SAT11_STACB
ID SAT11_STACB Reviewed; 526 AA.
AC A0A084API1;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Cytochrome P450 monooxygenase SAT11 {ECO:0000303|PubMed:25015739};
DE EC=1.-.-.- {ECO:0000305|PubMed:25015739};
DE AltName: Full=Satratoxin biosynthesis SC2 cluster protein 11 {ECO:0000303|PubMed:25015739};
GN Name=SAT11 {ECO:0000303|PubMed:25015739}; ORFNames=S7711_09749;
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: Cytochrome P450 monooxygenase; part of the satratoxin SC2
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=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
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 cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KL648628; KEY67210.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084API1; -.
DR SMR; A0A084API1; -.
DR EnsemblFungi; KEY67210; KEY67210; S7711_09749.
DR HOGENOM; CLU_001570_14_4_1; -.
DR OrthoDB; 1247045at2759; -.
DR Proteomes; UP000028045; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..526
FT /note="Cytochrome P450 monooxygenase SAT11"
FT /id="PRO_0000442399"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 455
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 526 AA; 59882 MW; C0C2570459620FDE CRC64;
MTIPTSFEML KGMHIKDAFL LIAMLYLGYL LCICFYNIYL HPLRHIPGSK LAVMGPYLEF
YHEVIRQGQY LWEIEKMHDK YGPIVRVNER EIHIRDSSYY HTIYAAGSRK TNKDAATVGA
FDVPNSTAAT VDHDQHRARR GYLNPYFSKR SLANLEPTIH ERISKLLNRL EQHQNNDDII
TLDGIFSALT ADVICSRFYG KHFDYLSIPD YHFVVRDGFQ GLTKLYHLGR FLPTLVTILK
CLPQQIIRLI LPNLADLIVM RDEIQANGIA QFTSSQTADS KASALVGALG DKNIPPHERT
VARLLDEGTV FLFAGTETTS RTLAVTMFYL LTNPDCLKKL RAELDTLPST EDYQHSLSTL
ESLPYLSGVV HEGLRLAFGP ITRSARVPMN VDLQYKEYTI PAGTPLSMST YFVHTDKELY
PEPEKFKPER WIQAAEENIP LKKFLTNFSQ GSRQCIGISM SFAEMYLTIS RVARAYNFEL
YETTAADLDM TYARIVPYPK EIPGKTEGLG EIRVKIVGKN HSQIEE
