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Protein

Dimethylaniline monooxygenase [N-oxide-forming] 3

Gene

FMO3

Organism
Oryctolagus cuniculus (Rabbit)
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.

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi9 – 14FADSequence analysis6
Nucleotide bindingi191 – 196NADPSequence analysis6

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.14.13.148. 1749.

Names & Taxonomyi

Protein namesi
Recommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 3 (EC:1.14.13.8)
Alternative name(s):
Dimethylaniline oxidase 3
FMO 1D1
FMO II
FMO form 2
Hepatic flavin-containing monooxygenase 3
Short name:
FMO 3
Trimethylamine monooxygenase (EC:1.14.13.148)
Gene namesi
Name:FMO3
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Chromosome 13

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001476582 – 531Dimethylaniline monooxygenase [N-oxide-forming] 3Add BLAST530

Proteomic databases

PRIDEiP32417.

Expressioni

Tissue specificityi

Liver.

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000003129.

Structurei

3D structure databases

ProteinModelPortaliP32417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FMO family.Curated

Keywords - Domaini

Transmembrane

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
GeneTreeiENSGT00760000119232.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiP32417.
KOiK00485.
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.

P32417-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKKVAIIGA GISGLASIRS CLEEGLEPTC FEMSDDIGGL WKFSDHAEEG
60 70 80 90 100
RASIYQSVFT NSSKEMMCFP DFPFPDDFPN FMHNSKLQEY ITTFAREKNL
110 120 130 140 150
LKYIQFKTLV SSIKKHPDFS VTGQWYVSTE RNGKKETAVF DAVMICSGHH
160 170 180 190 200
VYPNLPKDSF PGLKHFKGKS FHSREYKEPG IFKGKRVLVI GLGNSGCDIA
210 220 230 240 250
TELSHTAEQV VISSRSGSWV MSRVWDDGYP WDMLYVTRFQ TFLKNNLPTA
260 270 280 290 300
ISDWWYVKQM NAKFKHENYS LMPLNGTLRK EPVFNDDLPA RILCGTVSIK
310 320 330 340 350
PNVKEFTETS AIFEDGTVFE AIDSVIFATG YGYAYPFLDD SIIKSENNKV
360 370 380 390 400
TLFKGIFPPQ LEKPTMAVIG LVQSLGAAIP TTDLQARWAA QVIKGTCTLP
410 420 430 440 450
PVKDMMNDIH EKMGTKLKWF GKSETIQTDY INYMDELASF IGVKLNIPWL
460 470 480 490 500
FLTDPRLALE VFFGPCSPYQ FRLVGPGKWP GARQAILTQW DRSLKPMKTR
510 520 530
AVGHLQKPAL FSPWLKLLAI AVLLIAAVLV F
Length:531
Mass (Da):59,815
Last modified:January 23, 2007 - v3
Checksum:iA4505481077C6CC8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti76D → P AA sequence (PubMed:1898080).Curated1
Sequence conflicti81F → N AA sequence (PubMed:1898080).Curated1
Sequence conflicti128 – 130STE → ATC AA sequence (PubMed:1898080).Curated3
Sequence conflicti172 – 173HS → RQ AA sequence (PubMed:1898080).Curated2
Sequence conflicti197C → E AA sequence (PubMed:1898080).Curated1
Sequence conflicti306F → FKEF AA sequence (PubMed:1898080).Curated1
Sequence conflicti419W → T AA sequence (PubMed:1898080).Curated1
Sequence conflicti423S → W AA sequence (PubMed:1898080).Curated1
Sequence conflicti514 – 516WLK → ELW AA sequence (PubMed:1898080).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti279R → M.1
Natural varianti405M → V.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10391 mRNA. Translation: AAA21178.1.
PIRiB54096.
S18380.
RefSeqiNP_001075715.1. NM_001082246.1.
XP_008262186.1. XM_008263964.2.
UniGeneiOcu.1821.

Genome annotation databases

EnsembliENSOCUT00000003608; ENSOCUP00000003129; ENSOCUG00000003610.
GeneIDi100009065.
KEGGiocu:100009065.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10391 mRNA. Translation: AAA21178.1.
PIRiB54096.
S18380.
RefSeqiNP_001075715.1. NM_001082246.1.
XP_008262186.1. XM_008263964.2.
UniGeneiOcu.1821.

3D structure databases

ProteinModelPortaliP32417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000003129.

Proteomic databases

PRIDEiP32417.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOCUT00000003608; ENSOCUP00000003129; ENSOCUG00000003610.
GeneIDi100009065.
KEGGiocu:100009065.

Organism-specific databases

CTDi2328.

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
GeneTreeiENSGT00760000119232.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiP32417.
KOiK00485.
TreeFamiTF105285.

Enzyme and pathway databases

BRENDAi1.14.13.148. 1749.

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...

Entry informationi

Entry nameiFMO3_RABIT
AccessioniPrimary (citable) accession number: P32417
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: October 5, 2016
This is version 107 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.