NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Old Glory Red;
TISSUE=Corolla;
PubMed=10504566 [NCBI, ExPASy, EBI, Israel, Japan]
Brugliera F., Barri-Rewell G., Holton T.A., Mason J.G.;
"Isolation and characterization of a flavonoid 3'-hydroxylase cDNA clone corresponding to the Ht1 locus of Petunia hybrida.";
Plant J. 19:441-451(1999).

Comments

FUNCTION: Catalyzes the 3'-hydroxylation of the flavonoid B-ring to the 3',4'-hydroxylated state. Convert naringenin to eriodictyol and dihydrokaempferol to dihydroquercetin.
CATALYTIC ACTIVITY: A flavonoid + NADPH + O₂ = a 3'-hydroxyflavonoid + NADP⁺ + H₂O.
COFACTOR: Heme group (By similarity).
PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type III membrane protein (Potential).
TISSUE SPECIFICITY: High expression in petals and ovaries and to a lower extent in sepals, pedicels, anthers and stems. Not detected in leaves, style or roots.
DEVELOPMENTAL STAGE: High expression early in flower development and then declines as the corolla becomes fully pigmented and opened.
MISCELLANEOUS: May act as a membrane anchor for localization of other, soluble, flavonoid enzymes to the endoplasmic reticulum.
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

AF155332; AAD56282.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q9SBQ9.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0016711;	Molecular function: flavonoid 3'-monooxygenase 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: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

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.

ProtoNet

Q9SBQ9.

Other

UniRef

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

Keywords

Endoplasmic reticulum; Flavonoid biosynthesis; Heme; Iron; Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 512`	`512`	`Flavonoid 3'-monooxygenase.`	`PRO_0000052137`
`TRANSMEM`	`1 21`	`21`	`Potential.`
`TOPO_DOM`	`22 512`	`491`	`Cytoplasmic (Potential).`
`METAL`	`447 447`		`Iron (heme axial ligand) (By similarity).`

Sequence information

Length: 512 AA [This is the length of the unprocessed precursor]

Molecular weight: 56936 Da [This is the MW of the unprocessed precursor]

CRC64: 1843AC1BEB32BAE2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEILSLILYT VIFSFLLQFI LRSFFRKRYP LPLPPGPKPW PIIGNLVHLG PKPHQSTAAM 

        70         80         90        100        110        120 
AQTYGPLMYL KMGFVDVVVA ASASVAAQFL KTHDANFSSR PPNSGAEHMA YNYQDLVFAP 

       130        140        150        160        170        180 
YGPRWRMLRK ICSVHLFSTK ALDDFRHVRQ DEVKTLTRAL ASAGQKPVKL GQLLNVCTTN 

       190        200        210        220        230        240 
ALARVMLGKR VFADGSGDVD PQAAEFKSMV VEMMVVAGVF NIGDFIPQLN WLDIQGVAAK 

       250        260        270        280        290        300 
MKKLHARFDA FLTDILEEHK GKIFGEMKDL LSTLISLKND DADNDGGKLT DTEIKALLLN 

       310        320        330        340        350        360 
LFVAGTDTSS STVEWAIAEL IRNPKILAQA QQEIDKVVGR DRLVGELDLA QLTYLEAIVK 

       370        380        390        400        410        420 
ETFRLHPSTP LSLPRIASES CEINGYFIPK GSTLLLNVWA IARDPNAWAD PLEFRPERFL 

       430        440        450        460        470        480 
PGGEKPKVDV RGNDFEVIPF GAGRRICAGM NLGIRMVQLM IATLIHAFNW DLVSGQLPEM 

       490        500        510 
LNMEEAYGLT LQRADPLVVH PRPRLEAQAY IG

Q9SBQ9 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