[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Fuji; TISSUE=Peelings; Lee J.-R., Hong S.-T., Kim S.-R.; "Molecular cloning and expression of a flavonol synthase cDNA from 'Fuji' apple."; Submitted (JAN-1999) 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

AF119095; AAD26261.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q96323; 1GP6. [HSSP ENTRY / PDB]

ModBase

Q9XHG2.

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`	`1 337`	`337`	`Flavonol synthase/flavanone 3-hydroxylase.`	`PRO_0000067294`
`METAL`	`223 223`		`Iron (By similarity).`
`METAL`	`225 225`		`Iron (By similarity).`
`METAL`	`279 279`		`Iron (By similarity).`

Sequence information

Length: 337 AA [This is the length of the unprocessed precursor]

Molecular weight: 38123 Da [This is the MW of the unprocessed precursor]

CRC64: 49AE7236145A6072 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGVESVERER ESNEGTIPAE FIRSENEQPG ITTVHGKVLE VPIIDFSDPD EEKLIVQITE 

        70         80         90        100        110        120 
ASSNWGMYQI VNHDIPSEVI SKLQAVGKEF FELPQEEKEA YAKPPDSASI EGYGTKLFKE 

       130        140        150        160        170        180 
ISEGDTTKKG WVDNLFNKIW PPSVVNYQFW PKNPPSYREA NEEYAKHLHN VVEKLFRLLS 

       190        200        210        220        230        240 
LGLGLEGQEL KKAAGGDNLE YLLKINYYPP CPRPDLALGV VAHTDMSTVT ILVPNDVQGL 

       250        260        270        280        290        300 
QACKDGRWYD VKYIPNALVI HIGDQMEIMS NGKYTSVLHR TTVNKDKTRI SWPVFLEPPA 

       310        320        330 
DHVVGPHPQL VNAVNQPKYK TKKYGDYVYC KINKLPQ

Q9XHG2 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