[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Flower bud, and Petal; Henkel J., Forkmann G.; "Cloning and expression of a flavonol synthase gene from common stock (Matthiola incana)."; Submitted (APR-1997) 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.
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 ascorbate molecule per subunit.
COFACTOR: Binds 1 iron ion per subunit.
PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm.
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

AF001391; AAB58800.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q96323; 1GP6. [HSSP ENTRY / PDB]

ModBase

O04395.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0045431;	Molecular function: flavonol synthase activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0031418;	Molecular function: L-ascorbic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0045486;	Molecular function: naringenin 3-dioxygenase activity (inferred from electronic annotation from EC).
GO:0016702;	Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (inferred from electronic annotation from UniProtKB-KW).
GO:0009813;	Biological process: flavonoid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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

ProtoNet

O04395.

UniRef

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`	`<1 291`	`>291`	`Flavonol synthase/flavanone 3-hydroxylase.`	`PRO_0000067295`
`METAL`	`175 175`		`Iron (By similarity).`
`METAL`	`177 177`		`Iron (By similarity).`
`METAL`	`231 231`		`Iron (By similarity).`
`NON_TER`	`1 1`

Sequence information

Length: 291 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 33430 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 6B8E4E3D2834720A [This is a checksum on the sequence]

        10         20         30         40         50         60 
QVPVVDLSCP DEELVARTVV KASEDWGVFQ VVNHGIPTEL IQRLQKVGRE FFELPEAEKR 

        70         80         90        100        110        120 
SCAREAGSVE GYGRRIELDI KKRKGIVDQI YLSTWPPSSV NYRYWPKSPP DYREVNEEYA 

       130        140        150        160        170        180 
RHVKTLSEKI MEWLSEGLGL GREAIKEVNG CWYVMNINHY PPYPHSDSFN GLEPHTDING 

       190        200        210        220        230        240 
LTLIITNEIP GLQVFKDDHW IEVEYIPSAI IVNIGDQIMM LSNGKYKNVL HKTTVDKEKT 

       250        260        270        280        290 
RMSWPVLVSP TYDMVVGPLP ELTSEDDPPK FKPIAYKDYV HNKITFLKNK S

O04395 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