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Protein

Dimethylaniline monooxygenase [N-oxide-forming] 1

Gene

FMO1

Organism
Sus scrofa (Pig)
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

Sites

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

Regions

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

GO - Molecular functioni

GO - Biological processi

  • drug metabolic process Source: Ensembl
  • NADPH oxidation Source: BHF-UCL
  • organic acid metabolic process Source: BHF-UCL
  • toxin metabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

ReactomeiR-SSC-217271. FMO oxidises nucleophiles.
SABIO-RKP16549.

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 9

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 – 532531Dimethylaniline monooxygenase [N-oxide-forming] 1PRO_0000147641Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Glycosylationi120 – 1201N-linked (GlcNAc...) (high mannose)1 Publication

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

PaxDbiP16549.
PeptideAtlasiP16549.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiENSSSCG00000015268.
GenevisibleiP16549. SS.

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000016191.

Structurei

3D structure databases

ProteinModelPortaliP16549.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FMO family.Curated

Keywords - Domaini

Transmembrane

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
GeneTreeiENSGT00760000119232.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiP16549.
KOiK00485.
OMAiPSVMIEE.
OrthoDBiEOG091G0465.
TreeFamiTF105285.

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.
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. 3 hits.

Sequencei

Sequence statusi: Complete.

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

P16549-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSDDLGGL WRFTEHVEEG
60 70 80 90 100
RASLYKSVVS NSCKEMSCYP DFPFPEDYPN YVPNSHFLEY LRMYANQFNL
110 120 130 140 150
LKCIQFKTKV CSVTKHEDFN TTGQWDVVTL CEGKQESAVF DAVMVCTGFL
160 170 180 190 200
TNPYLPLDSF PGINTFKGQY FHSRQYKHPD IFKDKSVLVV GMGNSGTDIA
210 220 230 240 250
VEASHLAKKV FLSTTGGAWV ISRVFDSGYP WDMVFMTRFQ NMFRNSLPTP
260 270 280 290 300
IVNWLIAKKM NSWFNHANYG LIPEDRIQLR EPVLNDELPG RIITGKVLIK
310 320 330 340 350
PSIKEVKENS VVFNSSPEEE PIDIIVFATG YTFAFPFLDE SVVKVEDGQA
360 370 380 390 400
SLYKYIFPAH LQKPTLAVIG LIKPLGSLLP TGDTQARWAV RVLKGVNKLP
410 420 430 440 450
PSSVMIQEVN TRKENKPSGF GLCYCKALQS DYIAYIDELL TYIDAKPNMF
460 470 480 490 500
SLLLTDPHLA LTIFFGPCTP YQFRLTGPGK WEGARNAIMT QWDRTFKVTK
510 520 530
TRIVKESPSP FASLLKLFSF LALLVAIFQI FL
Length:532
Mass (Da):59,952
Last modified:January 23, 2007 - v3
Checksum:i5E475E7F2F3B8A67
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32031 mRNA. Translation: AAA31033.1.
PIRiA33768.
RefSeqiNP_999229.1. NM_214064.1.
XP_005656702.1. XM_005656645.2.
UniGeneiSsc.229.

Genome annotation databases

EnsembliENSSSCT00000016637; ENSSSCP00000016191; ENSSSCG00000015268.
GeneIDi397132.
KEGGissc:397132.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32031 mRNA. Translation: AAA31033.1.
PIRiA33768.
RefSeqiNP_999229.1. NM_214064.1.
XP_005656702.1. XM_005656645.2.
UniGeneiSsc.229.

3D structure databases

ProteinModelPortaliP16549.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000016191.

Proteomic databases

PaxDbiP16549.
PeptideAtlasiP16549.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000016637; ENSSSCP00000016191; ENSSSCG00000015268.
GeneIDi397132.
KEGGissc:397132.

Organism-specific databases

CTDi2326.

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
GeneTreeiENSGT00760000119232.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiP16549.
KOiK00485.
OMAiPSVMIEE.
OrthoDBiEOG091G0465.
TreeFamiTF105285.

Enzyme and pathway databases

ReactomeiR-SSC-217271. FMO oxidises nucleophiles.
SABIO-RKP16549.

Gene expression databases

BgeeiENSSSCG00000015268.
GenevisibleiP16549. SS.

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.
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. 3 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiFMO1_PIG
AccessioniPrimary (citable) accession number: P16549
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 129 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.