NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Flower bud;
PubMed=8223617 [NCBI, ExPASy, EBI, Israel, Japan]
Britsch L., Dedio J., Saedler H., Forkmann G.;
"Molecular characterization of flavanone 3 beta-hydroxylases. Consensus sequence, comparison with related enzymes and the role of conserved histidine residues.";
Eur. J. Biochem. 217:745-754(1993).

Comments

FUNCTION: Catalyzes the 3-beta-hydroxylation of 2S-flavonones 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.
COFACTOR: Ascorbate.
PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis .
SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X72594; CAA51192.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S38338; S38338.

3D structure databases

HSSP

Q96323; 1GP4. [HSSP ENTRY / PDB]

ModBase

Q05965.

Family and domain databases

InterPro

IPR005123; 2OG-FeII_Oase.
Graphical view of domain structure.

Pfam

PF03171; 2OG-FeII_Oxy; 1.
Pfam graphical view of domain structure.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; Oxidoreductase; Vitamin C.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 357`	`>357`	`Naringenin,2-oxoglutarate 3-dioxygenase.`	`PRO_0000067288`
`METAL`	`74 74`		`Iron (Potential).`
`METAL`	`216 216`		`Iron (Potential).`
`METAL`	`218 218`		`Iron (Potential).`
`METAL`	`274 274`		`Iron (Potential).`
`NON_TER`	`1 1`

Sequence information

Length: 357 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 39982 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: E74825D07C89D74E [This is a checksum on the sequence]

        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

Q05965 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools