SAT13_STACB
ID SAT13_STACB Reviewed; 2383 AA.
AC A0A084API3;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Highly reducing polyketide synthase SAT13 {ECO:0000303|PubMed:25015739};
DE EC=2.3.1.- {ECO:0000305|PubMed:25015739};
DE AltName: Full=Satratoxin biosynthesis SC2 cluster protein 13 {ECO:0000303|PubMed:25015739};
GN Name=SAT13 {ECO:0000303|PubMed:25015739}; ORFNames=S7711_09751;
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: Highly reducing polyketide synthase; part of the satratoxin
CC SC2 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 -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25015739}.
CC -!- MISCELLANEOUS: Trichothecenes are sesquiterpenoid toxins that act by
CC inhibiting protein biosynthesis. {ECO:0000305}.
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DR EMBL; KL648628; KEY67212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084API3; -.
DR SMR; A0A084API3; -.
DR EnsemblFungi; KEY67212; KEY67212; S7711_09751.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OrthoDB; 19161at2759; -.
DR Proteomes; UP000028045; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
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; -; 1.
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; IPR011032; GroES-like_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
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; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
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 Multifunctional enzyme; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW Transferase.
FT CHAIN 1..2383
FT /note="Highly reducing polyketide synthase SAT13"
FT /id="PRO_0000442402"
FT DOMAIN 2287..2364
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 9..436
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 536..828
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 922..1239
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1669..1977
FT /note="Enoylreductase (ER) domain"
FT REGION 2001..2184
FT /note="Catalytic ketoreductase (KRc) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 180
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000250|UniProtKB:L7X8J4"
FT ACT_SITE 626
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:L7X8J4"
FT ACT_SITE 954
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000250|UniProtKB:L7X8J4"
FT MOD_RES 2324
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2383 AA; 260819 MW; 7393F7F1717AF2A4 CRC64;
MSGPNPVPLA IVGIACRFPG DATNPERFWD LLANARSGWS RVPNDRWNEE AFWHPDPDDT
NGTNNHMGGH FLNQDLARFD AGFFNVTPQE AASMDPQQRL LLETTYEALE SAGIPQEHIR
GSNTAAYMAM FTRDYDRNVY KDMMSIPKYH VTGTGDAILA NRISHLFDLR GPSVTMDTGC
SGGLTAISHA CQALRSGLSD IGLAGAVNLI LTPDHMVGMS NLHMLNVNGR SFSFDSRGAG
YGRGEGVATL VIKRLDDAIR DKDPVRAILR DAAINQDGYT AGITLPSGRA QQALERRVWD
VLNLDPATVG YVEAHGTGTL AGDSAELEGI SKIFCENRDH GSPLIVGSVK SNIGHTECVS
GIAAVIKSTL ILENGTIPPN INFEQPRESL DLRNKKIKVP NALMPWPQTT GTARISVNSF
GYGGTNAHAV LERAERVIDT TCPQEDDAPQ LFIFSAASQT SLLGMLAANR DWVSENRERA
WVMRDLAYTL SQRRSLLPWR FSCVAANRSE LLETLSSVPQ NANSIARITP GSRISFIFTG
QGAQWAGMGR ELLSMPTFNS SLQRSNEILQ DLGCSWDLIE EVSKQKPESR LHEPELSQPL
TTAIQIALVD LFREWGIVPD SVIGHSSGEI GAAYTAGHIA HCQAIKVAYF RGFSSAWAAQ
AHKRGAMLAV GLGEYDVEPY LEQLGQGHAS IACQNSPNST TVSGDDAAIS ELSEILTKES
IFNRKLNITV AYHSHHMQTA ACQYKAALEP LLTNPSLDTG IEMFSTVTGS IKKDAFNSNY
WVENLVSKVR FCDGLQALCE STQASPLGSS KAERIFIEIG PHSALAGPTR QCIADLITPL
PYSYTSGLLR ETGAVKSALA MVGHIFNRGY SLNLAAISAS NKTSQYATVL SNLPSYHWDH
TRRHWNESRI SREYRFRKHP YHDLLGLRMT EVSPLRPSWR HMIGTKGLPW LADHVVDDLV
IFPGSGYLAM AIEACSQLAD DRYPGREIER FSLNDIFFLK GLIIPDDGAR VEVQLSLNPI
EPADKDTRMN VMQHEFSVTA FTDEARWNEH CRGNIVVVFK TSSATERLVA NGFTRGDMAA
QLDPVSGKLT HAGQLYPELR KAGNSYGLTF NGIQRMKIGA DSASSDVIIP DVVSRMPACH
MRPHIIHPTT LDILLHTTLP LVHQKLGVGS VMPVHIRNMD VSADIESTPR KMFRVVTTLT
SSHARAADTE LFVFSEEGHV DDTPVVSAAG MELRSFVARD SNDAGSSDGH RDICSELKWI
PDERFITAKH LQVLQPSILT KDALARCYAL MAQYLKQMAI KHSDLSVLEL GGDDTTSGAT
KTFLEVFHAG GTAPAMYDFC TSLKDFDVIQ RKLEAFDCEK VHKMEMKRIE LDAVSENRYD
VVLSCNTIYN AADVKSVLSH ARKLLKLDGV LLFVEDMSSR ESRSSSEWSK LMSEASFKMQ
LAVTDNDATR QLTFFATRAV EDAIASVHNV SIVSGCNLPL HIQNFLPQIE SELGSKGMQV
TRSRWDKLPP NGTDIYIIVD DGSRPILSGI NQDRFRIVTG LLQKTARIIW LSVQDDETFR
FNPRKHLITG LSRTAHAENE GLDMVTIDVQ ETLNQKTQPE VIGFLSQVVG LFDCKHITRE
REYVYNGTDI LIPRLIPHQR LNLQVSGKIG TSIEAMAFTN SSVPLKLSDG QNRLVFVENM
DHKQALCHDY VEIETKAVGL PPGFNGVQSG NTVYEYAGII IAVGSEVSTL KAGDRAVAYS
STPCANVLRV PAIQAQLIPS NLSFKDAAAM PRALMAVSHA LVHIANVQPG QVVFVDDAAT
EIGLAAICVA QNLGSTLIAA VSTKEEAAFI KNTFKVPSRH IVPRDSYFGQ RQVRTLVRPN
GGLDVILGCG KSPVTAVTSE LLKPFGLLVH VRNRASDPKR YDGTGYPPNL TVASFDIDSL
LQASTKNSAE LFQKVMEMVN RGMIPPSQSI VAIEAGIKIE EAISLAQKQG SMKKCVLEFN
ENSIVNVETS FHHIPSLKPH ATYVVAGGLG DLGQRLLRLM AQAGARHLVS LSRKGAGSKE
FRGLEKELKG VHPGCSLLAI DCDILREESV SAALAEIKQQ GFPTVKGVVQ SAVILKDATL
DSMTAELFNS VVSVKAEGTL NLHRVFIQEE LAFFISFSSV MSIIGGKAQA NYNAGNAVQD
AFAQFERRNP HCFYMSLNIG GIKDAAVNND AIVQSIRRQG LTQISHEELS SYLKYAFSDD
ARKTGCKQPV IGFTAETIVS TTAVNGTAHT PMFTHVRQKP TAKTTVGNVN EKRSFKDIVN
SGTNKGEISE FVARSICDKI ADLTGIDLAE VNLDSGISDY GLDSLVSIEL RNWLMREFDS
PIQSSEVLDS HGIRDLAQKV VSRSRLVTTE TDVVHTVNGE APT
