SAT7_STACB
ID SAT7_STACB Reviewed; 470 AA.
AC A0A084B9Z5;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=FAD-dependent monooxygenase SAT7 {ECO:0000303|PubMed:25015739};
DE EC=1.-.-.- {ECO:0000305|PubMed:25015739};
DE AltName: Full=Satratoxin biosynthesis SC1 cluster protein 7 {ECO:0000303|PubMed:25015739};
GN Name=SAT7 {ECO:0000303|PubMed:25015739}; ORFNames=S7711_07281;
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: FAD-dependent monooxygenase; 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=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25015739}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Trichothecenes are sesquiterpenoid toxins that act by
CC inhibiting protein biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; KL647604; KEY74374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084B9Z5; -.
DR SMR; A0A084B9Z5; -.
DR EnsemblFungi; KEY74374; KEY74374; S7711_07281.
DR HOGENOM; CLU_009665_6_3_1; -.
DR OrthoDB; 521070at2759; -.
DR Proteomes; UP000028045; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Membrane; Monooxygenase; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..470
FT /note="FAD-dependent monooxygenase SAT7"
FT /id="PRO_0000442414"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 58..59
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 268..270
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 351
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 361..365
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
SQ SEQUENCE 470 AA; 50994 MW; D9A004F81C7319F8 CRC64;
MSTSTSEPGA IAGLPLGAEV RTDGDATGLS VAIVGGGIVG IALALGLVER GVRVSVYERA
QELPEIGVGF AFNGAARKSM ARLSPLVMAA VERVANENEQ AYDNYWDGYT STAEDDESST
ASKRGKLLFR MPNSNMAWWS CLRSQFLNEM LQALPPGTVT FGKELDSYDD PFDTSDPVRL
RFTDGTTAAA NVLIGSDGLR SRVRQQLFAT SHPEVCNPTY THKTCYRAVI PMAAAESAMG
LSKPHNHCMH TGPRAHVLSY PIAQHKLVNV VLFVTHDEPW VDGTGDEAIS VPRMTRPGDK
KVLQNRLADW RPEVRNLVAQ LPDAPTAWGI FDTAEHPVPF YAAGRVGLVG DAAHASSPHH
GAGAGFGVED ALALAVALGM ATEKKQSVAA ALQAFNDVRY DRTQWLIRSS KETGDIYEWK
HFGVGGDPVK IRAELEGRQK TIWDYDVDAM AEEVKTRYEA RVTSETTAHQ
