NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Lambrusco Foglia Frastagliata;
DOI=10.1007/BF00029856; PubMed=8193299 [NCBI, ExPASy, EBI, Israel, Japan]
Sparvoli F., Martin C., Scienza A., Gavazzi G., Tonelli C.;
"Cloning and molecular analysis of structural genes involved in flavonoid and stilbene biosynthesis in grape (Vitis vinifera L.).";
Plant Mol. Biol. 24:743-755(1994).

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

X75965; CAA53579.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

P41090.

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`	`1 364`	`364`	`Naringenin,2-oxoglutarate 3-dioxygenase.`	`PRO_0000067290`
`METAL`	`76 76`		`Iron (Potential).`
`METAL`	`218 218`		`Iron (Potential).`
`METAL`	`220 220`		`Iron (Potential).`
`METAL`	`276 276`		`Iron (Potential).`

Sequence information

Length: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 40875 Da [This is the MW of the unprocessed precursor]

CRC64: 2C1FBEEF1EADD674 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAPTTLTALA GEKTLQSSFV RDEDERPKVA YNDFSNEIPV ISLTKESMKL AAVVDEICRK 

        70         80         90        100        110        120 
IVEACEDWGI FQVVNHGVDS NLISEMTRLA REFFALPPEE NVRFDMSGGK KGGFIVSSHL 

       130        140        150        160        170        180 
QGEAVQDWRE IVTYFSYPLR TRDYSRWPDK PEGWRSVTQE YSEKLMGLAC KLLEVLSEAM 

       190        200        210        220        230        240 
DLDKDALTNA CVDMDQKVVV NFYPQCPQPD LTLGLKRHTD PGTITLLLQD QVGGLQATRD 

       250        260        270        280        290        300 
GGKTWITVQP VEGAFVVNLG DHGHYLSNGR FKNADHQAVV NSNHSRLSIA TFQNPAPEAT 

       310        320        330        340        350        360 
VYPLKIREGE KAVLEGPITF AEMYRRKMSK DLELARLKKL AKEQQLQDVE KAKLESKPID 


QILA

P41090 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