Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dimethylaniline monooxygenase [N-oxide-forming] 2

Gene

FMO2

Organism
Macaca mulatta (Rhesus macaque)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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

Protein has several cofactor binding sites:

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, Magnesium, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 2 (EC:1.14.13.8)
Alternative name(s):
Dimethylaniline oxidase 2
FMO 1B1
Pulmonary flavin-containing monooxygenase 2
Short name:
FMO 2
Gene namesi
Name:FMO2
OrganismiMacaca mulatta (Rhesus macaque)
Taxonomic identifieri9544 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca
Proteomesi
  • UP000006718 Componenti: Unplaced

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 – 535534Dimethylaniline monooxygenase [N-oxide-forming] 2PRO_0000147647Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Cross-linki492 – 492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Interactioni

Protein-protein interaction databases

STRINGi9544.ENSMMUP00000025933.

Structurei

3D structure databases

ProteinModelPortaliQ28505.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FMO family.Curated

Keywords - Domaini

Transmembrane

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiQ28505.
KOiK00485.

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.
IPR002254. Flavin_mOase_2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01122. FMOXYGENASE2.
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

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

Q28505-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGV WRFKEKVEDG
60 70 80 90 100
RASIYQSVVT NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL
110 120 130 140 150
LKYIQFQTTV LSVRKCPDFS SSGQWKVVTQ SNGKEQSAVF DAVMVCTGHH
160 170 180 190 200
FLPHIPLKSF PGIERFKGQY FHSRQYKHPD GFEGKRILVI GMGNSGSDIA
210 220 230 240 250
VELSKSAAQV FISTRHGTWV MSRVSEDGYP WDSVFHTRFR SMLRNVLPRT
260 270 280 290 300
VVKWMIEQQM NQWFNHENYG LEPQNKYIMK EPVLNDDVPS RLLCGAIKVK
310 320 330 340 350
STVKELTETS AIFEDGTVEE NIDVIIFATG YSFSFPFLED SLVKVENNMV
360 370 380 390 400
SLYKYIFPAH LEKSTFACIG LIQPLGSIFP TAELQARWVT RVFKGLCHLP
410 420 430 440 450
SERTMMMDII KRNEKRIDLF GESQSQTLQT NYVDYLDELA LEIGAKPDFC
460 470 480 490 500
SLLFKDPKLA VRLFFGPCNS YQYRLAGPGQ WEGARSAIFT QKQRILKPLK
510 520 530
TRVLKDSSNF PVSFLLKILG LVAVVVAFFC QLQWS
Length:535
Mass (Da):60,961
Last modified:January 23, 2007 - v2
Checksum:i85621203B07CCFAE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59453 mRNA. Translation: AAB02939.1.
RefSeqiNP_001036242.1. NM_001042777.1.
UniGeneiMmu.3381.

Genome annotation databases

GeneIDi703639.
KEGGimcc:703639.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59453 mRNA. Translation: AAB02939.1.
RefSeqiNP_001036242.1. NM_001042777.1.
UniGeneiMmu.3381.

3D structure databases

ProteinModelPortaliQ28505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9544.ENSMMUP00000025933.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi703639.
KEGGimcc:703639.

Organism-specific databases

CTDi2327.

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiQ28505.
KOiK00485.

Miscellaneous databases

NextBioi19970251.

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.
IPR002254. Flavin_mOase_2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01122. FMOXYGENASE2.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Pulmonary flavin-containing monooxygenase (FMO) in rhesus macaque: expression of FMO2 protein, mRNA and analysis of the cDNA."
    Yueh M.-F., Krueger S.K., Williams D.E.
    Biochim. Biophys. Acta 1350:267-271(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiFMO2_MACMU
AccessioniPrimary (citable) accession number: Q28505
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: February 17, 2016
This is version 106 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, 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.