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Protein

Dimethylaniline monooxygenase [N-oxide-forming] 2

Gene

Fmo2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides.By similarity

Catalytic activityi

N,N-dimethylaniline + NADPH + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.

Cofactori

Protein has several cofactor binding sites:

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 146FADSequence analysis
Nucleotide bindingi191 – 1966NADPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, Magnesium, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 2 (EC:1.14.13.8)
Alternative name(s):
Dimethylaniline oxidase 2
Pulmonary flavin-containing monooxygenase 2
Short name:
FMO 2
Gene namesi
Name:Fmo2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628600. Fmo2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 535534Dimethylaniline monooxygenase [N-oxide-forming] 2PRO_0000147651Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki492 – 492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiQ6IRI9.
PRIDEiQ6IRI9.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004762.

Structurei

3D structure databases

ProteinModelPortaliQ6IRI9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FMO family.Curated

Keywords - Domaini

Transmembrane

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiQ6IRI9.
KOiK00485.
PhylomeDBiQ6IRI9.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR012143. DiMe-aniline_mOase.
IPR023753. FAD/NAD-binding_dom.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002254. Flavin_mOase_2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01122. FMOXYGENASE2.
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6IRI9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKKVAVIGA GVSGLISLKG CVDEGLEPTC FERTEDIGGL WRFKENVEDG
60 70 80 90 100
RASIYHSVIT NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL
110 120 130 140 150
LKYIQFQTTV ISVKKRPDFA SSGQWDVYVQ SNGKEQRAVF DAVMVCSGHH
160 170 180 190 200
IQPHLPLKSF PGIERFQGQY FHSRQYKHPV GYEGKRILVV GIGNSAADIA
210 220 230 240 250
SELSKRAAQV FVSTRHGSWV LSRISEDGYP WDMVFHTRFS SMLRNVLPRT
260 270 280 290 300
VVKWMMERQM NRWFNHENYG LVPQNKYLMK EPVLNDDLPS RLLYGAIKVK
310 320 330 340 350
TRVKELTETA VVFEDGTVEE DVDVIVFATG YTFSFPFLED SLVKVEDNKV
360 370 380 390 400
SLYKAMFPPH LEKPTLACIG LIQPLGSIFP TVELQARWAT RVFKGVCRLP
410 420 430 440 450
SETTMMADIA ERNEKRIDLF GKSQSQILQT NYIDYLDELA LEIGAKPDFI
460 470 480 490 500
SLLFKDPKLA VKLYFGPCNS YQYRLVGPGQ WEGARNAILT QKQRILKPLK
510 520 530
TRTLQTSASA PVSFLIKVLG LLAIVLAFFF KLHGF
Length:535
Mass (Da):60,899
Last modified:January 23, 2007 - v3
Checksum:i4BDABD847733F639
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC070904 mRNA. Translation: AAH70904.1.
RefSeqiNP_653338.2. NM_144737.2.
UniGeneiRn.3928.

Genome annotation databases

GeneIDi246245.
KEGGirno:246245.
UCSCiRGD:628600. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC070904 mRNA. Translation: AAH70904.1.
RefSeqiNP_653338.2. NM_144737.2.
UniGeneiRn.3928.

3D structure databases

ProteinModelPortaliQ6IRI9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004762.

Proteomic databases

PaxDbiQ6IRI9.
PRIDEiQ6IRI9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi246245.
KEGGirno:246245.
UCSCiRGD:628600. rat.

Organism-specific databases

CTDi2327.
RGDi628600. Fmo2.

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiQ6IRI9.
KOiK00485.
PhylomeDBiQ6IRI9.

Miscellaneous databases

NextBioi623556.
PROiQ6IRI9.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR012143. DiMe-aniline_mOase.
IPR023753. FAD/NAD-binding_dom.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002254. Flavin_mOase_2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01122. FMOXYGENASE2.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.

Entry informationi

Entry nameiFMO2_RAT
AccessioniPrimary (citable) accession number: Q6IRI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.