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Protein

Dimethylaniline monooxygenase [N-oxide-forming] 3

Gene

Fmo3

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

Functioni

Involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. It N-oxygenates primary aliphatic alkylamines as well as secondary and tertiary amines. Acts on TMA to produce TMA-N-oxide. Has activities of methimazole S-oxidation and NADPH oxidation associated with the N- or S-oxidation of trimethylamine and thioacetamide.

Catalytic activityi

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

Cofactori

FADBy similarity

Regions

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

GO - Molecular functioni

  • amino acid binding Source: RGD
  • flavin adenine dinucleotide binding Source: InterPro
  • monooxygenase activity Source: RGD
  • N,N-dimethylaniline monooxygenase activity Source: RGD
  • NADP binding Source: RGD
  • trimethylamine monooxygenase activity Source: UniProtKB-EC

GO - Biological processi

  • drug metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.14.13.8. 5301.
SABIO-RKQ9EQ76.

Names & Taxonomyi

Protein namesi
Recommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 3 (EC:1.14.13.8)
Alternative name(s):
Dimethylaniline oxidase 3
Hepatic flavin-containing monooxygenase 3
Short name:
FMO 3
Trimethylamine monooxygenase (EC:1.14.13.148)
Gene namesi
Name:Fmo3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619761. Fmo3.

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 – 531530Dimethylaniline monooxygenase [N-oxide-forming] 3PRO_0000147659Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei401 – 4011PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9EQ76.
PRIDEiQ9EQ76.

PTM databases

iPTMnetiQ9EQ76.

Expressioni

Tissue specificityi

Expressed in kidney and liver. Weakly expressed in lung. Does not seem to be expressed in brain, adipose tissue, or muscle.1 Publication

Interactioni

Protein-protein interaction databases

MINTiMINT-4578889.
STRINGi10116.ENSRNOP00000004864.

Structurei

3D structure databases

ProteinModelPortaliQ9EQ76.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FMO family.Curated

Keywords - Domaini

Transmembrane

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiQ9EQ76.
KOiK00485.
OrthoDBiEOG7GXPB6.
PhylomeDBiQ9EQ76.
TreeFamiTF105285.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
3.50.50.60. 2 hits.
InterProiIPR012143. DiMe-aniline_mOase.
IPR023753. FAD/NAD-binding_dom.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002255. Flavin_mOase_3.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01123. FMOXYGENASE3.
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

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

Q9EQ76-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRKVAVIGA GVSGLAAIRS CLEEGLEPTC FERSDDVGGL WKFSDHTEEG
60 70 80 90 100
RASIYQSVFT NSSKEMMCFP DFPYPDDFPN FMHNSKLQEY ITSFATEKNL
110 120 130 140 150
LKYIQFETLV TRINKCPDFS TTGKWEVTTE KNSKKETAVF DAVMICSGHH
160 170 180 190 200
VYPHLPKDSF PGLNRFKGKC FHSRDYKEPG TWKGKRVLVI GLGNSGCDIA
210 220 230 240 250
AELSHVAQQV IISSRSGSWV MSRVWNDGYP WDMVVITRFQ TFLKNNLPTA
260 270 280 290 300
ISDWWYMKQM NARFKHENYG LMPLNGTLRK EPVFNDELPA RILCGTVSIK
310 320 330 340 350
PNVKEFTETS AVFEDGTVFE GIDCVIFATG YGYAYPFLDD SIIKSRNNEV
360 370 380 390 400
TLYKGIFPPQ LEKPTMAVIG LVQSLGAAIP TTDLQARWAA QVIRGTCILP
410 420 430 440 450
SVNDMMDDID EKMGKKLKWF GNSTTIQTDY IVYMDELASF IGAKPNILWL
460 470 480 490 500
FLKDPRLAIE VFFGPCSPYQ FRLVGPGKWS GARNAILTQW DRSLKPMKTR
510 520 530
VVGGIQKPCL YSHFLRLLAV PVLIALFLVL I
Length:531
Mass (Da):59,960
Last modified:March 1, 2001 - v1
Checksum:i35A89988323B311F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti501 – 5011V → D in AAH87008 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF286595 mRNA. Translation: AAG44891.1.
BC087008 mRNA. Translation: AAH87008.1.
RefSeqiNP_445885.2. NM_053433.2.
UniGeneiRn.163228.

Genome annotation databases

GeneIDi84493.
KEGGirno:84493.
UCSCiRGD:619761. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF286595 mRNA. Translation: AAG44891.1.
BC087008 mRNA. Translation: AAH87008.1.
RefSeqiNP_445885.2. NM_053433.2.
UniGeneiRn.163228.

3D structure databases

ProteinModelPortaliQ9EQ76.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4578889.
STRINGi10116.ENSRNOP00000004864.

PTM databases

iPTMnetiQ9EQ76.

Proteomic databases

PaxDbiQ9EQ76.
PRIDEiQ9EQ76.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi84493.
KEGGirno:84493.
UCSCiRGD:619761. rat.

Organism-specific databases

CTDi2328.
RGDi619761. Fmo3.

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiQ9EQ76.
KOiK00485.
OrthoDBiEOG7GXPB6.
PhylomeDBiQ9EQ76.
TreeFamiTF105285.

Enzyme and pathway databases

BRENDAi1.14.13.8. 5301.
SABIO-RKQ9EQ76.

Miscellaneous databases

PROiQ9EQ76.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
3.50.50.60. 2 hits.
InterProiIPR012143. DiMe-aniline_mOase.
IPR023753. FAD/NAD-binding_dom.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002255. Flavin_mOase_3.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01123. FMOXYGENASE3.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing, tissue distribution, and heterologous expression of rat flavin-containing monooxygenase 3."
    Lattard V., Buronfosse T., Lachuer J., Longin-Sauvageon C., Moulin C., Benoit E.
    Arch. Biochem. Biophys. 391:30-40(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
  2. "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: Kidney.

Entry informationi

Entry nameiFMO3_RAT
AccessioniPrimary (citable) accession number: Q9EQ76
Secondary accession number(s): Q5PQV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 106 of the entry and version 1 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.