Reviewed, UniProtKB/Swiss-Prot P49109 (FMO5_CAVPO)

Names and origin

Protein names

Recommended name:
    Dimethylaniline monooxygenase [N-oxide-forming] 5
    EC=1.14.13.8
Alternative name(s):
    Hepatic flavin-containing monooxygenase 5
      Short name=FMO 5
    Dimethylaniline oxidase 5

Gene names

Name:

FMO5

Organism

Cavia porcellus (Guinea pig)

Taxonomic identifier

10141 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length	533 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme.
Catalytic activity	N,N-dimethylaniline + NADPH + O(2) = N,N-dimethylaniline N-oxide + NADP(+) + H(2)O.
Cofactor	FAD.
Subcellular location	Microsome membrane. Endoplasmic reticulum membrane.
Sequence similarities	Belongs to the FMO family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation Methylation
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: InterPro
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro flavin-containing monooxygenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 533	532	Dimethylaniline monooxygenase [N-oxide-forming] 5		PRO_0000147664
Regions
	Nucleotide binding	10 – 15	6	FAD Potential
	Nucleotide binding	192 – 197	6	NADP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylthreonine By similarity
	Modified residue	5	1	Omega-N-methylated arginine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P49109-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E0C06EE4C6B6EFDD	FASTA	533	60,125
	10 20 30 40 50 60 MTKKRIAVIG GGVSGLSSIK CCLEEGLEPV CFERSADIGG LWRFQENPEE GRASIYKSVI 70 80 90 100 110 120 INTSKEMMCF SDYPIPDHYP NFMHNSHVLE YFRMYAKEFG LLKYIQFKTT VCNVKKRPDF 130 140 150 160 170 180 STSGQWEVVT EHEGKTKVDV FDAVMVCTGH HTNAHLPLES FPGIEKFKGQ YFHSRDYKNP 190 200 210 220 230 240 EAFTGKRVVI IGIGNSGGDL AVEISHTAKQ VFLSTRRGSW ILNRVGKHGY PTDVLLSSRF 250 260 270 280 290 300 TYFLSKILGQ SLSNAYVEKQ MNERFDHEMF GLKPKHRAMS QHPTVNDDLP NRIIAGMVKV 310 320 330 340 350 360 KGNVKEFTET AAIFEDGSRE DDIDAVIFAT GYSFDFPFLE DSVKVVKNKV SLYKKVFPPN 370 380 390 400 410 420 LERPTLAIIG LIQPLGAIMP ISELQGRWAV QVFKGLKTLP SQSEMMAEIT KAQEEIAKRY 430 440 450 460 470 480 VDSQRHTIQG DYIQTMEEIA EFVGVKPNLL SLAFTDPKLA LKLFFGPCTP IHYRLQGPGK 490 500 510 520 530 WHGARKAILT TYDRIRKPLN TRETEKSNSM VSAVTTGCFM LAVVFFAIIM AYA

References

[1]

"Characterization of flavin-containing monooxygenase 5 (FMO5) cloned from human and guinea pig: evidence that the unique catalytic properties of FMO5 are not confined to the rabbit ortholog." Overby L.H., Buckpitt A.R., Lawton M.P., Atta-Asafo-Adjei E., Schulze J., Philpot R.M. Arch. Biochem. Biophys. 317:275-284(1995) [PubMed: 7872795] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Hartley. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L37081 mRNA. Translation: AAA67848.1.
PIR	S71617.
3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	P49109.
Family and domain databases
InterPro	IPR012143. dManiline_mOase. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000960. Flavin_mOase. IPR002257. Flavin_mOase_5. [Graphical view]
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
PIRSF	PIRSF000332. FMO. 1 hit.
PRINTS	PR00368. FADPNR. PR00370. FMOXYGENASE. PR01125. FMOXYGENASE5.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

FMO5_CAVPO

Accession

Primary (citable) accession number: P49109

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)