DE AltName: Full=Protein TRANSPARENT TESTA 6;
GN Name=F3H; Synonyms=TT6; OrderedLocusNames=At3g51240; ORFNames=F24M12.280;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Pelletier M.K., Shirley B.W.;
RT "A genomic clone encoding flavanone 3-hydroxylase from Arabidopsis
RT thaliana.";
RL (er) Plant Gene Register PGR95-080(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT F3H-1(TT6).
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=9770503; DOI=10.1073/pnas.95.21.12432;
RA Wisman E., Hartmann U., Sagasser M., Baumann E., Palme K., Hahlbrock K.,
RA Saedler H., Weisshaar B.;
RT "Knock-out mutants from an En-1 mutagenized Arabidopsis thaliana population
RT generate phenylpropanoid biosynthesis phenotypes.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12432-12437(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-358.
RC STRAIN=cv. Can-0, cv. Cha-0, cv. Col-2, cv. Cvi-0, cv. Gr-5, cv. Ita-0,
RC cv. Kas-1, cv. Kon, cv. La-0, cv. Me-0, cv. Mh-0, cv. Mr-0, cv. Nc-1,
RC cv. Per-1, cv. Ri-0, cv. Rsch-0, cv. Rub-1, cv. Tul-0, cv. Wassilewskija,
RC and cv. Yo-1; TISSUE=Leaf;
RX PubMed=11141187; DOI=10.1093/oxfordjournals.molbev.a003714;
RA Aguade M.;
RT "Nucleotide sequence variation at two genes of the phenylpropanoid pathway,
RT the FAH1 and F3H genes, in Arabidopsis thaliana.";
RL Mol. Biol. Evol. 18:1-9(2001).
RN [8]
RP INTERACTION.
RX PubMed=10536025; DOI=10.1073/pnas.96.22.12929;
RA Burbulis I.E., Winkel-Shirley B.;
RT "Interactions among enzymes of the Arabidopsis flavonoid biosynthetic
RT pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12929-12934(1999).
RN [9]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
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 -!- 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:0000250|UniProtKB:Q7XZQ7};
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;
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- SUBUNIT: Interacts with Dihydroflavonol-4-reductase (TT3), chalcone
CC synthase (TT4) and chalcone isomerase (TT5) to form a flavonoid enzyme
CC complex. {ECO:0000269|PubMed:10536025}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9S818-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; U33932; AAC49176.1; -; Genomic_DNA.
DR EMBL; AF064064; AAC68584.1; -; Genomic_DNA.
DR EMBL; AF064065; AAC68585.1; -; Genomic_DNA.
DR EMBL; AL132980; CAB62646.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78766.1; -; Genomic_DNA.
DR EMBL; AF428335; AAL16265.1; -; mRNA.
DR EMBL; AY058886; AAL24272.1; -; mRNA.
DR EMBL; AY116957; AAM51591.1; -; mRNA.
DR EMBL; AY087559; AAM65101.1; -; mRNA.
DR EMBL; AJ295606; CAC26961.1; -; Genomic_DNA.
DR EMBL; AJ295604; CAC26959.1; -; Genomic_DNA.
DR EMBL; AJ295605; CAC26960.1; -; Genomic_DNA.
DR EMBL; AJ295603; CAC26958.1; -; Genomic_DNA.
DR EMBL; AJ295587; CAC26942.1; -; Genomic_DNA.
DR EMBL; AJ295588; CAC26943.1; -; Genomic_DNA.
DR EMBL; AJ295589; CAC26944.1; -; Genomic_DNA.
DR EMBL; AJ295590; CAC26945.1; -; Genomic_DNA.
DR EMBL; AJ295591; CAC26946.1; -; Genomic_DNA.
DR EMBL; AJ295592; CAC26947.1; -; Genomic_DNA.
DR EMBL; AJ295593; CAC26948.1; -; Genomic_DNA.
DR EMBL; AJ295601; CAC26956.1; -; Genomic_DNA.
DR EMBL; AJ295602; CAC26957.1; -; Genomic_DNA.
DR EMBL; AJ295596; CAC26951.1; -; Genomic_DNA.
DR EMBL; AJ295594; CAC26949.1; -; Genomic_DNA.
DR EMBL; AJ295595; CAC26950.1; -; Genomic_DNA.
DR EMBL; AJ295599; CAC26954.1; -; Genomic_DNA.
DR EMBL; AJ295597; CAC26952.1; -; Genomic_DNA.
DR EMBL; AJ295598; CAC26953.1; -; Genomic_DNA.
DR EMBL; AJ295600; CAC26955.1; -; Genomic_DNA.
DR PIR; T45755; T45755.
DR RefSeq; NP_190692.1; NM_114983.3. [Q9S818-1]
DR AlphaFoldDB; Q9S818; -.
DR SMR; Q9S818; -.
DR BioGRID; 9605; 2.
DR IntAct; Q9S818; 3.
DR STRING; 3702.AT3G51240.1; -.
DR PaxDb; Q9S818; -.
DR PRIDE; Q9S818; -.
DR ProteomicsDB; 230032; -. [Q9S818-1]
DR EnsemblPlants; AT3G51240.1; AT3G51240.1; AT3G51240. [Q9S818-1]
DR GeneID; 824287; -.
DR Gramene; AT3G51240.1; AT3G51240.1; AT3G51240. [Q9S818-1]
DR KEGG; ath:AT3G51240; -.
DR Araport; AT3G51240; -.
DR TAIR; locus:2081008; AT3G51240.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; Q9S818; -.
DR OMA; GSHTDIQ; -.
DR OrthoDB; 755371at2759; -.
DR PhylomeDB; Q9S818; -.
DR BioCyc; ARA:AT3G51240-MON; -.
DR BioCyc; MetaCyc:AT3G51240-MON; -.
DR UniPathway; UPA00154; -.
DR PRO; PR:Q9S818; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S818; baseline and differential.
DR Genevisible; Q9S818; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IDA:TAIR.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IDA:TAIR.
DR GO; GO:0010224; P:response to UV-B; IMP:TAIR.
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; ATP-binding; Dioxygenase; Flavonoid biosynthesis;
KW Iron; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW Reference proteome; Vitamin C.
FT CHAIN 1..358
FT /note="Naringenin,2-oxoglutarate 3-dioxygenase"
FT /id="PRO_0000067283"
FT DOMAIN 190..294
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 275
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 285
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT VARIANT 77
FT /note="V -> L (in strain: cv. Ri-0, cv. Tul-0 and cv. Yo-
FT 1)"
FT VARIANT 148
FT /note="D -> N (in strain: cv. Cha-0, cv. Con, cv. Cvi-0,
FT cv. Gr-5, cv. Ita-0, cv. Kas-1, cv. La-0, cv. Ler, cv. Me-
FT 0, cv. Mh-0, cv. Nc-1, cv. Per-1, cv. Ri-0, cv. Rsch-0, cv.
FT Rub-1, cv. Tul-0, cv. Ws-0 and cv. Yo-1)"
FT VARIANT 158
FT /note="E -> K (in strain: cv. Me-0, cv. Mh-0, cv. Per-1 and
FT cv. Ws-0)"
FT VARIANT 350
FT /note="D -> A (in strain: cv. Cha-0, cv. Con, cv. Cvi-0,
FT cv. Gr-5, cv. Ita-0, cv. Kas-1, cv. La-0, cv. Ler, cv. Me-
FT 0, cv. Mh-0, cv. Nc-1, cv. Per-1, cv. Ri-0, cv. Rsch-0, cv.
FT Rub-1, cv. Tul-0, cv. Ws-0 and cv. Yo-1)"
FT VARIANT 354
FT /note="D -> N (in strain: cv. Me-0)"
FT MUTAGEN 248..358
FT /note="Missing: In f3h-1(tt6); reduced seed pigmentation."
SQ SEQUENCE 358 AA; 40276 MW; 16BB0A3B318E5524 CRC64;
MAPGTLTELA GESKLNSKFV RDEDERPKVA YNVFSDEIPV ISLAGIDDVD GKRGEICRQI
VEACENWGIF QVVDHGVDTN LVADMTRLAR DFFALPPEDK LRFDMSGGKK GGFIVSSHLQ
GEAVQDWREI VTYFSYPVRN RDYSRWPDKP EGWVKVTEEY SERLMSLACK LLEVLSEAMG
LEKESLTNAC VDMDQKIVVN YYPKCPQPDL TLGLKRHTDP GTITLLLQDQ VGGLQATRDN
GKTWITVQPV EGAFVVNLGD HGHFLSNGRF KNADHQAVVN SNSSRLSIAT FQNPAPDATV
YPLKVREGEK AILEEPITFA EMYKRKMGRD LELARLKKLA KEERDHKEVD KPVDQIFA
