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Identification
HMDB Protein ID HMDBP00143
Secondary Accession Numbers
  • 5375
Name Dimethylaniline monooxygenase [N-oxide-forming] 5
Synonyms
  1. Dimethylaniline oxidase 5
  2. FMO 5
  3. Hepatic flavin-containing monooxygenase 5
Gene Name FMO5
Protein Type Unknown
Biological Properties
General Function Involved in flavin-containing monooxygenase activity
Specific Function In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme.
Pathways
  • Drug metabolism - cytochrome P450
Reactions
N,N-Dimethylaniline + NADPH + Oxygen → Dimethylaniline-N-oxide + NADP + Water details
Trimethylamine + NADPH + Hydrogen Ion + Oxygen → Trimethylamine N-oxide + NADP + Water details
Tamoxifen + Oxygen + NADPH + Hydrogen Ion → Tamoxifen N-oxide + NADP + Water details
GO Classification
Cellular Component
intrinsic to endoplasmic reticulum membrane
intracellular membrane-bounded organelle
integral to membrane
Component
cell part
membrane part
intrinsic to membrane
intrinsic to organelle membrane
intrinsic to endoplasmic reticulum membrane
Function
binding
nucleotide binding
catalytic activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
nadp or nadph binding
monooxygenase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, nadh or nadph as one donor, and incorporation of one atom of oxygen
flavin-containing monooxygenase activity
oxidoreductase activity
fad or fadh2 binding
Molecular Function
NADP binding
flavin adenine dinucleotide binding
N,N-dimethylaniline monooxygenase activity
Process
metabolic process
oxidation reduction
Cellular Location
  1. Endoplasmic reticulum membrane
  2. Microsome membrane
Gene Properties
Chromosome Location 1
Locus 1q21.1
SNPs FMO5
Gene Sequence
>1602 bp
ATGACTAAGAAAAGAATTGCTGTGATTGGGGGAGGAGTGAGCGGGCTCTCTTCCATCAAG
TGCTGCGTAGAAGAAGGCTTGGAACCTGTCTGCTTTGAAAGGACTGATGACATCGGAGGG
CTCTGGAGGTTCCAGGAAAATCCTGAAGAAGGAAGGGCCAGTATTTACAAATCAGTGATC
ATCAATACTTCTAAAGAGATGATGTGCTTCAGTGACTATCCAATCCCAGATCATTATCCC
AACTTCATGCATAATGCCCAGGTCCTGGAGTATTTCAGGATGTATGCCAAAGAATTTGAC
CTTCTAAAGTATATTCGATTTAAGACCACTGTGTGCAGTGTGAAGAAGCAGCCTGATTTT
GCCACTTCAGGCCAATGGGAAGTGGTCACTGAATCTGAAGGGAAAAAGGAGATGAATGTC
TTTGATGGAGTCATGGTTTGCACTGGCCATCACACCAATGCTCATCTACCTCTGGAAAGC
TTCCCTGGAATTGAGAAGTTCAAAGGGCAGTACTTCCACAGTCGAGACTATAAGAACCCA
GAGGGATTCACTGGAAAGAGAGTCATTATAATTGGCATTGGGAATTCTGGAGGGGATCTG
GCTGTAGAGATTAGCCAAACAGCCAAGCAGGTTTTCCTCAGCACCAGGAGAGGGGCTTGG
ATCCTGAATCGTGTAGGGGACTACGGATATCCTGCTGATGTGTTGTTCTCTTCTCGACTT
ACACATTTTATATGGAAGATCTGTGGCCAATCATTAGCAAACAAATATTTGGAAAAAAAG
ATAAACCAAAGGTTTGACCATGAAATGTTTGGCCTGAAGCCTAAACACAGAGCTCTGAGT
CAGCATCCAACCTTAAATGATGACCTGCCAAATCGTATCATTTCTGGCTTGGTGAAAGTG
AAAGGAAATGTGAAGGAATTCACGGAGACAGCTGCCATATTTGAGGATGGCTCCAGGGAG
GATGACATTGATGCTGTTATCTTTGCCACAGGCTATAGCTTTGACTTTCCATTTCTGGAA
GATTCCGTCAAAGTGGTCAAAAACAAGATATCCCTGTATAAAAAGGTCTTCCCTCCTAAC
CTGGAAAGGCCAACTCTTGCAATCATAGGCTTGATTCAGCCCTTAGGAGCCATTATGCCC
ATTTCAGAGCTCCAAGGACGCTGGGCCACTCAGGTATTTAAAGGTCTAAAGACATTGCCC
TCACAGAGTGAAATGATGGCAGAAATATCTAAAGCTCAAGAGGAAATTGACAAAAGGTAT
GTGGAGAGCCAACGCCATACCATTCAGGGAGACTACATAGATACCATGGAAGAGCTTGCT
GATTTGGTGGGGGTCAGGCCCAATCTGCTGTCTCTGGCCTTCACTGACCCCAAGCTGGCA
TTACACTTATTACTGGGACCCTGCACTCCAATCCACTATCGTGTACAGGGCCCTGGAAAG
TGGGATGGGGCTCGAAAAGCTATCCTCACCACAGATGATCGCATCAGGAAGCCTCTGATG
ACAAGAGTAGTTGAAAGGAGTAGTTCTATGACTTCAACAATGACAATAGGCAAGTTTATG
CTAGCTCTTGCCTTCTTTGCTATAATTATAGCTTACTTCTAG
Protein Properties
Number of Residues 533
Molecular Weight 32480.04
Theoretical pI 8.313
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Dimethylaniline monooxygenase [N-oxide-forming] 5
MTKKRIAVIGGGVSGLSSIKCCVEEGLEPVCFERTDDIGGLWRFQENPEEGRASIYKSVI
INTSKEMMCFSDYPIPDHYPNFMHNAQVLEYFRMYAKEFDLLKYIRFKTTVCSVKKQPDF
ATSGQWEVVTESEGKKEMNVFDGVMVCTGHHTNAHLPLESFPGIEKFKGQYFHSRDYKNP
EGFTGKRVIIIGIGNSGGDLAVEISQTAKQVFLSTRRGAWILNRVGDYGYPADVLFSSRL
THFIWKICGQSLANKYLEKKINQRFDHEMFGLKPKHRALSQHPTLNDDLPNRIISGLVKV
KGNVKEFTETAAIFEDGSREDDIDAVIFATGYSFDFPFLEDSVKVVKNKISLYKKVFPPN
LERPTLAIIGLIQPLGAIMPISELQGRWATQVFKGLKTLPSQSEMMAEISKAQEEIDKRY
VESQRHTIQGDYIDTMEELADLVGVRPNLLSLAFTDPKLALHLLLGPCTPIHYRVQGPGK
WDGARKAILTTDDRIRKPLMTRVVERSSSMTSTMTIGKFMLALAFFAIIIAYF
GenBank ID Protein 189054435
UniProtKB/Swiss-Prot ID P49326
UniProtKB/Swiss-Prot Entry Name FMO5_HUMAN
PDB IDs Not Available
GenBank Gene ID AK314647
GeneCard ID FMO5
GenAtlas ID FMO5
HGNC ID HGNC:3773
References
General References
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  3. Overby LH, Buckpitt AR, Lawton MP, Atta-Asafo-Adjei E, Schulze J, Philpot RM: 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. Arch Biochem Biophys. 1995 Feb 20;317(1):275-84. [PubMed:7872795 ]
  4. Furnes B, Feng J, Sommer SS, Schlenk D: Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. Drug Metab Dispos. 2003 Feb;31(2):187-93. [PubMed:12527699 ]