NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Petal;
PubMed=8819318 [NCBI, ExPASy, EBI, Israel, Japan]
Tanaka Y., Yonekura K., Fukuchi-Mizutani M., Fukui Y., Fujiwara H., Ashikari T., Kusumi T.;
"Molecular and biochemical characterization of three anthocyanin synthetic enzymes from Gentiana triflora.";
Plant Cell Physiol. 37:711-716(1996).

Comments

FUNCTION: Catalyzes the 3'5'-hydroxylation of naringenin and eriodictyol to form 5,7,3,'4',5'-pentahydroxyflavanone and 3',5'-hydroxylation of dihydrokaempferol and dihydroquercetin to form dihydromyricetin (By similarity).
CATALYTIC ACTIVITY: A flavanone + NADPH + O₂ = a 3'-hydroxyflavanone + NADP⁺ + H₂O.
CATALYTIC ACTIVITY: A 3'-hydroxyflavanone + NADPH + O₂ = a 3',5'-dihydroxyflavanone + NADP⁺ + H₂O.
COFACTOR: Heme group (By similarity).
PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis .
SIMILARITY: Belongs to the cytochrome P450 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

D85184; BAA12735.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q96581.

Ontologies

GO:0033772;	Molecular function: flavonoid 3',5'-hydroxylase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001128; Cyt_P450.
IPR002401; Cyt_P450_E_grp-I.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.630.10; Cyt_P450; 1.

PANTHER

PTHR19383; Cyt_P450; 1.

Pfam

PF00067; p450; 1.
Pfam graphical view of domain structure.

PRINTS

PR00463; EP450I.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.

Other

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

Keywords

Heme; Iron; Metal-binding; Monooxygenase; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 516`	`516`	`Flavonoid 3',5'-hydroxylase.`	`PRO_0000052132`
`METAL`	`453 453`		`Iron (heme axial ligand) (By similarity).`

Sequence information

Length: 516 AA [This is the length of the unprocessed precursor]

Molecular weight: 58088 Da [This is the MW of the unprocessed precursor]

CRC64: 148259BB35743731 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSPIYTTLTL HLATALFLFF HVQKLVHYLH GKATGHRCRR LPPGPTGWPI LGALPLLGNM 

        70         80         90        100        110        120 
PHVTFANMAK KYGSVMYLKV GSHGLAIAST PDAAKAFLKT LDLNFSNRPP NAGATHLAYN 

       130        140        150        160        170        180 
AQDMVFAHYG PKWKLLRKLS NLHMLGGKAL ENWADVRKTE LGYMLKAMFE SSQNNEPVMI 

       190        200        210        220        230        240 
SEMLTYAMAN MLSQVILSRR VFNKKGAKSN EFKDMVVELM TSAGYFNIGD FIPSIGWMDL 

       250        260        270        280        290        300 
QGIEGGMKRL HKKFDVLLTR LLDDHKRTSQ ERKQKPDFLD FVIANGDNSD GERLNTDNIK 

       310        320        330        340        350        360 
ALLLNLFTAG TDTSSSIIEW ALAELLKNRT LLTRAQDEMD RVIGRDRRLL ESDIPNLPYL 

       370        380        390        400        410        420 
QAICKETFRK HPSTPLNLPR NCIRGHVDVN GYYIPKGTRL NVNIWAIGRD PSVWGDNPNE 

       430        440        450        460        470        480 
FDPERFLYGR NAKIDPRGNH FELIPFGAGR RICAGTRMGI LLVEYILGTL VHSFDWKLGF 

       490        500        510 
SEDELNMDET FGLALQKAVP LAAMVIPRLP LHVYAP

Q96581 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