Dimethylaniline monooxygenase [N-oxide-forming] 2

Preferred order of sections

Names and origin

Protein names

Recommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 2
EC=1.14.13.8

Alternative name(s):
Dimethylaniline oxidase 2
FMO 1B1
Pulmonary flavin-containing monooxygenase 2
Short name=FMO 2

Gene names

Name:	FMO2
Synonyms:	FMO-2

Organism

Cavia porcellus (Guinea pig)

Taxonomic identifier

10141 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length	535 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 By similarity. Magnesium By similarity.
Subcellular location	Microsome membrane. Endoplasmic reticulum membrane.
Tissue specificity	Lung.
Polymorphism	There are two allelic forms (A and B).
Sequence similarities	Belongs to the FMO family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Domain	Transmembrane
Ligand	FAD Flavoprotein Magnesium NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation Isopeptide bond Ubl conjugation
Gene Ontology (GO)
Biological process	NADPH oxidation Inferred from sequence or structural similarity. Source: UniProtKB
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	NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide 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

Removed By similarity

Chain

2 – 535

534

Dimethylaniline monooxygenase [N-oxide-forming] 2

PRO_0000147644

Regions

Nucleotide binding

9 – 14

6

FAD Potential

Nucleotide binding

191 – 196

6

NADP Potential

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Cross-link

492

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity

Natural variations

Natural variant

522

1

V → L in B form.

Natural variant

530

1

S → F in B form.

Sequences

Sequence

Length

Mass (Da)

Tools

P36366 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 10D9DDA06EB58DA2
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FASTA

535

60,942

        10         20         30         40         50         60 
MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGL WRFKENVEDG RASIYKSVIT 

        70         80         90        100        110        120 
NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRLFAKKFDL LKYIQFQTTV LTVKKHPDFS 

       130        140        150        160        170        180 
SSGQWEVVTQ SDGKEQSAVF DAVMVCSGHH ILPHIPLKSF PGIERFKGQY FHSRQYKHPA 

       190        200        210        220        230        240 
GFEGKRILVI GIGNSASDIA SELSKNAAQV FISTRNGSWV MSRISEDGYP WDMVFHTRFK 

       250        260        270        280        290        300 
SMLRNILPRT VSKWMMEQQL NRWFNHANYS LEPKNKYLMK EPILNDDLPS RILYGAVKVK 

       310        320        330        340        350        360 
SRVTQLTETS ALFEDGTVEE DIDVIVFATG YTFSFPFLEE SLVKIEHNMV SLYKYMFPPQ 

       370        380        390        400        410        420 
LEKPTLTCMG LIQPLGSIFP TVELQARWAT RVFKGLCHLP SEKTMMEDII KRNEKRIDLF 

       430        440        450        460        470        480 
GESQSQIVQT NYVDYLDELA LEIGAKPDLI SFLLKDPELA VKLCFGPCNS YQYRLVGPGQ 

       490        500        510        520        530 
WEGARRAILT QKQRILKPLK TRSVKAAPNL SASFLMKILA LVAVFVAFFS QLYGF

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References

[1]

"Guinea pig or rabbit lung flavin-containing monooxygenases with distinct mobilities in SDS-PAGE are allelic variants that differ at only two positions."
Nikbakht K.N., Lawton M.P., Philpot R.M.
Pharmacogenetics 2:207-216(1992) [PubMed: 1306120] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Hartley.
Tissue: Lung.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L10037 Genomic DNA. Translation: AAB59631.1.
3D structure databases
ProteinModelPortal	P36366.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSCPOT00000014127; ENSCPOP00000012602; ENSCPOG00000013986.
Phylogenomic databases
eggNOG	roNOG08104.
GeneTree	ENSGT00550000074292.
HOVERGEN	HBG002037.
InParanoid	P36366.
OrthoDB	EOG48SGT0.
Family and domain databases
InterPro	IPR012143. DiMe-aniline_mOase. IPR000960. Flavin_mOase. IPR020946. Flavin_mOase-like. IPR002254. Flavin_mOase_2. [Graphical view]
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
PIRSF	PIRSF000332. FMO. 1 hit.
PRINTS	PR00370. FMOXYGENASE. PR01122. FMOXYGENASE2.
ProtoNet	Search...

Entry information

Entry name

FMO2_CAVPO

Accession

Primary (citable) accession number: P36366
Secondary accession number(s): Q05194

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families