A0A023GL55 · A0A023GL55_AMBTT

Function

function

Acts as a Baeyer-Villiger monooxygenase on a broad range of substrates. Catalyzes the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Active on diverse carbonyl compounds, whereas soft nucleophiles are mostly non- or poorly reactive. In contrast with other forms of FMO it is non- or poorly active on 'classical' substrates such as drugs, pesticides, and dietary components containing soft nucleophilic heteroatoms. Able to oxidize drug molecules bearing a carbonyl group on an aliphatic chain, such as nabumetone and pentoxifylline. Also, in the absence of substrates, shows slow but yet significant NADPH oxidase activity. Acts as a positive modulator of cholesterol biosynthesis as well as glucose homeostasis, promoting metabolic aging via pleiotropic effects.

Catalytic activity

  • (2E)-geranial + NADPH + O2 + H+ = (1E)-2,6-dimethylhepta-1,5-dien-1-yl formate + NADP+ + H2O
    This reaction proceeds in the forward direction.
  • octan-3-one + NADPH + O2 + H+ = pentyl propanoate + NADP+ + H2O
    This reaction proceeds in the forward direction.
  • octan-3-one + NADPH + O2 + H+ = ethyl hexanoate + NADP+ + H2O
    This reaction proceeds in the forward direction.
  • sulcatone + NADPH + O2 + H+ = 4-methylpent-3-en-1-yl acetate + NADP+ + H2O
    This reaction proceeds in the forward direction.
  • NADPH + O2 + H+ = H2O2 + NADP+
    This reaction proceeds in the forward direction.
    EC:1.6.3.1 (UniProtKB | ENZYME | Rhea)
  • heptan-2-one + NADPH + O2 + H+ = pentyl acetate + NADP+ + H2O
    This reaction proceeds in the forward direction.
  • heptan-4-one + NADPH + O2 + H+ = propyl butanoate + NADP+ + H2O
    This reaction proceeds in the forward direction.
  • hexan-3-one + NADPH + O2 + H+ = propyl propanoate + NADP+ + H2O
    This reaction proceeds in the forward direction.
  • hexan-3-one + NADPH + O2 + H+ = ethyl butanoate + NADP+ + H2O
    This reaction proceeds in the forward direction.

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum membrane
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionhypotaurine dehydrogenase activity
Molecular FunctionN,N-dimethylaniline monooxygenase activity
Molecular FunctionNADP binding
Molecular FunctionNADPH oxidase H202-forming activity
Biological Processlipid metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Flavin-containing monooxygenase
  • EC number

Organism names

  • Taxonomic identifier
  • Strain
    • Mato Grasso do Sul
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Chelicerata > Arachnida > Acari > Parasitiformes > Ixodida > Ixodoidea > Ixodidae > Amblyomminae > Amblyomma

Accessions

  • Primary accession
    A0A023GL55

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane514-534Helical

Keywords

PTM/Processing

Keywords

Family & Domains

Sequence similarities

Belongs to the FMO family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    541
  • Mass (Da)
    61,544
  • Last updated
    2014-06-11 v1
  • Checksum
    165500E50F7EA1D2
MSEARGRVCVVGAGSSGLTTARQMLDYGFDVVLYERSGDVGGLWAYHDDDVEGQASVMRTTIINTSKEMSAFSDFPPPKDLPNYMHNTKMLGYFRSYADHFGVTKYVKTRHDVVQVTPAADYDKTGRWDVVVRDLETNTDRTETFEAVAVCVGHHVYPNVPSFKGQEKFRGRVLHTHSLKNADKFRDHRVAVVGIGNSAVDAVVDVSHVAIETYLSTRRGAWVAKRVGPNGMPIDIFLSTRLKNYLMHMLPESVSNDYVENILNGFFNHEVYGIKPKHRYNAQHPTVNDALPNLILSGKVQVKKNVVEFTEEGVLFEGDNKVTQLDDVILATGYQIKFPFLPKDVVSVVDNQVQLYKYVFPPHLKHPTMAIIGLIQPIGAIFPIAELQARWMAELLTKKRSLPSEEAMHENIRKKLAAMRRRYVDSPRHTIQVDWIDYMDELASQIGARPNMIKYLLTDYELFRALLGPCVPYQFRLEGPHRWPGARQAILDSRSRVMYPLNDRCSSFRRKDKGHFTFFNVCAFFFVLAVAYIFSGLRQHS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GBBM01000802
EMBL· GenBank· DDBJ
JAC34616.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help