Protein: AZAI_ASPNA
Sequence: MESLAQLPGIFLPLAGCVLALSLSALLAVGPIVRVTPTEVDICDLPAVREIHRVRGGYLKSEWYKSLTPPGVTSLLTLIEPTQYSEWRRLLAGPLSDTSLGKVEPMVTNHVHATIDRIASDLQSQGVSDLYKWWTYMATDVVSELSFGEPIGLLARPKETAWVMDYLDKVGIMHAWRTTFPFVFVLGRFMPVHPFKHAIQAIGLLGKWARRSIQQYRQHIQEQPESPKPTLFTKLFKADKFDDFQLTYLAGSYITAGSHTTAVTLLYLIYAICRDNEIRQKLLAEIRTLPENFRHDELRHLPYLNQVITETLRKYAVVSSALPRVVPAGGATLAGYYLPGGTTVSTQAYTLHRNEAIFPNPEKYKPNPKYSYLSMLSVWLIECRFDPSRWESPTQEMKDAYMPFGGASRMCIGNSLALMEIRLTTTLFLRRFPEVQMSRQNGMRDEDLAQEQYLIMAPRGHRLLVEA
What is the function of this protein?
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities (PubMed:22921072).  In the first step, the non-reducing polyketide synthase azaA forms the hexaketide precursor from successive condensations of five malonyl-CoA units, presumably with a simple acetyl-CoA starter unit (PubMed:22921072).  The reactive polyketide chain then undergoes a PT-mediated C2-C7 cyclization to afford the aromatic ring and is eventually released as an aldehyde through the R-domain (PubMed:22921072).  The putative ketoreductase azaE is proposed to catalyze the reduction of the terminal ketone resulting in the early culture product FK17-P2a (PubMed:22921072).  The monooxygenase azaH was demonstrated to be the only enzyme required to convert FK17-P2a to azanigerone E (PubMed:22921072).  AzaH first hydroxylates the benzaldehyde intermediate FK17-P2a at C4, which triggers the formation of the pyran-ring to afford azanigerone E (PubMed:22921072).  In parallel, the 2,4-dimethylhexanoyl chain is synthesized by the HR-PKS azaB and is proposed to be transferred to the C4-hydroxyl of azanigerone E by the acyltransferase azaD directly from the ACP domain of azaB (PubMed:22921072).  Alternatively, the 2,4-dimethyl-hexanoyl chain may be offloaded from the HR-PKS as a carboxylic acid and converted to an acyl-CoA by azaF (PubMed:22921072).  The resulting acyl-CoA molecule could then be taken up as a substrate by AzaD to form azanigerone B (PubMed:22921072).  To yield the carboxylic acid substituent in azanigerone A, the hydroxypropyl side chain of azanigerone B would need to undergo a C-C oxidative cleavage catalyzed by cytochrome P450 AzaI (PubMed:22921072).  AzaI is proposed to act on a vicinal diol that leads to a C-C bond scission either through an alkoxyradical intermediate or a peroxy complex (PubMed:22921072).  In the biosynthesis of azanigerone A, azanigerone B first undergoes hydroxylation at C10, possibly catalyzed by one of the two FAD-dependent monooxygenases encoded in the cluster, azaG or azaL, resulting in the vicinal diol azanigerone C (PubMed:22921072).  Oxidative cleavage of azanigerone C by azaI would yield the corresponding aldehyde derivative of azanigerone A (PubMed:22921072).  Finally, the dehydrogenase azaJ is proposed to convert the aldehyde functional group into the carboxylic acid, completing the conversion from azanigerone B to azanigerone A (PubMed:22921072).  Alternatively, the oxidation of aldehyde to carboxylic acid may be catalyzed by the same P450 enzyme azaI via consecutive oxidation or by endogenous alcohol dehydrogenase (PubMed:22921072).
What are the official names of this protein?
Cytochrome P450 monooxygenase azaI, Azaphilone biosynthesis cluster protein azaI.
What is the protein family that this protein belongs to?
Belongs to the cytochrome P450 family.