[1]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISEASE. DOI=10.1101/gr.240202; PubMed=12466292 [NCBI, ExPASy, EBI, Israel, Japan] Lunden A., Marklund S., Gustafsson V., Andersson L.; "A nonsense mutation in the FMO3 gene underlies fishy off-flavor in cow's milk."; Genome Res. 12:1885-1888(2002).

Comments

FUNCTION: Involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. It N-oxygenates primary aliphatic alkylamines as well as secondary and tertiary amines. Acts on TMA to produce TMA-N-oxide.
CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O₂ = N,N-dimethylaniline N-oxide + NADP⁺ + H₂O.
COFACTOR: FAD (By similarity).
SUBCELLULAR LOCATION: Microsome membrane (By similarity). Endoplasmic reticulum membrane (By similarity).
DISEASE: Defects in FMO3 are the cause of a fishy off-flavor in cow milk due to by an elevated level of trimethylamine (TMA) in body fluids.
SIMILARITY: Belongs to the FMO 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

AF488422; AAN27919.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_776482.1; -.

UniGene

Bt.12519

3D structure databases

ModBase

Q8HYJ9.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0031227;	Cellular component: intrinsic to endoplasmic reticulum membrane (inferred from electronic annotation from InterPro).
GO:0005792;	Cellular component: microsome (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0004499;	Molecular function: flavin-containing monooxygenase activity (inferred from electronic annotation from InterPro).
GO:0050661;	Molecular function: NADP 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

IPR000759; Adrndx_reductase.
IPR012143; dManiline_mOase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000960; Flavin_mOase.
IPR002255; Flavin_mOase_3.
IPR001100; Pyr_nuc-diS_OxRdtase.
Graphical view of domain structure.

Pfam

PF00743; FMO-like; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000332; FMO; 1.

PRINTS

PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00370; FMOXYGENASE.
PR01123; FMOXYGENASE3.
PR00411; PNDRDTASEI.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

Genome annotation databases

Ensembl

ENSBTAG00000020597; Bos taurus. [Contig view]

GeneID

281167; -.

KEGG

bta:281167; -.

Phylogenomic databases

HOVERGEN

Q8HYJ9; -.

Other

ProtoNet

Q8HYJ9.

UniRef

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

Keywords

Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase; Transmembrane.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 532`	`532`	`Dimethylaniline monooxygenase [N-oxide-forming] 3.`	`PRO_0000147652`
`NP_BIND`	`9 14`	`6`	`FAD (Potential).`
`NP_BIND`	`191 196`	`6`	`NADP (Potential).`

Sequence information

Length: 532 AA [This is the length of the unprocessed precursor]

Molecular weight: 60093 Da [This is the MW of the unprocessed precursor]

CRC64: 2CA5964889490CBA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVKKVAIIGA GISGLASIRN CLEEGLEPTC FEKGEDIGGL WKFSDHVEEG RASIYRSVFT 

        70         80         90        100        110        120 
NSSKEMTCFP DFPFPDDFPN FMHNSKLQEY ITMFAKEKNL LKYIQFKTIV SSVNKRPDFQ 

       130        140        150        160        170        180 
TTGQWDVITE KDGKKESAVF DAVMICSGHH VYPNIPKESF PGIKLFKGKC FHSRDYKEPG 

       190        200        210        220        230        240 
IFKGKRVLVI GLGNSGCDIA SELSHIAEKV IISSRSGSWV MSRVWDEGYP WDMLFITRFE 

       250        260        270        280        290        300 
TFLKNTLPTV ISNWWYMKQM NARFKHENYG LMPLNSTLRK EPVFNDELPA CILCGIVTIK 

       310        320        330        340        350        360 
PNVKEFTEDS AIFEDGTVFK AIDYVIFATG YSYAYPFLDD SIIKSRDNEV TLFKGIFPPP 

       370        380        390        400        410        420 
LEKPTLAVIG LVQSLGAAIP TTDLQSRWAV QVIKGTCPLP SVKDMMNDID EKMGKKLKLF 

       430        440        450        460        470        480 
GKSDTIQTDY VVYMDELASF IGAKPNIPWL FLTDPKLALE VYFGPCTPYQ FRLVGPGKWP 

       490        500        510        520        530 
GARNAILTQW DRLLKPMTTR VVGSPLKPCL FCNWFRPVLI SVVSIAALIV LF

Q8HYJ9 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