Dimethylaniline monooxygenase [N-oxide-forming] 1 - Oryctolagus cuniculus (Rabbit)

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Reviewed, UniProtKB/Swiss-Prot P17636 (FMO1_RABIT)

Last modified June 16, 2009. Version 76. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Dimethylaniline monooxygenase [N-oxide-forming] 1
    EC=1.14.13.8
Alternative name(s):
    Hepatic flavin-containing monooxygenase 1
    FMO form 1
      Short name=FMO 1
    FMO 1A1
    Dimethylaniline oxidase 1

Gene names

Name:

FMO1

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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Protein attributes

Sequence length	535 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. Form I catalyzes the N-oxygenation of secondary and tertiary amines.
Catalytic activity	N,N-dimethylaniline + NADPH + O₂ = N,N-dimethylaniline N-oxide + NADP⁺ + H₂O.
Cofactor	FAD.
Subcellular location	Microsome membrane. Endoplasmic reticulum membrane.
Tissue specificity	Liver.
Sequence similarities	Belongs to the FMO family.

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Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro microsome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro flavin-containing monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.2

Chain

2 – 535

534

Dimethylaniline monooxygenase [N-oxide-forming] 1

PRO_0000147642

Regions

Nucleotide binding

9 – 14

FAD Potential

Nucleotide binding

191 – 196

NADP Potential

Sites

Site

208

Important for substrate binding By similarity

Amino acid modifications

Modified residue

N-acetylalanine Ref.2

Experimental info

Sequence conflict

C → S AA sequence Ref.2

Sequence conflict

C → S AA sequence Ref.3

Sequence conflict

E → K AA sequence Ref.2

Sequence conflict

E → K AA sequence Ref.3

Sequence conflict

S → D AA sequence Ref.2

Sequence conflict

103

S → E AA sequence Ref.2

Sequence conflict

116

C → E AA sequence Ref.2

Sequence conflict

126

E → K AA sequence Ref.2

Sequence conflict

279

L → M AA sequence Ref.2

Sequence conflict

340

F → S AA sequence Ref.2

Sequence conflict

406

S → C AA sequence Ref.2

Sequence conflict

455

L → S AA sequence Ref.2

Sequence conflict

457

L → G AA sequence Ref.2

Sequence conflict

535

L → LES AA sequence Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P17636-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8EE95683FC3E43D5
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FASTA

535

60,183

        10         20         30         40         50         60 
MAKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSDDLGGL WRFTEHVEEG RASLYKSVVS 

        70         80         90        100        110        120 
NSCKEMSCYS DFPFPEDYPN YVPNSQFLDY LKMYADRFSL LKSIQFKTTV FSITKCQDFN 

       130        140        150        160        170        180 
VSGQWEVVTL HEGKQESAIF DAVMVCTGFL TNPHLPLGCF PGIKTFKGQY FHSRQYKHPD 

       190        200        210        220        230        240 
IFKDKRVLVV GMGNSGTDIA VEASHVAKKV FLSTTGGAWV ISRVFDSGYP WDMVFTTRFQ 

       250        260        270        280        290        300 
NFIRNSLPTP IVTWLVAKKM NSWFNHANYG LVPKDRIQLK EPVLNDELPG RIITGKVFIR 

       310        320        330        340        350        360 
PSIKEVKENS VVFGNAHNTP SEEPIDVIVF ATGYTFAFPF LDESVVKVED GQASLYKYIF 

       370        380        390        400        410        420 
PAHLQKPTLA VIGLIKPLGS MLPTGETQAR YTVQVFKGVI KLPPTSVMIK EVNERKENKH 

       430        440        450        460        470        480 
NGFGLCYCKA LQADYITYID DLLTSINAKP NLFSLLLTDP LLALTMFFGP YSPYQFRLTG 

       490        500        510        520        530 
PGKWKGARNA IMTQWDRTFK VTKTRIVQES SSPFESLLKL FAVLALLVSV FLIFL

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References

[1]	"The flavin-containing monooxygenase enzymes expressed in rabbit liver and lung are products of related but distinctly different genes." Lawton M.P., Gasser R., Tynes R.E., Hodgson E., Philpot R.M. J. Biol. Chem. 265:5855-5861(1990) [PubMed: 2318837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: New Zealand white.
[2]	"Covalent structure of liver microsomal flavin-containing monooxygenase form 1." Ozols J. J. Biol. Chem. 265:10289-10299(1990) [PubMed: 2355001] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-535. Tissue: Liver.
[3]	"Liver microsomes contain two distinct NADPH-Monooxygenases with NH2-terminal segments homologous to the flavin containing NADPH-monooxygenase of Pseudomonas fluorescens." Ozols J. Biochem. Biophys. Res. Commun. 163:49-55(1989) [PubMed: 2505769] [Abstract] Cited for: PROTEIN SEQUENCE OF 4-33 AND 224-247. Tissue: Liver.

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Cross-references

Sequence databases
	M32030 mRNA. Translation: AAA31278.1.
PIR	A35182. A35427.
RefSeq	NP_001075754.1.
UniGene	Ocu.1887
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	100009120.
Phylogenomic databases
HOVERGEN	P17636.
Enzyme and pathway databases
BRENDA	1.14.13.8. 255.
Family and domain databases
InterPro	IPR012143. dManiline_mOase. IPR000960. Flavin_mOase. IPR002253. Flavin_mOase_1. [Graphical view]
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
PIRSF	PIRSF000332. FMO. 1 hit.
PRINTS	PR00370. FMOXYGENASE. PR01121. FMOXYGENASE1.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

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Entry information

Entry name

FMO1_RABIT

Accession

Primary (citable) accession number: P17636

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 76 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents