Protein: CCSD_ASPCL
Sequence: MVNEISPRTLVLLAVTCSLLVLYFSTRERQPVMPRELPVVKAKSYHFEDIIVEGRKKYPDRPYLAVNNRHSFVVYPPSCFDEIKRLPEHSASAKDFFHTMNAGDWTYVGHETTPLLKTIIADLTRVIPARVNKRQQDTRMAFESIVGYAPEWKEIGLLMTTFEIVAKINACAFVGRELGTNNKWVKAVMQSPLVIHVAVLIMNACPALLRPLLAPLAFLPTKMNQWDMRRLLTPMLQEDMAIFKETKDRSELLRPKQNGKIPLTAMLLSRYKQGEATIRQLIVDYILISFDSTPSTASALYHVICELAAHPEAADVLRQELDEVMVDGKLPQTHLQELKRMDSFLRESFRLHPVSLFSLQRVLAKPVKLSVGPTIPAGAIIAVDAAAINRSPSLWKDPDEFDMNRFHDLRQVPGNENKFHLLNTGSDSPGWGDGTQACPGRFFANSTLKIAFAYILQNYDVKRKEGSSPPKMTPLANGTWAPDDKAAALFKSRN
What is the function of this protein?
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of a family of the mycotoxins cytochalasins E and K (PubMed:21983160).  The hybrid PKS-NRPS synthetase ccsA and the enoyl reductase ccsC are responsible for fusion of phenylalanine with an octaketide backbone and subsequent release of the stable tetramic acid precursor (PubMed:21983160, PubMed:27551732).  The polyketide synthase module (PKS) of the PKS-NRPS ccsA is responsible for the synthesis of the octaketide backbone (PubMed:21983160).  The downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the octaketide with a phenylalanine (PubMed:21983160).  A reductase-like domain (R) at the C-terminus catalyzes the reductive release of the polyketide-amino acid intermediate (PubMed:21983160).  Because ccsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ccsC (PubMed:21983160, PubMed:27551732).  Upon formation of the 11-membered carbocycle-fused perhydroisoindolone intermediate, a number of oxidative steps are required to afford the final cytochalasin E and K, including two hydroxylations at C17 and C18, one alcohol oxidation at C17, one epoxidation at C6 and C7 and two Baeyer-Villiger oxidations (PubMed:21983160).  The oxidative modification at C17, C18 and the C6-C7 epoxidation are likely to be catalyzed by the two cytochrome P450 oxygenases ccsD and ccsG (PubMed:21983160).  CcsD may be responsible for the epoxidation of the C6-C7 double bond (PubMed:21983160).  CcsG may be responsible for the successive oxidative modifications at C17 and C18 (PubMed:21983160).  The double Baeyer-Villiger oxidations of ketocytochalasin to precytochalasin and cytochalasin Z(16) are among the final steps leading to cytochalasin E and K and are catalyzed by ccsB (PubMed:21983160, PubMed:24838010).  The first oxygen insertion step follows that of the classic BVMO mechanism, generating the ester precytochalasin (PubMed:24838010).  Release of precytochalasin into an aqueous environment can generate the shunt product iso-precytochalasin through spontaneous isomerization (PubMed:24838010).  Alternatively, precytochalasin can undergo further oxidation by ccsB to yield the in-line carbonate-containing cytochalasin Z(16) (PubMed:24838010).  Cytochalasin Z(16) is a precursor to cytochalasin E and cytochalasin K, whereas iso-precytochalasin is a precursor to cytochalasin Z(17) and rosellichalasin (PubMed:21983160, PubMed:24838010).  The hydrolyase ccsE may catalyze hydrolysis of epoxide bond in cytochalasin E to afford cytochalasin K (PubMed:21983160).  The function of ccsF has not been assigned but it may play a role in post-PKS-NRPS biosynthetic step, resistance or transport of cytochalasins and related PKS-NRPS products (PubMed:21983160).
What are the official names of this protein?
Cytochrome P450 monooxygenase ccsD, Cytochalasin biosynthesis protein D.
What is the protein family that this protein belongs to?
Belongs to the cytochrome P450 family.
What are the subcellular locations of this protein?
Membrane; Single-pass membrane protein.