Reviewed, UniProtKB/Swiss-Prot P16549 (FMO1_PIG)

Names and origin

Protein names

Recommended name:
    Dimethylaniline monooxygenase [N-oxide-forming] 1
    EC=1.14.13.8
Alternative name(s):
    Hepatic flavin-containing monooxygenase 1
      Short name=FMO 1
    Dimethylaniline oxidase 1

Gene names

Name:	FMO1
Synonyms:	FMO-1

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	532 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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.
Subcellular location	Microsome membrane. Endoplasmic reticulum membrane.
Tissue specificity	Liver.
Sequence similarities	Belongs to the FMO family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro microsome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro flavin-containing monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 532	531	Dimethylaniline monooxygenase [N-oxide-forming] 1		PRO_0000147641
Regions
	Nucleotide binding	9 – 14	6	FAD Potential
	Nucleotide binding	191 – 196	6	NADP Potential
Sites
	Site	208	1	Important for substrate binding
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.2
	Glycosylation	120	1	N-linked (GlcNAc...) (high mannose) Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P16549-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 5E475E7F2F3B8A67	FASTA	532	59,952
	10 20 30 40 50 60 MAKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSDDLGGL WRFTEHVEEG RASLYKSVVS 70 80 90 100 110 120 NSCKEMSCYP DFPFPEDYPN YVPNSHFLEY LRMYANQFNL LKCIQFKTKV CSVTKHEDFN 130 140 150 160 170 180 TTGQWDVVTL CEGKQESAVF DAVMVCTGFL TNPYLPLDSF PGINTFKGQY FHSRQYKHPD 190 200 210 220 230 240 IFKDKSVLVV GMGNSGTDIA VEASHLAKKV FLSTTGGAWV ISRVFDSGYP WDMVFMTRFQ 250 260 270 280 290 300 NMFRNSLPTP IVNWLIAKKM NSWFNHANYG LIPEDRIQLR EPVLNDELPG RIITGKVLIK 310 320 330 340 350 360 PSIKEVKENS VVFNSSPEEE PIDIIVFATG YTFAFPFLDE SVVKVEDGQA SLYKYIFPAH 370 380 390 400 410 420 LQKPTLAVIG LIKPLGSLLP TGDTQARWAV RVLKGVNKLP PSSVMIQEVN TRKENKPSGF 430 440 450 460 470 480 GLCYCKALQS DYIAYIDELL TYIDAKPNMF SLLLTDPHLA LTIFFGPCTP YQFRLTGPGK 490 500 510 520 530 WEGARNAIMT QWDRTFKVTK TRIVKESPSP FASLLKLFSF LALLVAIFQI FL

References

[1]	"The flavin-containing monooxygenase expressed in pig liver: primary sequence, distribution, and evidence for a single gene." Gasser R., Tynes R.E., Lawton M.P., Korsmeyer K.K., Ziegler D.M., Philpot R.M. Biochemistry 29:119-124(1990) [PubMed: 2322534] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 137-151 AND 309-318. Tissue: Liver.
[2]	"N-terminus determination: FAD and NADP binding domain mapping of hog liver flavin-containing monooxygenase by tandem mass spectrometry." Guan S.H., Falick A.M., Cashman J.R. Biochem. Biophys. Res. Commun. 170:937-943(1990) [PubMed: 2383273] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-14 AND 185-202, ACETYLATION AT ALA-2. Tissue: Liver.
[3]	"An essential lysyl residue (Lys208) in the substrate-binding site of porcine FAD-containing monooxygenase." Wu R.-F., Ichikawa Y. Eur. J. Biochem. 229:749-753(1995) [PubMed: 7758472] [Abstract] Cited for: PROTEIN SEQUENCE OF 186-208. Tissue: Liver.
[4]	"N-glycosylation of pig flavin-containing monooxygenase form 1: determination of the site of protein modification by mass spectrometry." Korsmeyer K.K., Guan S., Yang Z.C., Falick A.M., Ziegler D.M., Cashman J.R. Chem. Res. Toxicol. 11:1145-1153(1998) [PubMed: 9778310] [Abstract] Cited for: GLYCOSYLATION AT ASN-120.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M32031 mRNA. Translation: AAA31033.1.
PIR	A33768.
RefSeq	NP_999229.1.
UniGene	Ssc.229
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	397132.
KEGG	ssc:397132.
Phylogenomic databases
HOVERGEN	P16549.
Enzyme and pathway databases
BRENDA	1.14.13.8. 249.
Family and domain databases
InterPro	IPR012143. dManiline_mOase. IPR000960. Flavin_mOase. IPR002253. Flavin_mOase_1. [Graphical view]
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
PIRSF	PIRSF000332. FMO. 1 hit.
PRINTS	PR00370. FMOXYGENASE. PR01121. FMOXYGENASE1.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

FMO1_PIG

Accession

Primary (citable) accession number: P16549

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 83 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)