| IED ID | IndEnz0005000104 |
| Enzyme Type ID | lipase000104 |
| Protein Name |
Highly reducing polyketide synthase SAT13 EC 2.3.1.- Satratoxin biosynthesis SC2 cluster protein 13 |
| Gene Name | SAT13 S7711_09751 |
| Organism | Stachybotrys chartarum (strain CBS 109288 / IBT 7711) (Toxic black mold) (Stilbospora chartarum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Stachybotryaceae Stachybotrys Stachybotrys chartarum (Toxic black mold) (Stilbospora chartarum) Stachybotrys chartarum (strain CBS 109288 / IBT 7711) (Toxic black mold) (Stilbospora chartarum) |
| Enzyme Sequence | MSGPNPVPLAIVGIACRFPGDATNPERFWDLLANARSGWSRVPNDRWNEEAFWHPDPDDTNGTNNHMGGHFLNQDLARFDAGFFNVTPQEAASMDPQQRLLLETTYEALESAGIPQEHIRGSNTAAYMAMFTRDYDRNVYKDMMSIPKYHVTGTGDAILANRISHLFDLRGPSVTMDTGCSGGLTAISHACQALRSGLSDIGLAGAVNLILTPDHMVGMSNLHMLNVNGRSFSFDSRGAGYGRGEGVATLVIKRLDDAIRDKDPVRAILRDAAINQDGYTAGITLPSGRAQQALERRVWDVLNLDPATVGYVEAHGTGTLAGDSAELEGISKIFCENRDHGSPLIVGSVKSNIGHTECVSGIAAVIKSTLILENGTIPPNINFEQPRESLDLRNKKIKVPNALMPWPQTTGTARISVNSFGYGGTNAHAVLERAERVIDTTCPQEDDAPQLFIFSAASQTSLLGMLAANRDWVSENRERAWVMRDLAYTLSQRRSLLPWRFSCVAANRSELLETLSSVPQNANSIARITPGSRISFIFTGQGAQWAGMGRELLSMPTFNSSLQRSNEILQDLGCSWDLIEEVSKQKPESRLHEPELSQPLTTAIQIALVDLFREWGIVPDSVIGHSSGEIGAAYTAGHIAHCQAIKVAYFRGFSSAWAAQAHKRGAMLAVGLGEYDVEPYLEQLGQGHASIACQNSPNSTTVSGDDAAISELSEILTKESIFNRKLNITVAYHSHHMQTAACQYKAALEPLLTNPSLDTGIEMFSTVTGSIKKDAFNSNYWVENLVSKVRFCDGLQALCESTQASPLGSSKAERIFIEIGPHSALAGPTRQCIADLITPLPYSYTSGLLRETGAVKSALAMVGHIFNRGYSLNLAAISASNKTSQYATVLSNLPSYHWDHTRRHWNESRISREYRFRKHPYHDLLGLRMTEVSPLRPSWRHMIGTKGLPWLADHVVDDLVIFPGSGYLAMAIEACSQLADDRYPGREIERFSLNDIFFLKGLIIPDDGARVEVQLSLNPIEPADKDTRMNVMQHEFSVTAFTDEARWNEHCRGNIVVVFKTSSATERLVANGFTRGDMAAQLDPVSGKLTHAGQLYPELRKAGNSYGLTFNGIQRMKIGADSASSDVIIPDVVSRMPACHMRPHIIHPTTLDILLHTTLPLVHQKLGVGSVMPVHIRNMDVSADIESTPRKMFRVVTTLTSSHARAADTELFVFSEEGHVDDTPVVSAAGMELRSFVARDSNDAGSSDGHRDICSELKWIPDERFITAKHLQVLQPSILTKDALARCYALMAQYLKQMAIKHSDLSVLELGGDDTTSGATKTFLEVFHAGGTAPAMYDFCTSLKDFDVIQRKLEAFDCEKVHKMEMKRIELDAVSENRYDVVLSCNTIYNAADVKSVLSHARKLLKLDGVLLFVEDMSSRESRSSSEWSKLMSEASFKMQLAVTDNDATRQLTFFATRAVEDAIASVHNVSIVSGCNLPLHIQNFLPQIESELGSKGMQVTRSRWDKLPPNGTDIYIIVDDGSRPILSGINQDRFRIVTGLLQKTARIIWLSVQDDETFRFNPRKHLITGLSRTAHAENEGLDMVTIDVQETLNQKTQPEVIGFLSQVVGLFDCKHITREREYVYNGTDILIPRLIPHQRLNLQVSGKIGTSIEAMAFTNSSVPLKLSDGQNRLVFVENMDHKQALCHDYVEIETKAVGLPPGFNGVQSGNTVYEYAGIIIAVGSEVSTLKAGDRAVAYSSTPCANVLRVPAIQAQLIPSNLSFKDAAAMPRALMAVSHALVHIANVQPGQVVFVDDAATEIGLAAICVAQNLGSTLIAAVSTKEEAAFIKNTFKVPSRHIVPRDSYFGQRQVRTLVRPNGGLDVILGCGKSPVTAVTSELLKPFGLLVHVRNRASDPKRYDGTGYPPNLTVASFDIDSLLQASTKNSAELFQKVMEMVNRGMIPPSQSIVAIEAGIKIEEAISLAQKQGSMKKCVLEFNENSIVNVETSFHHIPSLKPHATYVVAGGLGDLGQRLLRLMAQAGARHLVSLSRKGAGSKEFRGLEKELKGVHPGCSLLAIDCDILREESVSAALAEIKQQGFPTVKGVVQSAVILKDATLDSMTAELFNSVVSVKAEGTLNLHRVFIQEELAFFISFSSVMSIIGGKAQANYNAGNAVQDAFAQFERRNPHCFYMSLNIGGIKDAAVNNDAIVQSIRRQGLTQISHEELSSYLKYAFSDDARKTGCKQPVIGFTAETIVSTTAVNGTAHTPMFTHVRQKPTAKTTVGNVNEKRSFKDIVNSGTNKGEISEFVARSICDKIADLTGIDLAEVNLDSGISDYGLDSLVSIELRNWLMREFDSPIQSSEVLDSHGIRDLAQKVVSRSRLVTTETDVVHTVNGEAPT |
| Enzyme Length | 2383 |
| Uniprot Accession Number | A0A084API3 |
| Absorption | |
| Active Site | ACT_SITE 180; /note=For beta-ketoacyl synthase activity; /evidence=ECO:0000250|UniProtKB:L7X8J4; ACT_SITE 626; /note=For malonyltransferase activity; /evidence=ECO:0000250|UniProtKB:L7X8J4; ACT_SITE 954; /note=For beta-hydroxyacyl dehydratase activity; /evidence=ECO:0000250|UniProtKB:L7X8J4 |
| 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 satratoxin SC2 cluster involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings (PubMed:25015739). Satratoxins are suggested to be made by products of multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins in all, including polyketide synthases, acetyltransferases, and other enzymes expected to modify the trichothecene skeleton (PubMed:25015739). SC1 encodes 10 proteins, SAT1 to SAT10 (PubMed:25015739). The largest are SAT8, which encodes a putative polyketide synthase (PKS) with a conventional non-reducing architecture, and SAT10, a putative protein containing four ankyrin repeats and thus may be involved in protein scaffolding (PubMed:25015739). The putative short-chain reductase SAT3 may assist the PKS in some capacity (PubMed:25015739). SAT6 contains a secretory lipase domain and acts probably as a trichothecene esterase (PubMed:25015739). SAT5 encodes a putative acetyltransferase, and so, with SAT6, may effect endogenous protection from toxicity (PubMed:25015739). The probable transcription factor SAT9 may regulate the expression of the SC1 cluster (PubMed:25015739). SC2 encodes proteins SAT11 to SAT16, the largest of which encodes the putative reducing PKS SAT13 (PubMed:25015739). SAT11 is a cytochrome P450 monooxygenase, while SAT14 and SAT16 are probable acetyltransferases (PubMed:25015739). The SC2 cluster may be regulated by the transcription factor SAT15 (PubMed:25015739). SC3 is a small cluster that encodes 5 proteins, SAT17 to SAT21 (PubMed:25015739). SAT21 is a putative MFS-type transporter which may have a role in exporting secondary metabolites (PubMed:25015739). The four other proteins putatively encoded in SC3 include the taurine hydroxylase-like protein SAT17, the O-methyltransferase SAT18, the acetyltransferase SAT19, and the Cys6-type zinc finger SAT20, the latter being probably involved in regulation of SC3 expression (PubMed:25015739). {ECO:0000305|PubMed:25015739}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25015739}. |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Modified residue (1); Region (5) |
| Keywords | Multifunctional enzyme;Oxidoreductase;Phosphopantetheine;Phosphoprotein;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 2324; /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 | 260,819 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |