Q05965 (FL3H_MATIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Naringenin,2-oxoglutarate 3-dioxygenase
EC=1.14.11.9

Alternative name(s):
FHT
Flavanone-3-hydroxylase
Short name=F3H

Gene names

Name:

FHT

Organism

Matthiola incana (Common stock) (Cheiranthus incanus)

Taxonomic identifier

3724 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	357 AA.
Sequence status	Fragment.
Protein existence	Evidence at transcript 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.
Sequence similarities	Belongs to the iron/ascorbate-dependent oxidoreductase family. Contains 1 Fe2OG dioxygenase domain.

Ontologies

Keywords
Biological process	Flavonoid biosynthesis
Ligand	Iron Metal-binding Vitamin C
Molecular function	Dioxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	flavonoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW metal 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 – 357	›357	Naringenin,2-oxoglutarate 3-dioxygenase		PRO_0000067288
Regions
	Domain	189 – 293	105	Fe2OG dioxygenase
Sites
	Metal binding	74	1	Iron Potential
	Metal binding	216	1	Iron Potential
	Metal binding	218	1	Iron Potential
	Metal binding	274	1	Iron Potential
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q05965 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: E74825D07C89D74E	FASTA	357	39,982
	10 20 30 40 50 60 APGTLTELAG ESKLNSKFVR DEDERPKVAY NEFSDEIPVI SLAGIDDVDG KRGEICREIV 70 80 90 100 110 120 EACENWGIFQ VVDHGVDTSL VADMTRLARD FFALPPEEKL RFDMSGGKKG GFIVSSHLQG 130 140 150 160 170 180 EAVQDWREIV TYFSYPVRNR DYSRWPDKPQ GWAKVTEEYS EKLMGLACKL LEVLSEAMGL 190 200 210 220 230 240 EKESLTNACV DMDQKIVVNY YPKCPQPDLT LGLKRHTDPG TITLLLQDQV GGLQATRDDG 250 260 270 280 290 300 NTWITVQPVE GAFVVNLGDH GHFLSNGRFK NADHQAVVNS NSSRLSIATF QNPAPEATVY 310 320 330 340 350 PLKVREGEKA IMEEPITFAE MYKRKMGRDL ELARLKKLAK EEHNHKEAAK PLDQILA

References

[1]	"Molecular characterization of flavanone 3 beta-hydroxylases. Consensus sequence, comparison with related enzymes and the role of conserved histidine residues." Britsch L., Dedio J., Saedler H., Forkmann G. Eur. J. Biochem. 217:745-754(1993) [PubMed: 8223617] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Flower bud.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X72594 mRNA. Translation: CAA51192.1.
PIR	S38338.
3D structure databases
ProteinModelPortal	Q05965.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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_MATIN

Accession

Primary (citable) accession number: Q05965

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	September 21, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program