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Protein

Dimethylaniline monooxygenase [N-oxide-forming] 3

Gene

FMO3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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.1 Publication

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

ReactomeiR-BTA-217271. FMO oxidises nucleophiles.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 16

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Involvement in diseasei

Defects in FMO3 are the cause of a fishy off-flavor in cow milk due to by an elevated level of trimethylamine (TMA) in body fluids.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 532531Dimethylaniline monooxygenase [N-oxide-forming] 3PRO_0000147652Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8HYJ9.
PeptideAtlasiQ8HYJ9.
PRIDEiQ8HYJ9.

Expressioni

Gene expression databases

BgeeiENSBTAG00000020597.
ExpressionAtlasiQ8HYJ9. baseline.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000027444.

Structurei

3D structure databases

ProteinModelPortaliQ8HYJ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FMO family.Curated

Keywords - Domaini

Transmembrane

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
GeneTreeiENSGT00760000119232.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiQ8HYJ9.
KOiK00485.
OMAiQVIKGTC.
OrthoDBiEOG091G0465.
TreeFamiTF105285.

Family and domain databases

Gene3Di3.50.50.60. 4 hits.
InterProiIPR012143. DiMe-aniline_mOase.
IPR023753. FAD/NAD-binding_dom.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002255. Flavin_mOase_3.
[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.

Q8HYJ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKKVAIIGA GISGLASIRN CLEEGLEPTC FEKGEDIGGL WKFSDHVEEG
60 70 80 90 100
RASIYRSVFT NSSKEMTCFP DFPFPDDFPN FMHNSKLQEY ITMFAKEKNL
110 120 130 140 150
LKYIQFKTIV SSVNKRPDFQ TTGQWDVITE KDGKKESAVF DAVMICSGHH
160 170 180 190 200
VYPNIPKESF PGIKLFKGKC FHSRDYKEPG IFKGKRVLVI GLGNSGCDIA
210 220 230 240 250
SELSHIAEKV IISSRSGSWV MSRVWDEGYP WDMLFITRFE TFLKNTLPTV
260 270 280 290 300
ISNWWYMKQM NARFKHENYG LMPLNSTLRK EPVFNDELPA CILCGIVTIK
310 320 330 340 350
PNVKEFTEDS AIFEDGTVFK AIDYVIFATG YSYAYPFLDD SIIKSRDNEV
360 370 380 390 400
TLFKGIFPPP LEKPTLAVIG LVQSLGAAIP TTDLQSRWAV QVIKGTCPLP
410 420 430 440 450
SVKDMMNDID EKMGKKLKLF GKSDTIQTDY VVYMDELASF IGAKPNIPWL
460 470 480 490 500
FLTDPKLALE VYFGPCTPYQ FRLVGPGKWP GARNAILTQW DRLLKPMTTR
510 520 530
VVGSPLKPCL FCNWFRPVLI SVVSIAALIV LF
Length:532
Mass (Da):60,093
Last modified:March 1, 2003 - v1
Checksum:i2CA5964889490CBA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF488422 mRNA. Translation: AAN27919.1.
RefSeqiNP_776482.1. NM_174057.2.
UniGeneiBt.12519.

Genome annotation databases

EnsembliENSBTAT00000027444; ENSBTAP00000027444; ENSBTAG00000020597.
GeneIDi281167.
KEGGibta:281167.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF488422 mRNA. Translation: AAN27919.1.
RefSeqiNP_776482.1. NM_174057.2.
UniGeneiBt.12519.

3D structure databases

ProteinModelPortaliQ8HYJ9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000027444.

Proteomic databases

PaxDbiQ8HYJ9.
PeptideAtlasiQ8HYJ9.
PRIDEiQ8HYJ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000027444; ENSBTAP00000027444; ENSBTAG00000020597.
GeneIDi281167.
KEGGibta:281167.

Organism-specific databases

CTDi2328.

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
GeneTreeiENSGT00760000119232.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiQ8HYJ9.
KOiK00485.
OMAiQVIKGTC.
OrthoDBiEOG091G0465.
TreeFamiTF105285.

Enzyme and pathway databases

ReactomeiR-BTA-217271. FMO oxidises nucleophiles.

Gene expression databases

BgeeiENSBTAG00000020597.
ExpressionAtlasiQ8HYJ9. baseline.

Family and domain databases

Gene3Di3.50.50.60. 4 hits.
InterProiIPR012143. DiMe-aniline_mOase.
IPR023753. FAD/NAD-binding_dom.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002255. Flavin_mOase_3.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01123. FMOXYGENASE3.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiFMO3_BOVIN
AccessioniPrimary (citable) accession number: Q8HYJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: March 1, 2003
Last modified: September 7, 2016
This is version 91 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.