SAT8_STACB
ID SAT8_STACB Reviewed; 2602 AA.
AC A0A084B9Z6;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Non-reducing polyketide synthase SAT8 {ECO:0000303|PubMed:25015739};
DE EC=2.3.1.- {ECO:0000305|PubMed:25015739};
DE AltName: Full=Satratoxin biosynthesis SC1 cluster protein 8 {ECO:0000303|PubMed:25015739};
GN Name=SAT8 {ECO:0000303|PubMed:25015739}; ORFNames=S7711_07282;
OS Stachybotrys chartarum (strain CBS 109288 / IBT 7711) (Toxic black mold)
OS (Stilbospora chartarum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1280523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, AND
RP FUNCTION.
RC STRAIN=CBS 109288 / IBT 7711;
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the satratoxin SC1
CC cluster involved in the biosynthesis of satratoxins, trichothecene
CC mycotoxins that are associated with human food poisonings
CC (PubMed:25015739). Satratoxins are suggested to be made by products of
CC multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins in
CC all, including polyketide synthases, acetyltransferases, and other
CC enzymes expected to modify the trichothecene skeleton
CC (PubMed:25015739). SC1 encodes 10 proteins, SAT1 to SAT10
CC (PubMed:25015739). The largest are SAT8, which encodes a putative
CC polyketide synthase (PKS) with a conventional non-reducing
CC architecture, and SAT10, a putative protein containing four ankyrin
CC repeats and thus may be involved in protein scaffolding
CC (PubMed:25015739). The putative short-chain reductase SAT3 may assist
CC the PKS in some capacity (PubMed:25015739). SAT6 contains a secretory
CC lipase domain and acts probably as a trichothecene esterase
CC (PubMed:25015739). SAT5 encodes a putative acetyltransferase, and so,
CC with SAT6, may affect endogenous protection from toxicity
CC (PubMed:25015739). The probable transcription factor SAT9 may regulate
CC the expression of the SC1 cluster (PubMed:25015739). SC2 encodes
CC proteins SAT11 to SAT16, the largest of which encodes the putative
CC reducing PKS SAT13 (PubMed:25015739). SAT11 is a cytochrome P450
CC monooxygenase, while SAT14 and SAT16 are probable acetyltransferases
CC (PubMed:25015739). The SC2 cluster may be regulated by the
CC transcription factor SAT15 (PubMed:25015739). SC3 is a small cluster
CC that encodes 5 proteins, SAT17 to SAT21 (PubMed:25015739). SAT21 is a
CC putative MFS-type transporter which may have a role in exporting
CC secondary metabolites (PubMed:25015739). The four other proteins
CC putatively encoded in SC3 include the taurine hydroxylase-like protein
CC SAT17, the O-methyltransferase SAT18, the acetyltransferase SAT19, and
CC the Cys6-type zinc finger SAT20, the latter being probably involved in
CC regulation of SC3 expression (PubMed:25015739).
CC {ECO:0000305|PubMed:25015739}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000255};
CC Note=Binds 1 phosphopantetheine covalently. {ECO:0000255};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25015739}.
CC -!- DOMAIN: Multidomain protein; including an N-terminal starter unit:ACP
CC transacylase (SAT) domain, a beta-ketoacyl synthase (KS) domain, a
CC malonyl-CoA:ACP transacylase (MAT) domain, a product template domain, a
CC acyl carrier protein (ACP) domain, a methyltransferase domain and a
CC reductive NADPH-binding domain that is required for NADPH-dependent
CC product release (PubMed:25015739). {ECO:0000305|PubMed:25015739}.
CC -!- MISCELLANEOUS: Trichothecenes are sesquiterpenoid toxins that act by
CC inhibiting protein biosynthesis. {ECO:0000305}.
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DR EMBL; KL647604; KEY74375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084B9Z6; -.
DR SMR; A0A084B9Z6; -.
DR EnsemblFungi; KEY74375; KEY74375; S7711_07282.
DR HOGENOM; CLU_000022_6_2_1; -.
DR OrthoDB; 13314at2759; -.
DR Proteomes; UP000028045; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR041068; HTH_51.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Phosphopantetheine; Phosphoprotein; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..2602
FT /note="Non-reducing polyketide synthase SAT8"
FT /id="PRO_0000442401"
FT DOMAIN 1658..1733
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 379..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..825
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 926..1216
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000255"
FT REGION 1331..1616
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1737..1772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1979..2150
FT /note="Methyltransferase domain"
FT /evidence="ECO:0000255"
FT REGION 2229..2530
FT /note="NADPH-binding domain"
FT /evidence="ECO:0000255"
FT COMPBIAS 1745..1772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /note="Nucleophile; for transacylase activity"
FT /evidence="ECO:0000250|UniProtKB:A0A0K0MCJ4"
FT ACT_SITE 249
FT /note="Proton donor/acceptor; for transacylase activity"
FT /evidence="ECO:0000250|UniProtKB:A0A0K0MCJ4"
FT ACT_SITE 571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1692
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2602 AA; 283398 MW; 66F5F6A33B5DA342 CRC64;
MATTLLLFGP QAASMSKQSI TQLQVALRDQ EWAFDALSNV QPIIQRASTS ISGLDQISLD
ERLADLTRWL KHGPKDQEEL AEIPNIMLAP LTTLSHLVQY RRYIERHYPN ESDAHAALLQ
QKPVATLGFC NGLLAAFATT SSATLNDWER YAAVATRLAL LVGAVIDAAD ELQPHGPAAS
YGVSWRDIDG ARQLEQILSP FPGDAYVSVW YDRSRATVTV SKHLVRTVLH LVEAAGMAVV
PVRLRGRYHS RQHAEVAEAL IRLCDAEPDL LALPDARNLC LPTYSNVGHG EVVREGRLHE
IALQAMLVQQ CDWYSTLSGI TDESQVQVVC LSEVSTLPPS LTFKLKPQME YFAPLEEKTA
PKDNFSGRAD GGSQFSFSML ENSTSPPSPA ATSSNSHCEY SVDPRDIAIV GMSVKVAGAD
DVVEYESILR GGVSQHQQVR KNRVPFGYNS FRPEEPGHKW YGNFVRDVDA FDHKFFRKSS
RESAAMDPQQ RLVLQAAYQA VEQSGYYASG TEPDQHIGVY LGTCATDYEQ NANCHAPGAF
TVTGLLRGFI AGRISHFFGW TGPAMTYDTA CSGSAVAIHS AVQALVSGEC SAALAGGVNT
IGNEVWFQNL AGAQFLSPTG QCKPFDDAAD GYCRGEGIAC VVLKPMAKAI ADGNQIFGRI
ASSAVHQSVN CTPLFVPNVP SLSRLFGDVM RQARLEPHDI SFVEAHGTGT PVGDPVEYES
IRAILGGPLR DKPLSLGSAK GLVGHTESTS GVVSLVKVLL MMQSGFIPPQ ASYSKLSHRI
APSASAMIQV STTLQPWTDS YKAALINNYG ASGSNAAMVV TQGPAQTARS PRGEADGAHL
PFWIPGFDSA RIAAYCARLS AFIEANRSTI HLADIAYNIS RQSNRTLSHA LLFRCNSIDS
LVGQLSSAAA PQTVQVKPSR PVILCFGGQM STFVGLNREI YDSSPILRDH LSQCDAAIRA
LGFGSIFPSI FATIPIEDTV LLQTVLFSFQ YACAKSWIDC GVRPTAVVGH SFGEITALCI
AEVLSLDDTI KLVTRRAKVV RDSWGADRGV MMAVEGEVDQ VERLLEEANK DLDTHSPASI
ACYNGLRNFT LAGSTLAMER VALALSSSAY ASIRGKKLNV TNAFHSALVD PLLQELEQAG
SDLTFNKARI KVERATKEST TGEPCAPKFV GEHMRNPVFF RQAAQRLARD NPSAVWIEAG
SATKITAMAR RSLDSNAESH FQGITVTGED GLDKLTEATL SLWKQGLNVA FWAHHGPQAT
RDHQPLLLPP YQFEKSRHWL DVKAPPVMLA DTAQGDNGPL FGLLTFVGFQ DAEERRARFK
INTESERYKS LVIPHIIART APICPATLEY SLAIQALLTL RDHKHFESRD MHPVIRDMRN
DAPLCLNSDQ STWLDLEANK TSPRSLVWKV FTAPVSRQLD SHNDSDETLC AQGKLDLLSS
SETTEFAQYE QLATYDACVS LLQDDDGDVS GLQGRSVYRS LADVVDYGVH YQKVRRVSGR
NSESAGIVRG ASGGNWLSDL PIIDSFSQVA GVWVNCLADR TPGSDDLFLA TGCETIMTSP
TFLHADRGGK SWHVWAKHHR ESERSYRTDV LVFDATNGQL ADVFLGIAYT RIPRHSMTRL
LSKLSEPSAL QAQAALPSST GHEGLTAKTA SSQRLGQDTL KQTVGQIIAS LSGVEAAQIT
DESALADIGI DSLAGMELAR DIESVLGCKL DLEELLFTHD TFGAFVRYIS KVVNGEDDLG
TPSHSDNDSH VTGTTATPNS SSASSDTHHG NSKLQIAVAQ SSQADASSSS PLPPQHVISS
FEQVKLSTDQ RIREEKADNT DDIIVSRSNL LCVALVVEAF EQLGCPLRGV PAGEALKRIQ
HAPQHARLVD WLYRFLEDEA RLINTEGTLI LRTSNGAPNK TSQAIFQDLE HANDRWIESH
RLANYAGKNL ADVVSGKKEG IHVLFGSAEG RELVRGLYSG LPFNCLFYKQ VRDTISLIVE
KVKDDFQGPL RILEMGAGTG GTTQVLAPFL ATLDIPVEYT MTDLSPYMVA QAQRSFGTKY
PFMHFAVHDI EKPPAESLLG TQHIIVASNA VHATANLADS AANIRSTLRP DGILLLVEMT
ESLPFVDIVF GLLEGWWRFA DGREHAIVPA EQWEARLRDA GYGHVDWTDG VFSENRLQKV
ILAMASELPD GLPVSSGVPE PVQPALEVTT TVAREANAEA YVTQYSADFT YDGESSGNIE
AHEAQDSRIV VVTGATGSLG SHMVASFAES PSVTSVVCIN RRNSGKATAL ERQQEAFTSR
GITLSPDAFG KLRVFATDTA QPQLGLPLEE YEWLVTHATH IVHNAWPMSA SRPIQAFQPQ
FKTMSRLLDL AAAIAQQSTS RFVVFQLISS IGVVGSAPMI DTRVPERRVP VSYTLPNGYC
EAKWVCEQLL NETLHQYPER FRAMVVRPGQ IAGSSVNGVW NPVEHFPALV RSSQALRAFP
ALGGTLQWIP VDVAAGTVAD LALNQQAGEP VYHIDNPVGQ SWSNMVPILA DELNIPGERI
IPLGEWVRKV KRSSLLETEN PASRLPDFFE QHFERMSCGG LILDVALATK RSGTLAAQGA
VSADTARKYI QTWKDMKFLD RY
