Protein: NSRD_ASPN1
Sequence: MTKETYVSATAVVSGSFLSGSMMSLSALVIPLFLDTIDDGPQLLRQWARLYHYGSIYMPALCVATCGIYGYVALSKRAAISPLWSPYVLAAVSTLAMVPFTWWVMVPTNNTLFGLHRSAESTELGVVQVLVVKWAWLHVVRSLYPLFGAFLGFRALIRELRT
What is the function of this protein?
Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of the tetrahydroxanthone dimer neosartorin, which exhibits antibacterial activity (PubMed:30394754, PubMed:32105084, PubMed:33891392).  The two different monomeric units appear to be synthesized by the same set of enzymes, among which the Baeyer-Villiger monooxygenase nsrF is the key enzyme for the divergence of the biosynthetic routes (PubMed:32105084).  The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase nsrB (PubMed:32105084).  The atrochrysone carboxyl ACP thioesterase nsrC then breaks the thioester bond and releases the atrochrysone carboxylic acid from AacuL (PubMed:32105084).  Atrochrysone carboxylic acid is decarboxylated by the decarboxylase nsrE, and oxidized by the anthrone oxygenase nsrD to yield emodin (PubMed:32105084).  Emodin is then reduced to emodin hydroquinone by the oxidoreductase nsrR (PubMed:32105084).  A-ring reduction by the short chain dehydrogenase nsrJ, dehydration by the scytalone dehydratase-like protein nsrI and probable spontaneous re-oxidation, results in overall deoxygenation to chrysophanol (PubMed:32105084).  The Baeyer-Villiger monooxygenase nsrF accepts chrysophanol as a substrate to insert one oxygen atom at two different positions to yield the precursors of both monomric units (PubMed:30394754, PubMed:32105084, PubMed:33891392).  NsrF is promiscuous/flexible in interacting with the 2 (non methylated and methylated) aromatic rings of chrysophanol, thus diverging the biosynthetic pathway at this point (PubMed:30394754, PubMed:32105084, PubMed:33891392).  After the hydrolysis of the lactones, methylesterification by the methyltransferase nsrG yields respectively moniliphenone and 2,2',6'-trihydroxy-4-methyl-6-methoxya-cyldiphenylmethanone (PubMed:30394754, PubMed:32105084).  The next steps are the hydroxylation by the FAD-dependent monooxygenase nsrK, followed by isomerization by the monooxygenase nsrQ (PubMed:32105084).  The short chain dehydrogenase/reductase nsrO then catalyzes the C-5 ketoreduction to give the xanthone skeleton of blennolide C and 5-acetylblennolide A (PubMed:32105084).  The acetyltransferase nsrL has a strict substrate specificity and uses only blennolide A but not blennolide C to yield 5-acetylblennolide A as the single-acetylated product (PubMed:30394754).  In the final step of the biosynthesis, the heterodimerization of the 2 xanthones, blennolide C and 5-acetylblennolide A, is catalyzed by the cytochrome P450 monooxygenase nsrP (PubMed:30394754).  NsrP can utilize at least three different xanthones as its substrates to perform the dimerization reaction (PubMed:30394754).
What are the official names of this protein?
Anthrone oxygenase nsrD, Neosartorin biosynthesis cluster protein D.
What is the protein family that this protein belongs to?
Belongs to the anthrone oxygenase family.
What are the subcellular locations of this protein?
Membrane; Multi-pass membrane protein.