Detail Information for IndEnz0010001783
IED ID IndEnz0010001783
Enzyme Type ID esterase001783
Protein Name Non-reducing polyketide synthase SAT8
EC 2.3.1.-
Satratoxin biosynthesis SC1 cluster protein 8
Gene Name SAT8 S7711_07282
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 MATTLLLFGPQAASMSKQSITQLQVALRDQEWAFDALSNVQPIIQRASTSISGLDQISLDERLADLTRWLKHGPKDQEELAEIPNIMLAPLTTLSHLVQYRRYIERHYPNESDAHAALLQQKPVATLGFCNGLLAAFATTSSATLNDWERYAAVATRLALLVGAVIDAADELQPHGPAASYGVSWRDIDGARQLEQILSPFPGDAYVSVWYDRSRATVTVSKHLVRTVLHLVEAAGMAVVPVRLRGRYHSRQHAEVAEALIRLCDAEPDLLALPDARNLCLPTYSNVGHGEVVREGRLHEIALQAMLVQQCDWYSTLSGITDESQVQVVCLSEVSTLPPSLTFKLKPQMEYFAPLEEKTAPKDNFSGRADGGSQFSFSMLENSTSPPSPAATSSNSHCEYSVDPRDIAIVGMSVKVAGADDVVEYESILRGGVSQHQQVRKNRVPFGYNSFRPEEPGHKWYGNFVRDVDAFDHKFFRKSSRESAAMDPQQRLVLQAAYQAVEQSGYYASGTEPDQHIGVYLGTCATDYEQNANCHAPGAFTVTGLLRGFIAGRISHFFGWTGPAMTYDTACSGSAVAIHSAVQALVSGECSAALAGGVNTIGNEVWFQNLAGAQFLSPTGQCKPFDDAADGYCRGEGIACVVLKPMAKAIADGNQIFGRIASSAVHQSVNCTPLFVPNVPSLSRLFGDVMRQARLEPHDISFVEAHGTGTPVGDPVEYESIRAILGGPLRDKPLSLGSAKGLVGHTESTSGVVSLVKVLLMMQSGFIPPQASYSKLSHRIAPSASAMIQVSTTLQPWTDSYKAALINNYGASGSNAAMVVTQGPAQTARSPRGEADGAHLPFWIPGFDSARIAAYCARLSAFIEANRSTIHLADIAYNISRQSNRTLSHALLFRCNSIDSLVGQLSSAAAPQTVQVKPSRPVILCFGGQMSTFVGLNREIYDSSPILRDHLSQCDAAIRALGFGSIFPSIFATIPIEDTVLLQTVLFSFQYACAKSWIDCGVRPTAVVGHSFGEITALCIAEVLSLDDTIKLVTRRAKVVRDSWGADRGVMMAVEGEVDQVERLLEEANKDLDTHSPASIACYNGLRNFTLAGSTLAMERVALALSSSAYASIRGKKLNVTNAFHSALVDPLLQELEQAGSDLTFNKARIKVERATKESTTGEPCAPKFVGEHMRNPVFFRQAAQRLARDNPSAVWIEAGSATKITAMARRSLDSNAESHFQGITVTGEDGLDKLTEATLSLWKQGLNVAFWAHHGPQATRDHQPLLLPPYQFEKSRHWLDVKAPPVMLADTAQGDNGPLFGLLTFVGFQDAEERRARFKINTESERYKSLVIPHIIARTAPICPATLEYSLAIQALLTLRDHKHFESRDMHPVIRDMRNDAPLCLNSDQSTWLDLEANKTSPRSLVWKVFTAPVSRQLDSHNDSDETLCAQGKLDLLSSSETTEFAQYEQLATYDACVSLLQDDDGDVSGLQGRSVYRSLADVVDYGVHYQKVRRVSGRNSESAGIVRGASGGNWLSDLPIIDSFSQVAGVWVNCLADRTPGSDDLFLATGCETIMTSPTFLHADRGGKSWHVWAKHHRESERSYRTDVLVFDATNGQLADVFLGIAYTRIPRHSMTRLLSKLSEPSALQAQAALPSSTGHEGLTAKTASSQRLGQDTLKQTVGQIIASLSGVEAAQITDESALADIGIDSLAGMELARDIESVLGCKLDLEELLFTHDTFGAFVRYISKVVNGEDDLGTPSHSDNDSHVTGTTATPNSSSASSDTHHGNSKLQIAVAQSSQADASSSSPLPPQHVISSFEQVKLSTDQRIREEKADNTDDIIVSRSNLLCVALVVEAFEQLGCPLRGVPAGEALKRIQHAPQHARLVDWLYRFLEDEARLINTEGTLILRTSNGAPNKTSQAIFQDLEHANDRWIESHRLANYAGKNLADVVSGKKEGIHVLFGSAEGRELVRGLYSGLPFNCLFYKQVRDTISLIVEKVKDDFQGPLRILEMGAGTGGTTQVLAPFLATLDIPVEYTMTDLSPYMVAQAQRSFGTKYPFMHFAVHDIEKPPAESLLGTQHIIVASNAVHATANLADSAANIRSTLRPDGILLLVEMTESLPFVDIVFGLLEGWWRFADGREHAIVPAEQWEARLRDAGYGHVDWTDGVFSENRLQKVILAMASELPDGLPVSSGVPEPVQPALEVTTTVAREANAEAYVTQYSADFTYDGESSGNIEAHEAQDSRIVVVTGATGSLGSHMVASFAESPSVTSVVCINRRNSGKATALERQQEAFTSRGITLSPDAFGKLRVFATDTAQPQLGLPLEEYEWLVTHATHIVHNAWPMSASRPIQAFQPQFKTMSRLLDLAAAIAQQSTSRFVVFQLISSIGVVGSAPMIDTRVPERRVPVSYTLPNGYCEAKWVCEQLLNETLHQYPERFRAMVVRPGQIAGSSVNGVWNPVEHFPALVRSSQALRAFPALGGTLQWIPVDVAAGTVADLALNQQAGEPVYHIDNPVGQSWSNMVPILADELNIPGERIIPLGEWVRKVKRSSLLETENPASRLPDFFEQHFERMSCGGLILDVALATKRSGTLAAQGAVSADTARKYIQTWKDMKFLDRY
Enzyme Length 2602
Uniprot Accession Number A0A084B9Z6
Absorption
Active Site ACT_SITE 130; /note=Nucleophile; for transacylase activity; /evidence=ECO:0000250|UniProtKB:A0A0K0MCJ4; ACT_SITE 249; /note=Proton donor/acceptor; for transacylase activity; /evidence=ECO:0000250|UniProtKB:A0A0K0MCJ4; ACT_SITE 571; /evidence=ECO:0000255|PROSITE-ProRule:PRU10022
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 2.3.1.-
Enzyme Function FUNCTION: Non-reducing polyketide synthase; part of the satratoxin SC1 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); Compositional bias (1); Domain (1); Modified residue (1); Region (7)
Keywords Acyltransferase;Methyltransferase;Multifunctional enzyme;NADP;Phosphopantetheine;Phosphoprotein;S-adenosyl-L-methionine;Transferase
Interact With
Induction
Subcellular Location
Modified Residue MOD_RES 1692; /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 283,398
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda