NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pistil;
PubMed=9025306 [NCBI, ExPASy, EBI, Israel, Japan]
van Eldik G.J., Ruiter R.K., Reijnen W.H., van Herpen M.M.A., Schrauwen J.A.M., Wullems G.J.;
"Regulation of flavonol biosynthesis during anther and pistil development, and during pollen tube growth in Solanum tuberosum.";
Plant J. 11:105-113(1997).

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 iron ion per subunit (By similarity).
COFACTOR: Binds 1 ascorbate molecule per subunit (By similarity).
PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm.
DEVELOPMENTAL STAGE: Temporally expressed during 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

X92178; CAA63092.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T07373; T07373.

3D structure databases

HSSP

Q96323; 1GP6. [HSSP ENTRY / PDB]

ModBase

Q41452.

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`	`1 349`	`349`	`Flavonol synthase/flavanone 3-hydroxylase.`	`PRO_0000067297`
`METAL`	`238 238`		`Iron (By similarity).`
`METAL`	`240 240`		`Iron (By similarity).`
`METAL`	`291 291`		`Iron (By similarity).`

Sequence information

Length: 349 AA [This is the length of the unprocessed precursor]

Molecular weight: 39728 Da [This is the MW of the unprocessed precursor]

CRC64: ADBBC3F6B10A0E05 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKTIQGQSAT TALTMEVARV QAISSITKCM DTIPSEYIRS ENEQPAATTL QGVVLEVPVI 

        70         80         90        100        110        120 
DISNVDDDEE KLVKEIVEAS KEWGIFQVIN HGIPDEVIEN LQKVGKEFFE EVPQEEKELI 

       130        140        150        160        170        180 
AKKPGAQSLE GYGTSLQKEI EGKKGWVDHL FHKIWPPSAI NYRYWPKNPP SYREANEEYA 

       190        200        210        220        230        240 
KWLRKVADGI FRSLSLGLGL EGHEMMEAAG SEDIVYMLKI NYYPPCPRPD LALGVVAHTD 

       250        260        270        280        290        300 
MSYITLLVPN EVQVFKDGHW YDVNYIPNAI IVHIGDQVEI LSNGKYKSVY HRTTVNKYKT 

       310        320        330        340 
RMSWPVFLEP SSEHEVGPIP NLINEANPPK FKTKKYKDYV YCKLNKLPQ

Q41452 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