[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Satsuma Mandarin; DOI=10.1034/j.1399-3054.2002.1140211.x; PubMed=11903972 [NCBI, ExPASy, EBI, Israel, Japan] Moriguchi T., Kita M., Ogawa K., Tomono Y., Endo T., Omura M.; "Flavonol synthase gene expression during citrus fruit development."; Physiol. Plantarum 114:251-258(2002).
[2]	PROTEIN SEQUENCE OF 1-14, CHARACTERIZATION, AND MUTAGENESIS OF GLY-68 AND GLY-261. PubMed=12180990 [NCBI, ExPASy, EBI, Israel, Japan] Wellmann F., Lukacin R., Moriguchi T., Britsch L., Schiltz E., Matern U.; "Functional expression and mutational analysis of flavonol synthase from Citrus unshiu."; Eur. J. Biochem. 269:4134-4142(2002).
[3]	FUNCTION. DOI=10.1016/S0031-9422(02)00567-8; PubMed=12620339 [NCBI, ExPASy, EBI, Israel, Japan] Lukacin R., Wellmann F., Britsch L., Martens S., Matern U.; "Flavonol synthase from Citrus unshiu is a bifunctional dioxygenase."; Phytochemistry 62:287-292(2003).

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).
TISSUE SPECIFICITY: In the juice sacs/segment epidermis (edible part) at the early developmental stage.
DEVELOPMENTAL STAGE: Increases in the peel during fruit maturation.
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

AB011796; BAA36554.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q96323; 1GP6. [HSSP ENTRY / PDB]

ModBase

Q9ZWQ9.

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; Direct protein sequencing; Flavonoid biosynthesis; Iron; Metal-binding; Oxidoreductase; Vitamin C.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 335`	`335`	`Flavonol synthase/flavanone 3-hydroxylase.`	`PRO_0000067292`
`METAL`	`221 221`		`Iron (By similarity).`
`METAL`	`223 223`		`Iron (By similarity).`
`METAL`	`277 277`		`Iron (By similarity).`
`MUTAGEN`	`68 68`		`G->A: Reduces activity 95%.`
`MUTAGEN`	`68 68`		`G->P: Results in complete loss of activity.`
`MUTAGEN`	`207 207`		`P->G: No effect.`
`MUTAGEN`	`261 261`		`G->A: Reduces activity 95%.`
`MUTAGEN`	`261 261`		`G->P: Results in complete loss of activity.`

Sequence information

Length: 335 AA [This is the length of the unprocessed precursor]

Molecular weight: 37899 Da [This is the MW of the unprocessed precursor]

CRC64: 157E1AFA4C47564B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEVERVQAIA SLSHSNGTIP AEFIRPEKEQ PASTTYHGPA PEIPTIDLDD PVQDRLVRSI 

        70         80         90        100        110        120 
AEASREWGIF QVTNHGIPSD LICKLQAVGK EFFELPQEEK EVYSRPADAK DVQGYGTKLQ 

       130        140        150        160        170        180 
KEVEGKKSWV DHLFHRVWPP SSINYRFWPK NPPSYRAVNE EYAKYMREVV DKLFTYLSLG 

       190        200        210        220        230        240 
LGVEGGVLKE AAGGDDIEYM LKINYYPPCP RPDLALGVVA HTDLSALTVL VPNEVPGLQV 

       250        260        270        280        290        300 
FKDDRWIDAK YIPNALVIHI GDQIEILSNG KYKAVLHRTT VNKDKTRMSW PVFLEPPADT 

       310        320        330 
VVGPLPQLVD DENPPKYKAK KFKDYSYCKL NKLPQ

Q9ZWQ9 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