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Protein

Dimethylaniline monooxygenase [N-oxide-forming] 1

Gene

Fmo1

Organism
Rattus norvegicus (Rat)
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. Form I catalyzes the N-oxygenation of secondary and tertiary amines.

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei208 – 2081Important for substrate bindingBy similarity

Regions

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

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: InterPro
  • monooxygenase activity Source: RGD
  • N,N-dimethylaniline monooxygenase activity Source: RGD
  • NADP binding Source: InterPro

GO - Biological processi

  • drug metabolic process Source: Ensembl
  • NADPH oxidation Source: Ensembl
  • organic acid metabolic process Source: Ensembl
  • response to lipopolysaccharide Source: RGD
  • response to osmotic stress Source: RGD
  • toxin metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.14.13.8. 5301.
ReactomeiR-RNO-217271. FMO oxidises nucleophiles.
SABIO-RKP36365.

Names & Taxonomyi

Protein namesi
Recommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 1 (EC:1.14.13.8)
Alternative name(s):
Dimethylaniline oxidase 1
Hepatic flavin-containing monooxygenase 1
Short name:
FMO 1
Gene namesi
Name:Fmo1
Synonyms:Fmo-1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi2622. Fmo1.

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 – 532531Dimethylaniline monooxygenase [N-oxide-forming] 1PRO_0000147643Add
BLAST

Proteomic databases

PaxDbiP36365.
PRIDEiP36365.

PTM databases

iPTMnetiP36365.
PhosphoSiteiP36365.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiENSRNOG00000034191.
GenevisibleiP36365. RN.

Interactioni

Protein-protein interaction databases

MINTiMINT-4580076.
STRINGi10116.ENSRNOP00000044613.

Structurei

3D structure databases

ProteinModelPortaliP36365.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FMO family.Curated

Keywords - Domaini

Transmembrane

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
GeneTreeiENSGT00760000119232.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiP36365.
KOiK00485.
OMAiPSVMIEE.
PhylomeDBiP36365.
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.
IPR002253. Flavin_mOase_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01121. FMOXYGENASE1.
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

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

P36365-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSCDLGGL WRFTEHVEEG
60 70 80 90 100
RASLYNSVVS NSSKEMSCYS DFPFPEDYPN FVPNSLFLEY LQLYATQFNL
110 120 130 140 150
LRCIYFNTKV CSITKRPDFA VSGQWEVVTV CQGKQSSDTF DAVMVCTGFL
160 170 180 190 200
TNPHLPLDSF PGIQTFKGQY FHSRQYKHPD VFKDKRVLVV GMGNSGTDIA
210 220 230 240 250
VEASHLAKKV FLSTTGGAWV ISRVFDSGYP WDMIFMTRFQ NMLRNLLPTP
260 270 280 290 300
VVSWLISKKM NSWFNHVNYG VAPEDRTQLR EPVLNDELPG RIITGKVLIK
310 320 330 340 350
PSIKEVKENS VVFNNTPKEE PIDVIVFATG YSFAFPFLDE SIVKVEDGQA
360 370 380 390 400
SLYKYIFPAH LPKPTLAVIG LIKPLGSMIP TGETQARWVV QVLKGATTLP
410 420 430 440 450
PPSVMMKEVN ERKKNKHSGF GLCYCKALQS DYITYIDDLL TSINAKPDLR
460 470 480 490 500
AMLLTDPRLA LSIFFGPCTP YHFRLTGPGK WEGARKAILT QWDRTVNVTK
510 520 530
TRTVQETPST FETLLKLFSF LALLVAVFFI FL
Length:532
Mass (Da):59,825
Last modified:October 25, 2005 - v2
Checksum:i188EABAF96653977
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411D → A in AAA41165 (PubMed:8504165).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84719 mRNA. Translation: AAA41165.1.
BC061567 mRNA. Translation: AAH61567.1.
PIRiS33758.
RefSeqiNP_036924.1. NM_012792.1.
XP_006250207.1. XM_006250145.2.
XP_006250208.1. XM_006250146.2.
UniGeneiRn.867.

Genome annotation databases

EnsembliENSRNOT00000041908; ENSRNOP00000044613; ENSRNOG00000034191.
ENSRNOT00000081551; ENSRNOP00000073105; ENSRNOG00000034191.
GeneIDi25256.
KEGGirno:25256.
UCSCiRGD:2622. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84719 mRNA. Translation: AAA41165.1.
BC061567 mRNA. Translation: AAH61567.1.
PIRiS33758.
RefSeqiNP_036924.1. NM_012792.1.
XP_006250207.1. XM_006250145.2.
XP_006250208.1. XM_006250146.2.
UniGeneiRn.867.

3D structure databases

ProteinModelPortaliP36365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4580076.
STRINGi10116.ENSRNOP00000044613.

PTM databases

iPTMnetiP36365.
PhosphoSiteiP36365.

Proteomic databases

PaxDbiP36365.
PRIDEiP36365.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000041908; ENSRNOP00000044613; ENSRNOG00000034191.
ENSRNOT00000081551; ENSRNOP00000073105; ENSRNOG00000034191.
GeneIDi25256.
KEGGirno:25256.
UCSCiRGD:2622. rat.

Organism-specific databases

CTDi2326.
RGDi2622. Fmo1.

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
GeneTreeiENSGT00760000119232.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiP36365.
KOiK00485.
OMAiPSVMIEE.
PhylomeDBiP36365.
TreeFamiTF105285.

Enzyme and pathway databases

BRENDAi1.14.13.8. 5301.
ReactomeiR-RNO-217271. FMO oxidises nucleophiles.
SABIO-RKP36365.

Miscellaneous databases

PROiP36365.

Gene expression databases

BgeeiENSRNOG00000034191.
GenevisibleiP36365. RN.

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.
IPR002253. Flavin_mOase_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01121. FMOXYGENASE1.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiFMO1_RAT
AccessioniPrimary (citable) accession number: P36365
Secondary accession number(s): Q6P7Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 25, 2005
Last modified: September 7, 2016
This is version 127 of the entry and version 2 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.