[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Old Glory Blue; TISSUE=Petal; PubMed=7904213 [NCBI, ExPASy, EBI, Israel, Japan] Holton T.A., Brugliera F., Tanaka Y.; "Cloning and expression of flavonol synthase from Petunia hybrida."; Plant J. 4:1003-1010(1993).

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.
DEVELOPMENTAL STAGE: Expressed at highest level during the first stage of flower development.
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

Z22543; CAA80264.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S33510; S33510.

3D structure databases

HSSP

Q96323; 1GP6. [HSSP ENTRY / PDB]

ModBase

Q07512.

Family and domain databases

InterPro

IPR005123; 2OG-FeII_Oase.
IPR002283; Isopenicillin-N_synthase.
Graphical view of domain structure.

Pfam

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

PRINTS

PR00682; IPNSYNTHASE.

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`	`1 348`	`348`	`Flavonol synthase/flavanone 3-hydroxylase.`	`PRO_0000067296`
`METAL`	`234 234`		`Iron (By similarity).`
`METAL`	`236 236`		`Iron (By similarity).`
`METAL`	`290 290`		`Iron (By similarity).`

Sequence information

Length: 348 AA [This is the length of the unprocessed precursor]

Molecular weight: 39427 Da [This is the MW of the unprocessed precursor]

CRC64: B39E1E4381DE6379 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKTAQGVSAT LTMEVARVQA IASLSKCMDT IPSEYIRSEN EQPAATTLHG VVLQVPVIDL 

        70         80         90        100        110        120 
RDPDENKMVK LIADASKEWG IFQLINHGIP DEAIADLQKV GKEFFEHVPQ EEKELIAKTP 

       130        140        150        160        170        180 
GSNDIEGYGT SLQKEVEGKK GWVDHLFHKI WPPSAVNYRY WPKNPPSYRE ANEEYGKRMR 

       190        200        210        220        230        240 
EVVDRIFKSL SLGLGLEGHE MIEAAGGDEI VYLLKINYYP PCPRPDLALG VVAHTDMSYI 

       250        260        270        280        290        300 
TILVPNEVQG LQVFKDGHWY DVKYIPNALI VHIGDQVEIL SNGKYKSVYH RTTVNKDKTR 

       310        320        330        340 
MSWPVFLEPP SEHEVGPIPK LLSEANPPKF KTKKYKDYVY CKLNKLPQ

Q07512 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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