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Protein

Dimethylaniline monooxygenase [N-oxide-forming] 2

Gene

FMO2

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

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

Enzyme and pathway databases

BRENDAi1.14.13.8. 1749.

Names & Taxonomyi

Protein namesi
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 namesi
Name:FMO2
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

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 methionineiRemoved1 Publication
Chaini2 – 535534Dimethylaniline monooxygenase [N-oxide-forming] 2PRO_0000147650Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Expressioni

Tissue specificityi

Lung.

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000004486.

Structurei

3D structure databases

ProteinModelPortaliP17635.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FMO family.Curated

Keywords - Domaini

Transmembrane

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiP17635.
KOiK00485.

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.

P17635-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGL WRFKENVEDG
60 70 80 90 100
RASIYQSVIT NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL
110 120 130 140 150
LKYIQFQTTV ISVKKRPDFA SSGQWEVVTQ SNSKQQSAVF DAVMVCSGHH
160 170 180 190 200
ILPNIPLKSF PGIEKFKGQY FHSRQYKHPA GLEGKRILVI GIGNSASDIA
210 220 230 240 250
VELSKKAAQV YISTRKGSWV MSRISEDGYP WDMVFHTRFS SMLRNVLPRM
260 270 280 290 300
IVKWMMEQQM NRWFNHENYG LAPENKYLMK EPVLNDDLPS RILYGTIKVK
310 320 330 340 350
RRVKELTESA AIFEDGTVEE DIDVIVFATG YTFAFPFLEE SLVKIEDNMV
360 370 380 390 400
SLYKYMFPPQ LEKSTFACLG LIQPLGSIFP TVELQARWAT RVFKGLCSLP
410 420 430 440 450
SKETMMADII KRNENRIALF GESLSQKLQT NYIDYLDELA LEIGAKPDLV
460 470 480 490 500
SFLFKDPKLA VKLYFGPCNS YQYRLVGPGQ WEGARNAIFT QKQRILKPLK
510 520 530
TRTLKASSNF PVSFLLKFLG LFALVLAFLF QLQWF
Length:535
Mass (Da):61,144
Last modified:January 23, 2007 - v3
Checksum:iD51910BDA41C55C2
GO

Polymorphismi

There are two allelic forms.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti120 – 1201A → S in PFMO-2 and PFMO-4.
Natural varianti136 – 1361Q → E in PFMO-2 and PFMO-4.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32029 mRNA. Translation: AAA31442.1.
PIRiB35182.
RefSeqiNP_001075753.1. NM_001082284.1.
UniGeneiOcu.1946.

Genome annotation databases

GeneIDi100009119.
KEGGiocu:100009119.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32029 mRNA. Translation: AAA31442.1.
PIRiB35182.
RefSeqiNP_001075753.1. NM_001082284.1.
UniGeneiOcu.1946.

3D structure databases

ProteinModelPortaliP17635.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000004486.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009119.
KEGGiocu:100009119.

Organism-specific databases

CTDi2327.

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiP17635.
KOiK00485.

Enzyme and pathway databases

BRENDAi1.14.13.8. 1749.

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...

Entry informationi

Entry nameiFMO2_RABIT
AccessioniPrimary (citable) accession number: P17635
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 120 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, Direct protein sequencing, 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.