Protein: FMQC_ASPFU
Sequence: MPDLIQTKSVVLGYGVKMVLAPAKAARSLLIREEAVWRFSLPRVLSTPTTMLETTEPIAHASELDKPSIVVTNTEVDSEDNTSSVLGRYIPQKCLQNARLAAVNSCVNEIFEARFRERPDAPAVCAWDGSYTYRELNDRSSALAHKLRRRGVQAEVLVALLFEKSKFSVVAMHAVIKAGGAFQLWDPSLPVARLGGMFAESKAHLVLASAANARLAAEISENVMVVDESLVPPWESAPLNPGTQPENALYCVFTSGSTGKPKGFLMDHRAFCTCALGVGELLGLNGASRLIQFSANSFDLATFDHILPFLCGACLCIPSEEERKGDLTRAFNRYRATHAVLTPTVSRLLEPEKLTTLQVLLLAGEAPSREDIRRWASTVGLLNGYSPAEAGCITIVNPSLQESHPSKIGFPVSVVPWVVDPDDCNRLVPAGEVGELVLQGHTLARGYFGRPDQSKAAFIPTPAWVRQFGYETYGRLYRTGDLVRFDAEDESLVYIGRKDSQVKIRGQRLELGEVEHALQQFFPRPQIVVVELLTAEDREPALVGFVYQPGSSQHMPAPPQHQDNSLFLVADDQFCADAQKALASLRDILPPYMIPSDLLRISHLPMVPSGKTDRRLIRMRAVDLAPEERRKYSSVLGQSRDQPVTQLEESLLGLWATCLKLPPSQIGVLDNFFHLGGGSLEAIHLAAEARNMGFAELSSAAVFQCPTIREMAGMLDGVTASVQEQDPRGCTSFQLESSLVAELLRKSQCTLEDLQEGFLPLTPFQEKTAKMKPMHLLLDIPGIDHSRLEAAWALVLEKHISFRSIYVEHQGRVYQAFLRQPDTVSIPIRWCDEPVHECAARFCEQDVDLILDGRPWWSMTRINNKIDSVLVLRLTHAQWDALTLDVLFKDFMAAYESRELSRRDLEFPAYMRFRLRHNASPATVRFWSTFLHGSRLTQPLLLDGAAEVDPGNEAMVFVSQQIPMLTPPHGITLGSVFRAAWAFVLARYTGQEDVVFGEFVEGRSLLVKSVEKVTGCAAAETPMRIVVSPTASVRDLLKHSQEQYVARIPYETCELEDIVPSSTSWPTDTTFNHILVIQHEPVLPPVALDGRPCPHRWAFHGRLEDVYVQMVFGPDTLHVGMSGPEIRLSRTIATQLVEKLASTITQFNDRPEALLSEITV
What is the function of this protein?
Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the antitumor fumiquinazolines that confer a dual-usage capability to defend against phagocytes in the environment and animal hosts (PubMed:20225828, PubMed:20804163, PubMed:21899262, PubMed:24612080, PubMed:33705521).  The simplest member is fumiquinazoline F (FQF) with a 6-6-6 tricyclic core derived from anthranilic acid (Ant), tryptophan (Trp), and alanine (Ala) (PubMed:20225828).  The trimodular NRPS fmqA is responsible for FQF formation (PubMed:20225828).  Modules 1, 2 and 3 of fmqA are predicted to activate and load Ant, Trp and Ala, respectively, providing for the assembly of an Ant-Trp-Ala-S-enzyme intermediate that would undergo double cyclization for chain release and generation of the tricyclic 6-6-6 product fumiquinazoline F (PubMed:20225828).  The presence of an E domain predicted for module 2 of fmqA is consistent with epimerization of L-Trp to D-Trp during assembly to generate the R-stereocenter at C14 of FQF (PubMed:20225828).  The FAD-dependent monooxygenase fmqB and the monomodular NRPS fmqC then maturate FQF to FQA (PubMed:20804163).  FmqB oxidizes the 2',3'-double bond of the indole side chain of FQF, and fmqC activates L-Ala as the adenylate, installs it as the pantetheinyl thioester on its carrier protein domain, and acylates the oxidized indole for subsequent intramolecular cyclization to create the 6-5-5-imidazolindolone of FQA (PubMed:20804163).  The FAD-linked oxidoreductase fmqD introduces a third layer of scaffold complexity by converting FQA to the spirohemiaminal FQC, presumably by catalyzing the formation of a transient imine within the pyrazinone ring (PubMed:21899262).  FQC subsequently converts nonenzymatically to the known cyclic aminal FQD (PubMed:21899262).
What are the official names of this protein?
Nonribosomal peptide synthetase fmqC, Fumiquinazoline biosynthesis cluster protein C.
What is the protein family that this protein belongs to?
Belongs to the NRP synthetase family.
What are the subcellular locations of this protein?
Cytoplasm.