ATR3_STAC4
ID ATR3_STAC4 Reviewed; 478 AA.
AC A0A084R1J1;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Cytochrome P450 monooxygenase ATR3 {ECO:0000303|PubMed:25015739};
DE EC=1.-.-.- {ECO:0000305|PubMed:25015739};
DE AltName: Full=Core atranone cluster (CAC) protein 3 {ECO:0000303|PubMed:25015739};
GN Name=ATR3 {ECO:0000303|PubMed:25015739}; ORFNames=S40285_03328;
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: Cytochrome P450 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=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25015739}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KL659308; KFA70076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084R1J1; -.
DR SMR; A0A084R1J1; -.
DR EnsemblFungi; KFA70076; KFA70076; S40285_03328.
DR HOGENOM; CLU_022195_1_0_1; -.
DR OMA; EYIMISA; -.
DR OrthoDB; 467733at2759; -.
DR Proteomes; UP000028524; 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; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
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; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..478
FT /note="Cytochrome P450 monooxygenase ATR3"
FT /id="PRO_0000442385"
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 478 AA; 53631 MW; 74CFBE92A62AE6EB CRC64;
METLSQRITS MESVQLQGIA VAFVTASALY YVLPAAISHI QLSALPMLGK TEVVVIPPKL
LSELSKSPRT LSAEIAGNEF IAGKYTKVKA LTPILLHSIT KYLIPSLGRN AVVMSEEVSN
AVRLGIPTCN DWTGVNIYPK IMRMVTVSTG RFLVGSELNR SEDYIDTVHN YALDVSSAQS
AVHKMHPWIR PLLAEWLPEI RRLRKRTEEA FALFESLIKE RMKMQRELSE SELPDDLLQW
MIANRHNYNN EDAHDLVYSQ LGLTFTANHS TASTITNALY TLATMGDLID VIRDDITQAL
AESGGQFTSK ALDSMWKFDS FIKETVRMNP LVMSVAVRKV VEPIKLPSGQ VIPTGVTLET
PLVAVNLDDQ IFPNADVFDP MRFYNLREKD RKQGDAREAE FNQLISSSTS HMSWGFGKHT
CPGRAFAAQQ IKMILAHIIL RYDIKLVGDS TDRYENIPKG HLSLPDPTKD ILMKRREI
