| IED ID | IndEnz0007000537 |
| Enzyme Type ID | catalase000537 |
| Protein Name |
Highly reducing polyketide synthase cnsI EC 2.3.1.- Communesin biosynthesis cluster protein I |
| Gene Name | cnsI PEX2_055430 |
| Organism | Penicillium expansum (Blue mold rot fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Penicillium Penicillium expansum (Blue mold rot fungus) |
| Enzyme Sequence | MSTETQPEMASTPPEPIAIIGMSCRLSGEASSVDGFWDMLRNGRTGHGRVPSSRYEASAWYHPNQDRKGGINHDSGFFLEEDPSRFDAPFFSITAKEAAGMDPTQRLLLEVAYETFENSGVPMESLPGSRTGVFTGCMTNDYELLSTGDLYNMPHNAATGNARAMLANRLSWFFDLRGPSIMLDTACSSSLTALHLASKSLRDGECEMALVSGASLILHPNFTQRLSSMHMLSPDGISHSFDASANGYGRGEGFAAVLLKPLRTALADNDAIRAIIRATGINQDGRTPGITMPSRQAQAGLIRALYGPGLPSLQETAFFEAHGTGTKVGDPTELSAIGECLMGAETSTNDRLYVGSVKGNIGHTEGAAGVASLIKVVLCLENDMLVPNAGFSKLNSNIHLDKWLLRLSDKTIRWPSHLPRRASINSFGFGGSNAHAIVESASTYLERPAALLSGLDKGEPQIVVFSTHDKTGIDRVAAKWGPFLQAQIDAEQNISFRDIAYTMYARRSQLSFRSFAVAGSLGQLRDALQQGLPHFLRANGTAHANLAFVFTGQGAQWAQMGVELLQVTSFRESITRSEQILSSLGCPWNLFEEIQVEAATSRMNQPDRSQSICCALQIALVNLLASWGVHPKATVGHSSGEIGAAYAAGFITQEDAIRIAYFRGLCSLQVACHGRAGAMLAANLSLPDAQTYLQGVPPRSVVVACVNGPKSVTLSGDADRIDQLEKQLQADGLFARKLRVETAYHSPHMNMVAEGYRHDLQDIQPAKCGESSIAMFSSVTKERVYATDMTADYWVRNLVSPVEFLSAVTSLANMTEASQYRHRAVAVKWSAFLEIGPHEALKGPFLQVLKSINAGLSTVPYHALVRRHADALQTTLNVAGLLWCIGIPIDIEAVNSSINTAVPQLMHNLPSYPWNHQGSFWHEPVASARLRKRREPHHDLLGSPMDFQNDTEPRWRNFLRVSDIPWLADHVVADSILFPAAGMIVMVAEAGRILANTSLRLEGIEFNDLAFLQGLVIPDDDRGVETVLHVAPYHELAEWYEFTLFSLPEDGPWVRHATGTFTLHYDARGVPLNVEEWGLSVERFRKIQTAECETNRDAVYEWLSQTGGVTMGPAFQSVSRAAFCTEENRLWIEGEVTDTRTMMPSEYASPCFIHPTSLDTLFQAAVLSCSDALGNQNAKIPVGVDRLYLSTTWDLQQGDYFSVHTETCLNDGDSRLDSIASDVSWSQPRVVLKGVRLGPVPMSKVPSTSTTAGVDSGTSRFSSIVWAQHLESPTSPALAGHDRDGQLTDWVRDICYTYGNACALVVTQPSWKSPAMTSIQTVRPQLGSRPCLQGLTIVIVGLDKAADEFATAVTRLMPGAQVKQIAALQDFSPSTFNESFFDVVLVDQPCIGNAADADVLLTSLSSTTKQDGVLAVRTYDSQLDPMDYIQRSSEWKVSGRIRDGDFLLAHRQRIPAPLDSTIFVLMPDTEQIPPTFRVALERALSAVGVKLCPVDVEDINGLAGKMVISLLEFRHPWTSKWTSVAMAQFKMLLEARYILWVSPIPILSKDASAASFGASTGLLRTLRNEQPGVTLPQVQYDPDDPNSETSLAQGILQVIQLTLVPVPHRNHDMEYRLQHGRLLVPRVVSEAVVDDKMQTLLHGPRPILARLADDPRALRFHAGSPDGHGGQWVEDRQLVSDVPDDHVEVQLSLRSVVARGSRNFNAHESRLSVVEAVGVIRKLGFAGSTDLSVGDIVVLLVPGAGTVDGMSNRIQVSSKAVAKLPAQLTLAQAVTVPLAYILAYTSLFDIARLGPNCRVLLVGPVGPILRALLSCALEIRGMQVYVATEERAVVEELVAQYAIAPEYVLSIHGGLDGRIADLTEGKGVTAVLSCLGGSSGRLAARCLGSGGHYVDLTGEMNLAALPKAVVSQGCTFTSVNLNSMLQNQSEKVYSSFRRAVATIGLHHQIQPTSIFPISKWAEAESLARQTGISVAIDFTDPGQVPVVPALQEPVNLPPQQTYLLAGGLGMIGLGFAKTLVDSGARHLVILSRSGVLQPSQRIAVASLADQGCHVEIIRCDISQEADLQQVLSQVRSQNWQLKGIIQCATVLKDAAFHTMTFEDWASSTNPKILGTLNLHKVFVDVDLDFFITLSSVSGLIGNIGQANYAAGNVFMDELMIWRRAHGLPGHSIDIGLVPDASGMSDMAETAEVRRSRYSHLEGTEITLRELQMLLRVIILGDIPVPVQIIAGITDDLPREGASSWQYDRKLDHRVRLGHSEPDNMPAQISELLKSSPTIEDASYVVNQALREYLASAMATTADTIDSDLPLSSLGVDSLKVTEVQNWVSRKMGAQLSSFDFLGMQPLRVLSEKIAAQSAFVTVS |
| Enzyme Length | 2363 |
| Uniprot Accession Number | A0A0A2JW91 |
| Absorption | |
| Active Site | ACT_SITE 187; /note=For beta-ketoacyl synthase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10022; ACT_SITE 638; /note=For malonyltransferase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10022; ACT_SITE 970; /note=For beta-hydroxyacyl dehydratase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10022 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 2.3.1.- |
| Enzyme Function | FUNCTION: Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of communesins, a prominent class of indole alkaloids with great potential as pharmaceuticals (PubMed:25571861). Communesins are biosynthesized by the coupling of tryptamine and aurantioclavine, two building blocks derived from L-tryptophan (PubMed:25571861). The L-tryptophan decarboxylase cnsB converts L-tryptophan to tryptamine, whereas the tryptophan dimethylallyltransferase cnsF converts L-tryptophan to 4-dimethylallyl tryptophan which is further transformed to aurantioclavine by the aurantioclavine synthase cnsA, probably aided by the catalase cnsD (PubMed:25571861). The cytochrome P450 monooxygenase cnsC catalyzes the heterodimeric coupling between the two different indole moieties, tryptamine and aurantioclavine, to construct vicinal quaternary stereocenters and yield the heptacyclic communesin scaffold (PubMed:26963294). The O-methyltransferase cnsE then methylates the communesin scaffold to produce communesin K, the simplest characterized communesin that contains the heptacyclic core (PubMed:25571861). The dioxygenase cnsJ converts communesin K into communesin I (PubMed:25571861). Acylation to introduce the hexadienyl group at position N16 of communesin I by the acyltransferase cnsK leads to the production of communesin B. The hexadienyl group is produced by the highly reducing polyketide synthase cnsI, before being hydrolytically removed from cnsI by the serine hydrolase cnsH, converted into hexadienyl-CoA by the CoA ligase cnsG, and then transferred to communesin I by cnsK (PubMed:25571861). Surprisingly, cnsK may also be a promiscuous acyltransferase that can tolerate a range of acyl groups, including acetyl-, propionyl-, and butyryl-CoA, which lead to communesins A, G and H respectively (PubMed:25571861). The roles of the alpha-ketoglutarate-dependent dioxygenases cnsM and cnsP have still to be determined (PubMed:25571861). {ECO:0000269|PubMed:25571861, ECO:0000269|PubMed:26963294}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:25571861}. |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Modified residue (1); Region (5) |
| Keywords | Multifunctional enzyme;Oxidoreductase;Phosphopantetheine;Phosphoprotein;Reference proteome;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 2317; /note=O-(pantetheine 4'-phosphoryl)serine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00258 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 256,832 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |