ATR8_STAC4
ID ATR8_STAC4 Reviewed; 625 AA.
AC A0A084R1J7;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Baeyer-Villiger monooxygenase ATR8 {ECO:0000303|PubMed:25015739};
DE EC=1.14.13.- {ECO:0000305|PubMed:25015739};
DE AltName: Full=Core atranone cluster (CAC) protein 8 {ECO:0000303|PubMed:25015739};
GN Name=ATR8 {ECO:0000303|PubMed:25015739}; ORFNames=S40285_03333;
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, AND
RP FUNCTION.
RC STRAIN=IBT 40285;
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: Baeyer-Villiger monooxygenase; part of the core atranone
CC cluster (CAC) which products are predicted to catalyze most or all
CC steps of mycotoxin atranone synthesis, starting from geranylgeranyl
CC pyrophosphate (GGPP) (PubMed:25015739). The initial cyclization of GGPP
CC to dolabellane is probably performed by the terpene cyclase ATR13
CC (PubMed:25015739). The Baeyer-Villiger oxidation near the end of the
CC atranone synthesis, which converts atranones D and E to atranones F and
CC G is predicted to be catalyzed by the monooxygenase ATR8
CC (PubMed:25015739). Of the CAC's other predicted gene products, the
CC reducing PKS ATR6 might synthesize a polyketide chain
CC (PubMed:25015739). This polyketide is probably transferred onto the
CC atranone backbone by the polyketide transferase ATR5 (By similarity).
CC Other predicted CAC products include 4 oxygenases (ATR2, ATR3, ATR4,
CC and ATR14), 3 short-chain reductases (ATR7, ATR9, and ATR10), and a
CC methyltransferase (ATR12) (PubMed:25015739). These may all be involved
CC in the various steps of atranone biosynthesis, although their specific
CC roles must await experimental determination (PubMed:25015739).
CC {ECO:0000250|UniProtKB:Q4WAY4, ECO:0000305|PubMed:25015739}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q47PU3};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q47PU3};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25015739}.
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; KL659308; KFA70082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084R1J7; -.
DR SMR; A0A084R1J7; -.
DR EnsemblFungi; KFA70082; KFA70082; S40285_03333.
DR HOGENOM; CLU_006937_8_2_1; -.
DR OMA; HIAYIIA; -.
DR OrthoDB; 405736at2759; -.
DR Proteomes; UP000028524; Unassembled WGS sequence.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..625
FT /note="Baeyer-Villiger monooxygenase ATR8"
FT /id="PRO_0000442403"
FT BINDING 112
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 120..123
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 130..132
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 132
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 138
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 266..272
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 289..290
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 405..406
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT SITE 406
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
SQ SEQUENCE 625 AA; 70493 MW; 4DC6B30489E4037C CRC64;
MAVEKVQAFE KVSIPTEKQP GSEDLGFDPA ELQKKYEAER NLRIQNGGVS QYRSAWKSGF
GYYLEDPNAD ANFSRDPISA RYDVVIMGGG FSGLLVAARL VQQGITNFTI LDKSADFGGT
WYWSRYPGAQ CDVDSTIYLP LLEEVGYIPK EKYSFGPEIL EHAQRIAKHF GLYPKALFQT
EVKTCHWSEE DSLWTVQTDR GDNLRAQFIV SAFGISHMPK LPGISGIENF QGKSFHASRW
DYNYTGGDST GNMTKLADKR VGIIGTGATA IQVVPKLAES AKELYVFQRT PSSVDVRNNR
PTDAEWAKTL RPGWQQERID NFYAITTGEN VTEDLIDDGW TEIFRLVAAP FFASADIEQS
LENRMEQVQI ADFKKMESVR ARVDSLVKDP ATAASLKPWY NQFCKRPCFH DEYLQAFNHP
NVTLVDTRGH GVDAVTTKGV LAQGKEYELD CLIYSTGYEW YTEWEQRTRS QVYGRNGLTI
TKKWSQGITT YHGWGVHGFP NFMVLSSAQV NNVPNYTHMV GYLSRHLAYI VRTCKDRGIK
SVEPTATAES KWVQQVVEQG AARRDQMKLC TPGYLNHEGD ITEKTDRLYS YNGSGDSKFQ
IILDKWRDDG KLVGLSIDCA TEADL
