[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Old Glory Blue; TISSUE=Petal; DOI=10.1038/366276a0; PubMed=8232589 [NCBI, ExPASy, EBI, Israel, Japan] Holton T.A., Brugliera F., Lester D.R., Tanaka Y., Hyland C.D., Menting J.G.T., Lu C.-Y., Farcy E., Stevenson T.W., Cornish E.C.; "Cloning and expression of cytochrome P450 genes controlling flower colour."; Nature 366:276-279(1993).
[2]	NUCLEOTIDE SEQUENCE. STRAIN=cv. Falcon Blue; TISSUE=Petal; Ohbayashi M., Shimada Y., Nakano R., Kiyokawa S., Kikuchi Y.; "Molecular cloning of cDNA encoding flavonoid-3',5'-hydroxylase from Petunia hybrida."; Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE. Hwang T.S., Chen Y.C., Wu R.Y.; "Cloning and sequencing of the genomic flavonoid 3',5'-hydroxylase (F3',5'Hase) gene from Petunia hybrida."; Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE. STRAIN=cv. Carnival violet; TISSUE=Petal; Baek S.H.; "Isolation and characterization of cytochrome P450 genes."; Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE OF 1-425. STRAIN=cv. Blue-star; TISSUE=Flower; Toguri T., Azuma M., Ohtani T.; "The cloning and characterization of a cDNA encoding a cytochrome P450 from the flowers of Petunia hybrida."; Plant Sci. 94:119-126(1993).

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.
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 .
SUBCELLULAR LOCATION: Microsome (Potential). Endoplasmic reticulum (By similarity).
TISSUE SPECIFICITY: Flowers.
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

Z22545; CAA80266.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D14588; BAA03438.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF081575; AAC32274.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY245545; AAO91941.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X71130; CAA50442.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S32110; S32110.
S38985; S38985.

3D structure databases

ModBase

P48418.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-12020; -.

Ontologies

GO:0005783;	Cellular component: endoplasmic reticulum (inferred from electronic annotation from UniProtKB-KW).
GO:0005792;	Cellular component: microsome (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0033772;	Molecular function: flavonoid 3',5'-hydroxylase activity (inferred from electronic annotation from EC).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
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

ProtoNet

P48418.

UniRef

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

Keywords

Endoplasmic reticulum; Heme; Iron; Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 506`	`506`	`Flavonoid 3',5'-hydroxylase 1.`	`PRO_0000052129`
`METAL`	`443 443`		`Iron (heme axial ligand) (By similarity).`

Sequence information

Length: 506 AA [This is the length of the unprocessed precursor]

Molecular weight: 56548 Da [This is the MW of the unprocessed precursor]

CRC64: FCF3F9623BD82B3E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMLLTELGAA TSIFLIAHII ISTLISKTTG RHLPPGPRGW PVIGALPLLG AMPHVSLAKM 

        70         80         90        100        110        120 
AKKYGAIMYL KVGTCGMAVA STPDAAKAFL KTLDINFSNR PPNAGATHLA YNAQDMVFAH 

       130        140        150        160        170        180 
YGPRWKLLRK LSNLHMLGGK ALENWANVRA NELGHMLKSM SDMSREGQRV VVAEMLTFAM 

       190        200        210        220        230        240 
ANMIGQVMLS KRVFVDKGVE VNEFKDMVVE LMTIAGYFNI GDFIPCLAWM DLQGIEKRMK 

       250        260        270        280        290        300 
RLHKKFDALL TKMFDEHKAT TYERKGKPDF LDVVMENGDN SEGERLSTTN IKALLLNLFT 

       310        320        330        340        350        360 
AGTDTSSSAI EWALAEMMKN PAILKKAQAE MDQVIGRNRR LLESDIPNLP YLRAICKETF 

       370        380        390        400        410        420 
RKHPSTPLNL PRISNEPCIV DGYYIPKNTR LSVNIWAIGR DPQVWENPLE FNPERFLSGR 

       430        440        450        460        470        480 
NSKIDPRGND FELIPFGAGR RICAGTRMGI VMVEYILGTL VHSFDWKLPS EVIELNMEEA 

       490        500 
FGLALQKAVP LEAMVTPRLQ LDVYVP

P48418 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