[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Furnes B., Sommer S., Feng J., Schlenk D.; "Sequencing of pulmonary flavin-containing monooxygenase (FMO2) from gorilla."; Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides.
CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O₂ = N,N-dimethylaniline N-oxide + NADP⁺ + H₂O.
COFACTOR: FAD (By similarity).
COFACTOR: Magnesium (By similarity).
SUBCELLULAR LOCATION: Microsome membrane. Endoplasmic reticulum membrane.
SIMILARITY: Belongs to the FMO family.

Copyright

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Cross-references

Sequence databases

EMBL

AY132306; AAN06320.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY132299; AAN06320.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY132300; AAN06320.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY132301; AAN06320.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY132302; AAN06320.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY132303; AAN06320.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY132304; AAN06320.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY132305; AAN06320.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q8HZ69.

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:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
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

IPR012143; dManiline_mOase.
IPR000960; Flavin_mOase.
IPR002254; Flavin_mOase_2.
Graphical view of domain structure.

Pfam

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

PIRSF

PIRSF000332; FMO; 1.

PRINTS

PR00370; FMOXYGENASE.
PR01122; FMOXYGENASE2.

ProDom

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

Phylogenomic databases

HOVERGEN

Q8HZ69; -.

Other

ProtoNet

Q8HZ69.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 535`	`534`	`Dimethylaniline monooxygenase [N-oxide-forming] 2.`	`PRO_0000147645`
`NP_BIND`	`9 14`	`6`	`FAD (Potential).`
`NP_BIND`	`191 196`	`6`	`NADP (Potential).`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`

Sequence information

Length: 535 AA [This is the length of the unprocessed precursor]

Molecular weight: 60866 Da [This is the MW of the unprocessed precursor]

CRC64: B74F5608F5B51DD3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGV WRFKENVEDG RASIYQSVVT 

        70         80         90        100        110        120 
NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL LKYIQFQTTV LSVRKCPDFS 

       130        140        150        160        170        180 
SSGQWKVVTQ SNGKEQNAVF DAVMVCSGHH ILPHIPLKSF PGIERFKGQY FHSRQYKHPD 

       190        200        210        220        230        240 
GFEGKRILVI GMGNSGSDIA VELSKNAAQV FISTRHGTWV MSRISEDGYP WDAVFHTRFR 

       250        260        270        280        290        300 
SMLRNVLPRT AVKWMIEQQM NRWFNHENYG LEPQNKYIMK EPVLNDDVPS RLLCGAIKVK 

       310        320        330        340        350        360 
STVKELTETS AIFEDGTVEE NIDVIIFATG YSFSFPFLED SLVKVENNMV SLYKYIFPAH 

       370        380        390        400        410        420 
LDKSTLACIG LIQPLGSIFP TAELQARWVT RVFKGLCSLP SERTMMMDII KRNEKRIDLF 

       430        440        450        460        470        480 
GESQSQTLQT NYVDYLDELA LEIGAKPDFC SLLFKDPKLA VRLYFGPCNS YQYRLVGPGQ 

       490        500        510        520        530 
WEGARNAILT QKQRILKPLK TRALKDSSNF SVSFLLKILG LLAVVVAFFC QLQWS

Q8HZ69 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