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Showing Protein Putative dimethylaniline monooxygenase [N-oxide-forming] 6 (HMDBP01904)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 7 metabolites
Identification
HMDB Protein ID HMDBP01904
Secondary Accession Numbers
  • 7310
Name Putative dimethylaniline monooxygenase [N-oxide-forming] 6
Synonyms
  1. Dimethylaniline oxidase 6
  2. FMO 6
  3. Flavin-containing monooxygenase 6
Gene Name FMO6P
Protein Type Unknown
Biological Properties
General Function Involved in flavin-containing monooxygenase activity
Specific Function It is probable that this protein is only produced in very small quantity or not at all as the gene coding for it seems to be unable to produce full length transcripts.
Pathways Not Available
Reactions
N,N-Dimethylaniline + NADPH + Oxygen → Dimethylaniline-N-oxide + NADP + Water details
GO Classification
Cellular Component
intrinsic to endoplasmic reticulum membrane
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 Not Available
Locus Not Available
SNPs FMO6P
Gene Sequence Not Available
Protein Properties
Number of Residues 539
Molecular Weight Not Available
Theoretical pI Not Available
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Putative dimethylaniline monooxygenase [N-oxide-forming] 6
MSKRVGIIGAGVSGLAAIWCCLEEGLEPTCFERSDDVGGLWKFSDHTEEGRASIYQSVFT
NSSKEMMCFPDFPYPDDYPNYIHHSKLQEYIKTYAQKKDLLRYIQFETLVSGIKKCPSFL
VTGQWVVVTEKDGKQESTIFDAVMICSGHHVYPNLPTDSFPGLDQFRGNYLHSRDYKNPE
AFKGKRVLVIGLGNSGSDIAVELSRLATQVIISTRSASWVMSRVWDDGYPWDMMYVTRFA
SFLRNVLPSFISDWLYVQKMNTWFKHENYGLMPLNGSLRKEPVFNDELPSRILCGTLSIK
PSVKEFTETSAVFEDGTMFEAIDSVIFATGYDYSYPFLDETIMKSRNNEVTLFKGIFPPL
MEKPTLAVIGLVQSLGAAIPTADLQAWWAAKVFANSCTLPTTNEMMDDTDEKMGKKLKCM
FSSFFMFGQSQTLQTDYITYVDELGSFIGAKPNIPWLFLTDPRLALEVYFGPCSPYQFRL
MGPGKWDGARNAILTQWNRTVKPTRTRVVSEVQRPHPFYNLLKMLSFPLLLLAVTLTFY
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID O60774
UniProtKB/Swiss-Prot Entry Name FMO6_HUMAN
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID FMO6P
GenAtlas ID FMO6P
HGNC ID HGNC:24024
References
General References
  1. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed:16710414 ]
  2. 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 ]
  3. Hines RN, Hopp KA, Franco J, Saeian K, Begun FP: Alternative processing of the human FMO6 gene renders transcripts incapable of encoding a functional flavin-containing monooxygenase. Mol Pharmacol. 2002 Aug;62(2):320-5. [PubMed:12130684 ]