Protein: SPKS1_STRTC
Sequence: MSPTAEIPKPVAVVGISAEFPSGTLSDANFDHQSFFDFLLSGKDAVERIPKDRFNIDGWQGSHLGQILPEDACFLKNVHLFDHFEFGISSKDALTMGAGTRKLVEHSFLALLDSGINCRSQNVAAFSSAVAFDLLSAADADEFEPRDGFGGGAAAVANRISYQLDLLGPSIPVDTACSSSLMALHLGVQSLRAGECEAAVIGGSQINHRFLDWIFYSQLSILSPGGKSIPFDSSADGFGRGEAVVVLVVKLLEDAIRDGDKIYATVLNTAVNSTGSAGPVKTPIAESQAAAMLTAYKGIGRSPSEADFIECHATGTSVGDPVEANWVGNHFKRDSELLIGSVKGNVGHTEITSFLTSFSKVISMFDTNRIPPQANFKEPNPAIHWEEYNMRTPTQIEGFTTRNPSGKRLASINASGLLGANGHVIAESPPPKAAKPSALPTGMPVLLMAAGLSPRSTTAIAADLSKLASEIPDELPILSNIFGRRARQLTWRAAAISTSDGPFVFPAPRFVPRGTPQLVFVFSGQGPQHIEMGRQLFKYYPVFRDSILKMDKVHVELTGKSIVKDLGFFGETRSSTALPDVWPVGLTVPSIAMIQMALVDLLAAFGIRPNLVFGHSAGEAAMSYTSGALPQELAMEIAVRRSQAMSIVEGSGGMAAVSCAPSVAREIVQEVLDEAGPDSGVLEIGCFNAPEAFTISGTHALLDKAVAIASGRGLFARKIKARVPGHCTLMEPCKERYVEQMEVAFSRYPGAHVPVVPTFSTQTGARWESEFTPEYMWNNGRVPVQFEQTVTAVVQEMPEAIFVEIGPHPALSSYISGMGAKPDKVVCPMRRVKNVTGFNEIFELLTAVGNLSTLGVNTINFHAVNATDCLEISKPIPAYPFAPKTMPFYSESSELAVKMKRSRKGPLNYDTLAVNALTHPDLAEHVIKGEPILPATGFFEMIFEEGARTIWDIELRSLLPLLPEKVLNVNVKSDGHAWSIVSSSGGRNPRLHATGFMTTEVMDKDAGPIDLAAIRARTTPADISNLYAILNNTAAFGPLYRRIEACYEGDHEILYQVRGNAPELTAHYNYVFHPSLLDSCIHGLLHPVFTGNADKSVFYLPSHIGRVTLYDRAIEEAVPETLYSYVVPHDWTPDSIACDAFIVNERGERLVTLIDCVLSKHWTGAVPTRPDTSYEYIYQPLGLPAAELVKSEAQQQDYAFLDAIVAHADEKVAPPSANGHANGHANGSANGSAVGTVGEDRKVFEEIVQSIASDELELKASSILGLFSASLDAPVAAVRQILDHAAKSGKQVVRILDIGDATASLYKQINAFASEYPSLRVDYTACGHEHATLDLRLASYNVDNVSKQAGLSPSTYDVIIETHTLGFAAELDRSLEYLHGLLLPGGFLVALEANGSAQASGGKWIDQVFSPQGRWSGLRSGKQHHRLSQSEWSGQLQKAKFQVVDGAQDAENTLFLTLLAQKHSLSTVSASSAASSAKVEEPAVFSFDHSRVLDLQKTVLASMSSGASNTKLWIESTTGTFDGAVATGFARSLMRELVAVDVRLVLFDPAWKAESRIPAIRQLSTLPSLESEIVLDASGVVMVPRLRSYAPRAPDSLDTTKYWVVDETKTVVQPAQPLPGPHQVLVKISSLSEAEGGLRGIVGTVARSGSSQWPVGAHVVTVAPSALSNFTLVHEGQLAQAPQTADEHSTAKVALLLVFAALGLRLDSRPLQSLQQIKVVVIHTGTVASSLARLLEYLGVKPVLVAPSLPLLLPRLSPGDVIIGGLSAAFARTVPRINGVSVFNWEDPEQGALAAVAQNPWLVGTTVDAHLARALPQVSVEGSSLTPDQLLPSDFSVSQSLALADDKTYLVLGGIGSLGLQIAIWMYQKGARHIVLTSRTGVSRLAGTKNRSLRGAVEYLKTLPDLELRLEPCDASSEESLSKLISSLDRPLAGAMLTAAVMADGLFLKQSADTYPIPFKPKTDAYFAFEKVVDIKKLDFLLAVSSVAGFGAAGQTNYASANTGIEYLTARYPNAWSFVAPGIADSNVGFDLFTSTNSHLEQWESSTMNSYEICLCLEDGLLRMANNERISIYVPNLNWDAISQSVSESVLYNHLVKLDAATDELEVEDPYEVLQEIVLKFVDASEEEFERNVPLTSYGLDSLSAARMSTALKPYLAITQIQLLGDLSLDDLVEKMQATKHVAVEETAVSTAEKPFAWDAMHQPGQTILKFNIGSGTPLIILHGGAGDTAAFRAIQEQFSTPLWAIQPTPEAPLDTVDTLAQFYFEKIKEARPAGPYRIAGFSASSMVTLRLAQLLEANEDEIAQLTFVDHFPLFFTSAIHGFTEDHKTFEDLTAYGRKASVALVAECCRRDTATARRLYGENLVAASNGQPSATNAMESWEWIQKTTRMNLKQVVDFGGGWEAWASSDATTRMEAARRRMVEEIAKVKAPMNVMIANWGIRALINSEWTDLGISRGGREVRTQYYDAGHFDIFEKPDFSRNLEFDWVDPHPVHQLATMIHNPAMNDLRALFKILDTKALQVMADTISQNPVVGSEISRQRLFEVCKEFVRTQKHSTWTDEEYEHSKALFPTYFETTERISKVHPSIMESPAAAVGALYSDDMIDGFYRQNKVFTSMNQEAAKTFKALVSSPDFGKQRPIRVLEVGAGVGGLTKFLVEALCDMPNADVEYTVTDLSYTLASSLAESFSYKNMVAKMYDLSKKPSEQGLQLGHYDVITGLNVIHAVPDLNATLTDLHSLLAPGGRILIVDTDGTARTSNPPRPGAIWNDFIWGSFQGWFGYTDDRTHCTIDEDEWRKRLTATGYSNVQVCHEDAGTCILFEAEKV
What is the function of this protein?
Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta-methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain (PubMed:30258052).  Strobilurin biosynthesis begins with construction of benzoyl CoA by step-wise elimination of ammonia from phenylalanine by the phenylalanine ammonia-lyase str11, oxygenation by str8 and retro-Claisen reaction to form benzoic acid, which is activated to its CoA thiolester benzoyl CoA by the dedicated CoA ligase str10 (PubMed:30258052).  Benzoyl CoA forms the starter unit for the highly reducing polyketide synthase stpks1 that produces the polyketide prestrobilutin A (PubMed:30258052).  The FAD-dependent oxygenase str9 then catalyzes the key oxidative rearrangement responsible for the creation of the beta-methoxyacrylate toxophore (PubMed:30258052).  Str9 performs epoxidation of the 2,3 olefin of prestrobilutin A, followed by Meinwald rearrangement to furnish the aldehyde intermediate (Probable).  Rapid enolization of the aldehyde intermediate would give the beta-methoxyacrylate skeleton and methylations catalyzed by str2 and str3 complete the synthesis and lead to the production of strobilurin A (Probable).  The short-chain dehydrogenase stl2 and the dehydrogenase str4 play a role in the shunt pathway leading to the production of bolineol (PubMed:30258052).  The cluster encodes no obvious halogenase gene that could be involved in production of strobilurin B, nor any obvious dimethylallyl-transferase that could be involved in the production of strobilurin G (Probable).  It is possible that unknown proteins encoded in, or near, the cluster (such as str1 or stl1) may form new classes of halogenases or dimethylally-transferases, or that the responsible genes are located elsewhere on the genome (Probable).  Similarly, proteins encoded by str5/str6 hydrolases appear to have no chemical role in the biosynthesis of strobilurin A (Probable).  Finally, no obvious self-resistance gene is found within the cluster (Probable).
What are the official names of this protein?
Highly reducing polyketide synthase stpks1, Strobilurin A biosynthesis cluster protein pks1.