[1]	NUCLEOTIDE SEQUENCE [MRNA]. Nielsen K.M.; "cDNA cloning of flavonol synthase and antisense suppression of expression in Lisianthus grandiflorum grise."; Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Catalyzes the formation of flavonols from dihydroflavonols. It can act on dihydrokaempferol to produce kaempferol, on dihydroquercetin to produce quercitin and on dihydromyricetin to produce myricetin (By similarity).
CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O₂ = a flavonol + succinate + CO₂ + H₂O.
CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O₂ = a dihydroflavonol + succinate + CO₂.
COFACTOR: Binds 1 iron ion per subunit (By similarity).
COFACTOR: Binds 1 ascorbate molecule per subunit (By similarity).
PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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

AF240764; AAF64168.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q96323; 1GP6. [HSSP ENTRY / PDB]

ModBase

Q9M547.

Ontologies

GO:0045431;	Molecular function: flavonol synthase activity (inferred from electronic annotation from EC).
GO:0045486;	Molecular function: naringenin 3-dioxygenase activity (inferred from electronic annotation from EC).
QuickGo view.

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

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 334`	`334`	`Flavonol synthase/flavanone 3-hydroxylase.`	`PRO_0000067293`
`METAL`	`220 220`		`Iron (By similarity).`
`METAL`	`222 222`		`Iron (By similarity).`
`METAL`	`276 276`		`Iron (By similarity).`

Sequence information

Length: 334 AA [This is the length of the unprocessed precursor]

Molecular weight: 38081 Da [This is the MW of the unprocessed precursor]

CRC64: 4097830ABE2534E2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEVQRVQEIA SLSKVIDTIP AEYIRSENEQ PVISTVHGVV LEVPVIDLSD SDEKKIVGLV 

        70         80         90        100        110        120 
SEASKEWGIF QVVNHGIPNE VIRKLQEVGK HFFELPQEEK ELIAKPEGSQ SIEGYGTRLQ 

       130        140        150        160        170        180 
KEVDGKKGWV DHLFHKIWPP SAINYQFWPK NPPAYREANE EYAKRLQLVV DNLFKYLSLG 

       190        200        210        220        230        240 
LDLEPNSFKD GAGGDDLVYL MKINYYPPCP RPDLALGVAH TDMSAITVLV PNEVPGLQVY 

       250        260        270        280        290        300 
KDGHWYDCKY IPNALIVHIG DQVEIMSNGK YKSVYHRTTV NKEKTRMSWP VFLEPPPDHE 

       310        320        330 
VGPIPKLVNE ENPAKFKTKK YKDYAYCKLN KLPQ

Q9M547 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