NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
TISSUE=Leaf;
PubMed=10074715 [NCBI, ExPASy, EBI, Israel, Japan]
Saito K., Kobayashi M., Gong Z., Tanaka Y., Yamazaki M.;
"Direct evidence for anthocyanidin synthase as a 2-oxoglutarate-dependent oxygenase: molecular cloning and functional expression of cDNA from a red forma of Perilla frutescens.";
Plant J. 17:181-189(1999).

Comments

FUNCTION: Oxidation of leucoanthocyanidins into anthocyanidins.
CATALYTIC ACTIVITY: Leucocyanidin + 2-oxoglutarate + O₂ = cis- and trans-dihydroquercetins + succinate + CO₂ + H₂O.
COFACTOR: Binds 1 iron ion per subunit (By similarity).
COFACTOR: Binds 1 ascorbate molecule per subunit (By similarity).
PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis .
TISSUE SPECIFICITY: Expressed in red but not in green forma of P.frutescens. In red forma, it is predominantly expressed in stems and leaves, but not in roots.
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

AB003779; BAA20143.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q96323; 1GP5. [HSSP ENTRY / PDB]

SMR

O04274; 11-356.

ModBase

O04274.

Ontologies

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:0050589;	Molecular function: leucocyanidin oxygenase 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

O04274.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; Oxidoreductase; Vitamin C.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 362`	`362`	`Leucoanthocyanidin dioxygenase.`	`PRO_0000067302`
`ACT_SITE`	`304 304`		`Potential.`
`METAL`	`238 238`		`Iron (By similarity).`
`METAL`	`240 240`		`Iron (By similarity).`
`METAL`	`294 294`		`Iron (By similarity).`

Sequence information

Length: 362 AA [This is the length of the unprocessed precursor]

Molecular weight: 40826 Da [This is the MW of the unprocessed precursor]

CRC64: 7A03B4E86F91E1EA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVTSAMGPSP RVEELARSGL DTIPKDYVRP EEELKSIIGN ILAEEKSSEG PQLPTIDLEE 

        70         80         90        100        110        120 
MDSRDEEGRK KCHEELKKAA TDWGVMHLIN HGIPEELIDR VKAAGKEFFE LPVEEKEAYA 

       130        140        150        160        170        180 
NDQAAGNVQG YGSKLANNAS GQLEWEDYFF HCVYPEHKTD LSIWPTKPPD YIPATSEYAK 

       190        200        210        220        230        240 
QLRALATKIL SVLSIGLGLE KGRLEKEVGG AEDLIVQMKI NFYPKCPQPE LALGWEAHTD 

       250        260        270        280        290        300 
VSALTFILHN MVPGLQLFYE DKWVTAKCVP NSIIMHIGDT LEILSNGKYK SILHRGLVNK 

       310        320        330        340        350        360 
EKVRISWAVF CEPPKEKIVL QPLPETVSEV EPPRFPPRTF AQHLKHKLFR KTDGDLDEKP 


TY

O04274 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