Reviewed, UniProtKB/Swiss-Prot Q9S818 (FL3H_ARATH)

Names and origin

Protein names

Recommended name:
    Naringenin,2-oxoglutarate 3-dioxygenase
      Short name=Naringenin 3-dioxygenase
    EC=1.14.11.9
Alternative name(s):
    Flavanone 3-hydroxylase
    F3H
    Protein TRANSPARENT TESTA 6

Gene names

Name:	F3H
Synonyms:	TT6
Ordered Locus Names:	At3g51240
ORF Names:	F24M12.280

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the 3-beta-hydroxylation of 2S-flavanones to 2R,3R-dihydroflavonols which are intermediates in the biosynthesis of flavonols, anthocyanidins, catechins and proanthocyanidins in plants.
Catalytic activity	A flavanone + 2-oxoglutarate + O2 = a dihydroflavonol + succinate + CO2.
Cofactor	Iron. Ascorbate.
Pathway	Secondary metabolite biosynthesis; flavonoid biosynthesis.
Subunit structure	Interacts with Dihydroflavonol-4-reductase (TT3), chalcone synthase (TT4) and chalcone isomerase (TT5) to form a flavonoid enzyme complex. Ref.7
Sequence similarities	Belongs to the iron/ascorbate-dependent oxidoreductase family. Contains 1 Fe2OG dioxygenase domain.

Ontologies

Keywords
Biological process	Flavonoid biosynthesis
Ligand	ATP-binding Iron Metal-binding Nucleotide-binding Vitamin C
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	flavonoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to UV-B Inferred from mutant phenotype. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW naringenin 3-dioxygenase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 358	358	Naringenin,2-oxoglutarate 3-dioxygenase		PRO_0000067283
Regions
	Domain	190 – 294	105	Fe2OG dioxygenase
Sites
	Metal binding	75	1	Iron Potential
	Metal binding	217	1	Iron Potential
	Metal binding	219	1	Iron Potential
	Metal binding	275	1	Iron Potential
Natural variations
	Natural variant	77	1	V → L in strain: cv. Ri-0, cv. Tul-0 and cv. Yo-1.
	Natural variant	148	1	D → N in strain: cv. Cha-0, cv. Con, cv. Cvi-0, cv. Gr-5, cv. Ita-0, cv. Kas-1, cv. La-0, cv. Ler, cv. Me-0, cv. Mh-0, cv. Nc-1, cv. Per-1, cv. Ri-0, cv. Rsch-0, cv. Rub-1, cv. Tul-0, cv. Ws-0 and cv. Yo-1.
	Natural variant	158	1	E → K in strain: cv. Me-0, cv. Mh-0, cv. Per-1 and cv. Ws-0.
	Natural variant	350	1	D → A in strain: cv. Cha-0, cv. Con, cv. Cvi-0, cv. Gr-5, cv. Ita-0, cv. Kas-1, cv. La-0, cv. Ler, cv. Me-0, cv. Mh-0, cv. Nc-1, cv. Per-1, cv. Ri-0, cv. Rsch-0, cv. Rub-1, cv. Tul-0, cv. Ws-0 and cv. Yo-1.
	Natural variant	354	1	D → N in strain: cv. Me-0.
Experimental info
	Mutagenesis	248 – 358	111	Missing in f3h-1(tt6); reduced seed pigmentation.

Sequences

	Sequence		Length	Mass (Da)
	Q9S818-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 16BB0A3B318E5524	FASTA	358	40,276
	10 20 30 40 50 60 MAPGTLTELA GESKLNSKFV RDEDERPKVA YNVFSDEIPV ISLAGIDDVD GKRGEICRQI 70 80 90 100 110 120 VEACENWGIF QVVDHGVDTN LVADMTRLAR DFFALPPEDK LRFDMSGGKK GGFIVSSHLQ 130 140 150 160 170 180 GEAVQDWREI VTYFSYPVRN RDYSRWPDKP EGWVKVTEEY SERLMSLACK LLEVLSEAMG 190 200 210 220 230 240 LEKESLTNAC VDMDQKIVVN YYPKCPQPDL TLGLKRHTDP GTITLLLQDQ VGGLQATRDN 250 260 270 280 290 300 GKTWITVQPV EGAFVVNLGD HGHFLSNGRF KNADHQAVVN SNSSRLSIAT FQNPAPDATV 310 320 330 340 350 YPLKVREGEK AILEEPITFA EMYKRKMGRD LELARLKKLA KEERDHKEVD KPVDQIFA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A genomic clone encoding flavanone 3-hydroxylase from Arabidopsis thaliana." Pelletier M.K., Shirley B.W. Plant Gene Register PGR95-080 Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Landsberg erecta.
[2]	"Knock-out mutants from an En-1 mutagenized Arabidopsis thaliana population generate phenylpropanoid biosynthesis phenotypes." Wisman E., Hartmann U., Sagasser M., Baumann E., Palme K., Hahlbrock K., Saedler H., Weisshaar B. Proc. Natl. Acad. Sci. U.S.A. 95:12432-12437(1998) [PubMed: 9770503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT F3H-1(TT6). Strain: cv. Columbia and cv. Landsberg erecta.
[3]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Nucleotide sequence variation at two genes of the phenylpropanoid pathway, the FAH1 and F3H genes, in Arabidopsis thaliana." Aguade M. Mol. Biol. Evol. 18:1-9(2001) [PubMed: 11141187] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 15-358. Strain: cv. Can-0, cv. Cha-0, cv. Col-2, cv. Cvi-0, cv. Gr-5, cv. Ita-0, cv. Kas-1, cv. Kon, cv. La-0, cv. Me-0, cv. Mh-0, cv. Mr-0, cv. Nc-1, cv. Per-1, cv. Ri-0, cv. Rsch-0, cv. Rub-1, cv. Tul-0, cv. Wassilewskija and cv. Yo-1. Tissue: Leaf.
[7]	"Interactions among enzymes of the Arabidopsis flavonoid biosynthetic pathway." Burbulis I.E., Winkel-Shirley B. Proc. Natl. Acad. Sci. U.S.A. 96:12929-12934(1999) [PubMed: 10536025] [Abstract] Cited for: INTERACTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U33932 Genomic DNA. Translation: AAC49176.1. AF064064 Genomic DNA. Translation: AAC68584.1. AF064065 Genomic DNA. Translation: AAC68585.1. AL132980 Genomic DNA. Translation: CAB62646.1. AF428335 mRNA. Translation: AAL16265.1. AY058886 mRNA. Translation: AAL24272.1. AY116957 mRNA. Translation: AAM51591.1. AY087559 mRNA. Translation: AAM65101.1. AJ295606 Genomic DNA. Translation: CAC26961.1. AJ295604 Genomic DNA. Translation: CAC26959.1. AJ295605 Genomic DNA. Translation: CAC26960.1. AJ295603 Genomic DNA. Translation: CAC26958.1. AJ295587 Genomic DNA. Translation: CAC26942.1. AJ295588 Genomic DNA. Translation: CAC26943.1. AJ295589 Genomic DNA. Translation: CAC26944.1. AJ295590 Genomic DNA. Translation: CAC26945.1. AJ295591 Genomic DNA. Translation: CAC26946.1. AJ295592 Genomic DNA. Translation: CAC26947.1. AJ295593 Genomic DNA. Translation: CAC26948.1. AJ295601 Genomic DNA. Translation: CAC26956.1. AJ295602 Genomic DNA. Translation: CAC26957.1. AJ295596 Genomic DNA. Translation: CAC26951.1. AJ295594 Genomic DNA. Translation: CAC26949.1. AJ295595 Genomic DNA. Translation: CAC26950.1. AJ295599 Genomic DNA. Translation: CAC26954.1. AJ295597 Genomic DNA. Translation: CAC26952.1. AJ295598 Genomic DNA. Translation: CAC26953.1. AJ295600 Genomic DNA. Translation: CAC26955.1.
IPI	IPI00539054.
PIR	T45755.
RefSeq	NP_190692.1.
UniGene	At.21413 At.23201 At.67970 Rra.424 Rsa.22223 Rsa.5996
3D structure databases
SMR	Q9S818. Positions 1-329, 36-331.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9S818. 3 interactions.
STRING	Q9S818.
Proteomic databases
PRIDE	Q9S818.
Genome annotation databases
GeneID	824287.
GenomeReviews	Gene locus AT3G51240 in contig BA000014_GR.
KEGG	ath:AT3G51240.
NMPDR	fig|3702.1.peg.16376.
Organism-specific databases
TAIR	At3g51240.
Phylogenomic databases
eggNOG	KOG0143.
InParanoid	Q9S818.
OMA	PPEDKLR.
Enzyme and pathway databases
BRENDA	1.14.11.9. 302.
Gene expression databases
ArrayExpress	Q9S818.
Genevestigator	Q9S818.
GermOnline	AT3G51240. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR005123. Oxoglutarate/Fe-dep_oxygenase. [Graphical view]
Pfam	PF03171. 2OG-FeII_Oxy. 1 hit. [Graphical view]
PROSITE	PS51471. FE2OG_OXY. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FL3H_ARATH

Accession

Primary (citable) accession number: Q9S818
Secondary accession number(s): Q38877 , Q9C526, Q9C528, Q9C530, Q9C563, Q9C5V7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 13, 2002
Last sequence update:	May 1, 2000
Last modified:	February 9, 2010
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)