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Protein

Dimethylaniline monooxygenase [N-oxide-forming] 5

Gene

Fmo5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme.By similarity

Catalytic activityi

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

Cofactori

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 156FADSequence analysis
Nucleotide bindingi192 – 1976NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 5 (EC:1.14.13.8)
Alternative name(s):
Dimethylaniline oxidase 5
Hepatic flavin-containing monooxygenase 5
Short name:
FMO 5
Gene namesi
Name:Fmo5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628602. Fmo5.

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
Chaini1 – 533533Dimethylaniline monooxygenase [N-oxide-forming] 5PRO_0000147668Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Dimethylated arginine1 Publication
Modified residuei54 – 541PhosphoserineBy similarity
Modified residuei56 – 561PhosphotyrosineBy similarity
Modified residuei58 – 581PhosphoserineBy similarity
Modified residuei284 – 2841PhosphothreonineBy similarity
Modified residuei401 – 4011PhosphoserineBy similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ8K4C0.
PRIDEiQ8K4C0.

PTM databases

iPTMnetiQ8K4C0.
PhosphoSiteiQ8K4C0.

Interactioni

Protein-protein interaction databases

MINTiMINT-4578318.

Structurei

3D structure databases

ProteinModelPortaliQ8K4C0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FMO family.Curated

Keywords - Domaini

Transmembrane

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiQ8K4C0.
KOiK00485.
OrthoDBiEOG7GXPB6.
PhylomeDBiQ8K4C0.
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.
IPR002257. Flavin_mOase_5.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01125. FMOXYGENASE5.
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

Q8K4C0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKKRIAVIG SGASGLTCIK CCLEEGLEPV CFERSDDIGG LWRYQENPEK
60 70 80 90 100
GRASIYKSVI INTSKEMMCF SDYPIPDHYP NFMHNSQVLE YFRMYAKEFG
110 120 130 140 150
LLKYIQFKTT VCSVKKQPDF STSGQWQVVT EHEGKQQVDV FDGVLVCTGH
160 170 180 190 200
HTDPHLPLDS FPGIEKFKGK YFHSREYKNP VEFTGKRVIV IGIGNSGGDL
210 220 230 240 250
AVEISHTAKQ VFLSTRRGAW ILNRVGKRGY PIDILLSSRI TNYLSKICGS
260 270 280 290 300
ALKNRYMEKQ LNQRFDHEMF GLKPKHSALG QHPTINDDLP NRIISGLVKV
310 320 330 340 350
KGNVKEFTET AAIFEDGSRE DDIDVVIFAT GYSFAFPFLE DSVKVVQNKV
360 370 380 390 400
SLYKKVFPPN LEKPTLAIIG LIQPLGAIMP ISELQGRWAT QVFKGLKKLP
410 420 430 440 450
SQSEMMAEIN KTREEMAKRY VDSQRHTIQG DYIDTMEEIA DLVGVRPNLL
460 470 480 490 500
SLAFTDPKLA FQLLVGPCTP VQYRLQGPGK WAGARKTILT TEDRIRKPLM
510 520 530
TRVVERDSSG TSLVTVRVLM LAVTFLAVIL AYF
Length:533
Mass (Da):60,056
Last modified:January 23, 2007 - v3
Checksum:iA16A10779E91A8F8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341R → M in AAH70883 (PubMed:15489334).Curated
Sequence conflicti50 – 501K → E in AAH70883 (PubMed:15489334).Curated
Sequence conflicti136 – 1361Q → E in AAH70883 (PubMed:15489334).Curated
Sequence conflicti228 – 2281R → H in AAH70883 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF458413 mRNA. Translation: AAM46761.1.
BC070883 mRNA. Translation: AAH70883.1.
RefSeqiNP_653340.1. NM_144739.1.
UniGeneiRn.7038.

Genome annotation databases

GeneIDi246248.
KEGGirno:246248.
UCSCiRGD:628602. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF458413 mRNA. Translation: AAM46761.1.
BC070883 mRNA. Translation: AAH70883.1.
RefSeqiNP_653340.1. NM_144739.1.
UniGeneiRn.7038.

3D structure databases

ProteinModelPortaliQ8K4C0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4578318.

PTM databases

iPTMnetiQ8K4C0.
PhosphoSiteiQ8K4C0.

Proteomic databases

PaxDbiQ8K4C0.
PRIDEiQ8K4C0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi246248.
KEGGirno:246248.
UCSCiRGD:628602. rat.

Organism-specific databases

CTDi2330.
RGDi628602. Fmo5.

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiQ8K4C0.
KOiK00485.
OrthoDBiEOG7GXPB6.
PhylomeDBiQ8K4C0.
TreeFamiTF105285.

Miscellaneous databases

PROiQ8K4C0.

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.
IPR002257. Flavin_mOase_5.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01125. FMOXYGENASE5.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing of flavin-containing monooxygenase 5 (FMO5) in the rat."
    Lattard V., Benoit E.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  3. Cited for: METHYLATION AT ARG-5, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiFMO5_RAT
AccessioniPrimary (citable) accession number: Q8K4C0
Secondary accession number(s): Q6IRL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 99 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, 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.