SAT2_STACB
ID SAT2_STACB Reviewed; 354 AA.
AC A0A084B9Z0;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Short-chain dehydrogenase/reductase SAT2 {ECO:0000303|PubMed:25015739};
DE EC=1.-.-.- {ECO:0000305|PubMed:25015739};
DE AltName: Full=Satratoxin biosynthesis SC1 cluster protein 2 {ECO:0000303|PubMed:25015739};
GN Name=SAT2 {ECO:0000303|PubMed:25015739}; ORFNames=S7711_07276;
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, FUNCTION,
RP AND PATHWAY.
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: Short-chain dehydrogenase/reductase; part of the satratoxin
CC SC1 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}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; KL647604; KEY74369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084B9Z0; -.
DR EnsemblFungi; KEY74369; KEY74369; S7711_07276.
DR HOGENOM; CLU_044999_0_0_1; -.
DR OrthoDB; 1164708at2759; -.
DR Proteomes; UP000028045; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NAD; NADP; Oxidoreductase.
FT CHAIN 1..354
FT /note="Short-chain dehydrogenase/reductase SAT2"
FT /id="PRO_0000442410"
FT BINDING 23..31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 53..55
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 86..88
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 210..216
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 245..247
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 354 AA; 38713 MW; 4496F49B8B9005E2 CRC64;
MPSLQVIRAA VAELPQGSSI VAAVAGGTTG IGSYLAKALA TTFASHGSKL RVYIVGRNAG
RAKTVISECQ KISPGSDWRF IHATDLALIS EVDKSSAEII KQETEAPFHG ELARLDLLYM
THAIPILGHK RTTEEGLDAL ESTIYYSRIR FILQLLPLLT ASPRVAHVIS VYAGGMENGV
KPDEEPIGFV PAEIYHFNTV RKYTTFMKTF VFEELAEKYA ERLSLIHIYP GLVDGPGFTQ
MPRWFRVLFT LMKPLTSLYM TRSEDCGMVM AYLATSRFSA KGSGQDAPTS TDTLAPKSSL
GVVGGGAYSL GQRADSQTPQ IMFEKSRKPD TSKKAWDHTI RTLDDIAKKN ATIA
